|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
125-218 |
1.10e-29 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 113.45 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 125 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 204
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 578817221 205 TQATDSILVFEVEV 218
Cdd:pfam00254 80 VIPPNATLVFEVEL 93
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
116-218 |
1.84e-26 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 104.49 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 116 QDLIVADGPAVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACA 195
Cdd:COG0545 4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....*.
gi 578817221 196 VGSEG---VIGwtqaTDSILVFEVEV 218
Cdd:COG0545 80 YGERGaggVIP----PNSTLVFEVEL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
552-814 |
1.80e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQE 631
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 632 TSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 712 KKtrvstdQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQN 791
Cdd:COG1196 397 EL------AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|...
gi 578817221 792 EQHIKELEKNKSQMSGVEAAASD 814
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
510-826 |
1.33e-18 |
|
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: 92.04 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 510 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 588
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 589 LKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 668
Cdd:TIGR02168 754 KELTELEAEIEELEERLEE-------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 669 ESLEKNLsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LA 746
Cdd:TIGR02168 827 ESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 747 SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
.
gi 578817221 826 V 826
Cdd:TIGR02168 981 I 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
495-736 |
3.46e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNS------LQTATENTQARVLHAEQ 568
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 569 EKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 648
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEQLSL 728
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLL 496
|
....*...
gi 578817221 729 VQAELQTQ 736
Cdd:COG1196 497 LEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
504-814 |
9.62e-18 |
|
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: 89.35 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QEN-ERLkQEILeksNRIEEQNDKISELIERNQRYVEQSNlmmEKRN----------NSLQTATENTQARVLHAEQEKAK 572
Cdd:TIGR02168 185 RENlDRL-EDIL---NELERQLKSLERQAEKAERYKELKA---ELRElelallvlrlEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 652
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 653 KVTSLEEELTDLRVEKESLEKNLSERKKKS-----------------AQERSQAEEEIDEIRKSYQEELDKLRQL---LK 712
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELeelesrleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLedrRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 713 KTRVSTDQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 790
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
330 340 350
....*....|....*....|....*....|
gi 578817221 791 NEQH------IKELEKNKSQMSGVEAAASD 814
Cdd:TIGR02168 498 QENLegfsegVKALLKNQSGLSGILGVLSE 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
492-819 |
7.73e-17 |
|
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: 86.28 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 492 TSMI-MSNIQR--IIQE----------NERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSN-------LMMEKRN-- 549
Cdd:TIGR02169 145 TDFIsMSPVERrkIIDEiagvaefdrkKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqaLLKEKREye 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 550 --------NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETEL----QMQLTESLKEtdlLRG 617
Cdd:TIGR02169 225 gyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGE---LEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 618 QLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR 697
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 698 ------KSYQEELDKLRQLLK--KTRVSTDQAAAEQLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRD---AY 766
Cdd:TIGR02169 382 etrdelKDYREKLEKLKREINelKRELDRLQEELQRLSEELADLNAA--------IAGIEAKINELEEEKEDKALeikKQ 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578817221 767 QQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKV 819
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
501-790 |
1.21e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 501 RIIQENERLKQEILEKSNRIEEQNDKISELIERNQryveqsnlMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAA 580
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 581 TAQVSHLQLKMTAHQKKETELQMQLTESL------------KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 648
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 649 QLELKVTSLEEELTDLRVEKESLE----------KNLSERKKKSAQERSQAEEEIDEIRKSYQE---ELDKLRQLLKKTR 715
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 716 VsTDQAAAEQLS----------------LVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC 777
Cdd:TIGR02169 924 A-KLEALEEELSeiedpkgedeeipeeeLSLEDVQAELQRVEEEIraLEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
330
....*....|...
gi 578817221 778 LALQAQITALTKQ 790
Cdd:TIGR02169 1003 KAILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
498-834 |
1.23e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 498 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 577
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 578 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSL 657
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 658 EEELTDLRVEKESLEKNLSE----RKKKSAQ------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLS 727
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 728 LVQAELQ-TQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMS 806
Cdd:TIGR02168 924 LAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578817221 807 GVEAAASDPSEKVKKIM--------------NQVFQSLRREF 834
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEeaieeidrearerfKDTFDQVNENF 1045
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
499-759 |
6.39e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTAT----------ENTQARVLH 565
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLaelarleqdiARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 566 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQ 645
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 646 NRKQLELKVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAA 722
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEealAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270
....*....|....*....|....*....|....*..
gi 578817221 723 AEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEV 759
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-838 |
8.94e-15 |
|
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: 79.72 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 555 ATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 634
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 635 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN---LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 712 KKTRVSTDQAAAEQLSLVqaELQTQWEAKCEHLLASAK---------DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQA 782
Cdd:TIGR02168 824 ERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAeieeleeliEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 783 QITALTKQNEQHIKELEKNKSQMSGVEAAAsdpsEKVKKIMNQVFQSLRREFELEE 838
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRL----EGLEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
573-838 |
1.86e-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: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 VTEELAAataQVSHLQ------LKMTAHQKKETELQMQLTesLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 646
Cdd:COG1196 194 ILGELER---QLEPLErqaekaERYRELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 647 RKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQllkktRVSTDQAAA 723
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAelaRLEQDIARLEERRRELEERLEEL----EEELAELEE-----ELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 724 EQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKN 801
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270
....*....|....*....|....*....|....*..
gi 578817221 802 KSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
499-840 |
2.93e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRnnslqtatentqarvlhAEQEKAKVTEELA 578
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL----LEELNKKIKDL-----------------GEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 579 AATAQVSHLQlkmtaHQKKETELQMQLTEslketdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLE 658
Cdd:TIGR02169 298 ELEAEIASLE-----RSIAEKERELEDAE---------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 659 EELTDLRVEKESLEKNLSERKKKSAQER---SQAEEEIDEIRKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQT 735
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRL--SEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 736 QWEAKCEHLlasAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkqnEQHIKELEKNKSQMSGVEAAASDP 815
Cdd:TIGR02169 442 EKEDKALEI---KKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL----QRELAEAEAQARASEERVRGGRAV 512
|
330 340
....*....|....*....|....*
gi 578817221 816 SEKVKKIMNQVFQSLRREFELEESY 840
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
558-798 |
5.11e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 558 NTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQM--QLTESLKETDLLRGQLTKVQAKLSELqetsEQ 635
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERL----DA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 636 AQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 715
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 716 VStdQAAAEQLSLVQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRDA-------YQQKLVQLQEKCL-ALQAQI-TA 786
Cdd:COG4913 763 VE--RELRENLEERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDAdleslpeYLALLDRLEEDGLpEYEERFkEL 839
|
250
....*....|..
gi 578817221 787 LTKQNEQHIKEL 798
Cdd:COG4913 840 LNENSIEFVADL 851
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
495-837 |
1.70e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.98 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEksnrIEEQNDKISELIERNQryveqsnlmmeKRNNSLQTATENTQARVLHAEQEKAKVT 574
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQ-----------QEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 575 EELAAATAQVSHLQLKMTAHQKKETELQMQLTE--SLKETDL---LRGQLTKVQAKLSELqetseqaQSKFKSEKQNRKQ 649
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnNQKEQDWnkeLKSELKNQEKKLEEI-------QNQISQNNKIISQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 650 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrKSYQEELDKLRQLLKKtrvstdqaaAEQLSlv 729
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQN---------QEKLN-- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 730 qAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL--------------------TK 789
Cdd:TIGR04523 408 -QQKDEQIKK-----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlsrsinkIK 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578817221 790 QN-EQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 837
Cdd:TIGR04523 482 QNlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
500-834 |
3.20e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 500 QRIIQENERLK------QEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 573
Cdd:COG4717 139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 TEELAAATAQVSHLQLKMTAHQKKETELQMQ--------------LTESLKETDLLRGQLTKVQAKL-----SELQETSE 634
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLlallfLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 635 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVeKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE--LDKLRQLLK 712
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 713 KTRVSTD-------------QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLA 779
Cdd:COG4717 378 EAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 780 LQAQITALTKQNE-----QHIKELEKNKSQMsgVEAAASDpsEKVKKIMNQVFQSLRREF 834
Cdd:COG4717 458 LEAELEQLEEDGElaellQELEELKAELREL--AEEWAAL--KLALELLEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
495-834 |
9.41e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRI-----IQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQA-------- 561
Cdd:PRK03918 370 KKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------LKKEIKELKKAIEELKKakgkcpvc 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 562 -RVLHAEQEK---AKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE-----SLKET-DLLRG--------QLTKVQ 623
Cdd:PRK03918 442 gRELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELaEQLKEleeklkkyNLEELE 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 624 AKLSELQETSEQA------QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQErsqAEEEIDEIR 697
Cdd:PRK03918 522 KKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELE 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 698 KSYQE---------ELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQtQWEAKCEHLLASAKDEhlqQYQEVcaqrdayQQ 768
Cdd:PRK03918 599 PFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------RE 666
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 769 KLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVfQSLRREF 834
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERV-EELREKV 730
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
503-825 |
1.72e-11 |
|
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: 68.45 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 503 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARVLHAEQE--KAKV 573
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 TEE----LAAATAQVSHLQLKMtahqKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNrKQ 649
Cdd:COG5185 311 TESleeqLAAAEAEQELEESKR----ETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFK-DT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 650 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLK-KTRVSTDQAAAEQLSL 728
Cdd:COG5185 386 IESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISeLNKVMREADEESQSRL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 729 VQA------ELQTQWEAKCEHL------LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC-LALQAQITALTKQNEQHI 795
Cdd:COG5185 466 EEAydeinrSVRSKKEDLNEELtqiesrVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLkDFMRARGYAHILALENLI 545
|
330 340 350
....*....|....*....|....*....|
gi 578817221 796 KELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:COG5185 546 PASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
582-841 |
1.48e-10 |
|
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: 65.86 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 582 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 661
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 662 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEqlslVQAELQtqwEAKC 741
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLN---RLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 742 EHLLASAKDEHLQQYQEVC-AQRDAYQQKLVQLQEKCLALQAQItaltKQNEQHIKELEKNKSqmsgveaaasDPSEKVK 820
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL----EELEAALRDLESRLG----------DLKKERD 892
|
250 260
....*....|....*....|.
gi 578817221 821 KIMNQVFQSLRREFELEESYN 841
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIE 913
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
441-839 |
1.74e-10 |
|
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: 65.51 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 441 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 515
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 516 KSNRIEE----QNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARvlhaEQEkakVTEELAAATAQVSHLQLKM 591
Cdd:pfam05483 389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEELKGK----EQE---LIFLLQAREKEIHDLEIQL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 592 TA-------HQKKETELQMQL-TESLKETDLL---------RGQLTKVQAKLS-ELQETSEQAQSKFKSEKQNRKQLElk 653
Cdd:pfam05483 460 TAiktseehYLKEVEDLKTELeKEKLKNIELTahcdkllleNKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIE-- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 654 vtSLEEELTDLRVEKESLEKNLSERK-------KKSAQERSQAEEEI--------------DEIRKSYQEELDKLRQLLK 712
Cdd:pfam05483 538 --NLEEKEMNLRDELESVREEFIQKGdevkcklDKSEENARSIEYEVlkkekqmkilenkcNNLKKQIENKNKNIEELHQ 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 713 KTRVSTDQAAAEQLSLVQAELQTQweaKCEHLLASAK---DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAYEIKVN---KLELELASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221 790 QNE---QH-----IKELEKNKSQMSGVeAAASDPSEKVKKIMNQVFQSLRREFELEES 839
Cdd:pfam05483 693 EIDkrcQHkiaemVALMEKHKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELS 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
615-820 |
3.40e-10 |
|
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: 63.24 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 615 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLserkKKSAQERSQAEEEID 694
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 695 EIRKSYQEELDKL-----------------------RQLLKKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDE 751
Cdd:COG4942 101 AQKEELAELLRALyrlgrqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAAL-----RAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 752 HLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVK 820
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
593-793 |
4.02e-10 |
|
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: 63.24 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 593 AHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLE 672
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 673 KNLSERKKKSAQ---------------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTdQAAAEQ 725
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAEL-EAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221 726 LSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQ 793
Cdd:COG4942 176 LEALLAELEEERAA-----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
493-826 |
5.36e-10 |
|
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: 63.89 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 493 SMIMSNIQRIIQENER---LKQEI-------LEKSNRIEEQNDKISELIERNQRYVEQ--------SNL-----MMEKRN 549
Cdd:TIGR04523 328 NQISQNNKIISQLNEQisqLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEiknlesqiNDLeskiqNQEKLN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 550 NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQmQLTESLKE-TDLLRGQLTKVQAKLSE 628
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-NTRESLETqLKVLSRSINKIKQNLEQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 629 LQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEkeslEKNLSERKKKSAQERSQAEEEIDEIrksyqeELDKLR 708
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKD------DFELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 709 QLLKKTRVSTDQaAAEQLSLVQAEL---QTQweakcehllasaKDEHLQQyqevcaqrdaYQQKLVQLQEKCLALQAQIT 785
Cdd:TIGR04523 557 ENLEKEIDEKNK-EIEELKQTQKSLkkkQEE------------KQELIDQ----------KEKEKKDLIKEIEEKEKKIS 613
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578817221 786 ALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 826
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
500-822 |
7.69e-10 |
|
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: 63.22 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 500 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkRNNSLQTATENTQARvlhaEQEKAKvTEELAA 579
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKR----ELERIR-QEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 580 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQetseqaqsKFKSEKQNRKQLELKVTSLEE 659
Cdd:pfam17380 373 EISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME--------QIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 660 ELTDLRVEKESLEKNLS-ERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ---LSLVQAELQT 735
Cdd:pfam17380 445 AREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerkRKLLEKEMEE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 736 QWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKclalqAQITALTKQNE--QHIKELEKNKSqmsgvEAAAS 813
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREmmRQIVESEKARA-----EYEAT 594
|
....*....
gi 578817221 814 DPSEKVKKI 822
Cdd:pfam17380 595 TPITTIKPI 603
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
497-713 |
1.30e-09 |
|
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: 62.35 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 497 SNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER------------NQRYVEQSNL-MMEKRNNSLQTATENTQARV 563
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldNTRESLETQLkVLSRSINKIKQNLEQKQKEL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 564 LHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE------SLK------ETDLLRGQLTKV----QAKLS 627
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisDLEdelnkdDFELKKENLEKEidekNKEIE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 628 ELQET---SEQAQSKFK-------SEKQN-RKQLELK---VTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAE 690
Cdd:TIGR04523 572 ELKQTqksLKKKQEEKQelidqkeKEKKDlIKEIEEKekkISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIK 651
|
250 260
....*....|....*....|...
gi 578817221 691 EEIDEIRKSYQEELDKLRQLLKK 713
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTK 674
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
123-241 |
1.34e-09 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 60.55 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 123 GPAVEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLRLKLGSgkVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVI 202
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTL----IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
|
90 100 110
....*....|....*....|....*....|....*....
gi 578817221 203 GWtqATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 241
Cdd:PRK10902 232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
507-797 |
1.73e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSNRIEEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQArvlhaeqEKAKVTEELaaataQVSH 586
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKA-------EEARIEEVM-----KLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 587 LQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ------------AQSKFKSEKQNRKQLELKV 654
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkikaAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 655 tslEEEltDLRVEKESLEKNlSERKKKSAQERSQAEEEI---DEIRKSYQEELDKLRQLLKKTRvsTDQAAAEQLSLVQA 731
Cdd:PTZ00121 1683 ---AEE--DEKKAAEALKKE-AEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEE 1754
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221 732 ElqtqwEAKCEHLlasaKDEHLQQYQEVCAQRDAY-QQKLVQLQEKCLALQAQITALTKQNEQHIKE 797
Cdd:PTZ00121 1755 E-----KKKIAHL----KKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
505-805 |
2.71e-09 |
|
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: 61.20 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 505 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLmmekrnnslqtATENTQARVLHAEQEKAKVTEEL-AAATAQ 583
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAAL-----------AGTEATSGASRSAQDLAELLSSFsGSSTTD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 VSHLQLKMTAHQKKET---ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE 660
Cdd:pfam05667 292 TGLTKGSRFTHTEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 661 LTDLRVEKESLEKNLsERKKKSAQERSQAEEEIdeirksyqeelDKLRQLLkktrvstdQAAAEQLslvqAELQTQWEAK 740
Cdd:pfam05667 372 LEELKEQNEELEKQY-KVKKKTLDLLPDAEENI-----------AKLQALV--------DASAQRL----VELAGQWEKH 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 741 CEHLLasakdEHLQQYQEVCA-QRDAYQQKLVQLQ---EKCLalqaQITALTKQNEQHIKELEKNKSQM 805
Cdd:pfam05667 428 RVPLI-----EEYRALKEAKSnKEDESQRKLEEIKelrEKIK----EVAEEAKQKEELYKQLVAEYERL 487
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
450-840 |
3.83e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 450 EIRMAVSKVADKMDHLMTKVEELQKHsAGNSMLipSMSVTMETSMimSNIQRIIQE-----NERLKQ------EILEKSN 518
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQ-AENARL--EMHFKLKEDH--EKIQHLEEEykkeiNDKEKQvsllliQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 519 R-------IEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLqlkm 591
Cdd:pfam05483 255 KmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 592 tahqKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRK--QLELKVTSLE-EELTDLR--- 665
Cdd:pfam05483 330 ----TEEKEAQMEELNKAKAAHSF--VVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSElEEMTKFKnnk 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 666 -VEKESLEKNLSERKK---------KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVStDQAAAEQLSLVQAELQ- 734
Cdd:pfam05483 404 eVELEELKKILAEDEKlldekkqfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTELEk 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 735 -----TQWEAKCEHLLASAKD---------EHLQQYQEVCAQRDAYQQKLVQ----LQEKCLALQAQITALTKQNEQHIK 796
Cdd:pfam05483 483 eklknIELTAHCDKLLLENKEltqeasdmtLELKKHQEDIINCKKQEERMLKqienLEEKEMNLRDELESVREEFIQKGD 562
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 578817221 797 E----LEKNKSQMSGVEAAASdPSEKVKKIMNQVFQSLRREFELEESY 840
Cdd:pfam05483 563 EvkckLDKSEENARSIEYEVL-KKEKQMKILENKCNNLKKQIENKNKN 609
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
449-673 |
4.48e-09 |
|
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: 60.84 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 449 TEIRMAVSKVADKMDHLMTKVEELQKhsagnsmlipsmsvtmETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKIS 528
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 529 ELIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 588
Cdd:TIGR02168 334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 589 lkmtAHQKKETELQMQLTESLKETDL--LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV 666
Cdd:TIGR02168 414 ----DRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
....*..
gi 578817221 667 EKESLEK 673
Cdd:TIGR02168 490 RLDSLER 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
499-841 |
4.52e-09 |
|
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: 60.80 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENER---LKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTE 575
Cdd:TIGR04523 67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK-LEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 576 ELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELqetsEQAQSKFKSEKQNRKQLELKVT 655
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQIS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 656 SLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDqaaaeQLSLVQAE 732
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTteiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-----QLNQLKSE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 733 LQTQWEAKCEHLLASAKDEHLQ---QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVE 809
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350
....*....|....*....|....*....|..
gi 578817221 810 AAASDPSEKVKKIMNQVfQSLRREFELEESYN 841
Cdd:TIGR04523 377 KENQSYKQEIKNLESQI-NDLESKIQNQEKLN 407
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
596-813 |
4.61e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 596 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskfksekqnRKQLELKVTSLEEELTDLRVEKESLEKnl 675
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----------LEELEAELEELREELEKLEKLLQLLPL-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 676 serkkksAQERSQAEEEIDEirksYQEELDKLRQllKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDE---H 752
Cdd:COG4717 131 -------YQELEALEAELAE----LPERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 753 LQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkQNEQHIKELEKNKSQMSGVEAAAS 813
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
495-733 |
1.07e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLK--QEILEKsnrIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqtaTENTQARVLHAEQEKAK 572
Cdd:COG4913 223 TFEAADALVEHFDDLEraHEALED---AREQIELLEPIRELAERYAAARERLAELE-------YLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQ-AKLSELQETSEQAQSKFKSEKQNRKQLE 651
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDE-------LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 652 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQL------LKKTRVSTDQ----- 720
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeiasLERRKSNIPArllal 445
|
250
....*....|....*
gi 578817221 721 --AAAEQLSLVQAEL 733
Cdd:COG4913 446 rdALAEALGLDEAEL 460
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
507-734 |
1.22e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.38 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTD 663
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 664 LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQ 734
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
505-834 |
1.47e-08 |
|
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: 59.21 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 505 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTatENTQARVLHAEQEKAKVTEELAAataQV 584
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCG---SC 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 585 SHLQLKMTAHQKKETeLQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 664
Cdd:TIGR00618 511 IHPNPARQDIDNPGP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 665 RVEKESLEKnlsERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQTQWEAKCEHL 744
Cdd:TIGR00618 590 QNITVRLQD---LTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKL-TALHALQLTLTQERVREHA 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 745 LASAKDEhLQQYQEVCAQRDAYQQKLVQLQEKCLALqAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMN 824
Cdd:TIGR00618 665 LSIRVLP-KELLASRQLALQKMQSEKEQLTYWKEML-AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
330
....*....|
gi 578817221 825 QVFQSLRREF 834
Cdd:TIGR00618 743 QSLKELMHQA 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
495-737 |
1.49e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVlhaEQEKAKVT 574
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 575 EELAAA--TAQVSHLQLKMTAHQKKETELQMQLTESLKETDllRGQLTKVQAKLSELQetseqaqskfksekQNRKQLEL 652
Cdd:COG4942 108 ELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELA--------------ALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 653 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEElDKLRQLLKKTRVSTDQAAAEQLSLVQAE 732
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 578817221 733 LQTQW 737
Cdd:COG4942 251 LKGKL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
497-846 |
1.50e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 497 SNIQRIIQENErlkQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLqtatENTQARVLHAEQEKAKVTEE 576
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 577 LAAATAQVSHLQLKMTAHQKKETELQmQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtS 656
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----E 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 657 LEEELTDLRVEKESLEKNLSE---------------------RKKKSAQERSQAEEEIDEIRKS---YQEELDKLRQLLK 712
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEEleerhelyeeakakkeelerlKKRLTGLTPEKLEKELEELEKAkeeIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 713 --KTRVSTDQAAAEQLS-------LVQAELQtqwEAKCEHLLASAKDEH---LQQYQEVCAQRDAYQQKLVQLqEKCLAL 780
Cdd:PRK03918 416 elKKEIKELKKAIEELKkakgkcpVCGRELT---EEHRKELLEEYTAELkriEKELKEIEEKERKLRKELREL-EKVLKK 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 781 QAQITALTKQNEQhIKELEK--NKSQMSGVEAAASDpSEKVKKIMNQV---FQSLRREFELEESYNGRTIL 846
Cdd:PRK03918 492 ESELIKLKELAEQ-LKELEEklKKYNLEELEKKAEE-YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAE 560
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
546-713 |
1.65e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 546 EKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMtahQKKETELQMqlteslketdlLRGQLTKVQAK 625
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEIEE-----------VEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 626 LSELQETSE-QA-QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 703
Cdd:COG1579 82 LGNVRNNKEyEAlQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 578817221 704 LDKLRQLLKK 713
Cdd:COG1579 162 EAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
442-707 |
1.73e-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: 58.93 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 442 TEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSmsvtmetsmIMSNIQRIIQENERLKQEILEKSNRIE 521
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE---------LEEDLSSLEQEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 522 EQNDKISEL------------------IERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:TIGR02169 769 ELEEDLHKLeealndlearlshsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 -------VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:TIGR02169 849 iksiekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 657 LEEELTDL----RVEKESLEKNLSERKKKSAQERSQAE---------------EEIDEIRKSYQEELDKL 707
Cdd:TIGR02169 929 LEEELSEIedpkGEDEEIPEEELSLEDVQAELQRVEEEiralepvnmlaiqeyEEVLKRLDELKEKRAKL 998
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
590-735 |
3.11e-08 |
|
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: 54.91 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 590 KMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskFKSEKQNRKQLELKVTSLEEELTDLRVEKE 669
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 670 SLEknlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtRVstdQAAAEQLSLVQAELQT 735
Cdd:pfam13851 110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
527-835 |
4.28e-08 |
|
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: 57.88 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 527 ISELIERNQRYvEQSNLMMEK-------RNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKET 599
Cdd:pfam01576 189 ISDLEERLKKE-EKGRQELEKakrklegESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 600 ELQMQLTESLKETDLLRGQLTKV-----------QAKLSELQET--SEQAQSKFKSEKQN-----RKQLELKVTSLEEEL 661
Cdd:pfam01576 268 ELEAQISELQEDLESERAARNKAekqrrdlgeelEALKTELEDTldTTAAQQELRSKREQevtelKKALEEETRSHEAQL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 662 TDLRVE------------------KESLEKNL----SERKKKSAQERS--QAEEEIDEIRKSYQEELDKLRQLLKKT-RV 716
Cdd:pfam01576 348 QEMRQKhtqaleelteqleqakrnKANLEKAKqaleSENAELQAELRTlqQAKQDSEHKRKKLEGQLQELQARLSESeRQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 717 STDqaAAEQLSLVQAELQT------QWEAKCEHLL--ASAKDEHLQQYQEVCA----QRDAYQQKLVQLQEKCLALQAQI 784
Cdd:pfam01576 428 RAE--LAEKLSKLQSELESvssllnEAEGKNIKLSkdVSSLESQLQDTQELLQeetrQKLNLSTRLRQLEDERNSLQEQL 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221 785 -------TALTKQNEQHIKELEKNKSQMSGvEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:pfam01576 506 eeeeeakRNVERQLSTLQAQLSDMKKKLEE-DAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
514-802 |
4.45e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 514 LEKSNRIEEQNDKISELIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQaRVLHAEQEKA 571
Cdd:PRK03918 100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLG-EVIKEIKRRI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 572 KVTEELAAATAQVshlqlkmtahQKKETELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSE---QAQSKFK 641
Cdd:PRK03918 179 ERLEKFIKRTENI----------EELIKEKEKELEEVLREINEisselpeLREELEKLEKEVKELEELKEeieELEKELE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 642 SEKQNRKQLELKVTSLEEELTDLRVEKESLEKNlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRvstdqa 721
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 722 aaEQLSLVQAELQtQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQ---QKLVQLQEkclaLQAQITALTKQN-EQHI 795
Cdd:PRK03918 321 --EEINGIEERIK-ELEEKEERLeeLKKKLKELEKRLEELEERHELYEeakAKKEELER----LKKRLTGLTPEKlEKEL 393
|
....*..
gi 578817221 796 KELEKNK 802
Cdd:PRK03918 394 EELEKAK 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
557-785 |
5.19e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 557 ENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKE--TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 634
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 635 QAQSKFKSEKQNRKQL--ELKVTSLEEELTDLRVEKESLEKNLSERkkksAQERSQAEEEIDEIRKSYQEELDKLRQLLk 712
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQRILASL- 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221 713 KTRVSTDQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEkcLALQAQIT 785
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALT 384
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
505-845 |
5.24e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 505 ENERLKQEILEKSN--RIEEQNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQARVLHAEQEKAKVTE--ELAA 579
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEakKKAE 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 580 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-----------RK 648
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaeekKK 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE---------EIDEIRKSyQEELDKLRQLLKKtrvSTD 719
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakkkaeeakKADEAKKK-AEEAKKAEEAKKK---AEE 1468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 720 QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvcAQRDAyqQKLVQLQEKCLALQAQITALTKQNEQHIKELE 799
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE--AKKKA--DEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578817221 800 KNKSQMSGvEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTI 845
Cdd:PTZ00121 1545 KKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
577-803 |
5.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 577 LAAATAQVSHLQLKMTAHQKKETELQmQLtESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsekqnrkqlELKVTS 656
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE-QI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 657 LEEELTDLRVEKESLEknlsERKKKSAQERSQAEEEIDEIRKSYQE----ELDKLRQLLKktrvstdqAAAEQLSLVQAE 732
Cdd:COG4913 293 LEAELEELRAELARLE----AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIE--------RLERELEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221 733 LQtQWEAKCEHL---LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH---IKELEKNKS 803
Cdd:COG4913 361 RA-RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLERRKS 436
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
510-802 |
5.53e-08 |
|
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: 57.44 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 510 KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE---ELAAATAQVSH 586
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsRVDLKLQELQH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 587 LQLKMTAHQKKETE---LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ-SKFKSEKQ-NRKQLEL--------- 652
Cdd:pfam15921 536 LKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELqefkilkdk 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 653 ---KVTSLEEELTDLRVEKESLEKNLSER---KKKSAQERSQAEEEIDEIR---KSYQEELDKLRQLLK---KTRVSTDQ 720
Cdd:pfam15921 616 kdaKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRnelNSLSEDYEVLKRNFRnksEEMETTTN 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 721 AAAEQLSLVQAEL-QTQWEAKC-EHLLASAKDEHLQQYQEVCAQR---DAYQQKLVQLQEkclalqaqitALTKQN-EQH 794
Cdd:pfam15921 696 KLKMQLKSAQSELeQTRNTLKSmEGSDGHAMKVAMGMQKQITAKRgqiDALQSKIQFLEE----------AMTNANkEKH 765
|
....*...
gi 578817221 795 IKELEKNK 802
Cdd:pfam15921 766 FLKEEKNK 773
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
568-739 |
5.55e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 568 QEKAKVTEELAAATAQVSHL--QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQ 645
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELeeELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 646 NRKQLElkvtSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 725
Cdd:COG4717 161 LEEELE----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170
....*....|....
gi 578817221 726 LSLVQAELQTQWEA 739
Cdd:COG4717 237 EAAALEERLKEARL 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
573-825 |
6.71e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 652
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 653 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQ----ERSQ------AEEE---IDEIRKsYQEELDKLRQLLKKTR-VST 718
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLRKEierlEWRQqtevlsPEEEkelVEKIKE-LEKELEKAKKALEKNEkLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 719 DQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEHLQQYQ---EVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI 795
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKeadELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270
....*....|....*....|....*....|..
gi 578817221 796 KELE--KNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:COG1340 244 KELKklRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
461-846 |
7.64e-08 |
|
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: 56.90 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 461 KMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERL--KQEILEKSNRIEEQNDKISELIERNQRYV 538
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELqeKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 539 EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQvshlqlkmtahqKKETELQMQLTESLKETDLlrgq 618
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL------------KKEEKEEEKSELSLKEKEL---- 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 619 ltkvqaklsELQETSEQAQSkfksekqNRKQLELKVTSLEEELTdlrvEKESLEKNLSERKKKSAQERSQAEEEIDEIRK 698
Cdd:pfam02463 777 ---------AEEREKTEKLK-------VEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 699 SYQEEL--DKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvcaqrdayQQKLVQLQEK 776
Cdd:pfam02463 837 ELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE--------KKELEEESQK 908
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221 777 CLALQAQITALTKQNEQHIKELEKNKSQ---MSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTIL 846
Cdd:pfam02463 909 LNLLEEKENEIEERIKEEAEILLKYEEEpeeLLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
588-799 |
8.69e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.84 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFkseKQNRKQLE---------------- 651
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKL---RQAQAELEalkddndeetretlst 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 652 LKVTSLEEELTDLRVEKESLEKNLSERKK-----KSAQERSQAeeEIDEirksYQEELDKLRQLLKKTRVSTDQAAAEQL 726
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSqlvslQTQPERAQA--ALYA----NSQRLQQIRNLLKGGKVGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 727 SLVQAELQtqweakcehlLASAKDEHLQQ-----------YQevcAQRDAYQQKLVQLQEKCLALQAQITA-LTKQNEQH 794
Cdd:PRK11281 195 VLLQAEQA----------LLNAQNDLQRKslegntqlqdlLQ---KQRDYLTARIQRLEHQLQLLQEAINSkRLTLSEKT 261
|
....*
gi 578817221 795 IKELE 799
Cdd:PRK11281 262 VQEAQ 266
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
507-819 |
1.01e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSN-----RIEEQNDKISELIERNQRYVEQSNLMMEKRNN--SLQTATENTQARVLHAEQEKAKVTEELAA 579
Cdd:PRK02224 190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEadEVLEEHEERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 580 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 652
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 653 KVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQ------EELDKLRQLLKKTRvstdQAAA 723
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREER----DELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 724 EQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQE----VCAQRDaYQQKLVQLQEKCLALQAQITALTKQNEQhIKE 797
Cdd:PRK02224 426 EREAELEATLRTARErvEEAEALLEAGKCPECGQPVEgsphVETIEE-DRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
330 340
....*....|....*....|..
gi 578817221 798 LEKNKSQMSGVEAAASDPSEKV 819
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELI 525
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
487-725 |
1.17e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 487 SVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA 566
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 567 EQEKaKVTEELAAATAQVSHLQLKMTAHQKKETELQ----MQLTESL---KETDL------LRGQLTKVQAKL---SELQ 630
Cdd:COG1340 85 EKLN-ELREELDELRKELAELNKAGGSIDKLRKEIErlewRQQTEVLspeEEKELvekikeLEKELEKAKKALeknEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 631 ETSEQAQSKFKSEKQNRKQLE----------LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsY 700
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKelaeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE-L 242
|
250 260
....*....|....*....|....*
gi 578817221 701 QEELDKLRQLLKKTRVSTDQAAAEQ 725
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEE 267
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
566-764 |
1.31e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 566 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKfksEKQ 645
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 646 NRKQLElKVTSlEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDEIRKSY---QEELDKLRQLLKKTRVSTDQAA 722
Cdd:COG1579 78 YEEQLG-NVRN-NKEYEALQKEIESLKRRISDLED----EILELMERIEELEEELaelEAELAELEAELEEKKAELDEEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578817221 723 AEqlslVQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRD 764
Cdd:COG1579 152 AE----LEAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
595-838 |
1.49e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 595 QKKETELQMQLTEslkeTDLLRGQ--LTKVQAKLSELQETSEQAQsKFKSEKQNRKQLELKVTsleeeLTDLRVEKESLE 672
Cdd:TIGR02168 173 RRKETERKLERTR----ENLDRLEdiLNELERQLKSLERQAEKAE-RYKELKAELRELELALL-----VLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 673 KNLSErKKKSAQERSQAEEEIDEirksYQEELDKLRqlLKKTRVSTDQAAAeqlslvQAELQTQWEAKcehllaSAKDEH 752
Cdd:TIGR02168 243 ELQEE-LKEAEEELEELTAELQE----LEEKLEELR--LEVSELEEEIEEL------QKELYALANEI------SRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 753 LQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRR 832
Cdd:TIGR02168 304 KQILRE----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
....*.
gi 578817221 833 EFELEE 838
Cdd:TIGR02168 374 LEELEE 379
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
587-811 |
1.96e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 54.16 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 587 LQLKMTAHQKKETELQMQLtESLKETDL--LRGQL-------TKVQAKLSELQETSEQAQSKFKSEKQNRkqlelkvTSL 657
Cdd:pfam00038 30 LETKISELRQKKGAEPSRL-YSLYEKEIedLRRQLdtltverARLQLELDNLRLAAEDFRQKYEDELNLR-------TSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 658 EEELTDLR--VEKESLEKNLSERKKKSAQErsqaeeEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQA--EL 733
Cdd:pfam00038 102 ENDLVGLRkdLDEATLARVDLEAKIESLKE------ELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 734 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRD-------AYQQKLVQLQEKCLALQAQITALTKQN-----------EQHI 795
Cdd:pfam00038 176 RAQYEEIAAKNREEAEEWYQSKLEELQQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKaslerqlaeteERYE 255
|
250
....*....|....*.
gi 578817221 796 KELEKNKSQMSGVEAA 811
Cdd:pfam00038 256 LQLADYQELISELEAE 271
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
498-837 |
1.97e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 498 NIQRIIQE----NERLKQEILEKSN---RIEEQNDKISELIErnqryvEQSNLMMEKRnnSLQTATENTQARVLHAEQEK 570
Cdd:PRK03918 166 NLGEVIKEikrrIERLEKFIKRTENieeLIKEKEKELEEVLR------EINEISSELP--ELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 571 akvtEELAAATAQVshlqLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ--AQSKFKSEKQNRK 648
Cdd:PRK03918 238 ----EEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 649 QlelkvtSLEEELTDLRVEKESLEKNLSERKKKSAqERSQAEEEIDEIRKSYQE------ELDKLRQLLKKTRVSTDQAA 722
Cdd:PRK03918 310 R------EIEKRLSRLEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 723 AEQLSLVQAELQTQWEAKCEHLLASAK-DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaltkqnEQHIKELekn 801
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------EEHRKEL--- 453
|
330 340 350
....*....|....*....|....*....|....*.
gi 578817221 802 ksqMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 837
Cdd:PRK03918 454 ---LEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
511-709 |
2.23e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 511 QEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLK 590
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-----------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 591 MTAHqKKETELQmQLTeslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvTSLEEELTDLRVEKES 670
Cdd:COG1579 82 LGNV-RNNKEYE-ALQ---KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578817221 671 LEKNLSERKKksaqERSQAEEEIDE-IRKSYqeelDKLRQ 709
Cdd:COG1579 154 LEAELEELEA----EREELAAKIPPeLLALY----ERIRK 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
566-817 |
3.24e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 566 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQET-SEQAQSKFKSEK 644
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 645 QNrKQLELKVTSleEELTDLrVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtrVSTDQAAAE 724
Cdd:COG3883 101 SV-SYLDVLLGS--ESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE--LEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 725 QLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQ 804
Cdd:COG3883 175 AQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|...
gi 578817221 805 MSGVEAAASDPSE 817
Cdd:COG3883 247 AGAGAAGAAGAAA 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
604-818 |
3.39e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 604 QLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERkKKSA 683
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 684 QERSQAEEEIDEI--RKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDEHLQQYQEVCA 761
Cdd:COG3883 96 YRSGGSVSYLDVLlgSESFSDFLDRLSAL--SKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221 762 QRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEK 818
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
504-820 |
5.25e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELA--A 579
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAEEAKKADEAKkkA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 580 ATAQVSHLQLKMTAHQKKETElQMQLTESLKETDLLRGQLTKVQA----------KLSELQETSE--QAQSKFKSEkQNR 647
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKAdeakkaeekkKADELKKAEElkKAEEKKKAE-EAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 648 KQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEE---IDEIRKSyQEELDKLRQLLKKTRVSTDQA 721
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEevmKLYEEEKKMKAEEAKKAEEAkikAEELKKA-EEEKKKVEQLKKKEAEEKKKA 1649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 722 -----AAEQLSLVQAELQTQWEA---KCEHLLASAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNE- 792
Cdd:PTZ00121 1650 eelkkAEEENKIKAAEEAKKAEEdkkKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEe 1727
|
330 340 350
....*....|....*....|....*....|....
gi 578817221 793 ------QHIKELEKNKSQmsgVEAAASDPSEKVK 820
Cdd:PTZ00121 1728 nkikaeEAKKEAEEDKKK---AEEAKKDEEEKKK 1758
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
499-715 |
6.24e-07 |
|
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: 53.82 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQaRVLHAEQEKAKVTEELA 578
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK-EEELEEQKLKDELESKE 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 579 AATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ-SKFKSEKQNRKQLELKVTSL 657
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEeNNKEEEEERNKRLLLAKEEL 972
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221 658 EEEltDLRVEKESLEKNLSERKKKSAQERsqAEEEIDEIRksyQEELDKLRQLLKKTR 715
Cdd:pfam02463 973 GKV--NLMAIEEFEEKEERYNKDELEKER--LEEEKKKLI---RAIIEETCQRLKEFL 1023
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
504-838 |
6.84e-07 |
|
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: 53.76 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:pfam15964 367 RQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMD 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 VSHL------QLKMTAHQKKETELQMQ--LTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVT 655
Cdd:pfam15964 447 VTKVcgemryQLNQTKMKKDEAEKEHReyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 656 SLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyqeeldkLRQLLKKTRVSTDQAAAEQLSLV--QAEL 733
Cdd:pfam15964 527 ESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQE--------------LTQKMQQMEAQHDKTVNEQYSLLtsQNTF 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 734 QTQWEAKCeHLLASAKDEHLQQYQEVCAQrdaYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAAS 813
Cdd:pfam15964 593 IAKLKEEC-CTLAKKLEEITQKSRSEVEQ---LSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQ 668
|
330 340
....*....|....*....|....*
gi 578817221 814 DPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:pfam15964 669 ATAQQLVQLLSKQNQLFKERQNLTE 693
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
510-800 |
7.07e-07 |
|
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: 53.80 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 510 KQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATENtQARVLHAEQEKAKVTEELAAATAQVSHLQL 589
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 590 kmtahQKKETELQMQLTEslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL---ELKVTSLEEELTDLRV 666
Cdd:COG3096 376 -----QLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 667 EKESLEKNLSERKkksaQERSQAEEEIDEIRKSYQ------------EELDKLRQLLKKTRVSTDQAA-----------A 723
Cdd:COG3096 449 KEQQATEEVLELE----QKLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQrlqqlraqlaeL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 724 EQLSLVQAELQTQWEAKCEHL---LASAKD-EHLQQYQEvcAQRDAYQQKLVQLQEKCLALQAQitalTKQNEQHIKELE 799
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIgqqLDAAEElEELLAELE--AQLEELEEQAAEAVEQRSELRQQ----LEQLRARIKELA 598
|
.
gi 578817221 800 K 800
Cdd:COG3096 599 A 599
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
557-843 |
7.64e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.64 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 557 ENTQARvlhaEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQL---TESLKETDLLRGQL-----------TKV 622
Cdd:pfam01576 5 EEMQAK----EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLaarkqeleeilHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 623 QAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN----------LSERKKKSAQERSQAEEE 692
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKikkleedillLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 693 IDEIRKSYQEELDKLRQLLKktrvstdqaaaeqlslvqaeLQTQWEAKCEHLLASAKDEHlQQYQEVCAQRDAYQQKLVQ 772
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSK--------------------LKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 773 LQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQsLRREFELEESYNGR 843
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE-LQEDLESERAARNK 289
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
499-838 |
1.04e-06 |
|
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: 53.05 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILE-----KSNRIEEQNDKisELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 573
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEeaagsRLKRKKKEALK--KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 TEELAAATAQVSHLQlkmtahqkketelqmqlteslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKqLELK 653
Cdd:pfam02463 222 EEEYLLYLDYLKLNE---------------------ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK-EEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 654 VTSLEEEL-----TDLRVEKESLEK-----NLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA 723
Cdd:pfam02463 280 EKKLQEEElkllaKEEEELKSELLKlerrkVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 724 EQLSLVQAELQTQWEAKCEHLLASA-------KDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK 796
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESErlssaakLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578817221 797 ELEKNKSQMSGVEAaasDPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:pfam02463 440 ELKQGKLTEEKEEL---EKQELKLLKDELELKKSEDLLKETQ 478
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
503-838 |
1.40e-06 |
|
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: 51.84 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 503 IQENERLKQEILEKSNRIEEqndkiseliernqryveqsnlMMEKRNnslqtatENTQARVLHAEQEKAKVTEELAAAta 582
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDE---------------------MMEEER-------ERALEEEEEKEEERKEERKRYRQE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 583 qvshLQLKMTAHQKKEtelQMQLTESLKETDLLRGQLTKVQAKlselqetsEQAQSKFKSEKQNRKQLELKVTSleeELT 662
Cdd:pfam13868 78 ----LEEQIEEREQKR---QEEYEEKLQEREQMDEIVERIQEE--------DQAEAEEKLEKQRQLREEIDEFN---EEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 663 DLRVEKESLEKNLSERK-----KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVstDQAAAEQL--SLVQAELQT 735
Cdd:pfam13868 140 AEWKELEKEEEREEDERileylKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELraKLYQEEQER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 736 QW-------EAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQhiKELEKNKSQMSGV 808
Cdd:pfam13868 218 KErqkereeAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE--KRRMKRLEHRREL 295
|
330 340 350
....*....|....*....|....*....|
gi 578817221 809 EAAASDPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:pfam13868 296 EKQIEEREEQRAAEREEELEEGERLREEEA 325
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
540-826 |
1.72e-06 |
|
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: 52.53 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 540 QSNLMMEKRNNSLQTATENTQARvlHAEQEkakvtEELAAATAQVSHLQLKMT----AHQKKETELQMQLTESLKEtdll 615
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREK--QAAAE-----EQLVQANGELEKASREETfartALKNARLDLRRLFDEKQSE---- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 616 rgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL-SERKKKSAQ-------ERS 687
Cdd:pfam12128 666 --KDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVeGALDAQLALlkaaiaaRRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 688 QAEEEIDEIRKSYQEELDKLrqllkktrvSTDQAAAEQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQEvcaQRDA 765
Cdd:pfam12128 744 GAKAELKALETWYKRDLASL---------GVDPDVIAKLKREIRTLERKIEriAVRRQEVLRYFDWYQETWLQ---RRPR 811
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 766 YQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 826
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
507-678 |
1.93e-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: 50.31 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENtqarvlhaeqekakvtEELAAATAQ 583
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQLGNVRNN----------------KEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 VSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQskfksekqnrKQLELKVTSLEEELTD 663
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKK----------AELDEELAELEAELEE 160
|
170
....*....|....*
gi 578817221 664 LRVEKESLEKNLSER 678
Cdd:COG1579 161 LEAEREELAAKIPPE 175
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
447-725 |
2.04e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.21 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 447 HNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSN---------IQRIIQENERLKQEILEKS 517
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNqarlqaledLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 518 NRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTahQKK 597
Cdd:PLN02939 177 MRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELI--EVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 598 ETELQMQLTEslKETDLLRGQLTKVQAKLSELQE--------------------------TSEQAQSKFKSEKQNRkQLE 651
Cdd:PLN02939 254 ETEERVFKLE--KERSLLDASLRELESKFIVAQEdvsklsplqydcwwekvenlqdlldrATNQVEKAALVLDQNQ-DLR 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 652 LKVTSLEEELTDLRVEKESLEK-NLSERKKKSAQERSQA-EEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 725
Cdd:PLN02939 331 DKVDKLEASLKEANVSKFSSYKvELLQQKLKLLEERLQAsDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
517-817 |
2.38e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 517 SNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENT----QARvLHAEQEKAKVTEELAAATAQVSHLQLKMT 592
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnQAR-LQALEDLEKILTEKEALQGKINILEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 593 ahqkkETELQMQLTESLK-ETDLLRGQLTKVQAKLSELQETSEQAqskfksekqnrkqlelkVTSLEEELTDLRVEKESL 671
Cdd:PLN02939 181 -----ETDARIKLAAQEKiHVEILEEQLEKLRNELLIRGATEGLC-----------------VHSLSKELDVLKEENMLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 672 EKNLSERKkksaqersqaeEEIDEIRKSYQE--ELDKLRQLLKKT------RVSTDQAAAEQLSLVQAELqtqWEAKCE- 742
Cdd:PLN02939 239 KDDIQFLK-----------AELIEVAETEERvfKLEKERSLLDASlrelesKFIVAQEDVSKLSPLQYDC---WWEKVEn 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 743 --HLLASAKD--EH----LQQYQEV--------------------CAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH 794
Cdd:PLN02939 305 lqDLLDRATNqvEKaalvLDQNQDLrdkvdkleaslkeanvskfsSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
|
330 340 350
....*....|....*....|....*....|
gi 578817221 795 IKELE------KNKSQMSGVEAAASD-PSE 817
Cdd:PLN02939 385 IKEFQdtlsklKEESKKRSLEHPADDmPSE 414
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
500-814 |
2.39e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 500 QRIIQENERLKQEILEKSNRIEEQNDKISE---------------------LIERN------------------------ 534
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAEterereelaeevrdlrerleeLEEERddllaeaglddadaeavearreel 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 535 -------QRYVEQSNLMMEKRNNSLQTATEN------------TQARVLHAEQEKAKvtEELAAATAQVSHLQLKMTAHQ 595
Cdd:PRK02224 320 edrdeelRDRLEECRVAAQAHNEEAESLREDaddleeraeelrEEAAELESELEEAR--EAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 596 KKETELQMQL------TESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEK-----QNRK---------QLELKV 654
Cdd:PRK02224 398 ERFGDAPVDLgnaedfLEELREErDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEgsphvetieEDRERV 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 655 TSLEEELTDLRVEKESLEK----------------NLSERKKKSAQERSQAEEEIDEiRKSYQEELDKLRQLLKKTRVST 718
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEErleraedlveaedrieRLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAEAEEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 719 DQAAAEQLSLVQAELQTQweAKCEHLLASAKD--EHLQQYQEVCAQRDAYQQKLVQLQEKclalQAQITALTKQNEQHIK 796
Cdd:PRK02224 557 REAAAEAEEEAEEAREEV--AELNSKLAELKEriESLERIRTLLAAIADAEDEIERLREK----REALAELNDERRERLA 630
|
410 420
....*....|....*....|....
gi 578817221 797 ELEKNKSQMSG------VEAAASD 814
Cdd:PRK02224 631 EKRERKRELEAefdearIEEARED 654
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
498-737 |
2.76e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 498 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERN-----QRY----VEQSNLMMEKRNNSLQTATE-----NTQARV 563
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLstlsLRQLESRLAQTLDQLQNAQNdlaeyNSQLVS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 564 LHAEQEKAKVteELAAATAQVSHL--QLKMTAHQKKET--ELQMQLTESLKETDLLRGQLTKVQAKLSELQETsEQAQSK 639
Cdd:PRK11281 154 LQTQPERAQA--ALYANSQRLQQIrnLLKGGKVGGKALrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDL-LQKQRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 640 FKSEKQNRkqlelkvtsLEEELTDLRvekESL-EKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVST 718
Cdd:PRK11281 231 YLTARIQR---------LEHQLQLLQ---EAInSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKAT 298
|
250 260
....*....|....*....|
gi 578817221 719 DQAAaeqlSLVQAELQT-QW 737
Cdd:PRK11281 299 EKLN----TLTQQNLRVkNW 314
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
600-797 |
2.86e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 51.23 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 600 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtSLEEEL-------TDLRVEKESLE 672
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENfrletarDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 673 KNLSERK------KKSAQERSQAEEEIDEIRKS-------------YQEELDKLRQLLKKTRVSTDQAAaeqlSLVQAEL 733
Cdd:pfam05622 94 KEVLELQhrneelTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNA----EYMQRTL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817221 734 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKE 797
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIE 233
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
462-797 |
3.55e-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: 51.05 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 462 MDHLMTKVEELQKHSAGNSML--IPSMSVtmetsmimsnIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE 539
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLlvVPRAEL----------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 540 QSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQmQLTESLKETDLLRgql 619
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 620 tkvQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSER----------------KKKSA 683
Cdd:pfam07888 149 ---ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRdtqvlqlqdtittltqKLTTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 684 QERSQAEEEIDEIRKSYQEEL-------DKLRQLLKKTRVSTDQAAAE----------------QLSLVQAELQTQWEAK 740
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLnaserkvEGLGEELSSMAAQRDRTQAElhqarlqaaqltlqlaDASLALREGRARWAQE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 741 CEHLLASAKDEH---------LQQYQEVCAQRDAYQQKL------------VQLQEKCLALQ---AQITALTKQNEQHIK 796
Cdd:pfam07888 306 RETLQQSAEADKdrieklsaeLQRLEERLQEERMEREKLevelgrekdcnrVQLSESRRELQelkASLRVAQKEKEQLQA 385
|
.
gi 578817221 797 E 797
Cdd:pfam07888 386 E 386
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
499-860 |
3.99e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.29 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEI-------LEKSNRIEEQNDKISEL-IERNQRYVEQSNLM-------MEKRNNSLQTATENTQARV 563
Cdd:pfam07111 68 ISRQLQELRRLEEEVrllretsLQQKMRLEAQAMELDALaVAEKAGQAEAEGLRaalagaeMVRKNLEEGSQRELEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 564 LHAEQEKAKVT---EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLsELQET-------- 632
Cdd:pfam07111 148 LHQEQLSSLTQaheEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEEL-EAQVTlveslrky 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 633 -SEQAQSKFKSE--KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQ 709
Cdd:pfam07111 227 vGEQVPPEVHSQtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 710 LLKKTRvstDQAAAEQLSLVQAELQTQWEAK-CEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALT 788
Cdd:pfam07111 307 LLNRWR---EKVFALMVQLKAQDLEHRDSVKqLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 789 KQNEQHIKELEKNKS---QMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE--SYNGR---TILGTIMNTIKMVTLQL 860
Cdd:pfam07111 384 RAQEARRRQQQQTASaeeQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNrlSYAVRkvhTIKGLMARKVALAQLRQ 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
525-814 |
4.06e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 525 DKISELIERNQRYVeqSNLMMEKRNNslqtATENTQaRVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQ 604
Cdd:PRK04863 257 DLFKHLITESTNYV--AADYMRHANE----RRVHLE-EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 605 LtESLKEtdllrgQLTKVQaklselqeTSEQAQskfksEKQNRKQLELkvtsleEELTDLRVEKESLEKNLSERKKKSAQ 684
Cdd:PRK04863 330 Y-QAASD------HLNLVQ--------TALRQQ-----EKIERYQADL------EELEERLEEQNEVVEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 685 ERSQAEEEIDEIRKS---YQEELDKLR----------QLLKKTRVSTDQA--AAEQLSLVQAELQTQWEAKCEHLLA--- 746
Cdd:PRK04863 384 RAEAAEEEVDELKSQladYQQALDVQQtraiqyqqavQALERAKQLCGLPdlTADNAEDWLEEFQAKEQEATEELLSleq 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 747 ------SAKDEHLQQYQEVCA-----QRDAYQQKLVQL-----QEKCLALQAQitaltkQNEQHIKELEKNKSQMSGVEA 810
Cdd:PRK04863 464 klsvaqAAHSQFEQAYQLVRKiagevSRSEAWDVARELlrrlrEQRHLAEQLQ------QLRMRLSELEQRLRQQQRAER 537
|
....
gi 578817221 811 AASD 814
Cdd:PRK04863 538 LLAE 541
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
575-800 |
4.35e-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: 51.11 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 575 EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQN 646
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladetlADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 647 RKQLELkvtsLEEELTDLRVEKESLEkNLSERKKKSAQERSQAEEEIDEI-----RK---SYQEEL----------DKLR 708
Cdd:COG3096 916 GKALAQ----LEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALsevvqRRphfSYEDAVgllgensdlnEKLR 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 709 QLLK-------KTRVSTDQAAAE--QLSLVQAELQTQWEAKCEhLLASAKDEhLQQY-------QEVCAQ--RDAYQQKL 770
Cdd:COG3096 991 ARLEqaeearrEAREQLRQAQAQysQYNQVLASLKSSRDAKQQ-TLQELEQE-LEELgvqadaeAEERARirRDELHEEL 1068
|
250 260 270
....*....|....*....|....*....|
gi 578817221 771 VQLQEKCLALQAQITALTKQNEQHIKELEK 800
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
567-840 |
4.36e-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: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 567 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 646
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 647 RKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQL 726
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 727 SL-VQAELQTQWEAKCehllasakdEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSqm 805
Cdd:TIGR00618 339 SIeEQRRLLQTLHSQE---------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR-- 407
|
250 260 270
....*....|....*....|....*....|....*
gi 578817221 806 sgvEAAASDPSEKVKKIMNQVFQSLRREFELEESY 840
Cdd:TIGR00618 408 ---EQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
625-744 |
5.16e-06 |
|
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: 47.30 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 625 KLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV-------EKESLEKNLSERKKK---SAQERSQA----- 689
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHknqqleeEVEKLEEQLKEAKEKaeeSEKLKTNNenltr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221 690 -----EEEIDEIRKSYQEELDKLRQllkktrvsTDQAAAEQLSLVQAELQT--QWEAKCEHL 744
Cdd:pfam12718 81 kiqllEEELEESDKRLKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
505-943 |
5.39e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 505 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE--ELAAATA 582
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 583 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA-----------KLSELQETSEQ---AQSKFKSEKQNRK 648
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeakkkaeeakKADEAKKKAEEakkAEEAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE--------EIDEIRKSyqEELDKLRQLLK--KTRVST 718
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaeeakKADEAKKA--EEAKKADEAKKaeEKKKAD 1549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 719 DQAAAEQLSLVQAELQTQWEAKCEH--LLASAKDEHLQQYQEvcaQRDAYQQKLVQLQEKCLALQAQitaltKQNEQHIK 796
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAK-----KAEEAKIK 1621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 797 --ELEKNKSQMSGVEAAASDPSEKVKKImnqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeQEKEESSSE 874
Cdd:PTZ00121 1622 aeELKKAEEEKKKVEQLKKKEAEEKKKA-----EELKKAEE--------------ENKIKAAEEA------KKAEEDKKK 1676
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 875 EEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQV--VEEAVPLPPQALTTSQDGHRRKGD 943
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
883-1096 |
6.64e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 883 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 962
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 963 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1041
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 1042 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1096
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
507-787 |
6.68e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSNRIEEQN---DKISELIERNQRYVEQSNLMMEKRNNSL---QTATENTQARVL---HAEQ--EKAK--- 572
Cdd:PRK04863 351 ERYQADLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIqyqQAVQalERAKqlc 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 ----------------VTEELAAATAQVSHLQLKMTAHQ--KKETELQMQLTESL-----------KETDLLR------- 616
Cdd:PRK04863 431 glpdltadnaedwleeFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIagevsrseawdVARELLRrlreqrh 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 617 --GQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEid 694
Cdd:PRK04863 511 laEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQQ-- 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 695 eirksyQEELDKLRQLLKKTRVS--TDQAAAEQLSlvqaelqtqwEAKCEHLLASAK-DEHLQQYQEvcaQRDAYQQKLV 771
Cdd:PRK04863 588 ------LEQLQARIQRLAARAPAwlAAQDALARLR----------EQSGEEFEDSQDvTEYMQQLLE---RERELTVERD 648
|
330
....*....|....*.
gi 578817221 772 QLQEKCLALQAQITAL 787
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
504-835 |
6.69e-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: 50.56 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 VSHL--QLKMTAHQKKETE-----LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:pfam01576 498 RNSLqeQLEEEEEAKRNVErqlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 657 LEEELTDLRVEKESLEKNLS--ERKKKS---------------AQERSQAE------------------------EEIDE 695
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSnlEKKQKKfdqmlaeekaisaryAEERDRAEaeareketralslaraleealeakEELER 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 696 IRKSYQEELDKL----------RQLLKKTRVSTDQAAAE---QLSLVQAELQTQWEAK--CEHLLASAKDEHLQQYQevc 760
Cdd:pfam01576 658 TNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEmktQLEELEDELQATEDAKlrLEVNMQALKAQFERDLQ--- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 761 AQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI---KELEKN-KSQMSGVEAAASDPSEKVK--KIMNQVFQSLRREF 834
Cdd:pfam01576 735 ARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakKKLELDlKELEAQIDAANKGREEAVKqlKKLQAQMKDLQREL 814
|
.
gi 578817221 835 E 835
Cdd:pfam01576 815 E 815
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
126-197 |
6.75e-06 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 47.02 E-value: 6.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221 126 VEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLrLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVG 197
Cdd:COG1047 1 IEKGDVVTLHYTLKL----EDGEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
588-815 |
6.76e-06 |
|
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: 48.84 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL-------------ELKV 654
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeilaSLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 655 TSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAE---EEIDEIRKsyqeELDKLRQLLKKTRVSTDQAAAEQLSLVQA 731
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPEraqQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 732 ELQtqweakcehlLASAKDEHLQQYQEVC--------AQRDAYQQKLVQLQEKCLALQAQItaltkqNEQHIKELEKN-- 801
Cdd:pfam12795 157 ELA----------ALKAQIDMLEQELLSNnnrqdllkARRDLLTLRIQRLEQQLQALQELL------NEKRLQEAEQAva 220
|
250
....*....|....
gi 578817221 802 KSQMSGVEAAASDP 815
Cdd:pfam12795 221 QTEQLAEEAAGDHP 234
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
510-690 |
7.95e-06 |
|
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: 49.83 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 510 KQEIL-EKSNRIEEqndKISELIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:pfam15066 357 KQQVFvDIINKLKE---NVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQLELKKIKVN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 584 VSHLQLK-MTAHQKKETE----LQMQLTESLKETDLLRGQLTKvqaklSELQETSEQAQSKFKSEKQNRKQLELkvtSLE 658
Cdd:pfam15066 428 YVHLQERyITEMQQKNKSvsqcLEMDKTLSKKEEEVERLQQLK-----GELEKATTSALDLLKREKETREQEFL---SLQ 499
|
170 180 190
....*....|....*....|....*....|...
gi 578817221 659 EELTdlRVEKESLEknlsERKK-KSAQERSQAE 690
Cdd:pfam15066 500 EEFQ--KHEKENLE----ERQKlKSRLEKLVAQ 526
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
596-711 |
8.93e-06 |
|
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: 46.09 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 596 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN----RKQL-ELK--VTSLEEELTDLRVEK 668
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLhaedIKALqALReeLNELKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578817221 669 ESLEKNLSERKKKSAQERSQAEEEIDEIRKSYqEELDKLRQLL 711
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
624-821 |
1.40e-05 |
|
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: 49.68 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 624 AKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEK--NLSERKKK-------------------- 681
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREyegyellkekealerqkeai 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 682 ----SAQERSQA--EEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA---EQLSLVQAELqtqweAKCEHLLASAKDEH 752
Cdd:TIGR02169 243 erqlASLEEELEklTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEI-----ASLERSIAEKEREL 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221 753 LQ---QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKK 821
Cdd:TIGR02169 318 EDaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
443-811 |
1.41e-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: 49.57 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 443 EARQhntEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEE 522
Cdd:COG3096 289 ELRR---ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 523 QNDKISELIERNQRYVEQSNLmMEKRNNSL-------QTATENTQARVLHAEQ-----EKAK------------VTEELA 578
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEA-AEEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARalcglpdltpenAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 579 AATAQVSHL---------QLKMTAHQKKETELQMQLTESL-----------KETDLLR---------GQLTKVQAKLSEL 629
Cdd:COG3096 445 AFRAKEQQAteevleleqKLSVADAARRQFEKAYELVCKIageversqawqTARELLRryrsqqalaQRLQQLRAQLAEL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 630 QETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEeldkLRQ 709
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE----LAA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 710 LLKKTRVStdQAAAEQLslvqaelqtqweakCEHLlasakDEHLQQYQEVcaqrDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:COG3096 600 RAPAWLAA--QDALERL--------------REQS-----GEALADSQEV----TAAMQQLLEREREATVERDELAARKQ 654
|
410 420
....*....|....*....|..
gi 578817221 790 QNEQHIKELeknkSQMSGVEAA 811
Cdd:COG3096 655 ALESQIERL----SQPGGAEDP 672
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
503-708 |
1.57e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 503 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATA 582
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 583 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQ------AKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578817221 657 LEEELTDLRVEKESLEKNLSERKKKSAQERSQ-AEEEIDEIrksyQEELDKLR 708
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEEAREDKErAEEYLEQV----EEKLDELR 673
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
620-819 |
1.82e-05 |
|
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: 47.64 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 620 TKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKEsleknlSERKKKSAQeRSQAEEEIDEIRKS 699
Cdd:pfam15397 63 KQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQ-IANLVRQLQQLKDS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 700 YQEELDKLRQLLKKTRvstdqaaaeqlslvqAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLvqlqEKCLA 779
Cdd:pfam15397 136 QQDELDELEEMRRMVL---------------ESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVM----LKEIE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578817221 780 lqaqitaltkQNEQHIKELEKN----KSQMSGVEAAASDPSEKV 819
Cdd:pfam15397 197 ----------QFREFIDELEEEipklKAEVQQLQAQRQEPREVI 230
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
507-805 |
2.37e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEIleksNRIEEQNDKISELIERNQRYVEQSNLMMekrNNSLQTATEntqarvlhAEQEkakvtEELAAATAQVSH 586
Cdd:PRK04863 789 EQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFI---GSHLAVAFE--------ADPE-----AELRQLNRRRVE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 587 LQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQNRKQLELkvtsLE 658
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LE 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 659 EELTDLRVEKESLEK-----NLSERKKKSAQERSQAEEEIDEIRK--SYQEEL----------DKLRQLLK--------- 712
Cdd:PRK04863 925 PIVSVLQSDPEQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAemlaknsdlnEKLRQRLEqaeqertra 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 713 KTRVSTDQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEhLQQY---------QEVCAQRDAYQQKLVQLQEKCLALQAQ 783
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASLKSSYDAKRQ-MLQELKQE-LQDLgvpadsgaeERARARRDELHARLSANRSRRNQLEKQ 1082
|
330 340
....*....|....*....|....*.
gi 578817221 784 IT----ALTKQNEQhIKELEKNKSQM 805
Cdd:PRK04863 1083 LTfceaEMDNLTKK-LRKLERDYHEM 1107
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
450-715 |
2.80e-05 |
|
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: 48.51 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 450 EIRMAVSKVADKMDHLMTKVEELQKHSAG--NSM--LIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQND 525
Cdd:TIGR01612 1115 KIKDDIKNLDQKIDHHIKALEEIKKKSENyiDEIkaQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 526 KISELIErnqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAtaqvshlqlkMTAHQKKETELQMQL 605
Cdd:TIGR01612 1195 LLNEIAE-----IEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKA----------MEAYIEDLDEIKEKS 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 606 TESLKETdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE------LKVTSLEEELTDLRVEKESLEKNLSERK 679
Cdd:TIGR01612 1260 PEIENEM----GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISdireksLKIIEDFSEESDINDIKKELQKNLLDAQ 1335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 680 KKSAQ-------------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 715
Cdd:TIGR01612 1336 KHNSDinlylneianiynilklnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
446-838 |
2.83e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 446 QHNTEIRMAVSKVADKMDHLMTKVEELQ-----KHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRI 520
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTEselkkKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 521 EEQ---------NDKISELIERNQRYVEQsnLMMEKRNNSLQTATENTQAR-------VLHAEQEKAKVTEELAAATAQV 584
Cdd:TIGR00606 768 EEQetllgtimpEEESAKVCLTDVTIMER--FQMELKDVERKIAQQAAKLQgsdldrtVQQVNQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 585 SHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQlelkVTSLEEELTDL 664
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLEKD 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 665 RVEKESLEKNLSERKKKSAQERSQAEEEIDEI---RKSYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaELQTQWEAKC 741
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQDGKDDYLKQKETELNTVNAQLE----ECEKHQEKIN 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 742 EHLLASAKDEHLQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELekNKSQMSGVEAAASDPSEKVKK 821
Cdd:TIGR00606 998 EDMRLMRQDIDTQKIQE----------RWLQDNLTLRKRENELKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDL 1065
|
410
....*....|....*..
gi 578817221 822 IMNQVFQSLRREFELEE 838
Cdd:TIGR00606 1066 IKRNHVLALGRQKGYEK 1082
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
595-786 |
3.00e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.15 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 595 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQ---ETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL 671
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 672 EKNLSERKKKSAQERSQAEEEIDEIRKSYQEE-----------LDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQwEAK 740
Cdd:pfam05622 383 KEQIEELEPKQDSNLAQKIDELQEALRKKDEDmkameerykkyVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEK-DKK 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 741 CEHLLASAKDEHLQQYQE------------VCAQRDAYQQKLVQLQ---EKCLALQAQITA 786
Cdd:pfam05622 462 IEHLERDFEKSKLQREQEeklivtawynmgMALHRKAIEERLAGLSspgQSFLARQRQATN 522
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
566-688 |
4.13e-05 |
|
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: 44.55 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 566 AEQEKAKVTEELAAATAQVSHLQLKM--------TAHQKKETELQMQlTESLKETDLLRGQLTKVQAKLSELQETSEQAQ 637
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLekqaeiarEAQQNYERELVLH-AEDIKALQALREELNELKAEIAELKAEAESAK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 578817221 638 SKFKSEKQnrkqlelkvtSLEEEltdlrveKESLEKNLSERKKKSAQERSQ 688
Cdd:pfam07926 85 AELEESEE----------SWEEQ-------KKELEKELSELEKRIEDLNEQ 118
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
507-713 |
4.89e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 45.82 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSNRIEEQNDKISELIErnqryveqsnlmmekrnnslqtatENTQARVLHAEQEKAkvteelaaataqVSH 586
Cdd:pfam05010 11 EKARNEIEEKELEINELKAKYEELRR------------------------ENLEMRKIVAEFEKT------------IAQ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 587 LqlkMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEeltdlRV 666
Cdd:pfam05010 55 M---IEEKQKQKELEHAEIQKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA-----RI 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578817221 667 EKEslEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:pfam05010 127 KKE--EQRYQALKAHAEEKLDQANEEIAQVRSKAKAETAALQASLRK 171
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
508-800 |
5.20e-05 |
|
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: 46.73 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 508 RLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAataqvshl 587
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 588 qlkmtahqkketeLQMQLTESLKETDLLRGQLT------KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 661
Cdd:pfam15905 127 -------------LEKQLLELTRVNELLKAKFSedgtqkKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 662 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRK--SYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaeLQTQWEA 739
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITElsCVSEQVEKYKLDIAQLEELLKEKNDEIES-----LKQSLEE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 740 KCEHLLASAKD--EHLQQYQEvcaqrdAYQQKLVQLQEKCLALQAQITALTK---QNEQHIKELEK 800
Cdd:pfam15905 269 KEQELSKQIKDlnEKCKLLES------EKEELLREYEEKEQTLNAELEELKEkltLEEQEHQKLQQ 328
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
563-732 |
7.14e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 46.79 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 563 VLHAEQEKAKVTEELAAATAQvshlQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkVQAKlSELQETSEQAQSKFKS 642
Cdd:PRK00106 21 LISIKMKSAKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 643 EKQNRKQLELKVT----SL---EEELTDLRVEKESLEKNLSErKKKSAQERsqaEEEIDEIRKSYQEELDKLRQLlkktr 715
Cdd:PRK00106 95 ERQELKQIESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL----- 165
|
170
....*....|....*..
gi 578817221 716 vstDQAAAEQLSLVQAE 732
Cdd:PRK00106 166 ---SQAEAREIILAETE 179
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
495-691 |
7.16e-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: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQT--ATENTQARVLHAeqe 569
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRsgGSVSYLDVLLGS--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 570 kakvtEELAAATAQVSHLQlKMTAHQKKETELQMQLTESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 648
Cdd:COG3883 112 -----ESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578817221 649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 691
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
501-812 |
7.50e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 501 RIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkrnnsLQTATENtQARVLHAEQEKAKV------- 573
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD-----VKTICEQ-EARIKDLEAQRAQLqagqpcp 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 ----TEELAAATAQVshlqLKMTAHQKKETELQMQLTESLKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSEKQNRKQ 649
Cdd:PRK10246 508 lcgsTSHPAVEAYQA----LEPGVNQSRLDALEKEVKKLGEEGAALRGQL---DALTKQLQRDESEAQSLRQEEQALTQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 650 LELKVTSL------EEELTDLRVEKESLEKNL---SERKKKSAQERSQAEEEIdeirkSYQEELDKLRQLLkktrvsTDQ 720
Cdd:PRK10246 581 WQAVCASLnitlqpQDDIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQQII-----QYQQQIEQRQQQL------LTA 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 721 AAAEQLSLVQAELQTQWeakcehllASAKDEHLQQYQEVCAQRDAYQQKLVQLQ-------------------------- 774
Cdd:PRK10246 650 LAGYALTLPQEDEEASW--------LATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetvaldnwrq 721
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 578817221 775 --EKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAA 812
Cdd:PRK10246 722 vhEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAS 761
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
628-831 |
7.63e-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: 47.25 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 628 ELQETSEQ-AQSKFKSEKQNR--KQLELKVTSL---------EEELTDLRVEKESLEKNLSERKKKSAQERSQAEeeide 695
Cdd:COG3096 793 ERDELAEQyAKASFDVQKLQRlhQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD----- 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 696 irkSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAK------CEHLlaSAKDEHLQQYQEVCAQRDAYQQK 769
Cdd:COG3096 868 ---QLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQafiqqhGKAL--AQLEPLVAVLQSDPEQFEQLQAD 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 770 LVQLQEKCLALQAQITALTK--QNEQHI------------KEL-EKNKSQMSGVEAAASDPSEKVKKI------MNQVFQ 828
Cdd:COG3096 943 YLQAKEQQRRLKQQIFALSEvvQRRPHFsyedavgllgenSDLnEKLRARLEQAEEARREAREQLRQAqaqysqYNQVLA 1022
|
...
gi 578817221 829 SLR 831
Cdd:COG3096 1023 SLK 1025
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
635-821 |
1.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 635 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEeynELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 712 K---KTRVSTD-----------QAAAEQLSLV-------QAELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQQKL 770
Cdd:COG3883 93 RalyRSGGSVSyldvllgsesfSDFLDRLSALskiadadADLLEELKADKAE--LEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578817221 771 VQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKK 821
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
499-740 |
1.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELA 578
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ--------AQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 579 AATAQVSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQEtsEQAQSKFKSEKQNRKQLELKVTSLE 658
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 659 EELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE 738
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
..
gi 578817221 739 AK 740
Cdd:COG4372 284 EL 285
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
618-758 |
1.08e-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: 46.10 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 618 QLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE--LTDLRVEKESLEKNLSERKK----KSAQERSQAEE 691
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQrlqlQAAQERARQQQ 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 692 EidEIRKSYQEeldkLRQllKKTRVSTDQAAAEQLSlvQAELQTQWEAKCEHLLASAKD---EHLQQYQE 758
Cdd:pfam15709 426 E--EFRRKLQE----LQR--KKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEerlEYQRQKQE 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
497-709 |
1.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 497 SNIQRIiqenERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNL--------MMEKRNNSLQTATENTQAR------ 562
Cdd:COG4913 607 DNRAKL----AALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeysWDEIDVASAEREIAELEAElerlda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 563 ----VLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESlkETDLLRGQLTKVQAKLSELQETSEQAQS 638
Cdd:COG4913 683 ssddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 639 KfKSEKQNRKQLELKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIDEIRkSYQEELDKLRQ 709
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAE---EELERAMRAFNREWPAETADLDADLESLP-EYLALLDRLEE 826
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
563-817 |
1.26e-04 |
|
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: 46.29 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 563 VLHAEQEKAKVTE--ELAAATAQVSHLQLKmtahqKKETELQMQLTE-SLKETDLLRGQLTKVQAKLSELQEtsEQAQSK 639
Cdd:pfam09731 235 VEKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 640 fkseKQNRKQLELKVTSLEEELTDLRVE-KESLEKNLSERKKksaQERSQAEEEIDEIRKSYQEELdklrqllkktrvst 718
Cdd:pfam09731 308 ----KREEKHIERALEKQKEELDKLAEElSARLEEVRAADEA---QLRLEFEREREEIRESYEEKL-------------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 719 dqaaaeqlslvQAELQTQWEAKCEHLlasaKDEHLQQYQEvcaqrdayqqklvqLQEKclALQAQITALTKQNEQHIKEL 798
Cdd:pfam09731 367 -----------RTELERQAEAHEEHL----KDVLVEQEIE--------------LQRE--FLQDIKEKVEEERAGRLLKL 415
|
250
....*....|....*....
gi 578817221 799 EKNKSQMSGVEAAASDPSE 817
Cdd:pfam09731 416 NELLANLKGLEKATSSHSE 434
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
501-707 |
1.35e-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: 44.13 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 501 RIIQENERLKQEILEKSNRIEEQN-DKI----SELIERNQRYVEQSNLMMEkrnnslqtatentqarvlhAEQEKAKVTE 575
Cdd:pfam13851 1 ELMKNHEKAFNEIKNYYNDITRNNlELIkslkEEIAELKKKEERNEKLMSE-------------------IQQENKRLTE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 576 ELAAATAQVSHLQLKMTAHQK----------KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQS--KFKSE 643
Cdd:pfam13851 62 PLQKAQEEVEELRKQLENYEKdkqslknlkaRLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQdvQQKTG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221 644 KQNRkQLELKVTSLEEELtdlrvekESLEKNLSERKKKS---AQERSQAEEEIDEIRKSYQEELDKL 707
Cdd:pfam13851 142 LKNL-LLEKKLQALGETL-------EKKEAQLNEVLAAAnldPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
514-709 |
1.43e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 514 LEKSNRIEEQND----KISELIERNQRYVEQSNLMMEK-----RNNSLQTATENTQARV------LHAEQEKAKVTEELA 578
Cdd:pfam00038 17 IDKVRFLEQQNKlletKISELRQKKGAEPSRLYSLYEKeiedlRRQLDTLTVERARLQLeldnlrLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 579 -----------------AATAQVSHLQLKMTA-----------HQKKETELQMQLTES--LKETDLLRGQ-LTKV----- 622
Cdd:pfam00038 97 lrtsaendlvglrkdldEATLARVDLEAKIESlkeelaflkknHEEEVRELQAQVSDTqvNVEMDAARKLdLTSAlaeir 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 623 ------------------QAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQ 684
Cdd:pfam00038 177 aqyeeiaaknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
|
250 260
....*....|....*....|....*
gi 578817221 685 ERSQAEEEIDEIrksyQEELDKLRQ 709
Cdd:pfam00038 257 QLADYQELISEL----EAELQETRQ 277
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
512-686 |
1.54e-04 |
|
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: 45.82 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 512 EILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELAAATaqvshlQ 588
Cdd:pfam05911 664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlesTKSQLQESEQLIAELRSELASLK------E 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 589 LKMTAhqkkETELQMQlTESLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTdlRVEK 668
Cdd:pfam05911 738 SNSLA----ETQLKCM-AESYEDLET---RLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNEK 807
|
170
....*....|....*....
gi 578817221 669 ESLEKNL-SERKKKSAQER 686
Cdd:pfam05911 808 KESSNCDaDQEDKKLQQEK 826
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
529-707 |
1.58e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.77 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 529 ELIERNQRYVEQSNLMmEKRNNSLQTATEN-TQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE 607
Cdd:pfam08614 4 ELIDAYNRLLDRTALL-EAENAKLQSEPESvLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 608 slketdllrgqltkVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL-------TDLRVEKESLekNLserkk 680
Cdd:pfam08614 83 --------------LNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELrekrklnQDLQDELVAL--QL----- 141
|
170 180
....*....|....*....|....*..
gi 578817221 681 ksaqERSQAEEEIDEIRKSYQEELDKL 707
Cdd:pfam08614 142 ----QLNMAEEKLRKLEKENRELVERW 164
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
582-746 |
1.62e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 582 AQVSHLQLKMTAHQK-KETELQMQLTESLKETDL-LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE---LKVTS 656
Cdd:TIGR00606 187 ALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 657 LEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR-------KSYQEELDKLRQLLKKTRVSTDQAAAEQLSLV 729
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYhnhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170
....*....|....*....
gi 578817221 730 --QAELQTQWEAKCEHLLA 746
Cdd:TIGR00606 347 veQGRLQLQADRHQEHIRA 365
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
582-789 |
1.77e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.61 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 582 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKvtsLEEEl 661
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR---LKAE- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 662 tdlRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQllkktrvstdqaAAEQLSLVQAELQTQWEAKC 741
Cdd:pfam09726 478 ---QEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQ------------RKRELESEIKKLTHDIKLKE 542
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578817221 742 EHLLA-SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:pfam09726 543 EQIRElEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETR 591
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
443-936 |
1.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 443 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEK---SNR 519
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 520 IEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ-LKMTAHQKKE 598
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 599 TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE---------QAQSKFKSEK-----QNRKQLELKVTSLEEELTDL 664
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkkadeakKAEEAKKADEakkaeEAKKADEAKKAEEKKKADEL 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 665 RVEKE---SLEKNLSERKKKSAQERSQAE---EEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE 738
Cdd:PTZ00121 1552 KKAEElkkAEEKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 739 AKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK---ELEKNKSQMSGVEAAASDP 815
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKKAEELKKKE 1711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 816 SEKVKKImnqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeqekeeSSSEEEEEKAEERPRRPSQEQSASA 895
Cdd:PTZ00121 1712 AEEKKKA-----EELKKAEE--------------ENKIKAEEAK-----------KEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 578817221 896 SSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQD 936
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
499-709 |
1.93e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEE 576
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---AEEKREaaAEAEEEAEEAREEVAELNSKLAELKER 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 577 L-------------AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkvQAKLSELQETSEQAqskfkse 643
Cdd:PRK02224 588 IeslerirtllaaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERA------- 658
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817221 644 KQNRKQLELKVTSLEEELTDLRVE----KESLE--KNLSERKKKSAQERSQAE---EEIDEIRKSYQEELDKLRQ 709
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEigavENELEelEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQ 733
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
589-714 |
1.98e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 44.72 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 589 LKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSekqnrkqLELKVTSLEEELTDLRVEK 668
Cdd:COG4026 121 LKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKK-------LREENSILEEEFDNIKSEY 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578817221 669 ESLEKNLSERKKKSAQERSQAEEEIDEIrksYQEELDKLRQLLKKT 714
Cdd:COG4026 194 SDLKSRFEELLKKRLLEVFSLEELWKEL---FPEELPEEDFIYFAT 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
616-829 |
2.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 616 RGQLTKVQAKLSELQETSEQAQSKfksEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDE 695
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRK---ALFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 696 IRKSYQEELDKLRQllkktrvstdqaAAEQLSLVQaelqtqweakcehllasakdehlQQYQEVCAQRDAYQQKLVQLQE 775
Cdd:COG4372 85 LNEQLQAAQAELAQ------------AQEELESLQ-----------------------EEAEELQEELEELQKERQDLEQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578817221 776 KCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQS 829
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
511-849 |
2.44e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 511 QEILEKSNRIEEQNDKISElIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLK 590
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLAC-IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS--AQR 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 591 MTAHQKKETELQMQLTE--SLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 668
Cdd:COG5022 877 VELAERQLQELKIDVKSisSLKLVNL---ELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 669 ESLEKNLSERK--KKSAQERS----QAEEEIDEIRKSyQEELDKLRQLLKKTRV--STDQAAAEQLSLVQAELQTQWEAk 740
Cdd:COG5022 954 PELNKLHEVESklKETSEEYEdllkKSTILVREGNKA-NSELKNFKKELAELSKqyGALQESTKQLKELPVEVAELQSA- 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 741 cEHLLASAKdEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaLTKQNEQHIKELEKNKSQMSGVEAA--------A 812
Cdd:COG5022 1032 -SKIISSES-TELSILKPLQKLKGLLLLENNQLQARYKALKLRRE-NSLLDDKQLYQLESTENLLKTINVKdlevtnrnL 1108
|
330 340 350
....*....|....*....|....*....|....*..
gi 578817221 813 SDPSEKVKKImnqVFQSLRREFELEESYNGRTILGTI 849
Cdd:COG5022 1109 VKPANVLQFI---VAQMIKLNLLQEISKFLSQLVNTL 1142
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
495-691 |
2.64e-04 |
|
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: 45.33 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKI---SELIERNQRYVEQSNLMMEKRNNSLqtaTENTQARVLHAEQEKA 571
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARR 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 572 KVTEELAAATAQVSH----LQLKMTAHQKKETELQmQLTESLKETDllrgqltkVQAKlselQETSEQAQSKfKSEKQNR 647
Cdd:COG3096 1002 EAREQLRQAQAQYSQynqvLASLKSSRDAKQQTLQ-ELEQELEELG--------VQAD----AEAEERARIR-RDELHEE 1067
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578817221 648 -KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 691
Cdd:COG3096 1068 lSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
567-826 |
2.78e-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: 45.01 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 567 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 646
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 647 RKQLELKVTSLEEELTDlrvEKESLEKNLSERKKKSaQERSQAEEEIDEIRK---SYQEELDKL-RQLLKKTRVSTD--- 719
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKE---NKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKqkeELENELNLLeKEKLNIQKNIDKikn 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 720 QAAAEQLSLVQAELQTQweakcEHLLASAKDEHL-QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKEL 798
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQ-----KNKSLESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260
....*....|....*....|....*...
gi 578817221 799 EKNKSQMSGVEAAASDPSEKVKKIMNQV 826
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
520-736 |
2.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 520 IEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ--LKMTAHQKK 597
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 598 ETELQMQLTESLKE----TDLLRG-----QLTKVQAKL----SELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 664
Cdd:COG3883 97 RSGGSVSYLDVLLGsesfSDFLDRlsalsKIADADADLleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221 665 RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 736
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
638-825 |
2.80e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 638 SKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsYQEELDKLRQLLKKTRVS 717
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 718 TDQaAAEQLSLVQAELQtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLV-------QLQEKCLALQAQITALTKQ 790
Cdd:COG1340 80 RDE-LNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVEKIKELEKELEKAKKA 155
|
170 180 190
....*....|....*....|....*....|....*
gi 578817221 791 NEQHiKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:COG1340 156 LEKN-EKLKELRAELKELRKEAEEIHKKIKELAEE 189
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
645-822 |
2.84e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 645 QNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDK-LRQLLKKTRVSTDQAAA 723
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYASVKA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 724 EQLSLVQAELQTQWEAKCEHLLASAKDEH-LQQYQEVcaqrdayqqKLVQLQEKclalqAQITALTKQNE---Q------ 793
Cdd:PRK00409 607 HELIEARKRLNKANEKKEKKKKKQKEKQEeLKVGDEV---------KYLSLGQK-----GEVLSIPDDKEaivQagimkm 672
|
170 180 190
....*....|....*....|....*....|.
gi 578817221 794 --HIKELEKNKSQmsgveaaasdPSEKVKKI 822
Cdd:PRK00409 673 kvPLSDLEKIQKP----------KKKKKKKP 693
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
607-715 |
3.04e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 607 ESLKEtdLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNR-KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQE 685
Cdd:COG2433 376 LSIEE--ALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453
|
90 100 110
....*....|....*....|....*....|..
gi 578817221 686 RSQAEEEIDEIRK--SYQEELDKLRQLLKKTR 715
Cdd:COG2433 454 RSEERREIRKDREisRLDREIERLERELEEER 485
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
595-802 |
3.04e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.71 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 595 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqskfksEKQNRKQLELKVTslEEELTDLRVEKESLEKN 674
Cdd:pfam03528 7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKE--------EDLKRQNAVLQEA--QVELDALQNQLALARAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 675 LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE------AKCEHLLASA 748
Cdd:pfam03528 77 MENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYREsaereiADLRRRLSEG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 749 KDEHLQQYQEVCAQRDAYQQKLV--QLQEKCLALQAQITaltkQNEQHIKELEKNK 802
Cdd:pfam03528 157 QEEENLEDEMKKAQEDAEKLRSVvmPMEKEIAALKAKLT----EAEDKIKELEASK 208
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
501-794 |
3.37e-04 |
|
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: 44.73 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 501 RIIQ-ENERLKQEILEKSNRIEEQNdKISELIERNQRYVEqsnlmmekRNNSLQTATENTQARvLHAEQEKAKVTEELAA 579
Cdd:pfam05557 10 RLSQlQNEKKQMELEHKRARIELEK-KASALKRQLDRESD--------RNQELQKRIRLLEKR-EAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 580 ATAQ----VSHLQLKMTAHQKKETELQMQLTESLKE--TDLLRGQLtKVQAKLSELQETSEQ---AQSKFKSEKQNRKQL 650
Cdd:pfam05557 80 LKKKyleaLNKKLNEKESQLADAREVISCLKNELSElrRQIQRAEL-ELQSTNSELEELQERldlLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 651 ELKVTSL---EEELTDLRVEKESLEKNLSERKKKSAQ---------ERSQAEEEIDEIRKS------YQEELDKLRQLLK 712
Cdd:pfam05557 159 EKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSElaripelekELERLREHNKHLNENienkllLKEEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 713 KTRVSTDQAAAEQLSL--VQAELQtQWE----AKCEHL----LASAKDEHLQQYQEVCAQRD--------AYQQKLVQLQ 774
Cdd:pfam05557 239 REEKYREEAATLELEKekLEQELQ-SWVklaqDTGLNLrspeDLSRRIEQLQQREIVLKEENssltssarQLEKARRELE 317
|
330 340
....*....|....*....|
gi 578817221 775 EKCLALQAQITALTKQNEQH 794
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRH 337
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
239-427 |
3.41e-04 |
|
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: 44.76 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 239 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 318
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 319 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 397
Cdd:pfam03154 260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321
|
170 180 190
....*....|....*....|....*....|..
gi 578817221 398 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 427
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
572-790 |
3.50e-04 |
|
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: 43.56 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 572 KVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKS--------- 642
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKElaeaiknli 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 643 ----------EKQNRKQLELKVTSLEEELTDL-RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:pfam06008 96 dnikeinekvATLGENDFALPSSDLSRMLAEAqRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 712 KKTRvstdqaaaEQLSLVQAELQTQWEAKCEHLLASAKDEHLQqyQEVCAQRDAYQQKLVQLQEkclaLQAQITALTKQ 790
Cdd:pfam06008 176 NALR--------DSLAEYEAKLSDLRELLREAAAKTRDANRLN--LANQANLREFQRKKEEVSE----QKNQLEETLKT 240
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
495-726 |
3.51e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRI---IQEN----ERLKQEILEKSNR-IEEQNDKISELIER----------NQRYVEQSNLMMEKRNNSLQTAT 556
Cdd:pfam06160 235 VDKEIQQLeeqLEENlallENLELDEAEEALEeIEERIDQLYDLLEKevdakkyvekNLPEIEDYLEHAEEQNKELKEEL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 557 ENTQARVLHAEQEKAKV---TEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQets 633
Cdd:pfam06160 315 ERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILE-------QLEEIEEEQEEFK--- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 634 EQAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEE-------IDEIRKSYQEE 703
Cdd:pfam06160 385 ESLQSLRKDELEAREKLDEFKLELRE--IKRLVEKSnlpGLPESYLDYFFDVSDEIEDLADElnevplnMDEVNRLLDEA 462
|
250 260
....*....|....*....|....
gi 578817221 704 LDKLRQLLKKTRVSTDQAA-AEQL 726
Cdd:pfam06160 463 QDDVDTLYEKTEELIDNATlAEQL 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
495-704 |
3.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEKS-NRIEEQNDKISELIERNQRYVEQSNlmMEKRNNSLQTATENTQARVLHAEQEKAKV 573
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD--AEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 TEELAAATAQVSHLQLKMTahQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqsKFKSEKQNRKQLELK 653
Cdd:PRK03918 639 EKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE----KLKEELEEREKAKKE 712
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578817221 654 VTSLEEELTDLRVEKESLeknlserKKKSAQERSQAEEEIDEIRKSYQEEL 704
Cdd:PRK03918 713 LEKLEKALERVEELREKV-------KKYKALLKERALSKVGEIASEIFEEL 756
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
503-803 |
4.13e-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: 44.65 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 503 IQENE-RLKQEILEKSNRIEEQNDKISELIERNQryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAT 581
Cdd:TIGR00606 370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 582 AQVSHLQLKMtahQKKETELQmQLTESLKETDLLRGQLTKVQAKLSELQETS--EQAQSKFKSEKQNRKQLELKVTSLEE 659
Cdd:TIGR00606 447 EILEKKQEEL---KFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 660 ELTDLRVEKESLEKNLSERKKKsaqerSQAEEEIDEIRKSYQEEL--------------DKLRQLLKKTRVSTDQAAAEQ 725
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDK-----MDKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 726 LSLVQAE-LQTQWEAKCEhllasAKDEHLQQYQ----EVCAQRDaYQQKLVQLQ---EKCLALQAQITALTKQNEQHIKE 797
Cdd:TIGR00606 598 KELASLEqNKNHINNELE-----SKEEQLSSYEdklfDVCGSQD-EESDLERLKeeiEKSSKQRAMLAGATAVYSQFITQ 671
|
....*.
gi 578817221 798 LEKNKS 803
Cdd:TIGR00606 672 LTDENQ 677
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
602-835 |
4.21e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 602 QMQLT-ESLKETDLLRGQLTKVQA-KLSELQETSEQA-----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKn 674
Cdd:PRK04778 55 KLNLTgQSEEKFEEWRQKWDEIVTnSLPDIEEQLFEAeelndKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLE- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 675 lSErkKKSAQERSQAEEEIDEIRK-------SYQEELDKLRQLLKKTRVSTDQ-----------AAAEQLSLVQAELqTQ 736
Cdd:PRK04778 134 -SE--EKNREEVEQLKDLYRELRKsllanrfSFGPALDELEKQLENLEEEFSQfveltesgdyvEAREILDQLEEEL-AA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 737 WEAKCEH---LLASAKDEHLQQYQEVcaqRDAYQQKLVQ---LQEkcLALQAQITALTKQ---NEQHIKELEknksqmsg 807
Cdd:PRK04778 210 LEQIMEEipeLLKELQTELPDQLQEL---KAGYRELVEEgyhLDH--LDIEKEIQDLKEQideNLALLEELD-------- 276
|
250 260 270
....*....|....*....|....*....|.
gi 578817221 808 VEAAasdpSEKVKKI---MNQVFQSLRREFE 835
Cdd:PRK04778 277 LDEA----EEKNEEIqerIDQLYDILEREVK 303
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
595-716 |
5.18e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 595 QKKETELQMQLTESLKETDLLRGQ-LTKVQAKLSELQETSEQAQSKFKSEKQnrkqLELKVTSLEEELTDLRVEKESLEK 673
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 674 NLSERKKKSAQERSQAEEEIDE--------------IRKSYQEELDKLRQL---LKKtRV 716
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
900-1136 |
6.12e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 900 PQAPLNRERPESPMVPSEQVVEeavPLPPQALTTSQDghrrkgdseAEALSEIKDGSLPPELscipshrvlgPPTSIPPE 979
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGE---PVHPRMLTWIRG---------LEELASDDAGDPPPPL----------PPAAPPAA 2563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 980 PlgpvsmdsecEESLAASPMAAKPDNPSgkVCVREVAPDGPLQESSTRLSLT---SDPEEGDPLALGPESPGEPQPPQLK 1056
Cdd:PHA03247 2564 P----------DRSVPPPRPAPRPSEPA--VTSRARRPDAPPQSARPRAPVDdrgDPRGPAPPSPLPPDTHAPDPPPPSP 2631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 1057 KDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLS-GDEEDELFKGATLKALRPKAQPeeededeVSMKGRPPPT 1135
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRRRAARPTVGS-------LTSLADPPPP 2704
|
.
gi 578817221 1136 P 1136
Cdd:PHA03247 2705 P 2705
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
434-678 |
6.39e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 434 GDMASFLMTEARQHNTEIRMavskVADKMDHLMTKV-------EELQKHSAGNsmlipsmsVTMETSMIMSN---IQRII 503
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQT----LDMKIDHIQQQIktynkniEEQRKKNGEN--------IARKQNKYDELveeAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QENERLKQEILEKSNRIEEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTATENtqarvLHAEQEK-AKVT 574
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 575 EELAAATAQVSHLQLKMTAHQKKE---TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQnrkqle 651
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE------ 379
|
250 260
....*....|....*....|....*..
gi 578817221 652 lKVTSLEEELTDLRVEKESLEKNLSER 678
Cdd:PHA02562 380 -ELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
497-718 |
6.50e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 497 SNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnLMMEKRNNSLQTATENTQARVLHAEQEK-----A 571
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE--LVEEAKTIKAEIEELTDELLNLVMDIEDpsaalN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 572 KVTEELAAATAQVSHLQLKMTAHQK----------------KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ 635
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 636 A---QSKFKSEKQNRKQLELKVTSLE---EELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDeirksyqeELDKLRQ 709
Cdd:PHA02562 339 LlelKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY--------HRGIVTD 410
|
....*....
gi 578817221 710 LLKKTRVST 718
Cdd:PHA02562 411 LLKDSGIKA 419
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
884-1053 |
6.56e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 884 PRRPSQeqsasassgqPQAPLNRERPESPMVP--SEQVVEEAVPLPPQALTTSQDGHRRKGDSEAE-----ALSEIKDGS 956
Cdd:PTZ00449 633 PKRPPP----------PQRPSSPERPEGPKIIksPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKEtkttvVLDESFESI 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 957 LPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNP--SGKVCVREVAPDGPLQESSTRL----SL 1030
Cdd:PTZ00449 703 LKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADTPLPDILAEEfkeeDI 782
|
170 180
....*....|....*....|....*
gi 578817221 1031 TSDPEEGDPLALGPESPGE--PQPP 1053
Cdd:PTZ00449 783 HAETGEPDEAMKRPDSPSEheDKPP 807
|
|
| NST1 |
pfam13945 |
Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly ... |
534-704 |
7.44e-04 |
|
Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly or indirectly, in the salt sensitivity of some cellular functions in yeast. It does this without affecting sodium accumulation. It negatively affects salt-tolerance through an interaction with the splicing factor Msl1p. This interaction stresses the importance of efficient RNA processing under salt stress conditions.
Pssm-ID: 372833 Cd Length: 186 Bit Score: 41.80 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 534 NQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQkkeTELQMQLTESLKETD 613
Cdd:pfam13945 6 NNNSQNQQQNQHDNNTVDHHSQVNSSKRKSKKKKKKKNRNGSNNNNDESSTSQSTPSPFAIT---TSSTRPVSNNPPLSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 614 LLRGQLTKVQAKLSELQETSEQaqskfkSEKQNRKQLELKVTslEEELTDL-RVEKESLEKNLSERKKKS------AQER 686
Cdd:pfam13945 83 SAASRSAHKNNKDRSIWNTSTQ------EERENIKEFWLSLG--EEERRSLvKVEKEAVLKKMKEQQKHScsctvcGRKR 154
|
170
....*....|....*...
gi 578817221 687 SQAEEEIDEIRKSYQEEL 704
Cdd:pfam13945 155 TAIEEELEVLYDAYYEEL 172
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
504-735 |
8.07e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QENERLKQEILEKSNRIEEQNDKISELIERN----QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAA 579
Cdd:PTZ00440 560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 580 ATAQVSHLQLKMTA--HQKKETE-LQMQLTESLKETDLLR-----------GQLTKVQAKLSELQET--SEQAQSKFKSE 643
Cdd:PTZ00440 640 LLDELSHFLDDHKYlyHEAKSKEdLQTLLNTSKNEYEKLEfmksdnidniiKNLKKELQNLLSLKENiiKKQLNNIEQDI 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 644 KQNRKQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQ 720
Cdd:PTZ00440 720 SNSLNQYTIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISND 799
|
250
....*....|....*..
gi 578817221 721 AAA--EQLSLVQAELQT 735
Cdd:PTZ00440 800 INIlkENKKNNQDLLNS 816
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
956-1136 |
8.61e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 956 SLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPE 1035
Cdd:PHA03307 92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 1036 EGDPLALGPES---PGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPShhSQRSSLSGDEEDELfkgatlkal 1112
Cdd:PHA03307 172 AALPLSSPEETaraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR--SAADDAGASSSDSS--------- 240
|
170 180
....*....|....*....|....
gi 578817221 1113 rpKAQPEEEDEDEVSMKGRPPPTP 1136
Cdd:PHA03307 241 --SSESSGCGWGPENECPLPRPAP 262
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
434-797 |
9.21e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 434 GDMASFLMTEARQH--------NTEIRMAVS-KVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMimsniQRIIQ 504
Cdd:PRK10246 156 GQFAAFLNAKPKERaelleeltGTEIYGQISaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASL-----QVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 505 ENERL--KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLH------AEQEKA----- 571
Cdd:PRK10246 231 EEKQLltAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRphweriQEQSAAlahtr 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 572 ----KVTEELAAATAQVSHL-QLKMTAHQKKETELQmQLTESLKETDLLR-------------GQLTKVQAKLSELQETS 633
Cdd:PRK10246 311 qqieEVNTRLQSTMALRARIrHHAAKQSAELQAQQQ-SLNTWLAEHDRFRqwnnelagwraqfSQQTSDREQLRQWQQQL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 634 EQAQSKFKS-----------------EKQNRKQ-LELKVTSLEEELTDLRVEKESLEKNLSerkkKSAQERSQAEEEIDE 695
Cdd:PRK10246 390 THAEQKLNAlpaitltltadevaaalAQHAEQRpLRQRLVALHGQIVPQQKRLAQLQVAIQ----NVTQEQTQRNAALNE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 696 IRKSYQEeldKLRQLLKKTRVSTDQAAAEQLSLVQAELQTqweAKCEHLLASAKDEHLQQYQEVC-----AQRDAYQQKL 770
Cdd:PRK10246 466 MRQRYKE---KTQQLADVKTICEQEARIKDLEAQRAQLQA---GQPCPLCGSTSHPAVEAYQALEpgvnqSRLDALEKEV 539
|
410 420
....*....|....*....|....*..
gi 578817221 771 VQLQEKCLALQAQITALTKQNEQHIKE 797
Cdd:PRK10246 540 KKLGEEGAALRGQLDALTKQLQRDESE 566
|
|
| AmmeMemoSam_B |
TIGR04336 |
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain ... |
946-1004 |
9.34e-04 |
|
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain family as the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility). Members of the present family occur as part of a three gene system with an uncharacterized radical SAM enzyme and a homolog of the mammalian protein AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Memo in humans has protein-protein interaction activity with binding of phosphorylated Try, but members of this family may be active as enzymes, as suggested by homology to a class of nonheme iron dioxygenases.
Pssm-ID: 275135 [Multi-domain] Cd Length: 269 Bit Score: 42.56 E-value: 9.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 946 AEALSEIKDGslPPELSCI--PSHRVLGPPTSIPPE-----PLGPVSMDSECEESLAASPMAAKPD 1004
Cdd:TIGR04336 55 AHAYAALKKG--RPETVVLlgPNHTGYGSGIALPPEgswetPLGDVPVDEELAEELLEHSPIIELD 118
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
443-806 |
9.42e-04 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 43.29 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 443 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMlipsmsvtmetsmimsNIQRIIQENERLKQEILEKSN---- 518
Cdd:COG4477 101 KAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNRE----------------EIEELKEKYRELRKTLLAHRHsfgp 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 519 ---RIEEQNDKISELIERNQRYVEQSNlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTA 593
Cdd:COG4477 165 aaeELEKQLEELEPEFEEFEELTESGD-YLEAREilEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 594 ------HQKKETELQmQLTESLKET--DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLR 665
Cdd:COG4477 244 qgyvleHLNIEKEIE-QLEEQLKEAleLLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 666 VEKESLEknlserkkksaqersqaeEEIDEIRKSYQ---EELDKLRQLLKktrvstdqaaaeQLSLVQAELQTqweakce 742
Cdd:COG4477 323 EQNRELK------------------EEIDRVQQSYRlneNELEKVRNLEK------------QIEELEKRYDE------- 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817221 743 hlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKqNEQHIKE-LEKNKSQMS 806
Cdd:COG4477 366 --IDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRK-DELEAREkLDELKKKLR 427
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
441-713 |
9.61e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 441 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNS----MLIPSMSVTMETSMIMSNIQRIIQENERLKQEI-LE 515
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELaLK 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 516 KSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARV-------------LHAEQEKAK-----VTEEL 577
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcqtlLRELETHIEeydreFNEIE 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 578 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRkQLELKVTSL 657
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA--HFNNNEEVTAALQTGAELSHLAAEIQFFNR-LREEDTHLL 801
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 658 EEELTDLRVEKESLEKNLSERKKKSAQERSQAEE----------EIDEIRKSYQEELDKLRQLLKK 713
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSrleeksatlgEITHQLLKYEECSKQLAQLTQE 867
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
460-703 |
9.88e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 460 DKMDHLMTKVEELQKHSagNSMLIPSMSVTMETSMIMSNIQRIIQENERL------KQEILEKSNRIEEQNDKISELIER 533
Cdd:PTZ00440 2342 QDENYGKDKNIELNNEN--NSYIIKTKEKINNLKEEFSKLLKNIKRNNTLcnnnniKDFISNIGKSVETIKQRFSSNLPE 2419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 534 NQRYV-------EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLqlkmTAHQKKETELQMQLT 606
Cdd:PTZ00440 2420 KEKLHqieenlnEIKNIMNETKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDLIENV----TSHNEKIKSELLIIN 2495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 607 ESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-RKQLELKVTSLEE-------ELTDL-------------- 664
Cdd:PTZ00440 2496 DALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYiINELESHVSKLNEllsyidnEIKELeneklkllekakie 2575
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 578817221 665 --RVEKESLEKNLSERKKKSAQERSQAEEEI--DEIRKSYQEE 703
Cdd:PTZ00440 2576 esRKERERIESETQEDNTDEEQINRQQQERLqkEEEQKAYSQE 2618
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
509-647 |
1.21e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 509 LKQEILEKSNRIEEQNDKISELIERnqryveqsnLMMEKRNN-SLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHL 587
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADL---------LSLERQGNqDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsEKQNR 647
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAK 173
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
499-772 |
1.32e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERN--QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvtEE 576
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE--DE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 577 LAAATAQVSHLQLKMTAHQKKETELQMQlteslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKE-----REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 657 LEEELtDLRvekESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 736
Cdd:pfam13868 231 ARQRQ-ELQ---QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR 306
|
250 260 270
....*....|....*....|....*....|....*.
gi 578817221 737 WEAKcehllasakdEHLQQYQEVCAQRDAYQQKLVQ 772
Cdd:pfam13868 307 AAER----------EEELEEGERLREEEAERRERIE 332
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
587-739 |
1.36e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 587 LQLKMTAHQKKETELQMQLTESLKE-TDLLRGQLTKVQAKLSELQEtseqAQSKFKSE-KQNRKQLELKVTSLEEELTD- 663
Cdd:cd22656 97 LELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVD----KLTDFENQtEKDQTALETLEKALKDLLTDe 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 664 -LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRqllKKTRVSTD-QAAAEQLSLVQA---------- 731
Cdd:cd22656 173 gGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLA---AALRLIADlTAADTDLDNLLAligpaipale 249
|
....*...
gi 578817221 732 ELQTQWEA 739
Cdd:cd22656 250 KLQGAWQA 257
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
495-726 |
1.37e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEI-------LEKSNR-IEEQNDKISELIERN---QRYVEQSN-------LMMEKRNNSLQTAT 556
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLeeldldeAEEKNEeIQERIDQLYDILEREvkaRKYVEKNSdtlpdflEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 557 ENTQA--RVLHAEQEKAK-VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQETs 633
Cdd:PRK04778 334 DRVKQsyTLNESELESVRqLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILK-------QLEEIEKEQEKLSEM- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 634 eqAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEEIDEIR---KSYQEELDK- 706
Cdd:PRK04778 406 --LQGLRKDELEAREKLERYRNKLHE--IKRYLEKSnlpGLPEDYLEMFFEVSDEIEALAEELEEKPinmEAVNRLLEEa 481
|
250 260
....*....|....*....|....
gi 578817221 707 ---LRQLLKKTRVSTDQAA-AEQL 726
Cdd:PRK04778 482 tedVETLEEETEELVENATlTEQL 505
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
552-835 |
1.42e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLKMTAHQKKeTELQMQLTESLKETDLLRGQLTKVQAK-LSELQ 630
Cdd:NF041483 224 LNAASTQAQEATDHAEQLRSSTAAESDQARRQAA--ELSRAAEQRM-QEAEEALREARAEAEKVVAEAKEAAAKqLASAE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 631 ETSEQAQSKFKSE-----KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAeeEIDEIRKSYQEELD 705
Cdd:NF041483 301 SANEQRTRTAKEEiarlvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAA--QLAKAARTAEEVLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 706 KLRQLLKktrvSTDQAAAEQLSLVQAELqtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQIT 785
Cdd:NF041483 379 KASEDAK----ATTRAAAEEAERIRREA----EAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAE 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221 786 AL---------------TKQNEQHIKE--------LEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:NF041483 451 QLraeavaegerirgeaRREAVQQIEEaartaeelLTKAKADADELRSTATAESERVRTEAIERATTLRRQAE 523
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
574-709 |
1.42e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 39.49 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 TEELAAATAQVSHLQLKMTAHQKKetelqmqlTESLK--ETDLlrgqltkvqAKLSELQETSEQAQSKFKSEKQNRKQLE 651
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAK--------IDALQvvEKDL---------RSCIKLLEEIEAELAKLEEAKKKLKELR 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221 652 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQ 709
Cdd:pfam18595 64 DALEEKEIELRELERREERLQRQLENAQEKLERLREQAEEKREAA----QARLEELRE 117
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
597-837 |
1.52e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 597 KETELQMQLTESLKEtdllRGQLTKVQAKLSELQETSEQAQSKFKSE-KQNRKQLELKVTSLEEELTDLRVEKESLEknl 675
Cdd:pfam07888 28 RAELLQNRLEECLQE----RAELLQAQEAANRQREKEKERYKRDREQwERQRRELESRVAELKEELRQSREKHEELE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 676 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEaKCEHLLASAKDEHlqq 755
Cdd:pfam07888 101 -EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDI-----KTLTQRVLERETELERMKE-RAKKAGAQRKEEE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 756 yqevcAQRDAYQQKLVQLQEKCLALQaqitaltkqneqhiKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:pfam07888 171 -----AERKQLQAKLQQTEEELRSLS--------------KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
..
gi 578817221 836 LE 837
Cdd:pfam07888 232 NE 233
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
621-800 |
1.68e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.65 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 621 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEIRKS 699
Cdd:pfam10368 1 SPEEKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELYEEIIELGMDEFDEIKKLSDEALENVEEREELlEKEKESIEEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 700 YqEELDKLRQLLKKTRvstDQAAAEQLSLVQAELQTQWEAkceHllasakDEHLQQYQE-VCAQRDAY---QQKLVQLQE 775
Cdd:pfam10368 81 K-EEFKKIKEIIEEIE---DEELKKEAEELIDAMEERYEA---Y------DELYDAYKKaLELDKELYemlKDEDLTLEE 147
|
170 180
....*....|....*....|....*
gi 578817221 776 kclaLQAQITALTKQNEQHIKELEK 800
Cdd:pfam10368 148 ----LQEQIEKINESYEEVKEANEQ 168
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
495-713 |
1.69e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQEnerlKQEILEKSNRIeeQN-DKISELIERNQRYVEQSNLMMEKRNNSLQTAT-ENTQARVLHAEQEKAK 572
Cdd:NF033838 63 VESHLEKILSE----IQKSLDKRKHT--QNvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTkKELDAAFEQFKKDTLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 VTEELAAATAQVSHLQLKmtAHQKKETELQMQLTESLKETDLLRGQlTKVQAKLSELQETSEQAQSKFKSEKQnrKQLEL 652
Cdd:NF033838 137 PGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAE-SDVEVKKAELELVKEEAKEPRDEEKI--KQAKA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221 653 KVTSLEEELTdlrvekeSLEKNLSERKK--KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:NF033838 212 KVESKKAEAT-------RLEKIKTDREKaeEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKR 267
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
329-423 |
1.83e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 42.76 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 329 QGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQA------PSAALMQVSSLDSHSAVSGN-AQSFQPYAGMQAY 401
Cdd:PRK10263 738 DGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQY 817
|
90 100
....*....|....*....|....
gi 578817221 402 AYPQASAVTSQ--LQPVRPLYPAP 423
Cdd:PRK10263 818 QQPQQPVAPQPqyQQPQQPVAPQP 841
|
|
| WH1 |
smart00461 |
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ... |
2-100 |
1.86e-03 |
|
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.
Pssm-ID: 214674 Cd Length: 106 Bit Score: 38.88 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 2 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 78
Cdd:smart00461 3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82
|
90 100
....*....|....*....|..
gi 578817221 79 RQnWSIMFESEKAAVEFNKQVC 100
Cdd:smart00461 83 CV-YGLNFASEEEAKKFRKKVL 103
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
495-800 |
1.93e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER-NQRYVEQSNLMMEKRnNSLQTATENTQARVLHAEQEKAKV 573
Cdd:PRK04778 106 EINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQlKDLYRELRKSLLANR-FSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 574 TEElaaaTAQVSHLQLKMTAHQKKETELQM-QLTESLKEtdLLRGQLTKVQAKLSELQETSEQAqskfksEKQNRKqleL 652
Cdd:PRK04778 185 VEL----TESGDYVEAREILDQLEEELAALeQIMEEIPE--LLKELQTELPDQLQELKAGYREL------VEEGYH---L 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 653 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQER-SQAEEEIDEI----------RKSYQEELDKLRQLLKKTRVSTDQA 721
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENLALLEELDLDEAEEKnEEIQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 722 AAEQLSLVQA------ELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQqklvQLQEKCLALQAQITALTKQNEQ-- 793
Cdd:PRK04778 330 KEEIDRVKQSytlnesELESVRQLEKQ--LESLEKQYDEITERIAEQEIAYS----ELQEELEEILKQLEEIEKEQEKls 403
|
....*...
gi 578817221 794 -HIKELEK 800
Cdd:PRK04778 404 eMLQGLRK 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
560-736 |
2.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 560 QARVLHAEQEKAKVTEElAAATAQVshlqlkmtahQKKETELQMQlteslKETDLLRGQLTK-VQAKLSELQETSEQAQS 638
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-AKKEAEA----------IKKEALLEAK-----EEIHKLRNEFEKeLRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 639 KFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKnlserkkksaqersqAEEEIDEIRKSYQEELDKLRQLlkktrvST 718
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEK---------------KEEELEELIEEQLQELERISGL------TA 152
|
170
....*....|....*...
gi 578817221 719 DQAAAEQLSLVQAELQTQ 736
Cdd:PRK12704 153 EEAKEILLEKVEEEARHE 170
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
652-786 |
2.07e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 652 LKVTSLEEELTDLRVEKESLEKnlserkkksaqERSQAEEEIDEirkSYQEELDKLRQLLKKTRvstdqaaaEQLslvqA 731
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221 732 ELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITA 786
Cdd:COG0542 458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| tig |
TIGR00115 |
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ... |
110-183 |
2.17e-03 |
|
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: 41.77 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 110 LDAVLSQ--DLIVADGPAVEVGDSLEVAYTGwlfqnHVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 183
Cdd:TIGR00115 131 LERLREQnaTLVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAG 199
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
659-790 |
2.30e-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: 39.16 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 659 EELTDLRVEKESLEKNLS--ERKKKSAQERSQAEEEI-DEIRKSYQEELdklrqLLKKTRVSTDQAAAEQLSLVQAELQt 735
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAAdaEAQLQKLQEDLEKQAEIaREAQQNYEREL-----VLHAEDIKALQALREELNELKAEIA- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578817221 736 QWEAKCEhllaSAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 790
Cdd:pfam07926 75 ELKAEAE----SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
500-824 |
2.31e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 500 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQT-------ATENTQARVLHAEQEKAK 572
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLAnrfsygpAIDELEKQLAEIEEEFSQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 573 VTEElaaaTAQVSHLQLKMTAHQ-KKETELQMQLTESLKEtdLLRGQLTKVQAKLSELQETSEQAQskfksekqnRKQLE 651
Cdd:pfam06160 165 FEEL----TESGDYLEAREVLEKlEEETDALEELMEDIPP--LYEELKTELPDQLEELKEGYREME---------EEGYA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 652 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEI----------RKSYQEELDKLRQLLKKTRVSTDQ 720
Cdd:pfam06160 230 LEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEiEERIDQLydllekevdaKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 721 AAAEQLSLVQA-ELQTQWEAKCEHLlasakDEHLQ----QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI 795
Cdd:pfam06160 310 LKEELERVQQSyTLNENELERVRGL-----EKQLEelekRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFK 384
|
330 340
....*....|....*....|....*....
gi 578817221 796 KELEknksQMSGVEAAASDPSEKVKKIMN 824
Cdd:pfam06160 385 ESLQ----SLRKDELEAREKLDEFKLELR 409
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
503-635 |
2.67e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.27 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 503 IQENERLKQEILEKSNRI-EEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE---NTQARVLHAEQEKAK-VTEEL 577
Cdd:pfam10368 27 LVELEKKEQELYEEIIELgMDEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEefkKIKEIIEEIEDEELKkEAEEL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221 578 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL----LRGQLTKVQAKLSELQETSEQ 635
Cdd:pfam10368 107 IDAMEERYEAYDELYDAYKKALELDKELYEMLKDEDLtleeLQEQIEKINESYEEVKEANEQ 168
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
610-696 |
3.51e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 610 KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL-EKNLSE--RKKKSAQER 686
Cdd:TIGR04320 254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATaqAALANAEAR 333
|
90
....*....|.
gi 578817221 687 -SQAEEEIDEI 696
Cdd:TIGR04320 334 lAKAKEALANL 344
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
685-800 |
3.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 685 ERSQAEEEIDEIRKSYqEELDKLRQLLKKTRVSTD------------QAAAEQLSLVQAELQT--QWEA-KCEHLLASAK 749
Cdd:COG4913 219 EEPDTFEAADALVEHF-DDLERAHEALEDAREQIEllepirelaeryAAARERLAELEYLRAAlrLWFAqRRLELLEAEL 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 750 DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQ--------ITALTKQNEQHIKELEK 800
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEE 356
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
883-1053 |
4.40e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 883 RPRRPSQEQSASASSGQPQAPLNRERPesPMVPSEQVVEEAVPLPPQAlttSQDGHRRKGDSEAEALSEIKDGSLPPELS 962
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTR--PAVASLSESRESLPSPWDP---ADPPAAVLAPAAALPPAASPAGPLPPPTS 2833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 963 CIPSHRVLGPPTSIPPEPL-GPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPdgPLQESSTRLSLTSDPEEGDPla 1041
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLgGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQPERPP-- 2909
|
170
....*....|..
gi 578817221 1042 lGPESPGEPQPP 1053
Cdd:PHA03247 2910 -QPQAPPPPQPQ 2920
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
496-799 |
4.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 496 MSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSlqtatENTQARVLHAEQEKAKVTE 575
Cdd:PRK01156 182 ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL-----KSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 576 ELAAATAQVSHLQLKMTAHQKKETELqMQLT---------------------ESLKET-DLLRGQLTKVQA---KLSELQ 630
Cdd:PRK01156 257 EIKTAESDLSMELEKNNYYKELEERH-MKIIndpvyknrnyindyfkykndiENKKQIlSNIDAEINKYHAiikKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 631 ETSEQAQSKfKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKsaQERSQAeeEIDEIRKSYQEELDKLRQL 710
Cdd:PRK01156 336 KDYNDYIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN--IERMSA--FISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 711 LKKTRVSTDQAAAEqlslvQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQ-------------RDAYQQKLVQLQEKC 777
Cdd:PRK01156 411 LNEINVKLQDISSK-----VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeeksnhiINHYNEKKSRLEEKI 485
|
330 340
....*....|....*....|..
gi 578817221 778 LALQAQITALTKQNEQHIKELE 799
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKE 507
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
509-732 |
4.46e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 509 LKQEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATentqaRVLHAEQEK-AKVTEELAAATAQVSHL 587
Cdd:PRK11637 52 IQQDIAAKEKSVRQQQQQRASLLAQ-----------LKKQEEAISQAS-----RKLRETQNTlNQLNKQIDELNASIAKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 588 -------------QLKMTAHQKKETELQMQLT--ESLKETDLLR--GQLTKV-QAKLSELQETSEQAQskfksekQNRKQ 649
Cdd:PRK11637 116 eqqqaaqerllaaQLDAAFRQGEHTGLQLILSgeESQRGERILAyfGYLNQArQETIAELKQTREELA-------AQKAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 650 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyQEELDKLRQllKKTRVSTDQAAAEQLSLV 729
Cdd:PRK11637 189 LEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD--------QQQLSELRA--NESRLRDSIARAEREAKA 258
|
...
gi 578817221 730 QAE 732
Cdd:PRK11637 259 RAE 261
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
623-709 |
4.69e-03 |
|
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: 38.75 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 623 QAKLSELQETSEQAQSKFKSEKQNRKQ----LELKVTSLEEELTDLRVEKESLEK-----------NLSERKKKSAQERS 687
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEEenrrleadhvsRLEEKEAELKKEYS 128
|
90 100
....*....|....*....|..
gi 578817221 688 QAEEEIDEIRKSYQEELDKLRQ 709
Cdd:pfam09744 129 KLHERETEVLRKLKEVVDRQRD 150
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
507-753 |
4.71e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEI-LEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVlhaEQEKAKVTEELAAATAQVS 585
Cdd:PRK05771 34 EDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV---EEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 586 HLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA------KLSELQETSEQAQSKFKSEKQNRK-----QLELKV 654
Cdd:PRK05771 111 ELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVyvvvvVLKELS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 655 TSLEEELTDLRVEKESLEknlseRKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdqaaaEQLSLVQAELQ 734
Cdd:PRK05771 191 DEVEEELKKLGFERLELE-----EEGTPSELIREIKEELEEIEKERESLLEELKELAKKY---------LEELLALYEYL 256
|
250
....*....|....*....
gi 578817221 735 TQWEAKCEHLLASAKDEHL 753
Cdd:PRK05771 257 EIELERAEALSKFLKTDKT 275
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
496-713 |
4.91e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 496 MSNIQRIIQENERLKQEILEKsnRIEEQNDKISEL------IERNQRYVEQsnlmMEKRNNSLQTATEN---TQARVLHA 566
Cdd:PRK04863 874 LSALNRLLPRLNLLADETLAD--RVEEIREQLDEAeeakrfVQQHGNALAQ----LEPIVSVLQSDPEQfeqLKQDYQQA 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 567 EQEKAKVTEELAAATAQVSHLqlkmtAHQKKETELQMqLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKF------ 640
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVVQRR-----AHFSYEDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqv 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 641 ----KSEKQNRKQLelkVTSLEEELTDLRVE-KESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQ---EELDKLRQLLK 712
Cdd:PRK04863 1022 laslKSSYDAKRQM---LQELKQELQDLGVPaDSGAEERARARRDELHARLSANRSRRNQLEKQLTfceAEMDNLTKKLR 1098
|
.
gi 578817221 713 K 713
Cdd:PRK04863 1099 K 1099
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
621-844 |
5.11e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 621 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELT--DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEiRK 698
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-RK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 699 SYQEELDKLRQLLKKTRVSTDQAAAEqlslvQAELQTQWEAKcehllasAKDEHLQQYQEVCAQRDAYQQKL---VQLQE 775
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAE-----EAKKKAEAEAK-------AKAEAEAKAKAEEAKAKAEAAKAkaaAEAAA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817221 776 KCLALQAQITALTKQ------NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRT 844
Cdd:TIGR02794 212 KAEAEAAAAAAAEAErkadeaELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFRGKT 286
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
442-783 |
5.72e-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: 40.96 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 442 TEARQhnTEIRMAVSKVAdKMDHLMTKVEELQKHSAGNSMLIPS--------MSVTMETSMIMSN-IQRIIQENERLKQE 512
Cdd:pfam10174 228 TKALQ--TVIEMKDTKIS-SLERNIRDLEDEVQMLKTNGLLHTEdreeeikqMEVYKSHSKFMKNkIDQLKQELSKKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 513 ILEKSNRIEEQNDKISElierNQRYVE---QSNLMMEKRNNSLQTATENTQARVLHAEQ---EKAK----VTEELAAATA 582
Cdd:pfam10174 305 LLALQTKLETLTNQNSD----CKQHIEvlkESLTAKEQRAAILQTEVDALRLRLEEKESflnKKTKqlqdLTEEKSTLAG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 583 QVSHLQLKMTAHQKKETELQMQLtESLKEtdllrgQLTKVQAKLSELQEtseqaqskfksekqnrkqlelKVTSLEEELT 662
Cdd:pfam10174 381 EIRDLKDMLDVKERKINVLQKKI-ENLQE------QLRDKDKQLAGLKE---------------------RVKSLQTDSS 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 663 DLRVEKESLEKNLSErkKKSAQERSQaeEEIDEIRKSYQEELDKLRQLLKKTRvstdqaaaEQLSLVQAELQTQweakcE 742
Cdd:pfam10174 433 NTDTALTTLEEALSE--KERIIERLK--EQREREDRERLEELESLKKENKDLK--------EKVSALQPELTEK-----E 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578817221 743 HLLASAKdEHLQQYQEVCAQRDAYQQKL----VQLQEKCLALQAQ 783
Cdd:pfam10174 496 SSLIDLK-EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQ 539
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
504-703 |
6.03e-03 |
|
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: 40.71 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 504 QENERLKQEILEKSNRIEEqndkisELIERNQRYVEQSNLMMEKRNNS--LQTATENTQARVLHAEQEKAKVTEElaaat 581
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMRE------ELELEQQRRFEEIRLRKQRLEEErqRQEEEERKQRLQLQAAQERARQQQE----- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 582 aqvshlqlkmtAHQKKETELQMQlteslketdllrgqltkvqaklsELQETSEQAQskfkSEKQNRKQLELKVT------ 655
Cdd:pfam15709 427 -----------EFRRKLQELQRK-----------------------KQQEEAERAE----AEKQRQKELEMQLAeeqkrl 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578817221 656 ---SLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 703
Cdd:pfam15709 469 memAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| Tig |
COG0544 |
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ... |
118-183 |
6.82e-03 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440310 [Multi-domain] Cd Length: 424 Bit Score: 40.11 E-value: 6.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 118 LIVADGPAvEVGDSLEVAYTGWlfqnhVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 183
Cdd:COG0544 151 LVPVERAA-EEGDRVTIDFEGT-----IDGEEFEGGKAED--YSLELGSGSFIPGFEEQLVGMKAG 208
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
465-708 |
7.23e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 465 LMTKVEELQKHSAGNSMLIPSMSVTMETSMIM---SNIQRIIQENERLKQEILEKSN-------RIEEQNDKISELIERN 534
Cdd:COG5022 919 LIENLEFKTELIARLKKLLNNIDLEEGPSIEYvklPELNKLHEVESKLKETSEEYEDllkkstiLVREGNKANSELKNFK 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 535 QRYVEQS-NLM-----------MEKRNNSLQTA-----TENTQARVLHAEQE-KAKVTEELAAATAQVSHLQL-KMTAHQ 595
Cdd:COG5022 999 KELAELSkQYGalqestkqlkeLPVEVAELQSAskiisSESTELSILKPLQKlKGLLLLENNQLQARYKALKLrRENSLL 1078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 596 KKETELQMQLTESL-KETDLLRGQLTKVQ-AKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLE-----EELTDLRVEK 668
Cdd:COG5022 1079 DDKQLYQLESTENLlKTINVKDLEVTNRNlVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEpvfqkLSVLQLELDG 1158
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 578817221 669 ESLEKNLSERKKKSA-----QERSQAEEEIDEIRKSYQEELDKLR 708
Cdd:COG5022 1159 LFWEANLEALPSPPPfaalsEKRLYQSALYDEKSKLSSSEVNDLK 1203
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
600-713 |
7.23e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 600 ELQMQLTESLKETDLLRGQltkVQAKLSELQETSEQAQSKFKSEKQNRKQlelkvtSLEEELTDLRVEKESLEKNLSERK 679
Cdd:PRK00409 527 ELERELEQKAEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEK------EAQQAIKEAKKEADEIIKELRQLQ 597
|
90 100 110
....*....|....*....|....*....|....
gi 578817221 680 KKsaQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:PRK00409 598 KG--GYASVKAHELIEARKRLNKANEKKEKKKKK 629
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
558-835 |
7.39e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.22 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 558 NTQARVLHAEQEKAK-----VTEELAaataQVSHLQLKMtahqkkETElqmQLTESLKE--TDLLRGQLTKVQAKLSELQ 630
Cdd:pfam06160 7 KIYKEIDELEERKNElmnlpVQEELS----KVKKLNLTG------ETQ---EKFEEWRKkwDDIVTKSLPDIEELLFEAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 631 ETSEQaqSKFKSEKQNRKQLELKVTSLEEELTDLRvekESLeKNLSERKKKSAQERSQAEEEIDEIRKSY---------- 700
Cdd:pfam06160 74 ELNDK--YRFKKAKKALDEIEELLDDIEEDIKQIL---EEL-DELLESEEKNREEVEELKDKYRELRKTLlanrfsygpa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 701 ----QEELDKLRQLLKKTRVSTDQ----AAAEQLSLVQ---AELQTQWEaKCEHLLASAKDEHLQQYQEVcaqRDAYQqk 769
Cdd:pfam06160 148 idelEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEeetDALEELME-DIPPLYEELKTELPDQLEEL---KEGYR-- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221 770 lvQLQEK-----CLALQAQITALTKQNEQHIKELEKNksQMSGVEAAASDPSEKvkkiMNQVFQSLRREFE 835
Cdd:pfam06160 222 --EMEEEgyaleHLNVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEER----IDQLYDLLEKEVD 284
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
566-839 |
7.48e-03 |
|
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: 40.40 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 566 AEQEKAKVTEELAAATAQVSHLQLKMtahQKKETELQmqltESLKETDLLRGQLTKVQAKLSElqETSEQAQSKFKSEKQ 645
Cdd:pfam05701 61 AEAAKAQVLEELESTKRLIEELKLNL---ERAQTEEA----QAKQDSELAKLRVEEMEQGIAD--EASVAAKAQLEVAKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 646 NRKQLELKVTSLEEELTDLRVEKESL--EKNLSERKkksAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA 723
Cdd:pfam05701 132 RHAAAVAELKSVKEELESLRKEYASLvsERDIAIKR---AEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 724 EQLSLVQAELQ--TQWEAKCEHllasAKDEHLQQYQEVCAQRDaYQQKLVQLQEKCLALQAQITALT--KQNEQHIKELE 799
Cdd:pfam05701 209 HRIGAALAREQdkLNWEKELKQ----AEEELQRLNQQLLSAKD-LKSKLETASALLLDLKAELAAYMesKLKEEADGEGN 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 578817221 800 KNKSQMSGVEAAASDPSE--KVK----------KIMNQVFQSLRREFELEES 839
Cdd:pfam05701 284 EKKTSTSIQAALASAKKEleEVKaniekakdevNCLRVAAASLRSELEKEKA 335
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
507-804 |
7.84e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.06 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 507 ERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENtqarvLHAEQEKAKVT-EELAAATAQVS 585
Cdd:pfam05622 186 ETYKRQVQELHGKLSEESKKADKLEFEYKK--------LEEKLEALQKEKER-----LIIERDTLRETnEELRCAQLQQA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 586 HLQLKMTAHQK-----------------KETELQMQLteslkETDLLR----GQLTKVQAKLSELQETSEQAQSKFksEK 644
Cdd:pfam05622 253 ELSQADALLSPssdpgdnlaaeimpaeiREKLIRLQH-----ENKMLRlgqeGSYRERLTELQQLLEDANRRKNEL--ET 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 645 QNRKQlelkvtslEEELTDLRVEKESLEKNLSERKKK---SAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQA 721
Cdd:pfam05622 326 QNRLA--------NQRILELQQQVEELQKALQEQGSKaedSSLLKQKLEEHLEKLHEA-QSELQKKKEQIEELEPKQDSN 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 722 AAEQLslvqAELQTQWEAKCEHLLASakDEHLQQYQE----VCAQRDAYQQKLVQLQekCLALQAQITALTKQNEQHIKE 797
Cdd:pfam05622 397 LAQKI----DELQEALRKKDEDMKAM--EERYKKYVEkaksVIKTLDPKQNPASPPE--IQALKNQLLEKDKKIEHLERD 468
|
....*..
gi 578817221 798 LEKNKSQ 804
Cdd:pfam05622 469 FEKSKLQ 475
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
658-744 |
8.29e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 38.88 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 658 EEELTDLRVEKEslEKNLSERKKKSAQERSQAEEEiDEIRKsyqEELDKLRQLLKKTRvstdqAAAEQLSLVqAELQTQW 737
Cdd:pfam15927 5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72
|
....*....
gi 578817221 738 E--AKCEHL 744
Cdd:pfam15927 73 EryMRCDGL 81
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
600-823 |
8.30e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 600 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQA----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 675
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENiarkQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 676 SERKKKSAQERSQAeEEIDEIRKSYQE-------------ELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQtqwEAKCE 742
Cdd:PHA02562 258 NKLNTAAAKIKSKI-EQFQKVIKMYEKggvcptctqqiseGPDRITKI--KDKLKELQHSLEKLDTAIDELE---EIMDE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 743 HLLASAKdehlqqYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ---NEQHIKELEKNKSQMSgveaaaSDPSEKV 819
Cdd:PHA02562 332 FNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIV------KTKSELV 399
|
....
gi 578817221 820 KKIM 823
Cdd:PHA02562 400 KEKY 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
508-707 |
8.47e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 508 RLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaEQEKAKVTEELAAATAQVSHL 587
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL--AGRLREVTLEGEGGSAGGSLT 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVE 667
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578817221 668 KESLEKNLSERKKKSAQERSQAEEEIDEIRKsyqeELDKL 707
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLER----EIEAL 779
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
460-854 |
8.76e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 460 DKMDHLMTKVEELQKhsagNSMLIPSMSVTMETSMI-MSNIQRIIQENERLKQEILEKSNRIE-----EQNDKI------ 527
Cdd:PTZ00440 863 QIVDNIIKDIENMNK----NINIIKTLNIAINRSNSnKQLVEHLLNNKIDLKNKLEQHMKIINtdniiQKNEKLnllnnl 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 528 ---SELIER--NQRYVEQSNLMMEKRNNSLQTATENTQARV-LHAEQEKAKVTE------ELAAATAQVSHLQLKMTAHQ 595
Cdd:PTZ00440 939 nkeKEKIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNDgTHLEKLDKEKDEwehfksEIDKLNVNYNILNKKIDDLI 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 596 KKETELQMQLTESLKeTDLLRGQLTKVQAKLSELQETSEQAQSKFKSE----------KQNRKQLELKVTSLEEELTDLR 665
Cdd:PTZ00440 1019 KKQHDDIIELIDKLI-KEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIdikkyknpkiKEEIKLLEEKVEALLKKIDENK 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 666 VEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyqeeLDKLRQLLKKTRVSTDQAAAEQLSLVQA-ELQTQWEAKCEHL 744
Cdd:PTZ00440 1098 NKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKS----LEKIYKQMEKTLKELENMNLEDITLNEVnEIEIEYERILIDH 1173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 745 LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL---------TKQNEQHIKELEKNKSQMSGvEAAASDP 815
Cdd:PTZ00440 1174 IVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTfeynayydkATASYENIEELTTEAKGLKG-EANRSTN 1252
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221 816 SEKVKKIMNQVFQSLRRE-----------------FELEESYNGRTILGTIMNTIK 854
Cdd:PTZ00440 1253 VDELKEIKLQVFSYLQQVikennkmenalheiknmYEFLISIDSEKILKEILNSTK 1308
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
572-744 |
8.97e-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: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 572 KVTEELAAATAQVSHLQLKMTAHQKketELQMQLTeslKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSE-KQNRKQL 650
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQ---ELVDRLE---KETEALRERL---QKDLEEVRAKLEPYLEELQAKlGQNVEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 651 ELKVTSLEEELTD-LRVEKESLEKNLSErkkKSAQERSQAEEEIDEIRKSYQEELDKLRQL-------LKKTRVSTDQAA 722
Cdd:pfam01442 72 RQRLEPYTEELRKrLNADAEELQEKLAP---YGEELRERLEQNVDALRARLAPYAEELRQKlaerleeLKESLAPYAEEV 148
|
170 180
....*....|....*....|..
gi 578817221 723 AEQLSLVQAELQTQWEAKCEHL 744
Cdd:pfam01442 149 QAQLSQRLQELREKLEPQAEDL 170
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
621-798 |
9.40e-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: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 621 KVQAKLSELQETSEQAQSKFKSEKQNrkqlelKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIdeirksy 700
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQE------LVDRLEKETEALR---ERLQKDLEEVRAKLEPYLEELQAKL------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 701 QEELDKLRQLLK------KTRVSTD-QAAAEQLSLVQAELQTQWEAKCEHLLAsakdeHLQQYQEvcAQRDAYQQKLVQL 773
Cdd:pfam01442 65 GQNVEELRQRLEpyteelRKRLNADaEELQEKLAPYGEELRERLEQNVDALRA-----RLAPYAE--ELRQKLAERLEEL 137
|
170 180
....*....|....*....|....*
gi 578817221 774 QEKclaLQAQITALTKQNEQHIKEL 798
Cdd:pfam01442 138 KES---LAPYAEEVQAQLSQRLQEL 159
|
|
|