|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
193-286 |
1.28e-25 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 101.89 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 193 AVEVGDSLEVAYTSWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKSWEDGMVGMRKGGKRLLIIPPACAAGSEGVIGW 272
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 1387290470 273 TPSTDSILVFEVEI 286
Cdd:pfam00254 80 VIPPNATLVFEVEL 93
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
190-286 |
1.22e-22 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 93.71 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 190 EGPAVEVGDSLEVAYTSWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKSWEDGMVGMRKGGKRLLIIPPACA---AGS 266
Cdd:COG0545 10 TGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAygeRGA 85
|
90 100
....*....|....*....|
gi 1387290470 267 EGVIGwtpsTDSILVFEVEI 286
Cdd:COG0545 86 GGVIP----PNSTLVFEVEL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-829 |
1.47e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATA 640
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEelAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 641 QVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELT 720
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 721 DLRTEKESLEKNLSERKKKSAQERcQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEakcE 800
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEE-EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR---L 493
|
250 260
....*....|....*....|....*....
gi 1387290470 801 QLLASAKNEHLQQYQEVCTQRDASQQQLL 829
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
566-871 |
3.33e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQR---IIQE-NERLKQeiLEKSSRIKEQNDKISELIERNQRYV-----EQSNLMMEKRNNSLQTAtENTQAKVTEELA 636
Cdd:COG1196 187 NLERledILGElERQLEP--LERQAEKAERYRELKEELKELEAELlllklRELEAELEELEAELEEL-EAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 637 AATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLE 716
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 717 EELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLL-KKARVSTDQAAAEQLSLVQAELQTQW 795
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 796 EAKCEQLLASAKnEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAAD 871
Cdd:COG1196 424 EELEEALAELEE-EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
578-883 |
6.49e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 578 KQEILEKSSRIKEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQAKVTE---ELAAATAQVSHLHLKMTAHQ 653
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISAlrkDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNL 733
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 734 sERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKArvstdQAAAEQLSLVQAELQTQWEAKCEQL--LASAKNEHL 811
Cdd:TIGR02168 834 -AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 812 QQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ-NAQHIKDLES-KAQTSGVEATAADPSEKVKKIMNQV 883
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
563-857 |
4.76e-15 |
|
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: 80.06 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILEkssrIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTaTENTQAKVTEELAAATAQV 642
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-LKDEQNKIKKQLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 643 SHLHLKMTAHQKKETELQVQLTE--SMKETDLLRgqlaQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELT 720
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDlnNQKEQDWNK----ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 721 DLRTEKESLEKNLSERKKksaqercqaeeEIDEIRKSHQEELDKLRQLLKKARvstdqaAAEQLSLVQAELQTQWEAKCE 800
Cdd:TIGR04523 353 NSESENSEKQRELEEKQN-----------EIEKLKKENQSYKQEIKNLESQIN------DLESKIQNQEKLNQQKDEQIK 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 801 QlLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL---REQNAQHIKDLE 857
Cdd:TIGR04523 416 K-LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntRESLETQLKVLS 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
566-838 |
9.13e-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: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEntqakVTEELAAATAQVSHL 645
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-----LEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 646 HLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTE 725
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 726 KESLEKNLSE----RKKKSAQ------ERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ-TQ 794
Cdd:TIGR02168 854 IESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRlEG 933
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 795 WEAKCEQLLASAKNEH-------LQQYQEVCTQRDASQQQLLQLEEKCSAL 838
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYsltleeaEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
616-886 |
1.33e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 616 RNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQ 695
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 696 SKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKsAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARvS 775
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE-LEELESRLEELEEQLETLRSKVAQLELQIASLN-N 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 776 TDQAAAEQLSLVQAELQtQWEAKCEQLLASAkneHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ---NAQH 852
Cdd:TIGR02168 401 EIERLEARLERLEDRRE-RLQQEIEELLKKL---EEAELKELQAELEELEEELEELQEELERLEEALEELREEleeAEQA 476
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387290470 853 IKDLESKAQTSGVEATA--------ADPSEKVKKIMNQVFQF 886
Cdd:TIGR02168 477 LDAAERELAQLQARLDSlerlqenlEGFSEGVKALLKNQSGL 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
559-859 |
2.94e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.75 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 559 ETSMIMSNIQRIIQENERLKQEILEKSSRI---KEQNDKISELIERNQRYVEQSNLMMEKRNNSLQtateNTQAKVtEEL 635
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLnqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN----QLKSEI-SDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 636 AAATAQVSHLHLK--MTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVT 713
Cdd:TIGR04523 301 NNQKEQDWNKELKseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 714 SLEEELTDLRTEKESLEKNLSERKKKSAQErcqaEEEIDEIRKSHqEELDKLRQLLKKARVS--------TDQAAAEQLS 785
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEK-ELLEKEIERLKETIIKnnseikdlTNQDSVKELI 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 786 LVQAE-LQTQWEAKCEQLLASAKNEHlQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNA---QHIKDLESK 859
Cdd:TIGR04523 456 IKNLDnTRESLETQLKVLSRSINKIK-QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISslkEKIEKLESE 532
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
569-864 |
9.62e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 569 RIIQENERLKQ------EILEKSSRIKEQNDKISELIERNQRYVEQsnlmmekrnnslQTATENTQAKVTEELAAATAQV 642
Cdd:COG1196 216 RELKEELKELEaellllKLRELEAELEELEAELEELEAELEELEAE------------LAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 643 SHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDL 722
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 723 RTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQL--LKKARVSTDQAAAEQLSLVQAELQTQWEAkcE 800
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeaLLERLERLEEELEELEEALAELEEEEEEE--E 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 801 QLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSG 864
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
533-889 |
1.78e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 533 LMTKVEELQKHSagNSLLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLM 612
Cdd:TIGR02169 693 LQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 613 MEKRNNsLQTATENTQA--------KVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAEL 684
Cdd:TIGR02169 771 EEDLHK-LEEALNDLEArlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 685 SEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKsaqeRCQAEEEIDEIRKsHQEELDK 764
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRK-RLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 765 LRQLLKKARVSTDQAAAEQLSLVQAE-----LQTQWEAKCEQL--LASAKNEHLQQYQEVctqrdasQQQLLQLEEKCSA 837
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEElsledVQAELQRVEEEIraLEPVNMLAIQEYEEV-------LKRLDELKEKRAK 997
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 838 LQAQVTSLREQnaqhIKDLESKAQTSGVEATaadpsEKVKKIMNQVFQFLRG 889
Cdd:TIGR02169 998 LEEERKAILER----IEEYEKKKREVFMEAF-----EAINENFNEIFAELSG 1040
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
509-922 |
2.02e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.76 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 583
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 584 KSSRIKE----QNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLHLKMTA------- 651
Cdd:pfam05483 389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAiktseeh 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 652 HQKKETELQVQL-------TESMKETDLLRGQLAQLQAELSE-VQETSQQVQSKLKSEKQSRRQLElRVTSLEEELTDLR 723
Cdd:pfam05483 469 YLKEVEDLKTELekeklknIELTAHCDKLLLENKELTQEASDmTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLR 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 724 TEKESLEKnlsERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLK--------KARVSTDQAAAEQLSLVQAELQTQW 795
Cdd:pfam05483 548 DELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnlKKQIENKNKNIEELHQENKALKKKG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 796 EAKCEQL-------------LASAKN---EHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLReqnaqhiKDLESK 859
Cdd:pfam05483 625 SAENKQLnayeikvnkleleLASAKQkfeEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ-------KEIDKR 697
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 860 AQTSGVEATAAdpSEKVKKIMNQVFQFLRGEFEL-----EEFYSGRTVLGTIMNTIKMVTLRLLNQHE 922
Cdd:pfam05483 698 CQHKIAEMVAL--MEKHKHQYDKIIEERDSELGLyknkeQEQSSAKAALEIELSNIKAELLSLKKQLE 763
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
569-871 |
1.14e-12 |
|
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: 72.90 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 569 RIIQENERLKQEILEKSSRIKEQNDK--------------ISELIERNQRYvEQSNLMMEKrnnsLQTATENTQAKVTEE 634
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKakslsklknkheamISDLEERLKKE-EKGRQELEK----AKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 635 LAAATAQVSHLHLKMtahQKKETELQVQLTESMKETdllrGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTS 714
Cdd:pfam01576 224 IAELQAQIAELRAQL---AKKEEELQAALARLEEET----AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 715 LEEELTDLRTEKESL--------------EKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLL---KKARVS-- 775
Cdd:pfam01576 297 LGEELEALKTELEDTldttaaqqelrskrEQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLeqaKRNKANle 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 776 -TDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEhlQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLreqnAQHIK 854
Cdd:pfam01576 377 kAKQALESENAELQAELRTLQQAKQDSEHKRKKLE--GQLQELQARLSESERQRAELAEKLSKLQSELESV----SSLLN 450
|
330
....*....|....*..
gi 1387290470 855 DLESKAQTSGVEATAAD 871
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLE 467
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
571-911 |
1.50e-12 |
|
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: 71.91 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 571 IQENERLKQEILEKSSRIKEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQakvtEELAAATAQVS 643
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTK----EKIAEYTKSID 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 644 -HLHLKMTAHQKKETELQVQLTESMKETDllrGQLAQLQAELSEVQETSQQVQSKLKSEKqSRRQLELRVTSLEEELTDL 722
Cdd:COG5185 307 iKKATESLEEQLAAAEAEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEI-ENIVGEVELSKSSEELDSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 723 RTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLvQAELQTQWEAKCEQL 802
Cdd:COG5185 383 KDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNEL-ISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 803 LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQA-----------QVTSLREQNAQHIKDLESKAQTSGVEATAAD 871
Cdd:COG5185 462 QSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAtleklraklerQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1387290470 872 PSEKVKKIMNQVFQFLRGEFELEEFYSGRTVLGTIMNTIK 911
Cdd:COG5185 542 ENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIE 581
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
537-878 |
1.53e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 537 VEELQKHSAGNSLLIPSMSVTMEtsmimSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKr 616
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 617 nnslqtatentqakvteelaaataqvshlhlkmtahqkketelqvqltesmketdlLRGQLAQLQAELSEVQETSQQVQS 696
Cdd:TIGR02169 320 --------------------------------------------------------AEERLAKLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 697 KLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEiRKSHQEELDKLRQLLKK--ARV 774
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-INELKRELDRLQEELQRlsEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 775 STDQAAAEQLSLVQAELQTQWEAKCEQLlaSAKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQhik 854
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAA---DLSKYEQELYDLKEEYDRVEKELSKLQRELAE--- 494
|
330 340
....*....|....*....|....
gi 1387290470 855 dLESKAQTSGVEATAADPSEKVKK 878
Cdd:TIGR02169 495 -AEAQARASEERVRGGRAVEEVLK 517
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
662-861 |
5.01e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 662 QLTESMKEtdLLRGQLAQLQAELSEVQETSQQVQsKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSE-RKKKS 740
Cdd:COG4717 50 RLEKEADE--LFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 741 AQERCQAEEEIDEIRKSHQEELDKLRQllkkaRVSTDQAAAEQLSLVQAELQtQWEAKCEQLLASAKNEHLQQYQEVCTQ 820
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEE-----RLEELRELEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387290470 821 RDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQ 861
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
651-851 |
1.86e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLE 730
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 731 KNLSERKKKSAQ---------------------------ERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTdQAAAEQ 783
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAEL-EAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 784 LSLVQAELQTQweakcEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQ 851
Cdd:COG4942 176 LEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
565-859 |
2.83e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 565 SNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNlMMEKRNNSLQTATENTQAKVTEElaaaTAQVSH 644
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIIKN----NSEIKD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 645 LhlkmtahQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRT 724
Cdd:TIGR04523 445 L-------TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 725 EKESL---EKNLSERKKKSAQERCQAEEEIDEIrkshqeELDKLRQLLKKARVSTDQaAAEQLSLVQAELqtqwEAKCEQ 801
Cdd:TIGR04523 518 KISSLkekIEKLESEKKEKESKISDLEDELNKD------DFELKKENLEKEIDEKNK-EIEELKQTQKSL----KKKQEE 586
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 802 llasaKNEHLQQYQevcTQRDASQQQLLQLEEKCSALQAQVTSLREQN---AQHIKDLESK 859
Cdd:TIGR04523 587 -----KQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELEKAKKENeklSSIIKNIKSK 639
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-855 |
1.70e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 565 SNIQRIiqenERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLmmekrnnsLQTATENTQAKVteELAAATAQVSH 644
Cdd:COG4913 607 DNRAKL----AALEAELAELEEELAEAEERLEALEAELDALQERREA--------LQRLAEYSWDEI--DVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 645 LhlkmtahqkkETELQvQLTESMKEtdllrgqLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRT 724
Cdd:COG4913 673 L----------EAELE-RLDASSDD-------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 725 EKESLEKNLSERKKKSAQERCqAEEEIDEIRKSHQEELDKLRQLLKKARvstdQAAAEQLSLVQAELQTQWEAKCEQLLA 804
Cdd:COG4913 735 RLEAAEDLARLELRALLEERF-AAALGDAVERELRENLEERIDALRARL----NRAEEELERAMRAFNREWPAETADLDA 809
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 805 SAknEHLQQYQEVCTQRDAS-----QQQLLQLEEKCSalQAQVTSLR---EQNAQHIKD 855
Cdd:COG4913 810 DL--ESLPEYLALLDRLEEDglpeyEERFKELLNENS--IEFVADLLsklRRAIREIKE 864
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
654-870 |
2.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQvqLtESMKE-----TDL---LRGQLAQLQAElSEVQETSQQVQSKLKsekqsRRQLELRV----------TSL 715
Cdd:COG1196 174 KEEAERK--L-EATEEnlerlEDIlgeLERQLEPLERQ-AEKAERYRELKEELK-----ELEAELLLlklreleaelEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 716 EEELTDLRTEKESLEKNLSERKKKSAQERCQ---AEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 792
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 793 -TQWEAKCEQLLASAKnEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 870
Cdd:COG1196 325 lAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
588-850 |
5.83e-10 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 62.25 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 588 IKEQNDKISELIERnQRYVEQSNLMMEkrnnslqtatentqAKVTEELAAATAQVSHLHLkmtAHQKKETELQVQLtesm 667
Cdd:pfam00038 6 LQELNDRLASYIDK-VRFLEQQNKLLE--------------TKISELRQKKGAEPSRLYS---LYEKEIEDLRRQL---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 668 ketDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKnlserkkksaqeRCQA 747
Cdd:pfam00038 64 ---DTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEA------------KIES 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 748 -EEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQA--ELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRD-- 822
Cdd:pfam00038 129 lKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAArn 208
|
250 260 270
....*....|....*....|....*....|...
gi 1387290470 823 -----ASQQQLLQLEEKCSALQAQVTSLREQNA 850
Cdd:pfam00038 209 gdalrSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
618-867 |
6.65e-10 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 63.78 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 618 NSLQTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKETELqvqltesmketdlLRGQLAQLQAELSEVQETSQQVQSK 697
Cdd:PRK11281 43 AQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ-------------LKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 698 LKSE-KQSRRQLELRvtSLEEELTDLRTEKESLEKNLSERKK-----KSAQERCQAeeEIDEirksHQEELDKLRQLLKK 771
Cdd:PRK11281 110 NDEEtRETLSTLSLR--QLESRLAQTLDQLQNAQNDLAEYNSqlvslQTQPERAQA--ALYA----NSQRLQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 772 ARVSTDQAAAEQLSLVQAELQtQWEAKCE---QLLASakNEHLQQ-YQEvctQRDASQQQLLQLEEKCSALQAQVTSLR- 846
Cdd:PRK11281 182 GKVGGKALRPSQRVLLQAEQA-LLNAQNDlqrKSLEG--NTQLQDlLQK---QRDYLTARIQRLEHQLQLLQEAINSKRl 255
|
250 260
....*....|....*....|.
gi 1387290470 847 EQNAQHIKDLESKAQTSGVEA 867
Cdd:PRK11281 256 TLSEKTVQEAQSQDEAARIQA 276
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
569-792 |
1.29e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.46 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 569 RIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQA------KVTEELAAATAQV 642
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQleeeleQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 643 SHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDL 722
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 723 RTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 792
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
575-790 |
1.43e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 575 ERLKQEILEKSSRIKEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQVSHLHLKMTAHQK 654
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEA 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 655 KETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQV-----QSKLKSEKQSRRQLE--LRVTSLEEELTDLRTEKE 727
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeeENKIKAAEEAKKAEEdkKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 728 SLEKNlSERKKKSAQERCQAEEEI---DEIRKSHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAE 790
Cdd:PTZ00121 1693 ALKKE-AEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE 1755
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
566-839 |
1.61e-09 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 62.62 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERN-----QRYVEQSNLMMEKRNNSLQTATENTQakvtEELAAATA 640
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ----NDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 641 QVSHLHLK-------MTAHQKKETELQVQLTESMKETDLLRG-QLAQLQAELS------EVQETSQQVQSKLKSEKQSRR 706
Cdd:PRK11281 150 QLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNTQLQDLLQKQR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 707 QL-ELRVTSLEEELTDLRTEkesleknLSERKKKSAQERCQAEEEIDEIRKSH-----QEELDKLRQLLKKARVSTDQAA 780
Cdd:PRK11281 230 DYlTARIQRLEHQLQLLQEA-------INSKRLTLSEKTVQEAQSQDEAARIQanplvAQELEINLQLSQRLLKATEKLN 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 781 aeqlSLVQAELQTqweakceqllasaKN--EHLQQyqevcTQRDasqqqllqLEEKCSALQ 839
Cdd:PRK11281 303 ----TLTQQNLRV-------------KNwlDRLTQ-----SERN--------IKEQISVLK 333
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
676-848 |
2.05e-09 |
|
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: 59.58 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 676 QLAQLQAELsevQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKEsleknlSERKKKSAQeRCQAEEEIDEIR 755
Cdd:pfam15397 64 QLQQAKAEL---QEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQ-IANLVRQLQQLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 756 KSHQEELDKLRQLLKKarvstdqaaaeqlslVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLL------ 829
Cdd:pfam15397 134 DSQQDELDELEEMRRM---------------VLESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVMLkeieqf 198
|
170 180
....*....|....*....|....
gi 1387290470 830 -----QLEEKCSALQAQVTSLREQ 848
Cdd:pfam15397 199 refidELEEEIPKLKAEVQQLQAQ 222
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-878 |
4.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEntqAKVTEELAAATAQVSHLHLKMTAH 652
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 653 QKKETElqVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRvtSLEEEltdlRTEKESLEKN 732
Cdd:PTZ00121 1557 LKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEA----KIKAEELKKA 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 733 LSERKKKSAQERCQAEE--EIDEIRKSHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAELQTQWEA---------KCEQ 801
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEAlkkeaeeakKAEE 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 802 LLASA-----KNEHLQQYQEVcTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAADPSEKV 876
Cdd:PTZ00121 1707 LKKKEaeekkKAEELKKAEEE-NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
..
gi 1387290470 877 KK 878
Cdd:PTZ00121 1786 DE 1787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
565-862 |
5.01e-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: 60.42 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 565 SNIQRIIQENERLK----QEILEKSSRIKEQNDKISELIERNQRYveqsnlmmEKRNNSLqtatENTQAKVTEELAAATA 640
Cdd:TIGR04523 127 NKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKKQKEEL--------ENELNLL----EKEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 641 QVSHLHLKMTAHQKKE---TELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLK-------------SEKQS 704
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnkikkqlSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 705 R--------RQLELRVTSLEEELTDLRTEKES-LEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLlKKARvs 775
Cdd:TIGR04523 275 EleqnnkkiKELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL-KKEL-- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 776 tdqaaaEQLSLVQAELQTQWEAKcEQLLASAKNEHlQQYQevctqrdasqQQLLQLEEKCSALQAQVTSLREQNAQ---H 852
Cdd:TIGR04523 352 ------TNSESENSEKQRELEEK-QNEIEKLKKEN-QSYK----------QEIKNLESQINDLESKIQNQEKLNQQkdeQ 413
|
330
....*....|
gi 1387290470 853 IKDLESKAQT 862
Cdd:TIGR04523 414 IKKLQQEKEL 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
561-806 |
7.01e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 561 SMIMSNIQRIIQENERLKQEILEKSS---------RIKEQNDKISELIERNQRYVEQsnlmmekrnnslqtatENTQAKV 631
Cdd:COG4717 37 STLLAFIRAMLLERLEKEADELFKPQgrkpelnlkELKELEEELKEAEEKEEEYAEL----------------QEELEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 632 TEELAAATAQVSHLhlkmtAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEvqetsqqvqskLKSEKQSRRQLELR 711
Cdd:COG4717 101 EEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPERLEE-----------LEERLEELRELEEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 712 VTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQllKKARVSTDQAAAEQLSLVQAEL 791
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--ELEELEEELEQLENELEAAALE 242
|
250
....*....|....*
gi 1387290470 792 QTQWEAKCEQLLASA 806
Cdd:COG4717 243 ERLKEARLLLLIAAA 257
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
609-834 |
7.48e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 609 SNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKE--TELQVQLTESMKETDLLRGQLAQLQAELSE 686
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 687 VQETSQQVQSKLKSEKQSRRQL--ELRVTSLEEELTDLRTEKESLEKNLSERkkksAQERCQAEEEIDEIRKSHQEELDK 764
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 765 LRQLLKKARvstdQAAAEQLSLVQAELQTQweakcEQLLASAkNEHLQQYQEVCTQRDASQQQLLQLEEK 834
Cdd:COG3206 314 ILASLEAEL----EALQAREASLQAQLAQL-----EARLAEL-PELEAELRRLEREVEVARELYESLLQR 373
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
634-822 |
8.87e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.24 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 634 ELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKseKQSRRQLELR-- 711
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK--KYEEQLGNVRnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 712 --VTSLEEELTDLRTEKESLEKNLSErkkksAQERcqaEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEqlslVQA 789
Cdd:COG1579 89 keYEALQKEIESLKRRISDLEDEILE-----LMER---IEELEEELAELEAELAELEAELEEKKAELDEELAE----LEA 156
|
170 180 190
....*....|....*....|....*....|...
gi 1387290470 790 ELQTQwEAKCEQLLASAKNEHLQQYQEVCTQRD 822
Cdd:COG1579 157 ELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
578-860 |
1.10e-08 |
|
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: 59.97 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 578 KQEILEKSSRIKEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATENtQAKVT---EELAAATAQVSHLHLKMTAHQK 654
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIEryqEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 655 KETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQL---ELRVTSLEEELTDLRTEKESLEK 731
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRAKEQQATE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 732 NLSERKKK---SAQERCQAEEEIDEIRK-----SHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAELqtqweAKCEQLL 803
Cdd:COG3096 456 EVLELEQKlsvADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYR--SQQALAQRLQQLRAQL-----AELEQRL 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387290470 804 ASAKN--EHLQQYQ-----------EVCTQRDASQQQLLQLEEKCSALQAQVTSLR---EQNAQHIKDLESKA 860
Cdd:COG3096 529 RQQQNaeRLLEEFCqrigqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRqqlEQLRARIKELAARA 601
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
567-859 |
1.16e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 567 IQRIIQENER---LKQEILEKSSRIKEQNDKISELIE---------------RNQRYVEQSNLMMEKR------------ 616
Cdd:TIGR04523 67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeqKNKLEVELNKLEKQKKenkknidkflte 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 617 --------------NNSL----------QTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKE---TELQVQLTESMKE 669
Cdd:TIGR04523 147 ikkkekeleklnnkYNDLkkqkeeleneLNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 670 TDLLRGQLAQLQAELSEVQETSQQVQSKLK-------------SEKQSR--------RQLELRVTSLEEELTDLRTEKES 728
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnkikkqlSEKQKEleqnnkkiKELEKQLNQLKSEISDLNNQKEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 729 -LEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLK--KARVSTDQAAAEQLSLVQAELQT---QWEAKCEQL 802
Cdd:TIGR04523 307 dWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKelTNSESENSEKQRELEEKQNEIEKlkkENQSYKQEI 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 803 --LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ---NAQHIKDLESK 859
Cdd:TIGR04523 387 knLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiikNNSEIKDLTNQ 448
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-858 |
1.18e-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: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 EELAAATAQVSHLhLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELseVQETSQQVQSKLKSEKQSRRQLELRV 712
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 713 TSLEEELTDLRtekESLEKNLSERKKKSAQERCQAEEEIDEIrkshQEELDKLRQLLKKARVSTDQAAAEQLSLVQ--AE 790
Cdd:COG4913 319 DALREELDELE---AQIRGNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEEFAALRAeaAA 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 791 LQTQWEAKcEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLES 858
Cdd:COG4913 392 LLEALEEE-LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
563-785 |
1.46e-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: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLM------MEKRNNSLQTATENTQAKVTEELA 636
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaelaeLEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 637 AATAQVSHLHLKMTAHQKketelqvQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLE 716
Cdd:COG4942 112 ALYRLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 717 EELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEiRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 785
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
573-791 |
1.67e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEkssRIKEQNDKISELIERNQRYVEQSNLM----MEKRNNSLQTATENTQakvtEELAAATAQVSHLHLK 648
Cdd:COG4913 245 EDAREQIELLE---PIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELR----AELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 649 MTAHQKKETELQVQLTESmketdllrG--QLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEK 726
Cdd:COG4913 318 LDALREELDELEAQIRGN--------GgdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387290470 727 ESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLlkKARVST----DQAA----AEQLSLVQAEL 791
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--ERRKSNiparLLALrdalAEALGLDEAEL 460
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
575-856 |
2.11e-08 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 57.77 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 575 ERLKQEILEKSSRIKEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQ-------TATENTQAKV---TEELAAATAQ 641
Cdd:pfam15742 5 EKLKYQQQEEVQQLRQNLQRLQILctsAEKELRYERGKNLDLKQHNSLLQeenikikAELKQAQQKLldsTKMCSSLTAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLHLKMtahqkKETELQV-QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRrqlelrvtsleeeLT 720
Cdd:pfam15742 85 WKHCQQKI-----RELELEVlKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVC-------------LT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 721 DLRT-EKESLEKNLSERKKKSAQERCQAEEEiDEIRK---SHQEELDKLRQLLKKARVSTDQAAAEQLSLVQaelqtQWE 796
Cdd:pfam15742 147 DTCIlEKKQLEERIKEASENEAKLKQQYQEE-QQKRKlldQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQ-----QQE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 797 AKCEQLLA--SAKNEHLQQYQEvctqrdasqqqllqLEEKCSALQAQVTSLREQNAQHIKDL 856
Cdd:pfam15742 221 AQLKQLENekRKSDEHLKSNQE--------------LSEKLSSLQQEKEALQEELQQVLKQL 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
572-883 |
2.88e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 572 QENERLKQEILEKSSRIKEQNDKISELIERNQRY-VEQSNLMMEKRNNSLQTATENTQAKVtEELAAATAQVSHLHLKMT 650
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLeKLLQLLPLYQELEALEAELAELPERL-EELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKETDL-LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRtEKESL 729
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKN-------------------------------------------LSERKKKSAQERCQAEEEIDEIRKSHQEELDKLR 766
Cdd:COG4717 246 KEArlllliaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 767 QLLKKARVSTDQAAAEQLSLVQA--ELQTQW------------EAKCEQLLASAKNEHLQQYQEVCTQrdasQQQLLQLE 832
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEElqELLREAeeleeelqleelEQEIAALLAEAGVEDEEELRAALEQ----AEEYQELK 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 833 EKCSALQAQVTSL---REQNAQHIKDLESKAQTSGVEATAADPSEKVKKIMNQV 883
Cdd:COG4717 402 EELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
631-890 |
3.69e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.46 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 631 VTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLEL 710
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 711 RVTSLEEELTDLRTEKESLEKNLSERKKKsaqercqaEEEIDEIRKSHQ-------------EELDKLRQLLKKARVSTD 777
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKL--------RKEIERLEWRQQtevlspeeekelvEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 778 Q--------AAAEQLSLVQAELQTQWEAKCEQLlasakNEHLQQYQEVCTQRDA--------------SQQQLLQLEEKC 835
Cdd:COG1340 158 KneklkelrAELKELRKEAEEIHKKIKELAEEA-----QELHEEMIELYKEADElrkeadelhkeiveAQEKADELHEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1387290470 836 SALQAQVTSLREQnaqhIKDLESKAQTSGVEATAADPSEKVKKIMNqvfQFLRGE 890
Cdd:COG1340 233 IELQKELRELRKE----LKKLRKKQRALKREKEKEELEEKAEEIFE---KLKKGE 280
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
468-896 |
4.45e-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: 57.67 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 468 AYAYPQAPAVASQLQPVRPLYPAPLSQPPHFQGSGDVASFLMTEARqHNTEIRmavsKVADKMDHLMTKVEELQKHSAGN 547
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK-VVEGIL----KDTELTKLKESAKAKESGLRKGV 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 548 SLLIPSMSVTmETSMIMSNIQRIIQENERL--KQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE 625
Cdd:pfam02463 653 SLEEGLAEKS-EVKASLSELTKELLEIQELqeKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 626 NTQAKVTEELAAATAQVSHLHLKMTahQKKETELQVQLTESMKETDLlrgqlaqlqaelsEVQETSQQVQSKlksekqsR 705
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSR--LKKEEKEEEKSELSLKEKEL-------------AEEREKTEKLKV-------E 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 706 RQLELRVTSLEEELtdlrTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 785
Cdd:pfam02463 790 EEKEEKLKAQEEEL----RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 786 LVQAELQTQWEAKCEQLLASAKNEHLQQYQEvctqrdASQQQLLQLEEKCSALQAQVTSLREQNAQHI----KDLESKAQ 861
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKEEAeillKYEEEPEE 939
|
410 420 430
....*....|....*....|....*....|....*
gi 1387290470 862 TSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEF 896
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
630-897 |
5.63e-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: 57.29 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 630 KVTEELAAATAQVSHLHLKMTAhQKKETELQVQLTESMKET-----DLLRGQLAQLQAELSEVQETSQQVQSKLKS--EK 702
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAEL-LTLRSQLLTLCTPCMPDTyherkQVLEKELKHLREALQQTQQSHAYLTQKREAqeEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 703 QSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSA-QERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAA 781
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 782 EQLSL-VQAELQTQWEAKCeqllasaknEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQnaqhIKDLESKA 860
Cdd:TIGR00618 336 QQSSIeEQRRLLQTLHSQE---------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK----LQSLCKEL 402
|
250 260 270
....*....|....*....|....*....|....*..
gi 1387290470 861 QTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEFY 897
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
676-878 |
6.11e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 676 QLAQLQAELSEVQETSQQVQSKLKSEKQSRRqlelrvtSLEEELTDLRTEKESLEKNLSERKKKSAQERCQ---AEEEID 752
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEK-------ALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 753 EIRKSHQEELDKLRQLLKKA----RVST--------------------------DQAAAEQLSLVQAELQTQWEAKCEQL 802
Cdd:COG4942 94 ELRAELEAQKEELAELLRALyrlgRQPPlalllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 803 --LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLrEQNAQHIKDLESKAQTSGVEATAADPSEKVKK 878
Cdd:COG4942 174 aeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
566-858 |
7.88e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQAKVTEELAAATAQVSHL 645
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 646 HLKMTAHQKKETELQVQLTESMKETDLLRGQL--AQLQAELSE------------------------------------- 686
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEarlllliaaallallglggsllsliltiagvlflvlg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 687 ---VQETSQQVQSKLKSEKQSRRQLELRVTSLE-EELTDLRTE---KESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQ 759
Cdd:COG4717 285 llaLLFLLLAREKASLGKEAEELQALPALEELEeEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 760 EE--LDKLRQLLKKARVSTDQAAAEQLSLVQA--ELQTQWEAKCEQLLASAKNEH----LQQYQEVCTQRDASQQQLLQL 831
Cdd:COG4717 365 LEelEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEelleALDEEELEEELEELEEELEEL 444
|
330 340
....*....|....*....|....*..
gi 1387290470 832 EEKCSALQAQVTSLReqnaQHIKDLES 858
Cdd:COG4717 445 EEELEELREELAELE----AELEQLEE 467
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
662-918 |
9.20e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.68 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 662 QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKkksa 741
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 742 QERCQAEEEIDEIRKShQEELDKLRQLLKKARVSTDQAAA---EQLSLVQAELQTQWE--AKCEQLLASAKNEHLQqyQE 816
Cdd:COG4372 108 EEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEIAereEELKELEEQLESLQEelAALEQELQALSEAEAE--QA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 817 VCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEF 896
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260
....*....|....*....|..
gi 1387290470 897 YSGRTVLGTIMNTIKMVTLRLL 918
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELE 286
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
692-861 |
1.09e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 692 QQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQercqAEEEIDEIRkshqEELDKLRQLLKK 771
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVE----ARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 772 ARvstdqaAAEQLSLVQAELQTQweakceQLLASAKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQ 851
Cdd:COG1579 85 VR------NNKEYEALQKEIESL------KRRISDLEDEILELME---RIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170
....*....|
gi 1387290470 852 HIKDLESKAQ 861
Cdd:COG1579 150 ELAELEAELE 159
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
563-736 |
1.22e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL----------IERNQRYVEQSNLMMEKRNNSLQTATENtqakvt 632
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteledlekeIKRLELEIEEVEARIKKYEEQLGNVRNN------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQEtsqqvqsklksekqsrrQLELRV 712
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------------ELDEEL 151
|
170 180
....*....|....*....|....
gi 1387290470 713 TSLEEELTDLRTEKESLEKNLSER 736
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPE 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
572-848 |
1.99e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 572 QENERLKQEILEKSSRIKEQNDKISELIERnqryVEQSNLMMEKRNNSLQTATENTQAKVTEElaaaTAQVSHLHLKMTA 651
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEE----TRQKLNLSTRLRQ 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 652 HQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEK 731
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 732 nlserkkksAQERCQaeEEIDEIrkshQEELDKLRQL---LKKARVSTDQAAAEQ--LSLVQAELQTQWEAKCEQ----- 801
Cdd:pfam01576 574 ---------TKNRLQ--QELDDL----LVDLDHQRQLvsnLEKKQKKFDQMLAEEkaISARYAEERDRAEAEAREketra 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 802 -LLASAKNEHLQQYQEV--------------CTQRDASQQQLLQLEEKCSALQAQVTSLREQ 848
Cdd:pfam01576 639 lSLARALEEALEAKEELertnkqlraemedlVSSKDDVGKNVHELERSKRALEQQVEEMKTQ 700
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
497-892 |
2.20e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 497 HFQGSGDVASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEE-----LQKHSagnsllipsmsvtmetsmimSNIQRII 571
Cdd:pfam15921 214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQ--------------------DRIEQLI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 572 QENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTA 651
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 652 HQKKETELQVQLTESMKETDLLRGQLAQLQAELsevqetsQQVQSKLKSEKQSRRQL-------ELRVTSLEEELTDLRT 724
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADL-------HKREKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNM 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 725 EKESLEKNLserkkKSAQERCQAEEEideirkshqeeldklRQLlkkARVSTDQAAAEQLSLVQAELQTQWE---AKCEQ 801
Cdd:pfam15921 427 EVQRLEALL-----KAMKSECQGQME---------------RQM---AAIQGKNESLEKVSSLTAQLESTKEmlrKVVEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 802 LlaSAKNEHLQQYQEVCTQRDASQQqllQLEEKCSALQAQVTSLRE------QNAQHIKDLESKAQTSGVEATAADPSEK 875
Cdd:pfam15921 484 L--TAKKMTLESSERTVSDLTASLQ---EKERAIEATNAEITKLRSrvdlklQELQHLKNEGDHLRNVQTECEALKLQMA 558
|
410
....*....|....*..
gi 1387290470 876 VKkimNQVFQFLRGEFE 892
Cdd:pfam15921 559 EK---DKVIEILRQQIE 572
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
625-771 |
2.24e-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: 53.39 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 625 ENTQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEV--QETSQQVQSKLKSEK 702
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 703 QSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKK 771
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
575-870 |
2.63e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 575 ERLKQEILEKSsrikEQNDKISELIERNQRYVEQSNLMMekrNNSLQTATENTQAkvtEELAAATAQVSHLHLKMTAHQK 654
Cdd:PRK04863 789 EQLRAEREELA----ERYATLSFDVQKLQRLHQAFSRFI---GSHLAVAFEADPE---AELRQLNRRRVELERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 655 KETELQVQLTESMKETDLLRGQLAQ--------LQAELSEVQETSQQVQSKLKSEKQSRRQLELrvtsLEEELTDLRTEK 726
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSDP 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 727 ESLEK-----NLSERKKKSAQERCQAEEEIDEiRKSH-------------QEELDKLRQLLKKARVSTDQA------AAE 782
Cdd:PRK04863 935 EQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQ-RRAHfsyedaaemlaknSDLNEKLRQRLEQAEQERTRAreqlrqAQA 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 783 QL---SLVQAELQTQWEAKcEQLLASAKNEhLQQY---------QEVCTQRDASQQQLLQLEEKCSALQAQVTS----LR 846
Cdd:PRK04863 1014 QLaqyNQVLASLKSSYDAK-RQMLQELKQE-LQDLgvpadsgaeERARARRDELHARLSANRSRRNQLEKQLTFceaeMD 1091
|
330 340
....*....|....*....|....
gi 1387290470 847 EQNAQhIKDLESKAQTSGVEATAA 870
Cdd:PRK04863 1092 NLTKK-LRKLERDYHEMREQVVNA 1114
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
215-309 |
2.83e-07 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 215 GQVFDSTANKDKLLRLKLGSgkVIKSWEDGMVGMRKGGKRLLIIPPACAAGSEGVIGwTPsTDSILVFEVEIRRVRFARD 294
Cdd:PRK10902 178 GKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IP-ANSTLVFDVELLDVKPAPK 253
|
90
....*....|....*
gi 1387290470 295 SGSDGHSVSSRDSAA 309
Cdd:PRK10902 254 ADAKPEADAKAADSA 268
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
651-851 |
3.28e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 52.69 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEvqetsqqvQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLE 730
Cdd:pfam12795 34 ASKQRAAAYQKALDDAPAELRELRQELAALQAKAEA--------APKEILASLSLEELEQRLLQTSAQLQELQNQLAQLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 731 KNLSERKKKSAQercqAEEEIDEIRKshqeELDKLRQLLKKARVSTDQAAAEQLSLVQAELQtqweakceqlLASAKNEH 810
Cdd:pfam12795 106 SQLIELQTRPER----AQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQAELA----------ALKAQIDM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387290470 811 LQQYQEVCT--------QRDASQQQLLQLEEKCSALQAQVTSLREQNAQ 851
Cdd:pfam12795 168 LEQELLSNNnrqdllkaRRDLLTLRIQRLEQQLQALQELLNEKRLQEAE 216
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
633-870 |
5.21e-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: 54.19 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQ---------------LQAELSEVQETSQQVQSK 697
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQanlladetladrleeLREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 698 -------------LKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDK 764
Cdd:COG3096 916 gkalaqleplvavLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNEKLRARLEQ 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 765 LRQLLKKARVSTDQAAAE--QLSLVQAELQTQWEAKCEQLlasakNEHLQQYQEVCTQRDAS------------QQQLLQ 830
Cdd:COG3096 996 AEEARREAREQLRQAQAQysQYNQVLASLKSSRDAKQQTL-----QELEQELEELGVQADAEaeerarirrdelHEELSQ 1070
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387290470 831 LEEKCSALQAQVTSLR---EQNAQHIKDLESKAQTSGVEATAA 870
Cdd:COG3096 1071 NRSRRSQLEKQLTRCEaemDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
565-771 |
6.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 565 SNIQRIIQENErlkQEILEKSSRIKEQNDKISELIERnQRYVEQSNLMMEKRNNSLqTATENTQAKVTEELAAATAQVSH 644
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI-EELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 645 LHLKMTAHQKKETELQVQ------LTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS---EKQSRRQLELRVTSL 715
Cdd:PRK03918 264 LEERIEELKKEIEELEEKvkelkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieeRIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 716 EEELTDLRTEKESLEKNLSE--------------RKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKK 771
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELyeeakakkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
575-876 |
7.34e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 575 ERLKQEILEKSS-----RIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQVSHLHLKM 649
Cdd:PRK02224 190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--EELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 650 TA------------HQKKET--ELQVQLTESMKETDL-------LRGQLAQLQAELSEVQETSQQVQ-------SKLKSE 701
Cdd:PRK02224 268 AEterereelaeevRDLRERleELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRvaaqahnEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 702 KQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAqercQAEEEIDEIRKSHQ---EELDKLRQLLKKARvSTDQ 778
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIE----ELEEEIEELRERFGdapVDLGNAEDFLEELR-EERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 779 AAAEQLSLVQAELQTQWE--AKCEQLLASAKNEHLQQYQE----VCTQRDASQQ------QLLQLEEKCSALQAQVTSLR 846
Cdd:PRK02224 423 ELREREAELEATLRTARErvEEAEALLEAGKCPECGQPVEgsphVETIEEDRERveeleaELEDLEEEVEEVEERLERAE 502
|
330 340 350
....*....|....*....|....*....|....*..
gi 1387290470 847 E--QNAQHIKDLESKAQTSG-----VEATAADPSEKV 876
Cdd:PRK02224 503 DlvEAEDRIERLEERREDLEeliaeRRETIEEKRERA 539
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
578-861 |
7.97e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 578 KQEILEKSSRI-------KEQNDKISELIERNQRYVEQSNLMMEKRNNSLQT---ATENTQAKVTEELAAATAQVSHL-H 646
Cdd:pfam15921 456 KNESLEKVSSLtaqlestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEkerAIEATNAEITKLRSRVDLKLQELqH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 647 LKMTA----HQKKETE-LQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQ-SKLKSEKQ-SRRQLEL--------- 710
Cdd:pfam15921 536 LKNEGdhlrNVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELqefkilkdk 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 711 ---RVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQE--ELDKLRQLLKKarvsTDQAAAEQLS 785
Cdd:pfam15921 616 kdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNElnSLSEDYEVLKR----NFRNKSEEME 691
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 786 LVQAELQTQweakceqlLASAKNEhLQQYQEVCTQRDASQQQLLQLeekCSALQAQVTSLREQnaqhIKDLESKAQ 861
Cdd:pfam15921 692 TTTNKLKMQ--------LKSAQSE-LEQTRNTLKSMEGSDGHAMKV---AMGMQKQITAKRGQ----IDALQSKIQ 751
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
626-812 |
1.01e-06 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 52.93 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 626 NTQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSR 705
Cdd:pfam09726 388 NNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTV 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 706 RQLELRvtsLEEEltdlRTEKESLEKNLSERKKKSAQERCQAEE----------EIDEIRKSHQEELD-KLRQLLKKARV 774
Cdd:pfam09726 468 QQLEKR---LKAE----QEARASAEKQLAEEKKRKKEEEATAARavalaaasrgECTESLKQRKRELEsEIKKLTHDIKL 540
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387290470 775 STDQAAaeQLSLVQAELQTQWE-AKCEQLLASA------KNEHLQ 812
Cdd:pfam09726 541 KEEQIR--ELEIKVQELRKYKEsEKDTEVLMSAlsamqdKNQHLE 583
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
648-793 |
1.45e-06 |
|
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: 50.29 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 648 KMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQvQSKlksEKQSRRQLELRVTSLEEELTDLRTEKE 727
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEK---DKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 728 SLEknlsERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKaRVstdQAAAEQLSLVQAELQT 793
Cdd:pfam13851 110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
573-862 |
1.61e-06 |
|
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: 52.34 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTAH 652
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTH 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 653 QKKET---ELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESL 729
Cdd:pfam05667 303 TEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNLsERKKKSAQERCQAEEEIdeirkshqeelDKLRQLLkkarvstdQAAAEQLslvqAELQTQWEAKCEQLLasaknE 809
Cdd:pfam05667 383 EKQY-KVKKKTLDLLPDAEENI-----------AKLQALV--------DASAQRL----VELAGQWEKHRVPLI-----E 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 810 HLQQYQEVCT-QRDASQQQLLQLEEkcsalqaqvtsLREQnaqhIKDLESKAQT 862
Cdd:pfam05667 434 EYRALKEAKSnKEDESQRKLEEIKE-----------LREK----IKEVAEEAKQ 472
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-878 |
1.75e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 572 QENERLKQEILEKSSRIKEQNDKISEliERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLHLKMT 650
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKE--EAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKETDllrgQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELR-VTSLEEELTDLRTEKESL 729
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkADEAKKKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNLSERKK----KSAQERCQAEE--EIDEIRKShqEELDKLRQLLKKARVSTdqaaAEQLSLVQAELQTQWEAKCEQ-- 801
Cdd:PTZ00121 1503 KKAAEAKKKadeaKKAEEAKKADEakKAEEAKKA--DEAKKAEEKKKADELKK----AEELKKAEEKKKAEEAKKAEEdk 1576
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290470 802 LLASAKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTsgVEATAADPSEKVKK 878
Cdd:PTZ00121 1577 NMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK--VEQLKKKEAEEKKK 1648
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
659-863 |
2.14e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 659 LQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEkqsrrQLELRVTSLEEELTDLRTEKESLEKNLSErkk 738
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAE--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 739 ksaqercqAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQW----------EAKCEQLLASAKN 808
Cdd:COG3206 238 --------AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialRAQIAALRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387290470 809 EHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQhIKDLESKAQTS 863
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVA 363
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
307-495 |
2.63e-06 |
|
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: 52.08 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 307 SAAPSPIPPADSISADPVVSPSTSVPFRSGESalrsksnSLSEHLTVNTNPDTVKAKLISRMAKMgQPMLPILPPqldsn 386
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQS-------TAAPHTLIQQTPTLHPQRLPSPHPPL-QPMTQPPPP----- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 387 dseiedvnaPRGAGQPLATPSVQPSLQP-AHPVlpqmtsqapQPSVSRLQTPSAAlmQVASLDSHSAVSGNAQSFQPYAG 465
Cdd:pfam03154 259 ---------SQVSPQPLPQPSLHGQMPPmPHSL---------QTGPSHMQHPVPP--QPFPLTPQSSQSQVPPGPSPAAP 318
|
170 180 190
....*....|....*....|....*....|....*
gi 1387290470 466 VQAYAYPQAPAVASQLQP-----VRPLYPAPLSQP 495
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSqqpprEQPLPPAPLSMP 353
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
565-770 |
2.99e-06 |
|
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: 51.98 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 565 SNIqrIIQENERLKQEILEKSSRiKEQndKISElIERNQRYVEQSNLMMEKRNNS---LQTATENTQAKVteelaaataq 641
Cdd:TIGR01612 1546 SEI--IIKEIKDAHKKFILEAEK-SEQ--KIKE-IKKEKFRIEDDAAKNDKSNKAaidIQLSLENFENKF---------- 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 vshlhLKMTAHQKKetelqvqLTESMKETDLLRGQLAQL-----QAELSEVQETSQQVQSKLKSEKQSRRQLELRVTsle 716
Cdd:TIGR01612 1610 -----LKISDIKKK-------INDCLKETESIEKKISSFsidsqDTELKENGDNLNSLQEFLESLKDQKKNIEDKKK--- 1674
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 717 eELTDLRTEKESLEKNLSERKKKSaqeRCQAEEEIDEIRKSHQEELDKLRQLLK 770
Cdd:TIGR01612 1675 -ELDELDSEIEKIEIDVDQHKKNY---EIGIIEKIKEIAIANKEEIESIKELIE 1724
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
530-783 |
3.61e-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: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 530 MDHLMTKVEELQKHSAGNSLL--IPSMSVtmetsmimsnIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVE 607
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLlvVPRAEL----------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 608 QSNLMMEKRNNSLQTATENTQAKvTEELAAATAQVSHLHLKMTAHQ----KKETELQVQLTESMKETDLLRGQLAQLQAE 683
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREK-HEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 684 LSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELD 763
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
250 260
....*....|....*....|
gi 1387290470 764 kLRQLLKKARVSTDQAAAEQ 783
Cdd:pfam07888 232 -NEALLEELRSLQERLNASE 250
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
573-841 |
4.40e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 49.95 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEkssRIKEQNDKISELIERNQRYVEQ-SNLMMEKRNNSLQTATENTQakVTEELAAATAQV--SHLHLKm 649
Cdd:pfam09728 82 QNKKLKEESKK---LAKEEEEKRKELSEKFQSTLKDiQDKMEEKSEKNNKLREENEE--LREKLKSLIEQYelRELHFE- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 650 taHQKKETELQVQLTES-MKETDLLRGQLAQlQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEltdlrteKES 728
Cdd:pfam09728 156 --KLLKTKELEVQLAEAkLQQATEEEEKKAQ-EKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEF-------QDT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 729 LEKNlserkkksaqercqaEEEIDEIRKSHQEELDKLRQLLKKArvstdqaaaeqlslvqAELQTQWEaKCEQLLASAKN 808
Cdd:pfam09728 226 LNKS---------------NEVFTTFKKEMEKMSKKIKKLEKEN----------------LTWKRKWE-KSNKALLEMAE 273
|
250 260 270
....*....|....*....|....*....|...
gi 1387290470 809 EHLQQYQEVctqrDASQQQLLQLEEKCSALQAQ 841
Cdd:pfam09728 274 ERQKLKEEL----EKLQKKLEKLENLCRALQAE 302
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-971 |
5.43e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 572 QENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRN--NSLQTATENTQAKVTEELAAATAQVSHLHLKM 649
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 650 TAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKqsRRQLELRVTsleEELtdlrteKESL 729
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKA---EEL------KKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNLSERKKKSAQERCQAE---EEIDEIRKSHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAE--LQTQWEAKCEQLLA 804
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMK--AEEAKKAEEAKIKAEelKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 805 SAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNaqhiKDLESKAQTSGVEATAADPSEKVKKIMNQVF 884
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE----EDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 885 QflrgefELEEFYSGRTVlgtimNTIKMVTLRLLNQHEQEKGESSNEEEEEEDEAQARSPSGQSQAPLDRESQgpPAVLS 964
Cdd:PTZ00121 1716 K------KAEELKKAEEE-----NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK--EAVIE 1782
|
....*..
gi 1387290470 965 EWVVQED 971
Cdd:PTZ00121 1783 EELDEED 1789
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
559-857 |
6.19e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 559 ETSMIMSNIQRI---IQENERLKQEILEKSSrikeQNDKISELIERNQRYVeqSNLMM---EKRNNSLQTATENTQakvt 632
Cdd:PRK04863 224 ENSGVRKAFQDMeaaLRENRMTLEAIRVTQS----DRDLFKHLITESTNYV--AADYMrhaNERRVHLEEALELRR---- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 eELAAAtaqvshlhlkmtahQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLK-SEKQSRRQLELr 711
Cdd:PRK04863 294 -ELYTS--------------RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRqQEKIERYQADL- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 712 vtsleEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKS---HQEELDKLR----------QLLKKARVSTDQ 778
Cdd:PRK04863 358 -----EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQALDVQQtraiqyqqavQALERAKQLCGL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 779 A--AAEQLSLVQAELQTQWEAKCEQLLA---------SAKNEHLQQYQEVC-----TQRDASQQQLLQLEEKCSALQAQV 842
Cdd:PRK04863 433 PdlTADNAEDWLEEFQAKEQEATEELLSleqklsvaqAAHSQFEQAYQLVRkiageVSRSEAWDVARELLRRLREQRHLA 512
|
330
....*....|....*
gi 1387290470 843 TSLrEQNAQHIKDLE 857
Cdd:PRK04863 513 EQL-QQLRMRLSELE 526
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
565-781 |
6.83e-06 |
|
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: 50.34 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 565 SNIQRIIQENERLKQEILEKSSRIKEQNDKISELIErnqryVEQSNLMMEKRNNSLQTATENtqakvteelaaataqvsh 644
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-----LSKSSEELDSFKDTIESTKES------------------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 645 LHLKMTAHQKKETELQVQLTESMKETDLLRGQL-AQLQAELSEVQETSQQVQSKLKSEKQSRRQLElrvtslEEELTDLR 723
Cdd:COG5185 393 LDEIPQNQRGYAQEILATLEDTLKAADRQIEELqRQIEQATSSNEEVSKLLNELISELNKVMREAD------EESQSRLE 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 724 TEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAA 781
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAE 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
559-813 |
7.63e-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: 49.53 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 559 ETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNnslqtatENTQAKVTEELAAA 638
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI-------LEYLKEKAEREEER 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 639 TAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSE---KQSRR-QLELRVTS 714
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRqelQQAREeQIELKERR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 715 LEEEltdLRTEKESLEKNLSERKKKSAQERCQAEEEIdEIRKSHQEELDKLRQLLKKARvstdqAAAEQLSLVQAELQTQ 794
Cdd:pfam13868 252 LAEE---AEREEEEFERMLRKQAEDEEIEQEEAEKRR-MKRLEHRRELEKQIEEREEQR-----AAEREEELEEGERLRE 322
|
250
....*....|....*....
gi 1387290470 795 WEAKCEQLLASAKNEHLQQ 813
Cdd:pfam13868 323 EEAERRERIEEERQKKLKE 341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
676-882 |
8.92e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 676 QLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIR 755
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 756 KShQEELDKLRQLLK--------------KARVSTDQAAAEQLSLVQAELQTQweakcEQLLASAKNEHLQQYQEVCTQR 821
Cdd:COG3883 97 RS-GGSVSYLDVLLGsesfsdfldrlsalSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 822 DASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAADPSEKVKKIMNQ 882
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
557-894 |
1.01e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 557 TMETSMIMSNIQRIIQE----NERLKQEILEK--SSRIKEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQAK 630
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHqkavSERQQQEKFEKmeQERLRQEKEEKAREVERRRK--------LEEAEKARQAEMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 631 VTEELAAATAQVSHLHLKMTAHQKKETElQVQLTESMKETDLLRgQLAQLQAELsevQETSQQVQSKLKSEKQSRRQLEL 710
Cdd:pfam17380 336 YAEQERMAMERERELERIRQEERKRELE-RIRQEEIAMEISRMR-ELERLQMER---QQKNERVRQELEAARKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 711 RVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQ--------LLKKARVSTDQAAAE 782
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQqeeerkrkKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 783 QLS--LVQAELQTQWEAKCEQllaSAKNEHLQQYQEVCTQRDASQQQLLQLEEKcsalqaqvtSLREQNAQHIKDLESKA 860
Cdd:pfam17380 491 EQRrkILEKELEERKQAMIEE---ERKRKLLEKEMEERQKAIYEEERRREAEEE---------RRKQQEMEERRRIQEQM 558
|
330 340 350
....*....|....*....|....*....|....
gi 1387290470 861 QTSGVEATAADPSEKVKKIMNQVFQFLRGEFELE 894
Cdd:pfam17380 559 RKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
679-851 |
1.22e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 47.46 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 679 QLQAELSEVQETSQQVQSKLKSEKQS-RRQLELRvtslEEELTDLRTEKESLEkNLSERKKKSAQERCQAEEEIDEIRKS 757
Cdd:pfam14988 26 QYVQECEEIERRRQELASRYTQQTAElQTQLLQK----EKEQASLKKELQALR-PFAKLKESQEREIQDLEEEKEKVRAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 758 HQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLAS-AKNEHLQQYQEVCTQRDASQQQLLQLEEKCS 836
Cdd:pfam14988 101 TAEKDREAHLQFLKEKALLEKQLQELRILELGERATRELKRKAQALKLaAKQALSEFCRSIKRENRQLQKELLQLIQETQ 180
|
170
....*....|....*
gi 1387290470 837 ALQAQVTSLREQNAQ 851
Cdd:pfam14988 181 ALEAIKSKLENRKQR 195
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
579-753 |
1.37e-05 |
|
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: 48.00 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 579 QEILEKSSRIKEQNDKISELIERnqryveqsnlmMEKRNNSLQTATENTQakvtEELAAATAQVSHLHLKMTAHQKKETE 658
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-----------LEDELAALEARLEAAK----TELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 659 LQVQLTE--SMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSER 736
Cdd:COG1579 78 YEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*..
gi 1387290470 737 KKKSAQERCQAEEEIDE 753
Cdd:COG1579 158 LEELEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-891 |
1.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 564 MSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL---IERNQRYVE------------------QSNLMMEKRNNSLQT 622
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELekrLEELEERHElyeeakakkeelerlkkrLTGLTPEKLEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 623 AtENTQAKVTEELAAATAQVSHL------------HLK------------MTAHQKKE--TELQVQLTESMKETDLLRGQ 676
Cdd:PRK03918 396 L-EKAKEEIEEEISKITARIGELkkeikelkkaieELKkakgkcpvcgreLTEEHRKEllEEYTAELKRIEKELKEIEEK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 677 LAQLQAELSEVQ-------------ETSQQV-----------------------------------QSKLKSEKQSRRQL 708
Cdd:PRK03918 475 ERKLRKELRELEkvlkkeseliklkELAEQLkeleeklkkynleelekkaeeyeklkekliklkgeIKSLKKELEKLEEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 709 ELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQErcqAEEEIDEIRKSHQE---------ELDKLRQLLKKARVSTDQA 779
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKA 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 780 AAEqLSLVQAELQtQWEAKCEQLLASAKNEhlqQYQEVctqrdasQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLES- 858
Cdd:PRK03918 632 FEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKTLEKl 699
|
410 420 430
....*....|....*....|....*....|...
gi 1387290470 859 KAQTSGVEaTAADPSEKVKKIMNQVfQFLRGEF 891
Cdd:PRK03918 700 KEELEERE-KAKKELEKLEKALERV-EELREKV 730
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
398-491 |
1.72e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 49.31 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 398 GAGQPLATPSVQPSLQPAHPVLPQMTSQ------APQPSVSRLQTPSAALMQVASLDSHSAVSGN-AQSFQPYAGVQAYA 470
Cdd:PRK10263 739 GPHEPLFTPIVEPVQQPQQPVAPQQQYQqpqqpvAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQYQ 818
|
90 100
....*....|....*....|...
gi 1387290470 471 YPQAPAVASQ--LQPVRPLYPAP 491
Cdd:PRK10263 819 QPQQPVAPQPqyQQPQQPVAPQP 841
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
566-872 |
2.64e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.64 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISE---LIERNQRYVEqsnlmMEKRNNSLQTATENTQAKVTEELAAATAQV 642
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvktICEQEARIKD-----LEAQRAQLQAGQPCPLCGSTSHPAVEAYQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 643 shlhLKMTAHQKKETELQVQLTESMKETDLLRGQL----AQLQAELSEVQETSQQVQSkLKSEKQSRRQlELRVT-SLEE 717
Cdd:PRK10246 523 ----LEPGVNQSRLDALEKEVKKLGEEGAALRGQLdaltKQLQRDESEAQSLRQEEQA-LTQQWQAVCA-SLNITlQPQD 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 718 ELTDLRTEKESLEKNL---SERKKKSAQERCQAEEEIdeirkSHQEELDKLRQLLkkarvsTDQAAAEQLSLVQAELQTQ 794
Cdd:PRK10246 597 DIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQQII-----QYQQQIEQRQQQL------LTALAGYALTLPQEDEEAS 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 795 WeakceqllASAKNEHLQQYQEVCTQRDASQQQLLQLE----------------------------EKCSALQAQVTSLR 846
Cdd:PRK10246 666 W--------LATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetvaldnwrqvhEQCLSLHSQLQTLQ 737
|
330 340
....*....|....*....|....*.
gi 1387290470 847 EQNAQHIKDLeSKAQTSGVEATAADP 872
Cdd:PRK10246 738 QQDVLEAQRL-QKAQAQFDTALQASV 762
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
511-800 |
3.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQK---------------------HSAGNSLlipsMSVTMETSMIMSNIQR 569
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrelteEHRKELL----EEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 570 IIQENERLKQE------ILEKSSRIKeQNDKISELIERNQRYVEQSNLmmEKrnnsLQTATENTQaKVTEELAAATAQVS 643
Cdd:PRK03918 471 IEEKERKLRKElrelekVLKKESELI-KLKELAEQLKELEEKLKKYNL--EE----LEKKAEEYE-KLKEKLIKLKGEIK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 644 HLHLKMtahqKKETELQVQLTESMKETDLLRGQLAQLQAELSE-----VQETSQQVQ----------------SKLKSEK 702
Cdd:PRK03918 543 SLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKelepfyneylelkdaeKELEREE 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 703 QSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSaqercqAEEEIDEIRKSHQE---ELDKLRQLLKKARVSTDQA 779
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------SEEEYEELREEYLElsrELAGLRAELEELEKRREEI 692
|
330 340
....*....|....*....|.
gi 1387290470 780 AAEqLSLVQAELQTQWEAKCE 800
Cdd:PRK03918 693 KKT-LEKLKEELEEREKAKKE 712
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
598-870 |
3.35e-05 |
|
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: 48.21 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 598 LIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTAHQKketelqvQLTESMKETDLLRGQL 677
Cdd:pfam07111 134 LEEGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAK-------QLAEAQKEAELLRKQL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 678 AQLQAELSE----VQETSQQVQSKLKSEKQSrRQLELRVTSLEEELTDLRTEKESLEKNLserkkKSAQERCQAeeeIDE 753
Cdd:pfam07111 207 SKTQEELEAqvtlVESLRKYVGEQVPPEVHS-QTWELERQELLDTMQHLQEDRADLQATV-----ELLQVRVQS---LTH 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 754 IRKSHQEELDKLRQLLKKarvstdqaaaeqlslvqaeLQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEE 833
Cdd:pfam07111 278 MLALQEEELTRKIQPSDS-------------------LEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRG 338
|
250 260 270
....*....|....*....|....*....|....*..
gi 1387290470 834 KCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 870
Cdd:pfam07111 339 QVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSA 375
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
696-862 |
3.67e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 696 SKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKsHQEELDKLRQLLKKARVS 775
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 776 TDQaAAEQLSLVQAElqtqweakceqlLASAKNEHlQQYQEVCTQRDASQQQLLQLEEKcsaLQAQVTSLREQNA--QHI 853
Cdd:COG1340 80 RDE-LNEKLNELREE------------LDELRKEL-AELNKAGGSIDKLRKEIERLEWR---QQTEVLSPEEEKElvEKI 142
|
....*....
gi 1387290470 854 KDLESKAQT 862
Cdd:COG1340 143 KELEKELEK 151
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
561-855 |
3.80e-05 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 46.90 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 561 SMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKrnnslqtatenTQAKVTEELAAATA 640
Cdd:pfam14915 2 CMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTK-----------TVFQYNGQLNVLKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 641 QVSHLHLKMtAHQKK-----ETELQ---VQLTESMKETDllRGQLAQLQAELS--EVQETSQQVQSKLKSEKQSRR---- 706
Cdd:pfam14915 71 ENTMLNSKL-ENEKQnkerlETEVEsyrSRLAAAIQDHE--QSQTSKRDLELAfqRERDEWLRLQDKMNFDVSNLRdene 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 707 ----QL---ELRVTSLEEELTDLR---TEK----ESLEKNLSerkkksaqercQAEEEIDEIRKSHQEELDKLRQLLKKa 772
Cdd:pfam14915 148 ilsqQLskaESKANSLENELHRTRdalREKtlllESVQRDLS-----------QAQCQKKELEHMYQNEQDKVNKYIGK- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 773 rvstDQAAAEQLSLVQAE---LQTQWEAKCEQLLASAK---NEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLR 846
Cdd:pfam14915 216 ----QESLEERLAQLQSEnmlLRQQLEDAQNKADAKEKtviDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLK 291
|
....*....
gi 1387290470 847 EQNAQHIKD 855
Cdd:pfam14915 292 ERLYQYEKE 300
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
621-870 |
4.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 621 QTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS 700
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 701 EKQSRRQLELRVTSleEELTDLRTEKESLEKnLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKkarvstdqaa 780
Cdd:COG3883 98 SGGSVSYLDVLLGS--ESFSDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKA---------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 781 aeQLSLVQAELQTQWEAKcEQLLASAKNehlqqyqevctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKA 860
Cdd:COG3883 165 --ELEAAKAELEAQQAEQ-EALLAQLSA-----------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|
gi 1387290470 861 QTSGVEATAA 870
Cdd:COG3883 231 AAAAAAAAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
568-861 |
4.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 568 QRIIQENERLKQEILEKSSRIKEqndkiselIERNQryveqsNLMMEKRNNSlqtateNTQAKVTEelaaatAQVSHLHL 647
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKN--------LDKNL------NKDEEKINNS------NNKIKILE------QQIKDLND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 648 KMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKE 727
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 728 SLEKNLSERKKksaqERCQAEEEIDEIR-----------------KSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQae 790
Cdd:TIGR04523 170 ELENELNLLEK----EKLNIQKNIDKIKnkllklelllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINE-- 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 791 LQTQWEAKCEQLLaSAKNEHlqqyQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQnaqhIKDLESKAQ 861
Cdd:TIGR04523 244 KTTEISNTQTQLN-QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE----ISDLNNQKE 305
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-879 |
4.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEI--LEKSSRIKEQNDKISEliERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMT 650
Cdd:PTZ00121 1221 EDAKKAEAVkkAEEAKKDAEEAKKAEE--ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKETDLLR-GQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKEsl 729
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-- 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 eKNLSERKKKSAQERCQAEE----------EIDEIRKSHQ-----EELDKLRQLLKKARvSTDQAAAEQLSLVQAELQTQ 794
Cdd:PTZ00121 1377 -KKKADAAKKKAEEKKKADEakkkaeedkkKADELKKAAAakkkaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAE 1454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 795 WEAKCEQLLASA----KNEHLQQYQEvcTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSgvEATAA 870
Cdd:PTZ00121 1455 EAKKAEEAKKKAeeakKADEAKKKAE--EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD--EAKKA 1530
|
....*....
gi 1387290470 871 DPSEKVKKI 879
Cdd:PTZ00121 1531 EEAKKADEA 1539
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
635-856 |
4.11e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 635 LAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQL-------------AQLQAELS------EVQETSQQVQ 695
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLeeleaaalqpgeeEELEEERRrlsnaeKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 696 SKLKSE--------KQSRRQLElRVTSLEEELTDLRTEKESLEKNLSErkkkSAQE--RCQAEEEIDEIRKSHQEE-LDK 764
Cdd:COG0497 233 EALSGGeggaldllGQALRALE-RLAEYDPSLAELAERLESALIELEE----AASElrRYLDSLEFDPERLEEVEErLAL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 765 LRQLLKKARVSTDQAAAeqlslvqaeLQTQWEAKCEQLLASAknEHLQQYQEvctQRDASQQQLLQLEEKCSAL-QAQVT 843
Cdd:COG0497 308 LRRLARKYGVTVEELLA---------YAEELRAELAELENSD--ERLEELEA---ELAEAEAELLEAAEKLSAArKKAAK 373
|
250
....*....|...
gi 1387290470 844 SLREQNAQHIKDL 856
Cdd:COG0497 374 KLEKAVTAELADL 386
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
580-744 |
6.63e-05 |
|
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: 47.36 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 580 EILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN-----TQAKVTEELAAataqvsHLHLKMTAHQK 654
Cdd:pfam05911 664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlestkSQLQESEQLIA------ELRSELASLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 655 KETELQVQLtESMKET-DLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTdlRTEKESLEKNL 733
Cdd:pfam05911 738 SNSLAETQL-KCMAESyEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNEKKESSNCD 814
|
170
....*....|..
gi 1387290470 734 -SERKKKSAQER 744
Cdd:pfam05911 815 aDQEDKKLQQEK 826
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
439-816 |
7.81e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 439 AALMQVASLDSHSAVSGNAQSFQPYAG-----VQAYAYPQAPAVASQLQPVRPLYPAPLSQPPHFQGSGDVASFLMT--- 510
Cdd:PLN02939 1 AAAAESAALLSHGCGPIRSRAPFYLPSrrrlaVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENtsl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 511 ------------EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMETSMIMSN---------IQR 569
Cdd:PLN02939 81 rtvmelpqkstsSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNqarlqaledLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 570 IIQENERLKQEILEKSSRIKEQNDKIsELIERNQRYVEQSNLMMEKRNNSLqtatentqakvTEELAAATAQVSHLHLkm 649
Cdd:PLN02939 161 ILTEKEALQGKINILEMRLSETDARI-KLAAQEKIHVEILEEQLEKLRNEL-----------LIRGATEGLCVHSLSK-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 650 tahqkketELQVQLTESMketdLLRGQLAQLQAELSEVQETSQQVqSKLKSE----KQSRRQLELRVTSLEEELTDLRTE 725
Cdd:PLN02939 227 --------ELDVLKEENM----LLKDDIQFLKAELIEVAETEERV-FKLEKErsllDASLRELESKFIVAQEDVSKLSPL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 726 K--------ESLEkNLSERKKKSAQERCQAEEEIDEIRKshqeELDKLRQLLKKARVStdQAAAEQLSLVQAELQTQWE- 796
Cdd:PLN02939 294 QydcwwekvENLQ-DLLDRATNQVEKAALVLDQNQDLRD----KVDKLEASLKEANVS--KFSSYKVELLQQKLKLLEEr 366
|
410 420
....*....|....*....|.
gi 1387290470 797 -AKCEQLLASakneHLQQYQE 816
Cdd:PLN02939 367 lQASDHEIHS----YIQLYQE 383
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
619-863 |
8.21e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 619 SLQTATEnTQAKVTEELAAATAQVSHLHLKMT----AHQKKETELQvQLTESMKETdllrgQLAQLQAELSEVQETSQQV 694
Cdd:pfam12128 612 ALQSARE-KQAAAEEQLVQANGELEKASREETfartALKNARLDLR-RLFDEKQSE-----KDKKNKALAERKDSANERL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 695 QSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSErkKKSAQErCQAEEEIDEIRKSHQEELDKLRQLLKK--A 772
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG--ALDAQL-ALLKAAIAARRSGAKAELKALETWYKRdlA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 773 RVSTDQAAAEQLSLVQAELQTQWEaKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQH 852
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIE-RIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
250
....*....|.
gi 1387290470 853 IKDLESKAQTS 863
Cdd:pfam12128 841 RAKLEMERKAS 851
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
655-832 |
8.48e-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: 46.96 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 655 KETELQVQLTESMKETDL-LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTS---LEEELTDLRTEKESLE 730
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimkLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 731 KNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEH 810
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEH 362
|
170 180
....*....|....*....|..
gi 1387290470 811 LQQYqEVCTQRDASQQQLLQLE 832
Cdd:TIGR00606 363 IRAR-DSLIQSLATRLELDGFE 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
555-771 |
8.80e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 555 SVTMETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELiernqryveqsnlmmEKRNNSLQtaTENTQAKVTEE 634
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL---------------EDELNKDD--FELKKENLEKE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 635 LAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAqlqaelsevqetsqqvqsklksekqsrrQLELRVTS 714
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE----------------------------EKEKKISS 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 715 LEEELTDLRTEKESLE---KNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKK 771
Cdd:TIGR04523 615 LEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
564-796 |
9.79e-05 |
|
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: 46.71 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 564 MSNIQRIIQENERL-KQEILEKSSRIKEQNDKISELIE---RNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEelaaat 639
Cdd:pfam01576 329 VTELKKALEEETRShEAQLQEMRQKHTQALEELTEQLEqakRNKANLEKAKQALESENAELQAELRTLQQAKQD------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 640 aqvshlhlkmTAHQKKETELQVQ-----LTESMKETDLLRGQLAQLQAEL---------------------SEVQETSQQ 693
Cdd:pfam01576 403 ----------SEHKRKKLEGQLQelqarLSESERQRAELAEKLSKLQSELesvssllneaegkniklskdvSSLESQLQD 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 694 VQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKE--------------SLEKNLSERKKKsAQERCQAEEEIDEIRKSHQ 759
Cdd:pfam01576 473 TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEeeeeakrnverqlsTLQAQLSDMKKK-LEEDAGTLEALEEGKKRLQ 551
|
250 260 270
....*....|....*....|....*....|....*..
gi 1387290470 760 EELDKLRQLLKKarvstDQAAAEQLSLVQAELQTQWE 796
Cdd:pfam01576 552 RELEALTQQLEE-----KAAAYDKLEKTKNRLQQELD 583
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
654-879 |
1.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQLTESMKETDLLRGQLAQ------LQAELSEVqETSQQVQSKLKSEKQsRRQLELRVTSLEEELTDLRTEKE 727
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREY-EGYELLKEKEALERQ-KEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 728 SLEKNLSERKKKSAQERCQ----AEEEIDEIRKSHQEELDKLRQLLKKARVSTDQA--AAEQLSLVQAEL---------- 791
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELedAEERLAKLEAEIdkllaeieel 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 792 ---QTQWEAKCEQL---LASAKNEH---LQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLR--------------EQ 848
Cdd:TIGR02169 342 ereIEEERKRRDKLteeYAELKEELedlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelqrlsEE 421
|
250 260 270
....*....|....*....|....*....|..
gi 1387290470 849 NAQHIKDLES-KAQTSGVEATAADPSEKVKKI 879
Cdd:TIGR02169 422 LADLNAAIAGiEAKINELEEEKEDKALEIKKQ 453
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
575-841 |
1.03e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 575 ERLKQEILEKSSRIKEQNDKISELIERN---QRYVE---QSNLMMEKRNNSLQTatentqakvteelaaataQVSHLHLK 648
Cdd:pfam10174 292 DQLKQELSKKESELLALQTKLETLTNQNsdcKQHIEvlkESLTAKEQRAAILQT------------------EVDALRLR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 649 MTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELsEVQETSQQV--------QSKLKSEKQSRRQLELRVTSLEEELT 720
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML-DVKERKINVlqkkienlQEQLRDKDKQLAGLKERVKSLQTDSS 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 721 DLRTEKESLEKNLSErkKKSAQERCQaeEEIDEIRKSHQEELDKLRQLLKKARvstdqaaaEQLSLVQAELQTQweakcE 800
Cdd:pfam10174 433 NTDTALTTLEEALSE--KERIIERLK--EQREREDRERLEELESLKKENKDLK--------EKVSALQPELTEK-----E 495
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1387290470 801 QLLASAKnEHLQQYQEVCTQRDASQQQL----LQLEEKCSALQAQ 841
Cdd:pfam10174 496 SSLIDLK-EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQ 539
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
676-766 |
1.05e-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: 44.15 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 676 QLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERkkksaqercqaEEEIDEIR 755
Cdd:pfam08614 58 LLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDR-----------EEELREKR 126
|
90
....*....|....
gi 1387290470 756 KSH---QEELDKLR 766
Cdd:pfam08614 127 KLNqdlQDELVALQ 140
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
568-861 |
1.09e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 568 QRIIQENERLKQEILEkssRIKEQNDKISELI---ERNQRYVEQSNLMMEKRNNSLQT---ATENTQAKVTEELAAATAQ 641
Cdd:pfam06160 85 KKALDEIEELLDDIEE---DIKQILEELDELLeseEKNREEVEELKDKYRELRKTLLAnrfSYGPAIDELEKQLAEIEEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLHLKMTAHQKKETELQVQLTEsmKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS--EKQSRRQLELRVTSLEEEL 719
Cdd:pfam06160 162 FSQFEELTESGDYLEAREVLEKLE--EETDALEELMEDIPPLYEELKTELPDQLEELKEgyREMEEEGYALEHLNVDKEI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 720 TDLRTEKESLEKNLSERKKKSAQERCQA-EEEIDEI----------RKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQ 788
Cdd:pfam06160 240 QQLEEQLEENLALLENLELDEAEEALEEiEERIDQLydllekevdaKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 789 A-ELQTQWEAKCEQLlasakNEHLQ----QYQEVCTQRDASQQ-------QLLQLEEKCSALQAQVTSLREQNAQHIKDl 856
Cdd:pfam06160 320 SyTLNENELERVRGL-----EKQLEelekRYDEIVERLEEKEVayselqeELEEILEQLEEIEEEQEEFKESLQSLRKD- 393
|
....*
gi 1387290470 857 ESKAQ 861
Cdd:pfam06160 394 ELEAR 398
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
627-772 |
1.25e-04 |
|
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: 44.28 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 627 TQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQsrr 706
Cdd:pfam05010 2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 707 QLELRVTSLEEELTDL----RTEKESLE--KNLSERKKKSAQERC----------------------QAEEEIDEIRKSH 758
Cdd:pfam05010 79 QALADLNSVEKSFSDLfkryEKQKEVISgyKKNEESLKKCAQDYLarikkeeqryqalkahaeekldQANEEIAQVRSKA 158
|
170
....*....|....
gi 1387290470 759 QEELDKLRQLLKKA 772
Cdd:pfam05010 159 KAETAALQASLRKE 172
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
620-833 |
1.25e-04 |
|
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: 46.17 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 620 LQTATEnTQAKVTEELAA-ATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKL 698
Cdd:pfam05701 252 LETASA-LLLDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSEL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 699 KSEKQ---SRRQLE----LRVTSLEEELTDLRTEKESL---EKNLSERKKKSAQERCQAEEEIDEIRKSHQeeldKLRQL 768
Cdd:pfam05701 331 EKEKAelaSLRQREgmasIAVSSLEAELNRTKSEIALVqakEKEAREKMVELPKQLQQAAQEAEEAKSLAQ----AAREE 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 769 LKKARVSTDQAAAEqLSLVQAELQ-TQWE---AKCEQLLASAKNEHLQQYQ---EVCTQRDASQQQLLQLEE 833
Cdd:pfam05701 407 LRKAKEEAEQAKAA-ASTVESRLEaVLKEieaAKASEKLALAAIKALQESEssaESTNQEDSPRGVTLSLEE 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
661-840 |
1.37e-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: 46.48 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 661 VQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQS--KLKSE--KQSRRQLELRvTSLEEELTDLRTEKESLEKNLSEr 736
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNaeRLLEEfcQRIGQQLDAA-EELEELLAELEAQLEELEEQAAE- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 737 kkkSAQERCQAEEEIDEIRKshqeeldKLRQLLKKARV-STDQAAAEQLSLvqaelQTQWEAKCEQLLASAKNEHLQQYQ 815
Cdd:COG3096 576 ---AVEQRSELRQQLEQLRA-------RIKELAARAPAwLAAQDALERLRE-----QSGEALADSQEVTAAMQQLLERER 640
|
170 180
....*....|....*....|....*
gi 1387290470 816 EVCTQRDASQQQLLQLEEKCSALQA 840
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQ 665
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
647-858 |
1.41e-04 |
|
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: 46.26 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 647 LKMTAHQKKEteLQVQLTES----MKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDL 722
Cdd:pfam15921 80 LEEYSHQVKD--LQRRLNESnelhEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 723 RTEKESLEKNlserkkksaqercqAEEEIDEIRK---SHQEELDKLRQLLKKARVSTDQAAAEQ--------------LS 785
Cdd:pfam15921 158 KCLKEDMLED--------------SNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASGKKIYEHdsmstmhfrslgsaIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 786 LVQAELQTQW----------EAKCEQLLASAKNEH---LQQYQEVCTQRDASQQ-QLLQLEEKCSALQAQVTSL------ 845
Cdd:pfam15921 224 KILRELDTEIsylkgrifpvEDQLEALKSESQNKIellLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIqsqlei 303
|
250 260
....*....|....*....|.
gi 1387290470 846 -----REQNA---QHIKDLES 858
Cdd:pfam15921 304 iqeqaRNQNSmymRQLSDLES 324
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
705-891 |
1.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 705 RRQLELRVTSLEEE----LTDLRTEKESLEKN-LSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQllKKARVSTDQA 779
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEaLLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQ--KEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 780 AAEQLslvQAELQTQWEA---------KCEQLLASAKNEHLQQYQEVC--TQRDASQQQLLQLEEKcsalqaqvtsLREQ 848
Cdd:PRK12704 104 LLEKR---EEELEKKEKEleqkqqeleKKEEELEELIEEQLQELERISglTAEEAKEILLEKVEEE----------ARHE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387290470 849 NAQHIKDLESKAqtsgvEATAadpSEKVKKIMNQVFQFLRGEF 891
Cdd:PRK12704 171 AAVLIKEIEEEA-----KEEA---DKKAKEILAQAIQRCAADH 205
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
656-848 |
1.56e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 656 ETELqVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKqsrRQLELRVTSLEEELTDLRTEKESleknLSE 735
Cdd:pfam01576 839 EAEL-LQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEK---RRLEARIAQLEEELEEEQSNTEL----LND 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 736 RKKKSAQE---------------------RCQAEEEIDEIRKSHQEELDKLRQLLKKArvstdqAAAEQLSLVQAELQTQ 794
Cdd:pfam01576 911 RLRKSTLQveqlttelaaerstsqksesaRQQLERQNKELKAKLQEMEGTVKSKFKSS------IAALEAKIAQLEEQLE 984
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 795 WEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ 848
Cdd:pfam01576 985 QESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQ 1038
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
730-848 |
1.79e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNLSERKKKSAQERcqaEEEIDEIRKSHQEELDKLRQLLKKARVSTDQ------AAAEQLSLVQAELQtQWEAKCEQLL 803
Cdd:pfam07926 2 ELSSLQSEIKRLKEE---AADAEAQLQKLQEDLEKQAEIAREAQQNYERelvlhaEDIKALQALREELN-ELKAEIAELK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1387290470 804 A---SAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ 848
Cdd:pfam07926 78 AeaeSAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
694-895 |
1.80e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 45.63 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 694 VQSKLKSEKQSRrqlELRVTSLEEELTDLRTEKE---SLEKNLSERKKKSAQERC--QAEEEIDEIRKSHQEELDKLRQL 768
Cdd:PRK00106 22 ISIKMKSAKEAA---ELTLLNAEQEAVNLRGKAErdaEHIKKTAKRESKALKKELllEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 769 LKkarvstdqaaaeQLSLVQAELQTQWEAKCEQLlaSAKNEHLQQYQEVCTQR----DASQQQLLQLEEKCSALQAQVTS 844
Cdd:PRK00106 99 LK------------QIESRLTERATSLDRKDENL--SSKEKTLESKEQSLTDKskhiDEREEQVEKLEEQKKAELERVAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 845 LREQNAQHI------KDL--ESKAQTSGVEATAADPSEKV-KKIMNQVFQFLRGEFELEE 895
Cdd:PRK00106 165 LSQAEAREIilaeteNKLthEIATRIREAEREVKDRSDKMaKDLLAQAMQRLAGEYVTEQ 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
663-896 |
2.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 663 LTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEK------NLSER 736
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 737 KKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTdqaaaeqlslvqaELqtQWEAKceqllasaknehlqQYQE 816
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-------------EL--KEKAE--------------EYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 817 VCTQRDASQQQLLQLEEKCSALQAQVTSLREQnaqhIKDLESKaqtsgveataadpSEKVKKIMNQVFQFLRGEFELEEF 896
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEK-------------EERLEELKKKLKELEKRLEELEER 360
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
626-769 |
2.41e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 626 NTQAKVTEELAAATAQVSHLhLKMTAHQKKETELQV-----QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS 700
Cdd:PRK09039 49 SGKDSALDRLNSQIAELADL-LSLERQGNQDLQDSVanlraSLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 701 EKQ----SRRQLELrvtsLEEELTDLRTEKESLEKNL--SERKKKSAQERCQA---------EEEIDEIRKSHQEELDKL 765
Cdd:PRK09039 128 EKQvsarALAQVEL----LNQQIAALRRQLAALEAALdaSEKRDRESQAKIADlgrrlnvalAQRVQELNRYRSEFFGRL 203
|
....
gi 1387290470 766 RQLL 769
Cdd:PRK09039 204 REIL 207
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
567-875 |
2.63e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 567 IQRIIQENERLKQEILEKSSRIKEQNDKISELIernqryveqsnlmmekrnNSLQTATENTQAKVTEELAAATAQVSHLH 646
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKV------------------SALQPELTEKESSLIDLKEHASSLASSGL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 647 LKMTAHQKKETELQVQLTESMK-ETDLLRGQLAQLQAELSE-----VQETSQQVQSKlkSEKQSRRQLElrVTSLEEELT 720
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKlENQLKKAHNAEEAVRTNPeindrIRLLEQEVARY--KEESGKAQAE--VERLLGILR 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 721 DLRTEKESLEKNLSE-RKKKSAQERCQAeEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEaKC 799
Cdd:pfam10174 590 EVENEKNDKDKKIAElESLTLRQMKEQN-KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALE-KT 667
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290470 800 EQLLASAKnehlqqyqevctQRDASQQQllQLEEKcsalQAQVTSLREQNAQHIKD-LESKAqtsgvEATAADPSEK 875
Cdd:pfam10174 668 RQELDATK------------ARLSSTQQ--SLAEK----DGHLTNLRAERRKQLEEiLEMKQ-----EALLAAISEK 721
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
652-895 |
2.70e-04 |
|
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: 45.35 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 652 HQKKETELQ--VQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESL 729
Cdd:pfam02463 197 LQELKLKEQakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNL-----SERKKKSAQERCQAEEEIDEIRKS---------HQEELDKLRQLLKKARVSTDQAAAEqLSLVQAELQTQW 795
Cdd:pfam02463 277 EEKEkklqeEELKLLAKEEEELKSELLKLERRKvddeeklkeSEKEKKKAEKELKKEKEEIEELEKE-LKELEIKREAEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 796 EAKCEQLLASAKNEHLQQyqevctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAADPSEK 875
Cdd:pfam02463 356 EEEEELEKLQEKLEQLEE------ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL 429
|
250 260
....*....|....*....|.
gi 1387290470 876 VKKIMNQVFQ-FLRGEFELEE 895
Cdd:pfam02463 430 EILEEEEESIeLKQGKLTEEK 450
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
514-856 |
3.20e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 514 QHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMEtsMIMSNIQRIIQE-------NERLKQEILEKSS 586
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP--GRQSIIDLKEKEipelrnkLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 587 RIKEQN-----------------------DKISELIERNQRYVEQ--SNLMMEKRNNSLQTATENTQAKvTEELAAATAQ 641
Cdd:TIGR00606 766 DIEEQEtllgtimpeeesakvcltdvtimERFQMELKDVERKIAQqaAKLQGSDLDRTVQQVNQEKQEK-QHELDTVVSK 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQlelrVTSLEEELTD 721
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLEK 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 722 LRTEKESLEKNLSERKKKsaqercqAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQ---LSLVQAELQtqweaK 798
Cdd:TIGR00606 921 DQQEKEELISSKETSNKK-------AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKeteLNTVNAQLE-----E 988
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 799 CEQLLASAKNEHLQQYQEVCTQRdaSQQQLLQLEEKCSALQAQVTSLREQNAQHIKDL 856
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRKRENELKEVEEELKQHLKEM 1044
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
629-790 |
3.50e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.47 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 629 AKVTEELAAATAQVSHLHLKMTAhqkkETELQVQLTESMKETDLLRGQLAqLQAElSEVQETSQQVQSKLKSEKQSRRQL 708
Cdd:PRK00106 29 AKEAAELTLLNAEQEAVNLRGKA----ERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKSERQELKQI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 709 ELRVT----SL---EEELTDLRTEKESLEKNLSErKKKSAQERcqaEEEIDEIRKSHQEELDKLRQLlkkarvstDQAAA 781
Cdd:PRK00106 103 ESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL--------SQAEA 170
|
....*....
gi 1387290470 782 EQLSLVQAE 790
Cdd:PRK00106 171 REIILAETE 179
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
622-864 |
3.56e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 622 TATENTQAKVTEELAAATAQVshlhlkmTAHQKKETE-LQVQLT--ESMKETdLLRGQlaQLQAELSEVQETSQQVQSKL 698
Cdd:PRK10929 19 AATAPDEKQITQELEQAKAAK-------TPAQAEIVEaLQSALNwlEERKGS-LERAK--QYQQVIDNFPKLSAELRQQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 699 KSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNlserkKKSAQERCQAEEEIDEIRKSHQEELDKLRQL------LKKA 772
Cdd:PRK10929 89 NNERDEPRSVPPNMSTDALEQEILQVSSQLLEKS-----RQAQQEQDRAREISDSLSQLPQQQTEARRQLneierrLQTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 773 RVSTDQAAAEQLSLVQAELQTQwEAKCEQL-LA--SAKNEhlqqyQEVCTQR-DASQQQLLQLEEKCSALQAQVTSLREQ 848
Cdd:PRK10929 164 GTPNTPLAQAQLTALQAESAAL-KALVDELeLAqlSANNR-----QELARLRsELAKKRSQQLDAYLQALRNQLNSQRQR 237
|
250
....*....|....*..
gi 1387290470 849 NA-QHIKDLESKAQTSG 864
Cdd:PRK10929 238 EAeRALESTELLAEQSG 254
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
528-910 |
3.68e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 528 DKMDHLMTKVEELQKHSAGNSLLIPSMSVTMETSMIMS----NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNq 603
Cdd:PTZ00440 481 DSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNnnfkNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDE- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 604 ryvEQSNLMMEKRNNSLQTATENTQA-----KVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKE--TDLLRGQ 676
Cdd:PTZ00440 560 ---KLKRSMKNDIKNKIKYIEENVDHikdiiSLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYilNKFYKGD 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 677 LAQLQAELSEVQETsqqvQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEI----- 751
Cdd:PTZ00440 637 LQELLDELSHFLDD----HKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIikkql 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 752 DEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLvqAELQTQWEAKCEQLLASAKN--EHLQQYQEVCTQRDASQQQLL 829
Cdd:PTZ00440 713 NNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKL--EVYKHQIINRKNEFILHLYEndKDLPDGKNTYEEFLQYKDTIL 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 830 QLEEKCSalqAQVTSLREqNAQHIKDLESKAQT--SGVEATAADPSEKVKKIMN----QVFQFLRGEFElEEFYSGRTVL 903
Cdd:PTZ00440 791 NKENKIS---NDINILKE-NKKNNQDLLNSYNIliQKLEAHTEKNDEELKQLLQkfptEDENLNLKELE-KEFNENNQIV 865
|
....*..
gi 1387290470 904 GTIMNTI 910
Cdd:PTZ00440 866 DNIIKDI 872
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
563-728 |
3.72e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQ-ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEntQAKVTEELAAATAQ 641
Cdd:COG5022 940 IDLEEGPSIEyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAE--LSKQYGALQESTKQ 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLHLKMTAHQ------KKETELQVQLTESMKETDLLRGQLAQLQAELSEVQ--ETSQQVQSKLKSEKQSRRQLELRVT 713
Cdd:COG5022 1018 LKELPVEVAELQsaskiiSSESTELSILKPLQKLKGLLLLENNQLQARYKALKlrRENSLLDDKQLYQLESTENLLKTIN 1097
|
170
....*....|....*
gi 1387290470 714 SLEEELTDLRTEKES 728
Cdd:COG5022 1098 VKDLEVTNRNLVKPA 1112
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
568-732 |
3.75e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 568 QRIIQENERLKQEILEKSSRIKEQNDKISELI------ERNQRYVEQSNLMMEKRNnsLQTATENTQAKVTEELAAATAQ 641
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLEleelrqERDLLREEIQKLRGQIQQ--LRTELQELEAQQQEEAESSREQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLH----LKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQ---SRRQLELRVTS 714
Cdd:pfam09787 95 LQELEeqlaTERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQsssSQSELENRLHQ 174
|
170 180
....*....|....*....|
gi 1387290470 715 LEEELTDLRTEKESL--EKN 732
Cdd:pfam09787 175 LTETLIQKQTMLEALstEKN 194
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
571-841 |
4.98e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 571 IQENERLKQEILEKSSRIKEQndkiseliernqryveqsnlMMEKRNNSLQTATENTQAKVTEELAAATAqvshLHLKMT 650
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEM--------------------MEEERERALEEEEEKEEERKEERKRYRQE----LEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVqltESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSE-KQSRRQLELRVTSLEEEltdlrtEKESL 729
Cdd:pfam13868 84 EREQKRQEEYE---EKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEiDEFNEEQAEWKELEKEE------EREED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNLSERKKKSAQERcQAEEEIDEIRKSHQEELDKLRQLLKKARVstDQAAAEQL--SLVQAELQTQWEAKCEQLlasak 807
Cdd:pfam13868 155 ERILEYLKEKAEREE-EREAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELraKLYQEEQERKERQKEREE----- 226
|
250 260 270
....*....|....*....|....*....|....
gi 1387290470 808 nehLQQYQEVCTQRDASQQQLLQLEEKCSALQAQ 841
Cdd:pfam13868 227 ---AEKKARQRQELQQAREEQIELKERRLAEEAE 257
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
514-755 |
5.01e-04 |
|
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: 44.34 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 514 QHNTEIRMAVSKVADkmdhlmTKVEELQKHSAGNSLLIPSMSVTMETSMIM-------SNIQRIIQENERLKQEILEKSS 586
Cdd:pfam15921 615 KKDAKIRELEARVSD------LELEKVKLVNAGSERLRAVKDIKQERDQLLnevktsrNELNSLSEDYEVLKRNFRNKSE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 587 RIKEQNDKISELIERNQRYVEQSNlmmekrnNSLQTaTENTQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTES 666
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTR-------NTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNA 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 667 MKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQ 746
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
....*....
gi 1387290470 747 AEEEIDEIR 755
Cdd:pfam15921 841 HTLDVKELQ 849
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
686-834 |
5.24e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 686 EVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEltdLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKL 765
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEE---IRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 766 RQLL-KKARVSTDQAAAEQLSlvQAELQTQWEAKCEQLLASAKNEHLQQYQEvctQRDASQQQLLQLEEK 834
Cdd:pfam15709 433 QELQrKKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEERLEYQRQ---KQEAEEKARLEAEER 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
633-816 |
5.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLqAELSEVQETSQQVQSKLKSEKQSRRQLELRV 712
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 713 TSLEEELTDLrtEKESLEKNLSERKKKSAQercqAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 792
Cdd:COG4717 416 GELEELLEAL--DEEELEEELEELEEELEE----LEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|....
gi 1387290470 793 TQWEAKceQLLASAKNEHLQQYQE 816
Cdd:COG4717 490 EEWAAL--KLALELLEEAREEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-791 |
5.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILEKS-SRIKEQNDKISELIERNQRYVEQSNLMMEKRnnslqtATENTQAKVTEELAAATAQ 641
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELE------REEKELKKLEEELDKAFEE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLHLKMTAHQKKETELQVQLTEsmKETDLLRGQLAQLQAELSevqetsqqvqsKLKSEKQsrrQLELRVTSLEEELTD 721
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELA-----------GLRAELE---ELEKRREEIKKTLEK 698
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 722 LRTEKESLEKnlserkkksaqercqAEEEIDEIRKShQEELDKLRQLLKKARVSTDQAAAEQLSLVQAEL 791
Cdd:PRK03918 699 LKEELEEREK---------------AKKELEKLEKA-LERVEELREKVKKYKALLKERALSKVGEIASEI 752
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
710-843 |
6.07e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 710 LRVTSLEEELTDLRTEKESLEKnlserkkksaqERCQAEEEIDEirkSHQEELDKLRQLLKKARvstdqaaaEQLslvqA 789
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 790 ELQTQWEAKCEQL--LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVT 843
Cdd:COG0542 458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
653-774 |
6.28e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 653 QKKETELQVQLTESMKETDLLRGQ-LAQLQAELSEVQETSQQVQSKLKSEKQsrrqLELRVTSLEEELTDLRTEKESLEK 731
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 732 NLSERKKKSAQERCQAEEEIDE--------------IRKSHQEELDKLRQL---LKKaRV 774
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
716-870 |
6.45e-04 |
|
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: 42.35 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 716 EEELTDLRTEKEslEKNLSERKKKSAQERCQAEEEiDEIRKshqEELDKLRQLLKKARvstdqAAAEQLSLVqAELQTQW 795
Cdd:pfam15927 5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 796 E--AKCEQL--LASAK--NEHLQQYQEVcTQRDASQ-----QQLLQLEEKCSAL------QAQVTSLREQNAQHIKDLES 858
Cdd:pfam15927 73 EryMRCDGLpdPRDEQeiNTFISLWREE-EEEDIDEvmetcTLVLELIEELEELlldtppEELAEKYVEQYKEVILVLRE 151
|
170
....*....|..
gi 1387290470 859 KAQTSGVEATAA 870
Cdd:pfam15927 152 LINKKIDEATAH 163
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
600-862 |
6.49e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 600 ERNQRYVEQSNLMMEKRNnsLQTATENTQAKVTEELAAATAQvshlhlkmtahQKKETELQVQLTEsmketdlLRGQLAQ 679
Cdd:PRK10246 378 DREQLRQWQQQLTHAEQK--LNALPAITLTLTADEVAAALAQ-----------HAEQRPLRQRLVA-------LHGQIVP 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 680 LQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRT--EKESLEKNL-SERKKKSAQERC----------- 745
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTicEQEARIKDLeAQRAQLQAGQPCplcgstshpav 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 746 ---QAEEEIDEIRKSHQEE----------------LDKLRQLLKKarvstDQAAAEQLSLVQAELQTQWEAKCEQLlasa 806
Cdd:PRK10246 518 eayQALEPGVNQSRLDALEkevkklgeegaalrgqLDALTKQLQR-----DESEAQSLRQEEQALTQQWQAVCASL---- 588
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 807 kNEHLQQYQEV---CTQRDASQQQLLQLEEKcSALQAQVTSLREQNAQHIKDLESKAQT 862
Cdd:PRK10246 589 -NITLQPQDDIqpwLDAQEEHERQLRLLSQR-HELQGQIAAHNQQIIQYQQQIEQRQQQ 645
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
308-503 |
6.60e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 308 AAPSPIPPadsiSADPVVSPSTSVPFRSGESALRS--KSNSLSEHLTVNTNPDTVKAKLISRMAKMGQPMLPILPPQLDS 385
Cdd:PHA03247 2825 AGPLPPPT----SAQPTAPPPPPGPPPPSLPLGGSvaPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL 2900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 386 NDSEIEDVNAPRGAGQPLATPSVQPSLQPAHPVLPQMTSQAPQPSvsrlqtpsaalmqvaslDSHSAVSGNAQSFQPYAG 465
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP-----------------TTDPAGAGEPSGAVPQPW 2963
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387290470 466 VQAYAYPQAPAVASQLQPVRPLYPAPLSQPPHFQGSGD 503
Cdd:PHA03247 2964 LGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSL 3001
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
555-813 |
6.89e-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: 43.98 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 555 SVTMETSMIMSNIQRIIQENERLKQEI-LEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvte 633
Cdd:pfam09731 173 AEISREKATDSALQKAEALAEKLKEVInLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYK--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 634 ELAAATAQVSHLHLKmtahqKKETELQVQLTE-SMKETDLLRGQLAQLQAELSEVQEtsQQVQSKLKSEKQSRRQLElrv 712
Cdd:pfam09731 250 ELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELKKREEKHIERALE--- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 713 tSLEEELTDLRTE-KESLEKNLSERKKksaQERCQAEEEIDEIRKSHQEeldKLRQLLKKARVSTDQAAAEQLSLVQAEL 791
Cdd:pfam09731 320 -KQKEELDKLAEElSARLEEVRAADEA---QLRLEFEREREEIRESYEE---KLRTELERQAEAHEEHLKDVLVEQEIEL 392
|
250 260
....*....|....*....|..
gi 1387290470 792 QTQWEAKCEQLLASAKNEHLQQ 813
Cdd:pfam09731 393 QREFLQDIKEKVEEERAGRLLK 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
700-895 |
6.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 700 SEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAqercqaEEEIDEIRKSHQEELDKLRQLLKKARVSTDQA 779
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG------LVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 780 AAeQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDL--E 857
Cdd:COG3206 239 EA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlaS 317
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387290470 858 SKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEE 895
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
614-782 |
7.68e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 614 EKRNNSL-QTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKEtelqvQLTESMKETDLLRGQLAQLQAELSEVQETSQ 692
Cdd:COG3524 164 EELVNQLsERAREDAVRFAEEEVERAEERLRDAREALLAFRNRN-----GILDPEATAEALLQLIATLEGQLAELEAELA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 693 QVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEirkshqeeldklrQLLKKA 772
Cdd:COG3524 239 ALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLLAEYERLELEREFAE-------------KAYTSA 305
|
170
....*....|
gi 1387290470 773 RVSTDQAAAE 782
Cdd:COG3524 306 LAALEQARIE 315
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
692-860 |
8.40e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 692 QQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKShQEELDKLRQLLKK 771
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-RSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 772 ARVSTdQAAAEQLSLVQAELQT------QWEAKCEQL------LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQ 839
Cdd:COG4372 85 LNEQL-QAAQAELAQAQEELESlqeeaeELQEELEELqkerqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180
....*....|....*....|.
gi 1387290470 840 AQVTSLREQNAQHIKDLESKA 860
Cdd:COG4372 164 EELAALEQELQALSEAEAEQA 184
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
676-829 |
8.47e-04 |
|
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: 43.59 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 676 QLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTE---KESLEKNLSERKKKsaqercqaeeEID 752
Cdd:pfam07111 74 ELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNLEEGSQR----------ELE 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290470 753 EIRKSHQEELDKLRQLLKKArVSTDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLL 829
Cdd:pfam07111 144 EIQRLHQEQLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTL 219
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
660-845 |
8.70e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 660 QVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKL-----KSEKQSRrQLELRVTSLEEELTDL-------RTEKE 727
Cdd:pfam12128 589 RIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangELEKASR-EETFARTALKNARLDLrrlfdekQSEKD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 728 SLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEqlslVQAELQTQwEAKCEQLLASAK 807
Cdd:pfam12128 668 KKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV----VEGALDAQ-LALLKAAIAARR 742
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387290470 808 NEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL 845
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTL 780
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
511-847 |
9.50e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSA---GNSLlIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSSR 587
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlnGQSV-CPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 588 IKEQNDKISELIERN--------QRYVEQSNLMMEKRNNslqtatentqakvTEELAAATAQVSHLHLKMTAHQKKETEL 659
Cdd:PRK01156 492 VKDIDEKIVDLKKRKeyleseeiNKSINEYNKIESARAD-------------LEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 660 QVQLTESmKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSekqsrrqLELRVTSLEEELTDLRTEKESL------EKNL 733
Cdd:PRK01156 559 KLEDLDS-KRTSWLNALAVISLIDIETNRSRSNEIKKQLND-------LESRLQEIEIGFPDDKSYIDKSireienEANN 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 734 SERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQwEAKCEQLLASAKNEHLQQ 813
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-DAKANRARLESTIEILRT 709
|
330 340 350
....*....|....*....|....*....|....
gi 1387290470 814 YQEVCTQRDASQQQLLQLEEKCSALQAQVTSLRE 847
Cdd:PRK01156 710 RINELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
654-794 |
9.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQlTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSrrqLELRVTSLEEELTDLRTEKESLEKnl 733
Cdd:PRK12704 55 KKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL---LEKREEELEKKEKELEQKQQELEK-- 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 734 serkkksaqercqAEEEIDEIRKSHQEELDKLRQLlkkarvSTDQAAAEQLSLVQAELQTQ 794
Cdd:PRK12704 129 -------------KEEELEELIEEQLQELERISGL------TAEEAKEILLEKVEEEARHE 170
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
679-802 |
1.05e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.75 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 679 QLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSErkKKSAQERCQA-EEEIDEIRKS 757
Cdd:pfam12718 18 ELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTN--NENLTRKIQLlEEELEESDKR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1387290470 758 HQEELDKLRQllkkarvsTDQAAAEQLSLVQAELQT--QWEAKCEQL 802
Cdd:pfam12718 96 LKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
663-775 |
1.26e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 663 LTESMKETDLLRGQLAQLQAELSEVQE---TSQ-------QVQSKLKSEKQSRRQLelrVTSLEEELTDL---------- 722
Cdd:PRK04863 980 LAKNSDLNEKLRQRLEQAEQERTRAREqlrQAQaqlaqynQVLASLKSSYDAKRQM---LQELKQELQDLgvpadsgaee 1056
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 723 --RTEKESLEKNLSE-RKKKSAQERCQA--EEEIDEIRK---SHQEELDKLRQLLKKARVS 775
Cdd:PRK04863 1057 raRARRDELHARLSAnRSRRNQLEKQLTfcEAEMDNLTKklrKLERDYHEMREQVVNAKAG 1117
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
564-744 |
1.35e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 564 MSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMME---KRNNSLQTATENTQAKVTEELAAATA 640
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEelnQRWEELRELAEERRQRLEEALDLQQF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 641 QVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRvtSLEEELT 720
Cdd:cd00176 112 FRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADE--EIEEKLE 189
|
170 180
....*....|....*....|....
gi 1387290470 721 DLRTEKESLEKNLSERKKKSAQER 744
Cdd:cd00176 190 ELNERWEELLELAEERQKKLEEAL 213
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
566-852 |
1.41e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQ---RYVEQSNLMMEKRNNSLQTATEnTQAKVTEELAAATAQV 642
Cdd:pfam05557 42 QLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRlkkKYLEALNKKLNEKESQLADARE-VISCLKNELSELRRQI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 643 SHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQ--------------------SKLKS-- 700
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKelefeiqsqeqdseivknskSELARip 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 701 --EKQSRRQLE----LRVTS-----LEEELTDLRTEKESLEKnlserkkksaqerCQAEEEIDEIRKSH-QEELdklrql 768
Cdd:pfam05557 201 elEKELERLREhnkhLNENIenkllLKEEVEDLKRKLEREEK-------------YREEAATLELEKEKlEQEL------ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 769 lkKARVSTDQAAAeqLSLVQAELQTqweAKCEQLLASAKNeHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ 848
Cdd:pfam05557 262 --QSWVKLAQDTG--LNLRSPEDLS---RRIEQLQQREIV-LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKK 333
|
....
gi 1387290470 849 NAQH 852
Cdd:pfam05557 334 LKRH 337
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
653-774 |
1.51e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 653 QKKETELQVQLtESMKEtdllrgQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKN 732
Cdd:pfam20492 5 EREKQELEERL-KQYEE------ETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1387290470 733 lserKKKSAQERCQAEEEIDEI---RKSHQEELDKLRQLLKKARV 774
Cdd:pfam20492 78 ----KEQLEAELAEAQEEIARLeeeVERKEEEARRLQEELEEARE 118
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
665-771 |
1.51e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.38 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 665 ESMKETDL-LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEltdLRTEKESLEKNlserKKKSAQE 743
Cdd:pfam11559 55 ESLNETIRtLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQK---LKNEKEELQRL----KNALQQI 127
|
90 100
....*....|....*....|....*...
gi 1387290470 744 RCQAEEEIdeirKSHQEELDKLRQLLKK 771
Cdd:pfam11559 128 KTQFAHEV----KKRDREIEKLKERLAQ 151
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
671-773 |
1.53e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 671 DLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSR-RQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEE 749
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100
....*....|....*....|....*.
gi 1387290470 750 EIDEIRK--SHQEELDKLRQLLKKAR 773
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEER 485
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
663-855 |
1.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 663 LTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLE-------------EELTDLRTEKESL 729
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEliaerretieekrERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 730 EKNLSERKKKSAQERCQAEEEIDEIRK--SHQEELDKLRQLLkkARVSTDQAAAEQLslvqaelqtqwEAKCEQLlasak 807
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAElnSKLAELKERIESL--ERIRTLLAAIADA-----------EDEIERL----- 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387290470 808 NEHLQQYQEVCTQRdasQQQLLQLEEKCSALQAQVTSLREQNAQHIKD 855
Cdd:PRK02224 612 REKREALAELNDER---RERLAEKRERKRELEAEFDEARIEEAREDKE 656
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
303-496 |
1.58e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 303 SSRDSAAPSPIPPADSISADPVVSPSTsvpfrSGESALRSKSNSLSEHLTVNTNPDTVKAKLISRMAKMGQPMLPILPPQ 382
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSP-----AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 383 ldsndseiedvnAPRgagQPLATPSVQPSLQPAHPVLPQMTSQ-APQPSVSRLQTPSAALMQVASLDSHSAVSGnaqsfq 461
Cdd:PHA03247 2682 ------------RPR---RRAARPTVGSLTSLADPPPPPPTPEpAPHALVSATPLPPGPAAARQASPALPAAPA------ 2740
|
170 180 190
....*....|....*....|....*....|....*.
gi 1387290470 462 PYAGVQAYAYPQAPA-VASQLQPVRPLYPAPLSQPP 496
Cdd:PHA03247 2741 PPAVPAGPATPGGPArPARPPTTAGPPAPAPPAAPA 2776
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
612-861 |
1.59e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 612 MMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTAH----QKKETELQVQLTESMKETDLLRGQLAQLQAELSEV 687
Cdd:PRK11637 1 MRGKAINTMTRAVKPRRFAIRPILYASVLSAGVLLCAFSAHasdnRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 688 QETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSER--------KKKSAQ-----ERCQAEEEI--- 751
Cdd:PRK11637 81 EEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQldaafrqgEHTGLQlilsgEESQRGERIlay 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 752 -DEIRKSHQEELDKLRQllkkarvSTDQAAAEQLSLVQAELQTQweakceQLLASAKnehlQQYQEVCTQRDASQQQLLQ 830
Cdd:PRK11637 161 fGYLNQARQETIAELKQ-------TREELAAQKAELEEKQSQQK------TLLYEQQ----AQQQKLEQARNERKKTLTG 223
|
250 260 270
....*....|....*....|....*....|.
gi 1387290470 831 LEEKCSALQAQVTSLReQNAQHIKDLESKAQ 861
Cdd:PRK11637 224 LESSLQKDQQQLSELR-ANESRLRDSIARAE 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
573-790 |
1.59e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEKSSRIKEQNDKISELIERNQRY--------------VEQSNLMMEkrnnSLQTATENTQAKVTEELAAA 638
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQLALQKmqsekeqltywkemLAQCQTLLR----ELETHIEEYDREFNEIENAS 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 639 TAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQlaQLQAELSEVQeTSQQVQSKLKSEKQSRRQLELRVTSLEEE 718
Cdd:TIGR00618 728 SSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN--NNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 719 LTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKShQEELDKLRQLLKKARVSTDQAAAEQLSLVQAE 790
Cdd:TIGR00618 805 EAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT-LGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
697-856 |
1.67e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 697 KLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKK----KSAQERCQAEEEIDEIR----------KSHQEEL 762
Cdd:pfam12128 245 KLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAelnqLLRTLDDQWKEKRDELNgelsaadaavAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 763 DKLRQLLK---KARVSTDQAAAEQLSLVQAELQTQ-------------WEAKCEQLLASAKNEHLQQYQEVCTQRDASQQ 826
Cdd:pfam12128 325 EALEDQHGaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIRE 404
|
170 180 190
....*....|....*....|....*....|.
gi 1387290470 827 QL-LQLEEKCSALQAQVTSLREQNAQHIKDL 856
Cdd:pfam12128 405 ARdRQLAVAEDDLQALESELREQLEAGKLEF 435
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
514-735 |
1.69e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 514 QHNTEIRMAVSKVAdkMDHLMTKVEELQKHSAGNSLliPSMSVTMETSMIMSNIQRIIQENERLKQ---EILEKSSRI-K 589
Cdd:pfam06008 35 ENAHKIQIEILEKE--LSSLAQETEELQKKATQTLA--KAQQVNAESERTLGHAKELAEAIKNLIDnikEINEKVATLgE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 590 EQNDKISELIERNQryVEQSNLMMEKRNNSLQTATENtqakVTEELAAATAQVSHLhlkmtahQKKETELQVQlTESMKE 669
Cdd:pfam06008 111 NDFALPSSDLSRML--AEAQRMLGEIRSRDFGTQLQN----AEAELKAAQDLLSRI-------QTWFQSPQEE-NKALAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 670 TdlLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSE 735
Cdd:pfam06008 177 A--LRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
674-801 |
1.69e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 674 RGQLAQLQAELSEvqetsqqvQSKLKSEKQSRRQLELRVTSLEEEltdlRTEKESLEKNLSERKKKSAQERCQ-AEEEID 752
Cdd:pfam05672 19 KRRQAREQREREE--------QERLEKEEEERLRKEELRRRAEEE----RARREEEARRLEEERRREEEERQRkAEEEAE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1387290470 753 EIRKSHQEELDKLRQLLKKARVSTdQAAAEQLSLVQAELQTQWEAKCEQ 801
Cdd:pfam05672 87 EREQREQEEQERLQKQKEEAEAKA-REEAERQRQEREKIMQQEEQERLE 134
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
571-863 |
1.75e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 571 IQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAK------VTEELAAATAQVSh 644
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKkrfsllKKETIYLQSAQRV- 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 645 lhlkmtahQKKETELQvQLTESMKETDLLRGQLAQLQAELSEV---QETSQQVQSKLKSEKQSRRQLELRVTSLEEELTD 721
Cdd:COG5022 878 --------ELAERQLQ-ELKIDVKSISSLKLVNLELESEIIELkksLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSI 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 722 LRTEKESLEKNLSERK--KKSAQERC----QAEEEIDEIRKShQEELDKLRQLLK-----KARVSTDQAAAEQLSLVQAE 790
Cdd:COG5022 949 EYVKLPELNKLHEVESklKETSEEYEdllkKSTILVREGNKA-NSELKNFKKELAelskqYGALQESTKQLKELPVEVAE 1027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 791 LQT---------------QWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQleekCSALQAQVTSLREQNAqhiKD 855
Cdd:COG5022 1028 LQSaskiissestelsilKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ----LYQLESTENLLKTINV---KD 1100
|
....*...
gi 1387290470 856 LESKAQTS 863
Cdd:COG5022 1101 LEVTNRNL 1108
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
657-771 |
1.90e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 657 TELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQsKLKSEKQS-------RRQLELRVTSLE-----EELTDLRT 724
Cdd:smart00787 154 EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK-QLEDELEDcdpteldRAKEKLKKLLQEimikvKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387290470 725 EKESLEKNLSERKKKSA---QERCQAEEEIDEIRKSHQEELDKLRQLLKK 771
Cdd:smart00787 233 ELQELESKIEDLTNKKSelnTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
511-740 |
1.92e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAgnsllipsmsvtmETSMIMSNIQRIIQENERLKQEILEKSSRIKE 590
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELE-------------ELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 591 QNDKISELIERNQRYVEQSNLMMEKRnnslqtatentqakvteelaaaTAQVSHLHLKMTAHQKKETELQVQLTESMKET 670
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERL----------------------QQEIEELLKKLEEAELKELQAELEELEEELEE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 671 dlLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKS 740
Cdd:TIGR02168 452 --LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
658-766 |
1.98e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 39.50 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 658 ELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSrrqlelrvtsLEEELTDLRTEKESLEKnlsERK 737
Cdd:pfam17675 13 ELDKQLEDAEKERDAYISFLKKLEKETPEELEELEKELEKLEKEEEE----------LLQELEELEKEREELDA---ELE 79
|
90 100
....*....|....*....|....*....
gi 1387290470 738 KKSAQERCQAEEEIDEIRKSHQEELDKLR 766
Cdd:pfam17675 80 ALEEELEALDEEEEEFWREYNALQLQLLE 108
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
563-898 |
2.11e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILE----------KSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNN-SLQTATENTQAKV 631
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTEllveqgrlqlQADRHQEHIRARDSLIQSLATRLELDGFERGPFSErQIKNFHTLVIERQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 632 TEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS--EKQSRRQLE 709
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRilELDQELRKA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 710 LRVTSLEEELTDLRTEKESlEKNLSERKKKSAQERCQAEEEIDEirKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQA 789
Cdd:TIGR00606 484 ERELSKAEKNSLTETLKKE-VKSLQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 790 ELQTQ-----WEAKCEQLLASAKNE----------------HLQQYQ-EVCTQRDASQQQLLQLEEK------CSALQAQ 841
Cdd:TIGR00606 561 ELTSLlgyfpNKKQLEDWLHSKSKEinqtrdrlaklnkelaSLEQNKnHINNELESKEEQLSSYEDKlfdvcgSQDEESD 640
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 842 VTSLREQNAQHIKDLESKAQTSGVEAT----AADPSEKVKKIMNQVFQflrGEFELEEFYS 898
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQfitqLTDENQSCCPVCQRVFQ---TEAELQEFIS 698
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
697-895 |
2.54e-03 |
|
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: 42.27 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 697 KLKSEKQSRRQLELRVtsLEEELTDLRTEKEslEKNLSERKKKSAQERCQAEEEI-DEIRKSHQEELDKLRQLLKKARVS 775
Cdd:pfam02463 177 KLIEETENLAELIIDL--EELKLQELKLKEQ--AKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 776 TDQAAAEQLSlvQAELQTQWEAKCEQLLASAKNEHLQQYQeVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKD 855
Cdd:pfam02463 253 IESSKQEIEK--EEEKLAQVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387290470 856 LESKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEE 895
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
|
| BAR |
pfam03114 |
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ... |
588-814 |
2.55e-03 |
|
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.
Pssm-ID: 460810 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 588 IKEQNDKISELIERNQRYVEQSNL-----MMEKRNNSLQTATENTQAKVTEelaaataQVSHLHlKMTAHQKKETELQVQ 662
Cdd:pfam03114 1 LKKQFNRASQLLGEKVGGAEKTKLdedfeELERRFDTTEKEIKKLQKDTKG-------YLQPNP-GARAKQTVLEQPEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 663 LTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS-EKQSRRQLELRVTSLEEELTDLRTEKESLE------KNLSE 735
Cdd:pfam03114 73 LAESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQlDDRVETNFLDPLRNLLKEFKEIQKHRKKLErkrldyDAAKT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 736 RKKKSAQER-------CQAEEEIDEIRKSHQEELDKLRQLLKKARVS-TDQAAAEQLSLVQAELQTQweAKCEQLLasak 807
Cdd:pfam03114 153 RVKKAKKKKsskakdeSQAEEELRKAQAKFEESNEQLKALLPNLLSLeVEFVVNQLVAFVEAQLDFH--RQCYQLL---- 226
|
....*..
gi 1387290470 808 nEHLQQY 814
Cdd:pfam03114 227 -EQLQQQ 232
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
665-770 |
2.60e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.25 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 665 ESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQER 744
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEV 211
|
90 100
....*....|....*....|....*.
gi 1387290470 745 CQAEEEIDEIrksHQEELDKLRQLLK 770
Cdd:COG4026 212 FSLEELWKEL---FPEELPEEDFIYF 234
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
678-792 |
2.70e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.25 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 678 AQLQAE------LSEVQETSQQVQSKLKSEKQSRR----QLELRVTSLEEELtDLRTEK-ESLEKNLSERKKKSAQERC- 745
Cdd:pfam12072 43 AKKEAEtkkkeaLLEAKEEIHKLRAEAERELKERRnelqRQERRLLQKEETL-DRKDESlEKKEESLEKKEKELEAQQQq 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1387290470 746 --QAEEEIDEIRKSHQEELDKLRQLlkkarvSTDQAAAEQLSLVQAELQ 792
Cdd:pfam12072 122 leEKEEELEELIEEQRQELERISGL------TSEEAKEILLDEVEEELR 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
559-771 |
2.76e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 559 ETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEkrnnSLQTATENTQAKVTEELAAA 638
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELESELEALLNER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 639 TAQVSHLHLKMTAHQKKETELQV---QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQ------------ 703
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRElesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleeaealenk 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 704 ---SRRQLELRVTSLEEELT----------------------------DLRTEKESLEknlserkkksaqercQAEEEID 752
Cdd:TIGR02168 963 iedDEEEARRRLKRLENKIKelgpvnlaaieeyeelkerydfltaqkeDLTEAKETLE---------------EAIEEID 1027
|
250 260
....*....|....*....|
gi 1387290470 753 -EIRKSHQEELDKLRQLLKK 771
Cdd:TIGR02168 1028 rEARERFKDTFDQVNENFQR 1047
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
658-845 |
2.86e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 658 ELQVQLTESMKE-TDLLRGQLAQLQAELSEVQETSQQvqSKLKSEKQSRRQLELRVtslEEELTDLRTEKESLEKNLSER 736
Cdd:PRK10246 216 EQVQSLTASLQVlTDEEKQLLTAQQQQQQSLNWLTRL--DELQQEASRRQQALQQA---LAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 737 KKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQT--QWEAKCEQLlaSAKNEHLQQY 814
Cdd:PRK10246 291 QLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSlnTWLAEHDRF--RQWNNELAGW 368
|
170 180 190
....*....|....*....|....*....|.
gi 1387290470 815 QEVCTQRDASQQQLLQLEEKCSALQAQVTSL 845
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQQLTHAEQKLNAL 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
573-792 |
2.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNlmmEKRNNSLQTatentQAKVT--EELAAATAQVSHLHlkmt 650
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAALLA-----EAGVEdeEELRAALEQAEEYQ---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKE--TDLLRGQLAQLQAELSEVQETSQQVQSKLKSekqsrrqlelrvtsLEEELTDLRTEKES 728
Cdd:COG4717 399 ELKEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEELEE--------------LREELAELEAELEQ 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290470 729 LEKnlserkkksaqercqaEEEIDEIRKSHQEELDKLRQLLKKARVstDQAAAEQLSLVQAELQ 792
Cdd:COG4717 465 LEE----------------DGELAELLQELEELKAELRELAEEWAA--LKLALELLEEAREEYR 510
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
566-748 |
3.05e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.40 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRyVEQSNLMMEKRnnslqtatentQAKVTEELAAATAQVShl 645
Cdd:COG2268 175 AITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETE-IAIAQANREAE-----------EAELEQEREIETARIA-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 646 hlkmtahqKKETELQVQLTESMKETDllrgqLAQLQAELS-EVQETSQQVQSKLKSEkQSRRQLELRVTSLEEELTDLRT 724
Cdd:COG2268 241 --------EAEAELAKKKAEERREAE-----TARAEAEAAyEIAEANAEREVQRQLE-IAEREREIELQEKEAEREEAEL 306
|
170 180
....*....|....*....|....
gi 1387290470 725 EKESLEKNLSERKKKSAQERCQAE 748
Cdd:COG2268 307 EADVRKPAEAEKQAAEAEAEAEAE 330
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
707-861 |
3.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 707 QLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIR---KSHQEELDKLRQLLKKARvSTDQAAAEQ 783
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQAR-SELEQLEEE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 784 LSLVQAELQTQweakceQLLASAKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQ 861
Cdd:COG4372 82 LEELNEQLQAA------QAELAQAQEELESLQE---EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
563-783 |
3.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENT-------QAKVT 632
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRSGGSVsyldvllGSESF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 EELAAATAQVShlhlKMTAHQKKETELQVQltesmketdlLRGQLAQLQAELSEVQETSQQVQSKLKSEKQsrrQLELRV 712
Cdd:COG3883 115 SDFLDRLSALS----KIADADADLLEELKA----------DKAELEAKKAELEAKLAELEALKAELEAAKA---ELEAQQ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290470 713 TSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQ 783
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
633-767 |
3.43e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 633 EELAAATAQVS--HLHLKMTAHQKKEtelqvqLTESMKEtdlLRGQLAQL------------QAELSEVQETSQQVQSKL 698
Cdd:pfam00038 142 EEVRELQAQVSdtQVNVEMDAARKLD------LTSALAE---IRAQYEEIaaknreeaeewyQSKLEELQQAAARNGDAL 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 699 KSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIrkshQEELDKLRQ 767
Cdd:pfam00038 213 RSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISEL----EAELQETRQ 277
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
654-801 |
3.75e-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: 41.48 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQlteSMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLE-------EELTDLRTEK 726
Cdd:pfam15709 375 REELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQElqrkkqqEEAERAEAEK 451
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 727 E---SLEKNLSERKKKSAQercQAEEEIDEIRKSHQEELDKLRQLLKKARvstdQAAAEQLSLVQAELQTQWEAKCEQ 801
Cdd:pfam15709 452 QrqkELEMQLAEEQKRLME---MAEEERLEYQRQKQEAEEKARLEAEERR----QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
194-261 |
3.91e-03 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 38.93 E-value: 3.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290470 194 VEVGDSLEVAYTSWLfqnhVLGQVFDSTANKDKLLrLKLGSGKVIKSWEDGMVGMRKGGKRLLIIPPA 261
Cdd:COG1047 1 IEKGDVVTLHYTLKL----EDGEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPE 63
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
673-892 |
4.17e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 673 LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQ-----LELRVTSLEEELTD-------LRTEKES-----LEKNLSE 735
Cdd:NF041483 96 LRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQqldqeLAERRQTVESHVNEnvawaeqLRARTESqarrlLDESRAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 736 RKKKSAQERCQAEEEIDEIRKSHQEELDKLR----QLLKKARvstdqAAAEQLsLVQAELQTQwEAK--CEQLLASAKNE 809
Cdd:NF041483 176 AEQALAAARAEAERLAEEARQRLGSEAESARaeaeAILRRAR-----KDAERL-LNAASTQAQ-EATdhAEQLRSSTAAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 810 HLQQYQEVCTQRDASQQQLLQLEEKCSALQAQ----VTSLREQNAQHIKDLES---------KAQTSGVEATAADPSEKV 876
Cdd:NF041483 249 SDQARRQAAELSRAAEQRMQEAEEALREARAEaekvVAEAKEAAAKQLASAESaneqrtrtaKEEIARLVGEATKEAEAL 328
|
250
....*....|....*.
gi 1387290470 877 KKIMNQVFQFLRGEFE 892
Cdd:NF041483 329 KAEAEQALADARAEAE 344
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
759-870 |
4.25e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 759 QEELDKLRQLLKKARVSTDQAAAEQLSLVQ-AELQTQWEAKcEQLLASAKNEhLQQYQEVCTQRDASQQQLLQLEEKCSA 837
Cdd:COG1566 82 QAALAQAEAQLAAAEAQLARLEAELGAEAEiAAAEAQLAAA-QAQLDLAQRE-LERYQALYKKGAVSQQELDEARAALDA 159
|
90 100 110
....*....|....*....|....*....|...
gi 1387290470 838 LQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 870
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
|
|
| Sds3 |
pfam08598 |
Sds3-like; Repression of gene transcription is mediated by histone deacetylases containing ... |
672-823 |
4.58e-03 |
|
Sds3-like; Repression of gene transcription is mediated by histone deacetylases containing repressor-co-repressor complexes, which are recruited to promoters of target genes via interactions with sequence-specific transcription factors. The co-repressor complex contains a core of at least seven proteins. This family represents the conserved region found in Sds3, Dep1 and BRMS1-homolog p40 proteins.
Pssm-ID: 430099 Cd Length: 218 Bit Score: 40.03 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 672 LLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELtdlrtEKESLEKNLSERKKKSAQERcqaEEEI 751
Cdd:pfam08598 19 LYRNKLTALQTELQLLHQGSHPELLQYYRDLEEERDAELKRLRLREEY-----QLKRIDIETKADRTAAHQEF---KKLV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290470 752 DEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYqEVCTQRDA 823
Cdd:pfam08598 91 KLLKEKLYDETTQKIYRLNEERRLLDLANTNSYLVDYKKTRSHTLAGLLNPNFTSRNNPVDPG-ELVTDRRS 161
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
572-773 |
4.64e-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: 40.99 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 572 QENERLKQEILEKSSRIKEQNDKISELIER-NQRYVeqsnlmmekrnnsLQTATENTQAKVTEELAAATAQVSHLHLKMT 650
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERvQQSYT-------------LNENELERVRGLEKQLEELEKRYDEIVERLE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 651 AHQKKETELQVQLTESMKetdllrgQLAQLQAELSEVQEtsqQVQSKLKSEKQSRRQLELRVTSLEEelTDLRTEKESLe 730
Cdd:pfam06160 354 EKEVAYSELQEELEEILE-------QLEEIEEEQEEFKE---SLQSLRKDELEAREKLDEFKLELRE--IKRLVEKSNL- 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387290470 731 KNLSErkkkSAQER-CQAEEEIDEIRKSHQE---ELDKLRQLLKKAR 773
Cdd:pfam06160 421 PGLPE----SYLDYfFDVSDEIEDLADELNEvplNMDEVNRLLDEAQ 463
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
513-730 |
4.80e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 513 RQHNTEIRMAVSKVADKMDHLMTKVEE----LQKHSAGNSLLipsmSVTMETSMIMSNIQRIIQENERLKQEILEKSSRI 588
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEaeaaLEEFRQKNGLV----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 589 KEQNDKISEliernqryveQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMK 668
Cdd:COG3206 243 AALRAQLGS----------GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290470 669 ET-DLLRGQLAQLQAELSEVQETSQQVQSKLKS--EKQSR-RQLELRVTSLEEELTDLRTEKESLE 730
Cdd:COG3206 313 RIlASLEAELEALQAREASLQAQLAQLEARLAElpELEAElRRLEREVEVARELYESLLQRLEEAR 378
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
517-777 |
4.94e-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: 41.03 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 517 TEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMETSMIMS--NIQRIIQENERLK---QEILEKSS---RI 588
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaaHEARIRELEEDIKtltQRVLERETeleRM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 589 KEQNDKIseLIERNQRYVEQSNLMM-----EKRNNSLQT---ATENTQAKVTEELAAATAQVSHLHLKMTAHQKKETE-- 658
Cdd:pfam07888 156 KERAKKA--GAQRKEEEAERKQLQAklqqtEEELRSLSKefqELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEne 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 659 --------LQVQLTESMKETDLLRGQLAQL------------QAELSEVQETSQQVQSKLK---------SEKQSRRQ-- 707
Cdd:pfam07888 234 alleelrsLQERLNASERKVEGLGEELSSMaaqrdrtqaelhQARLQAAQLTLQLADASLAlregrarwaQERETLQQsa 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 708 ---------LELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKS--------------HQEELDK 764
Cdd:pfam07888 314 eadkdriekLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvaqkekeqlqaeKQELLEY 393
|
330
....*....|...
gi 1387290470 765 LRQLLKKARVSTD 777
Cdd:pfam07888 394 IRQLEQRLETVAD 406
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
659-792 |
5.02e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 659 LQVQLTESMKETDLLRGQLAQLQAELSevqetsqqvqsklkSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSErkk 738
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLS--------------LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAE--- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 739 kSAQERCQAEEEIDEIRKshqeELDKLRQLLKKAR----VSTDQAAA--EQLSLVQAELQ 792
Cdd:PRK09039 107 -LAGAGAAAEGRAGELAQ----ELDSEKQVSARALaqveLLNQQIAAlrRQLAALEAALD 161
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
654-792 |
5.19e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKEslekNL 733
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLV----TL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290470 734 SERKKKSAQERCQAEEEIDEIRKSHqEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 792
Cdd:pfam10473 79 RSEKENLTKELQKKQERVSELESLN-SSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
574-764 |
5.46e-03 |
|
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: 40.56 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 574 NERLKQEILEKSSRiKEQNDKISELIE-RNQRYVEQSNLM-----MEKRNNSLQTATENTQAKVteelaaatAQVSHlHL 647
Cdd:pfam15905 138 NELLKAKFSEDGTQ-KKMSSLSMELMKlRNKLEAKMKEVMakqegMEGKLQVTQKNLEHSKGKV--------AQLEE-KL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 648 KMTAHQKKETELQVQ-LTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQ----LELRVTSLEEELTDL 722
Cdd:pfam15905 208 VSTEKEKIEEKSETEkLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEkeqeLSKQIKDLNEKCKLL 287
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1387290470 723 RTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDK 764
Cdd:pfam15905 288 ESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
571-957 |
5.86e-03 |
|
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: 41.09 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 571 IQENERLKQEILEKSSrikeQNDKISELIERNQRYVeQSNLMM---EKRNNSLQTAT-ENTQAKVTEELAAAtaqvshlh 646
Cdd:COG3096 238 LRENRMTLEAIRVTQS----DRDLFKHLITEATNYV-AADYMRhanERRELSERALElRRELFGARRQLAEE-------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 647 lkmtahqkketelQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLK-SEKQSRRQLELrvtsleEELTDLRTE 725
Cdd:COG3096 305 -------------QYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqQEKIERYQEDL------EELTERLEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 726 KESLEKNLSERKKKSAQERCQAEEEIDEIRKS---HQEELDKL----------RQLLKKARVSTDQA--AAEQLSLVQAE 790
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQqtraiqyqqaVQALEKARALCGLPdlTPENAEDYLAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 791 LQTQWEAKCEQLLA---------SAKNEHLQQYQEVC-----TQRDASQQQLLQLEEKCSALQAQVTSLrEQNAQHIKDL 856
Cdd:COG3096 446 FRAKEQQATEEVLEleqklsvadAARRQFEKAYELVCkiageVERSQAWQTARELLRRYRSQQALAQRL-QQLRAQLAEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 857 ESK-AQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEfysgrtvlgtimntikmvTLRLLNQHEQEKGESSNEEEEE 935
Cdd:COG3096 525 EQRlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEA------------------QLEELEEQAAEAVEQRSELRQQ 586
|
410 420
....*....|....*....|..
gi 1387290470 936 EDEAQARSPSGQSQAPLDRESQ 957
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQ 608
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
563-814 |
6.24e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 563 IMSNIQRIIQENERLKQEILE-KSSRIKEQNDKISELIErnQRYVeqsnlMMEKRNNSLQTATENtQAKVTEELAAATAQ 641
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEElDLDEAEEKNEEIQERID--QLYD-----ILEREVKARKYVEKN-SDTLPDFLEHAKEQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLhlkmtahqKKETElQVQLTESMKETDLLRGQlaQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTD 721
Cdd:PRK04778 326 NKEL--------KEEID-RVKQSYTLNESELESVR--QLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 722 LRTEKESLEKNLSERKKKSAQERCQAEE---EIDEIR----KSH---------------QEELDKLRQLLKKARVSTDqA 779
Cdd:PRK04778 395 IEKEQEKLSEMLQGLRKDELEAREKLERyrnKLHEIKryleKSNlpglpedylemffevSDEIEALAEELEEKPINME-A 473
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387290470 780 AAEQLSLVQAELQTqWEAKCEQLLASAK-NEHLQQY 814
Cdd:PRK04778 474 VNRLLEEATEDVET-LEEETEELVENATlTEQLIQY 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
682-879 |
6.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 682 AELSEVQETSQQVQSKLKSEKQSRRQL----------------------ELRV------TSLEEELTDLRT---EKESLE 730
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLceeknalqeqlqaetelcaeaeEMRArlaarkQELEEILHELESrleEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 731 KNLSERKKKSAQERCQAEEEIDEIR-----------------KSHQEE----------LDKLRQLLKK--ARVSTDQAAA 781
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEaarqklqlekvtteakiKKLEEDillledqnskLSKERKLLEEriSEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 782 EQLSLVQAELQTQWEAKCEQLLASAKNEHlQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQhiKDLESKAQ 861
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK--KEEELQAA 248
|
250
....*....|....*...
gi 1387290470 862 TSGVEATAADPSEKVKKI 879
Cdd:pfam01576 249 LARLEEETAQKNNALKKI 266
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
654-769 |
6.31e-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: 38.00 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSK--------------LKSEKQSRRQLELRVTSLEEEL 719
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNyerelvlhaedikaLQALREELNELKAEIAELKAEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387290470 720 TDLRTEKESLEKNLSERKKksaqercQAEEEIDEIRKSHqEELDKLRQLL 769
Cdd:pfam07926 81 ESAKAELEESEESWEEQKK-------ELEKELSELEKRI-EDLNEQNKLL 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
705-861 |
6.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 705 RRQLELRVTSLEEELTDLRTEKESLEKnlserkkksAQERCQAEEEIDEIRKSHQE---ELDKLRQLLKKARVSTDQAAA 781
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 782 EQLSLVQAELQTQWEakceqllasaknEHLQQYQEVCTQRDASQQQLLQLEEKCSALQ-AQVTSLREQNAQHIKDLESKA 860
Cdd:COG4913 291 ELLEAELEELRAELA------------RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERE 358
|
.
gi 1387290470 861 Q 861
Cdd:COG4913 359 R 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
566-739 |
6.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 566 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQ-SNLMMEKRNNSLQTATENTQAKVTEE---LAAATAQ 641
Cdd:PHA02562 214 NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAlNKLNTAAAKIKSKIEQFQKVIKMYEKggvCPTCTQQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 642 VSHLHLKMTAHQKKETELQVQLTESMKEtdllRGQLAQLQAELSEVQETSQQVQSKLKSEKQS--------RR------Q 707
Cdd:PHA02562 294 ISEGPDRITKIKDKLKELQHSLEKLDTA----IDELEEIMDEFNEQSKKLLELKNKISTNKQSlitlvdkaKKvkaaieE 369
|
170 180 190
....*....|....*....|....*....|..
gi 1387290470 708 LELRVTSLEEELTDLRTEKESLEKNLSERKKK 739
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
676-854 |
6.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 676 QLAQLQAELSEVQETSQQV---QSKLKSEKQSRRQLELRVTSL------EEELTDLRTEKESLEKNLSERKKKSAQERCQ 746
Cdd:PRK04863 787 RIEQLRAEREELAERYATLsfdVQKLQRLHQAFSRFIGSHLAVafeadpEAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 747 AeeeideirKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAK---------CEQL--LASAknehLQQYQ 815
Cdd:PRK04863 867 L--------EQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKrfvqqhgnaLAQLepIVSV----LQSDP 934
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387290470 816 EvctQRDASQQQLLQLEEKCSALQAQVTSLRE--QNAQHIK 854
Cdd:PRK04863 935 E---QFEQLKQDYQQAQQTQRDAKQQAFALTEvvQRRAHFS 972
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
662-861 |
6.92e-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: 38.78 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 662 QLTESMKEtdlLRGQLAQLQAELSEVqetSQQVQSKLKSEKQSRRQLelrvtsLEEELTDLRtekESLEKNLSERKKKSA 741
Cdd:pfam01442 1 LLEDSLDE---LSTYAEELQEQLGPV---AQELVDRLEKETEALRER------LQKDLEEVR---AKLEPYLEELQAKLG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 742 QE----RCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSlvqaELQTQWEAKCEQLLASAKnEHLQQYQE- 816
Cdd:pfam01442 66 QNveelRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQNVD----ALRARLAPYAEELRQKLA-ERLEELKEs 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387290470 817 VCTQRDASQQQLLQleekcsalqaQVTSLREQNAQHIKDLESKAQ 861
Cdd:pfam01442 141 LAPYAEEVQAQLSQ----------RLQELREKLEPQAEDLREKLD 175
|
|
| antiphage_ZorA_2 |
NF033915 |
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ... |
589-736 |
7.19e-03 |
|
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.
Pssm-ID: 411476 [Multi-domain] Cd Length: 383 Bit Score: 40.13 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 589 KEQNDKISELIER-NQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLHLK---------MTAHQKKETE 658
Cdd:NF033915 216 KESKEALQELHERiGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLEslvgnfmdgMTSAGREQGL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 659 LQVQLTESMKET-DLLRGQLAQLQAELSEVQETSQQVQSKLKSE------------KQSRRQLELRVtslEEELTDLRTE 725
Cdd:NF033915 296 QMQQAAADVNAAvSGMSERLNQLFNSLSEQQGRQMERAQQQSSTfetqlqrlsgsaNERQAQLEQRF---EELMSGLTEQ 372
|
170
....*....|.
gi 1387290470 726 KESLEKNLSER 736
Cdd:NF033915 373 LQTQLGAAQQR 383
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
517-776 |
7.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 517 TEIRMAVSKVADKMDHLMTKVEEL-QKHSAGNSLlipsmsVTMEtsmimSNIQRIIQENERLKQEILEKSSRIKEQNDKI 595
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeERLERAEDL------VEAE-----DRIERLEERREDLEELIAERRETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 596 SELIERNQRY----VEQSNLMMEKR-------------NNSLQTATE-----NTQAKVTEELAAATAQVSHLHLKMTAHQ 653
Cdd:PRK02224 540 EELRERAAELeaeaEEKREAAAEAEeeaeeareevaelNSKLAELKErieslERIRTLLAAIADAEDEIERLREKREALA 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 654 KKETELQVQLTESMKETDLLRGQ-----LAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKES 728
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1387290470 729 LEknlserkkkSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVST 776
Cdd:PRK02224 700 RE---------ALENRVEALEALYDEAEELESMYGDLRAELRQRNVET 738
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
673-861 |
7.89e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 673 LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELrvtsLEEELTDLRTEKESLEKNL-------------SERKKK 739
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEI----LEKELSSLAQETEELQKKAtqtlakaqqvnaeSERTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 740 SAQErcqAEEEIDEIRKSHQEELDKLRQLLKKArvstDQAAAEQLSLVQAELQtqweakceQLLASAKNEHLQQYQEVCT 819
Cdd:pfam06008 83 HAKE---LAEAIKNLIDNIKEINEKVATLGEND----FALPSSDLSRMLAEAQ--------RMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387290470 820 QR-DASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQ 861
Cdd:pfam06008 148 AElKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLS 190
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
652-773 |
8.17e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 38.74 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 652 HQKKETELQV----QLTESMKETDLLrgqlaQLQAElsevqetSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRtEKE 727
Cdd:pfam13870 20 HTLAKIQEKLeqkeELGEGLTMIDFL-----QLQIE-------NQALNEKIEERNKELKRLKLKVTNTVHALTHLK-EKL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1387290470 728 SLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKAR 773
Cdd:pfam13870 87 HFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLR 132
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
573-878 |
8.71e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 573 ENERLKQEILEKSSRIKEQNDkisELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEEL--------AAATAQVSH 644
Cdd:NF041483 503 ESERVRTEAIERATTLRRQAE---ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETeraiaarqAEAAEELTR 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 645 LHlkmTAHQKKETELQVQLTESMKETDLLRGQLAQLQAEL-SEVQETSQQVQSKLKSEKQSRRqlelrvTSLEEELTDLR 723
Cdd:NF041483 580 LH---TEAEERLTAAEEALADARAEAERIRREAAEETERLrTEAAERIRTLQAQAEQEAERLR------TEAAADASAAR 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 724 TEKESLEKNLserkkksaqeRCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQwEAKCEQLL 803
Cdd:NF041483 651 AEGENVAVRL----------RSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARR-RREAEETL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 804 ASAKNEHLQQYQEVCTQR-----------DASQQQLLQLEEKCSALQAQVTSLREQNAQHIKD----LESKAQ--TSGVE 866
Cdd:NF041483 720 GSARAEADQERERAREQSeellasarkrvEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEeeIAGLR 799
|
330
....*....|..
gi 1387290470 867 ATAADPSEKVKK 878
Cdd:NF041483 800 SAAEHAAERTRT 811
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
714-802 |
9.21e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 37.38 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 714 SLEEELTDLRTEKESLEKNLSERKKK--SAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVqaEL 791
Cdd:pfam04871 5 ELESEASSLKNENTELKAELQELSKQynSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELDDLL--LL 82
|
90
....*....|.
gi 1387290470 792 QTQWEAKCEQL 802
Cdd:pfam04871 83 LGDLEEKVEKY 93
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
653-792 |
9.54e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 40.03 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290470 653 QKKETE-LQVQLTESMKETDLLrgqLAQLQAELSEVQETSQQVQSKLKSEKQSRR--QLELRVTSLEEELTDLRTEKESL 729
Cdd:pfam14817 311 QWAHVQqFLNELAETRSRCQQL---QARLQGLKDEAELESLGIGDTSQNDSLLRQvlELELQAAGLAASRDTLRSECQQL 387
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387290470 730 EKNLSERKK--KSAQERCQAEEEIDEIRKSHQEEldkLRQLLKKarvstDQAAAEQLSLVQAELQ 792
Cdd:pfam14817 388 NKLARERQEalRSLQKKWQRILDFRQLVSELQEQ---IRALIKG-----NSAAKAFLIRQPAEAR 444
|
|
| COG5124 |
COG5124 |
Protein predicted to be involved in meiotic recombination [Cell division and chromosome ... |
703-764 |
9.95e-03 |
|
Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only];
Pssm-ID: 227453 [Multi-domain] Cd Length: 209 Bit Score: 38.78 E-value: 9.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290470 703 QSRRQLELRVTSLEEELTDLR----TEKESLEKNLSERKKK-SAQERCQAEEEIDEIRKSHQEELDK 764
Cdd:COG5124 75 QTLQKLYDSSELLKKKIQEVKqdiaTYKEEIDKEKATRRKKfTEGQKNYNREALLEKRKKEQDEIKK 141
|
|
| |
