|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
193-286 |
1.17e-29 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 113.45 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 193 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 272
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 150010552 273 TQATDSILVFEVEV 286
Cdd:pfam00254 80 VIPPNATLVFEVEL 93
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
184-286 |
1.95e-26 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 104.49 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 184 QDLIVADGPAVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACA 263
Cdd:COG0545 4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....*.
gi 150010552 264 VGSEG---VIGwtqaTDSILVFEVEV 286
Cdd:COG0545 80 YGERGaggVIP----PNSTLVFEVEL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
620-882 |
1.22e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 620 LQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQE 699
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 700 TSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 780 KKtrvstdQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQN 859
Cdd:COG1196 397 EL------AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|...
gi 150010552 860 EQHIKELEKNKSQMSGVEAAASD 882
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
578-894 |
7.35e-19 |
|
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: 93.20 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 578 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 656
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 657 LKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 736
Cdd:TIGR02168 754 KELTELEAEIEELEERLEE-------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 737 ESLEKNLsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LA 814
Cdd:TIGR02168 827 ESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 815 SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 893
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
.
gi 150010552 894 V 894
Cdd:TIGR02168 981 I 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-804 |
2.40e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNS------LQTATENTQARVLHAEQ 636
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 637 EKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 716
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 717 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEQLSL 796
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLL 496
|
....*...
gi 150010552 797 VQAELQTQ 804
Cdd:COG1196 497 LEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
572-882 |
4.37e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.50 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QEN-ERLkQEILeksNRIEEQNDKISELIERNQRYVEQSNlmmEKRN----------NSLQTATENTQARVLHAEQEKAK 640
Cdd:TIGR02168 185 RENlDRL-EDIL---NELERQLKSLERQAEKAERYKELKA---ELRElelallvlrlEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 720
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 721 KVTSLEEELTDLRVEKESLEKNLSERKKKS-----------------AQERSQAEEEIDEIRKSYQEELDKLRQL---LK 780
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELeelesrleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLedrRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 781 KTRVSTDQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 858
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
330 340 350
....*....|....*....|....*....|
gi 150010552 859 NEQH------IKELEKNKSQMSGVEAAASD 882
Cdd:TIGR02168 498 QENLegfsegVKALLKNQSGLSGILGVLSE 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-922 |
2.79e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.82 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 560 TSMI-MSNIQR--IIQE----------NERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSN-------LMMEKRN-- 617
Cdd:TIGR02169 145 TDFIsMSPVERrkIIDEiagvaefdrkKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqaLLKEKREye 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 618 --------NSLQTATENTQARVLHAEQEKAKVTEEL-------AAATAQVSHLQLKMtahQKKETELQMQLTESLKEtdl 682
Cdd:TIGR02169 225 gyellkekEALERQKEAIERQLASLEEELEKLTEEIselekrlEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGE--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 683 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEID 762
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 763 EIR------KSYQEELDKLRQLLK--KTRVSTDQAAAEQLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRD-- 832
Cdd:TIGR02169 379 EFAetrdelKDYREKLEKLKREINelKRELDRLQEELQRLSEELADLNAA--------IAGIEAKINELEEEKEDKALei 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 833 -AYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKimnqvfqslRREFELEESYNGR 911
Cdd:TIGR02169 451 kKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG---------GRAVEEVLKASIQ 521
|
410
....*....|.
gi 150010552 912 TILGTIMNTIK 922
Cdd:TIGR02169 522 GVHGTVAQLGS 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
569-858 |
5.27e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.05 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 569 RIIQENERLKQEILEKSNRIEEQNDKISELIERNQryveqsnlMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAA 648
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 649 TAQVSHLQLKMTAHQKKETELQMQLTESL------------KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 716
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 717 QLELKVTSLEEELTDLRVEKESLE----------KNLSERKKKSAQERSQAEEEIDEIRKSYQE---ELDKLRQLLKKTR 783
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 784 VsTDQAAAEQLS----------------LVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC 845
Cdd:TIGR02169 924 A-KLEALEEELSeiedpkgedeeipeeeLSLEDVQAELQRVEEEIraLEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
330
....*....|...
gi 150010552 846 LALQAQITALTKQ 858
Cdd:TIGR02169 1003 KAILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
566-902 |
7.38e-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: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 566 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 645
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 646 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSL 725
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 726 EEELTDLRVEKESLEKNLSE----RKKKSAQ------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLS 795
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 796 LVQAELQ-TQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMS 874
Cdd:TIGR02168 924 LAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 150010552 875 GVEAAASDPSEKVKKIM--------------NQVFQSLRREF 902
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEeaieeidrearerfKDTFDQVNENF 1045
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
567-827 |
4.98e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTAT----------ENTQARVLH 633
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLaelarleqdiARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 634 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQ 713
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 714 NRKQLELKVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAA 790
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEealAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270
....*....|....*....|....*....|....*..
gi 150010552 791 AEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEV 827
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-906 |
5.49e-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: 80.49 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 623 ATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 702
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 703 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN---LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 780 KKTRVSTDQAAAEQLSLVqaELQTQWEAKCEHLLASAK---------DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQA 850
Cdd:TIGR02168 824 ERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAeieeleeliEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 851 QITALTKQNEQHIKELEKNKSQMSGVEAAAsdpsEKVKKIMNQVFQSLRREFELEE 906
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRL----EGLEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
641-906 |
1.22e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEELAAataQVSHLQ------LKMTAHQKKETELQMQLTesLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 714
Cdd:COG1196 194 ILGELER---QLEPLErqaekaERYRELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 715 RKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQllkktRVSTDQAAA 791
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAelaRLEQDIARLEERRRELEERLEEL----EEELAELEE-----ELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 792 EQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKN 869
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270
....*....|....*....|....*....|....*..
gi 150010552 870 KSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE 906
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-908 |
1.31e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRnnslqtatentqarvlhAEQEKAKVTEELA 646
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL----LEELNKKIKDL-----------------GEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 647 AATAQVSHLQlkmtaHQKKETELQMQLTEslketdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLE 726
Cdd:TIGR02169 298 ELEAEIASLE-----RSIAEKERELEDAE---------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 727 EELTDLRVEKESLEKNLSERKKKSAQER---SQAEEEIDEIRKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQT 803
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRL--SEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 804 QWEAKCEHLlasAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkqnEQHIKELEKNKSQMSGVEAAASDP 883
Cdd:TIGR02169 442 EKEDKALEI---KKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL----QRELAEAEAQARASEERVRGGRAV 512
|
330 340
....*....|....*....|....*
gi 150010552 884 SEKVKKIMNQVFQSLRREFELEESY 908
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
563-905 |
2.85e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEILEksnrIEEQNDKISELIERNQryveqsnlmmeKRNNSLQTATENTQARVLHAEQEKAKVT 642
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQ-----------QEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 643 EELAAATAQVSHLQLKMTAHQKKETELQMQLTE--SLKETDL---LRGQLTKVQAKLSELQetSEQAQSkfkseKQNRKQ 717
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnNQKEQDWnkeLKSELKNQEKKLEEIQ--NQISQN-----NKIISQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 718 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrKSYQEELDKLRQLLKKtrvstdqaaAEQLSlv 797
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQN---------QEKLN-- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 798 qAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL--------------------TK 857
Cdd:TIGR04523 408 -QQKDEQIKK-----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlsrsinkIK 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 150010552 858 QN-EQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 905
Cdd:TIGR04523 482 QNlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-866 |
4.66e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 626 NTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQM--QLTESLKETDLLRGQLTKVQAKLSELqetsEQ 703
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERL----DA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 704 AQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 783
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 784 VStdQAAAEQLSLVQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRDA-------YQQKLVQLQEKCL-ALQAQI-TA 854
Cdd:COG4913 763 VE--RELRENLEERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDAdleslpeYLALLDRLEEDGLpEYEERFkEL 839
|
250
....*....|..
gi 150010552 855 LTKQNEQHIKEL 866
Cdd:COG4913 840 LNENSIEFVADL 851
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-902 |
1.31e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRI-----IQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATEntqarvlhaEQE 637
Cdd:PRK03918 370 KKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------LKKEIKELKKAIE---------ELK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 638 KAK---------VTEE-----LAAATAQVSHLQLKMTAHQKKETELQMQLTE------------SLKET-DLLRG----- 685
Cdd:PRK03918 433 KAKgkcpvcgreLTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkeseliKLKELaEQLKEleekl 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 686 ---QLTKVQAKLSELQETSEQA------QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQErsq 756
Cdd:PRK03918 513 kkyNLEELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE--- 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 757 AEEEIDEIRKSYQE---------ELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQtQWEAKCEHLLASAKDEhlqQYQEV 827
Cdd:PRK03918 590 LEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL 664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150010552 828 caqrdayQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVfQSLRREF 902
Cdd:PRK03918 665 -------REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERV-EELREKV 730
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
568-902 |
1.35e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 568 QRIIQENERLK------QEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 641
Cdd:COG4717 139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 TEELAAATAQVSHLQLKMTAHQKKETELQMQ--------------LTESLKETDLLRGQLTKVQAKL-----SELQETSE 702
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLlallfLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 703 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVeKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE--LDKLRQLLK 780
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 781 KTRVSTD-------------QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLA 847
Cdd:COG4717 378 EAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 848 LQAQITALTKQNE-----QHIKELEKNKSQMsgVEAAASDpsEKVKKIMNQVFQSLRREF 902
Cdd:COG4717 458 LEAELEQLEEDGElaellQELEELKAELREL--AEEWAAL--KLALELLEEAREEYREER 513
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
571-893 |
6.49e-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: 69.99 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 571 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARVLHAEQE--KAKV 641
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 TEE----LAAATAQVSHLQLKMtahqKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNrKQ 717
Cdd:COG5185 311 TESleeqLAAAEAEQELEESKR----ETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFK-DT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 718 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLK-KTRVSTDQAAAEQLSL 796
Cdd:COG5185 386 IESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISeLNKVMREADEESQSRL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 797 VQA------ELQTQWEAKCEHL------LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC-LALQAQITALTKQNEQHI 863
Cdd:COG5185 466 EEAydeinrSVRSKKEDLNEELtqiesrVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLkDFMRARGYAHILALENLI 545
|
330 340 350
....*....|....*....|....*....|
gi 150010552 864 KELEKNKSQMSGVEAAASDPSEKVKKIMNQ 893
Cdd:COG5185 546 PASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
509-907 |
2.85e-11 |
|
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: 67.82 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 583
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 584 KSNRIEE----QNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARvlhaEQEkakVTEELAAATAQVSHLQLKM 659
Cdd:pfam05483 389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEELKGK----EQE---LIFLLQAREKEIHDLEIQL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 660 TA-------HQKKETELQMQL-TESLKETDLL---------RGQLTKVQAKLS-ELQETSEQAQSKFKSEKQNRKQLElk 721
Cdd:pfam05483 460 TAiktseehYLKEVEDLKTELeKEKLKNIELTahcdkllleNKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIE-- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 722 vtSLEEELTDLRVEKESLEKNLSERK-------KKSAQERSQAEEEI--------------DEIRKSYQEELDKLRQLLK 780
Cdd:pfam05483 538 --NLEEKEMNLRDELESVREEFIQKGdevkcklDKSEENARSIEYEVlkkekqmkilenkcNNLKKQIENKNKNIEELHQ 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 781 KTRVSTDQAAAEQLSLVQAELQTQweaKCEHLLASAK---DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 857
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAYEIKVN---KLELELASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 150010552 858 QNE---QH-IKE----LEKNKSQMSGVeAAASDPSEKVKKIMNQVFQSLRREFELEES 907
Cdd:pfam05483 693 EIDkrcQHkIAEmvalMEKHKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELS 749
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
650-909 |
8.59e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 650 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 729
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 730 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEqlslVQAELQtqwEAKC 809
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLN---RLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 810 EHLLASAKDEHLQQYQEVC-AQRDAYQQKLVQLQEKCLALQAQItaltKQNEQHIKELEKNKSqmsgveaaasDPSEKVK 888
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL----EELEAALRDLESRLG----------DLKKERD 892
|
250 260
....*....|....*....|.
gi 150010552 889 KIMNQVFQSLRREFELEESYN 909
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIE 913
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-894 |
8.91e-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: 66.20 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 561 SMIMSNIQRIIQENER---LKQEI-------LEKSNRIEEQNDKISELIERNQRYVEQ--------SNL-----MMEKRN 617
Cdd:TIGR04523 328 NQISQNNKIISQLNEQisqLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEiknlesqiNDLeskiqNQEKLN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 618 NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQmQLTESLKE-TDLLRGQLTKVQAKLSE 696
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-NTRESLETqLKVLSRSINKIKQNLEQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 697 LQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEkeslEKNLSERKKKSAQERSQAEEEIDEIrksyqeELDKLR 776
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKD------DFELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 777 QLLKKTRVSTDQaAAEQLSLVQAEL---QTQweakcehllasaKDEHLQQyqevcaqrdaYQQKLVQLQEKCLALQAQIT 853
Cdd:TIGR04523 557 ENLEKEIDEKNK-EIEELKQTQKSLkkkQEE------------KQELIDQ----------KEKEKKDLIKEIEEKEKKIS 613
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 150010552 854 ALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 894
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
683-888 |
2.65e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 683 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLserkKKSAQERSQAEEEID 762
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 763 EIRKSYQEELDKL-----------------------RQLLKKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDE 819
Cdd:COG4942 101 AQKEELAELLRALyrlgrqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAAL-----RAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150010552 820 HLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVK 888
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
565-781 |
2.84e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 565 SNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER------------NQRYVEQSNL-MMEKRNNSLQTATENTQARV 631
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldNTRESLETQLkVLSRSINKIKQNLEQKQKEL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 632 LHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE------SLK------ETDLLRGQLTKV----QAKLS 695
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisDLEdelnkdDFELKKENLEKEidekNKEIE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 696 ELQET---SEQAQSKFK-------SEKQN-RKQLELK---VTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAE 758
Cdd:TIGR04523 572 ELKQTqksLKKKQEEKQelidqkeKEKKDlIKEIEEKekkISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIK 651
|
250 260
....*....|....*....|...
gi 150010552 759 EEIDEIRKSYQEELDKLRQLLKK 781
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTK 674
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
568-890 |
3.15e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 568 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkRNNSLQTATENTQARvlhaEQEKAKvTEELAA 647
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKR----ELERIR-QEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 648 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQetseqaqsKFKSEKQNRKQLELKVTSLEE 727
Cdd:pfam17380 373 EISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME--------QIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 728 ELTDLRVEKESLEKNLS-ERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ---LSLVQAELQT 803
Cdd:pfam17380 445 AREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerkRKLLEKEMEE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 804 QWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKclalqAQITALTKQNE--QHIKELEKNKSqmsgvEAAAS 881
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREmmRQIVESEKARA-----EYEAT 594
|
....*....
gi 150010552 882 DPSEKVKKI 890
Cdd:pfam17380 595 TPITTIKPI 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
661-861 |
3.34e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 661 AHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLE 740
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 741 KNLSERKKKSAQ---------------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTdQAAAEQ 793
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAEL-EAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150010552 794 LSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQ 861
Cdd:COG4942 176 LEALLAELEEERAA-----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
518-908 |
5.81e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.59 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 518 EIRMAVSKVADKMDHLMTKVEELQKHsAGNSMLipSMSVTMETSMimSNIQRIIQE-----NERLKQ------EILEKSN 586
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQ-AENARL--EMHFKLKEDH--EKIQHLEEEykkeiNDKEKQvsllliQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 587 R-------IEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLqlkm 659
Cdd:pfam05483 255 KmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 660 tahqKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRK--QLELKVTSLE-EELTDLR--- 733
Cdd:pfam05483 330 ----TEEKEAQMEELNKAKAAHSF--VVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSElEEMTKFKnnk 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 734 -VEKESLEKNLSERKK---------KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVStDQAAAEQLSLVQAELQ- 802
Cdd:pfam05483 404 eVELEELKKILAEDEKlldekkqfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTELEk 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 803 -----TQWEAKCEHLLASAKD---------EHLQQYQEVCAQRDAYQQKLVQ----LQEKCLALQAQITALTKQNEQHIK 864
Cdd:pfam05483 483 eklknIELTAHCDKLLLENKEltqeasdmtLELKKHQEDIINCKKQEERMLKqienLEEKEMNLRDELESVREEFIQKGD 562
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 150010552 865 E----LEKNKSQMSGVEAAASdPSEKVKKIMNQVFQSLRREFELEESY 908
Cdd:pfam05483 563 EvkckLDKSEENARSIEYEVL-KKEKQMKILENKCNNLKKQIENKNKN 609
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
575-865 |
9.57e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSNRIEEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQArvlhaeqEKAKVTEELaaataQVSH 654
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKA-------EEARIEEVM-----KLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 655 LQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ------------AQSKFKSEKQNRKQLELKV 722
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkikaAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 723 tslEEEltDLRVEKESLEKNlSERKKKSAQERSQAEEEI---DEIRKSYQEELDKLRQLLKKTRvsTDQAAAEQLSLVQA 799
Cdd:PTZ00121 1683 ---AEE--DEKKAAEALKKE-AEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEE 1754
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150010552 800 ElqtqwEAKCEHLlasaKDEHLQQYQEVCAQRDAY-QQKLVQLQEKCLALQAQITALTKQNEQHIKE 865
Cdd:PTZ00121 1755 E-----KKKIAHL----KKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
567-909 |
1.26e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENER---LKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTE 643
Cdd:TIGR04523 67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK-LEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 644 ELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELqetsEQAQSKFKSEKQNRKQLELKVT 723
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQIS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 724 SLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDqaaaeQLSLVQAE 800
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTteiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-----QLNQLKSE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 801 LQTQWEAKCEHLLASAKDEHLQ---QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVE 877
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350
....*....|....*....|....*....|..
gi 150010552 878 AAASDPSEKVKKIMNQVfQSLRREFELEESYN 909
Cdd:TIGR04523 377 KENQSYKQEIKNLESQI-NDLESKIQNQEKLN 407
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
573-873 |
1.32e-09 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 62.35 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 573 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLmmekrnnslqtATENTQARVLHAEQEKAKVTEEL-AAATAQ 651
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAAL-----------AGTEATSGASRSAQDLAELLSSFsGSSTTD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHLQLKMTAHQKKET---ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE 728
Cdd:pfam05667 292 TGLTKGSRFTHTEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 729 LTDLRVEKESLEKNLsERKKKSAQERSQAEEEIdeirksyqeelDKLRQLLkktrvstdQAAAEQLslvqAELQTQWEAK 808
Cdd:pfam05667 372 LEELKEQNEELEKQY-KVKKKTLDLLPDAEENI-----------AKLQALV--------DASAQRL----VELAGQWEKH 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150010552 809 CEHLLasakdEHLQQYQEVCA-QRDAYQQKLVQLQ---EKCLalqaQITALTKQNEQHIKELEKNKSQM 873
Cdd:pfam05667 428 RVPLI-----EEYRALKEAKSnKEDESQRKLEEIKelrEKIK----EVAEEAKQKEELYKQLVAEYERL 487
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
191-309 |
1.80e-09 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 191 GPAVEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLRLKLGSgkVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVI 270
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTL----IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
|
90 100 110
....*....|....*....|....*....|....*....
gi 150010552 271 GWtqATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 309
Cdd:PRK10902 232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
664-881 |
2.68e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 664 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskfksekqnRKQLELKVTSLEEELTDLRVEKESLEKnl 743
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----------LEELEAELEELREELEKLEKLLQLLPL-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 744 serkkksAQERSQAEEEIDEirksYQEELDKLRQllKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDE---H 820
Cdd:COG4717 131 -------YQELEALEAELAE----LPERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 821 LQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkQNEQHIKELEKNKSQMSGVEAAAS 881
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLLIAA 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-741 |
2.73e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 517 TEIRMAVSKVADKMDHLMTKVEELQKhsagnsmlipsmsvtmETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKIS 596
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 597 ELIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 656
Cdd:TIGR02168 334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 657 lkmtAHQKKETELQMQLTESLKETDL--LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV 734
Cdd:TIGR02168 414 ----DRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
....*..
gi 150010552 735 EKESLEK 741
Cdd:TIGR02168 490 RLDSLER 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
565-914 |
2.82e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 565 SNIQRIIQENErlkQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLqtatENTQARVLHAEQEKAKVTEE 644
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 645 LAAATAQVSHLQLKMTAHQKKETELQmQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtS 724
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----E 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 725 LEEELTDLRVEKESLEKNLSE---------------------RKKKSAQERSQAEEEIDEIRKS---YQEELDKLRQLLK 780
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEEleerhelyeeakakkeelerlKKRLTGLTPEKLEKELEELEKAkeeIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 781 --KTRVSTDQAAAEQLS-------LVQAELQtqwEAKCEHLLASAKDEH---LQQYQEVCAQRDAYQQKLVQLqEKCLAL 848
Cdd:PRK03918 416 elKKEIKELKKAIEELKkakgkcpVCGRELT---EEHRKELLEEYTAELkriEKELKEIEEKERKLRKELREL-EKVLKK 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 849 QAQITALTKQNEQhIKELEK--NKSQMSGVEAAASDpSEKVKKIMNQV---FQSLRREFELEESYNGRTIL 914
Cdd:PRK03918 492 ESELIKLKELAEQ-LKELEEklKKYNLEELEKKAEE-YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAE 560
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
575-802 |
5.80e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.53 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAKVTEELAAATAQ 651
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTD 731
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 732 LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQ 802
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
573-902 |
6.90e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.37 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 573 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTatENTQARVLHAEQEKAKVTEELAAataQV 652
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCG---SC 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 653 SHLQLKMTAHQKKETeLQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 732
Cdd:TIGR00618 511 IHPNPARQDIDNPGP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 733 RVEKESLEKnlsERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQTQWEAKCEHL 812
Cdd:TIGR00618 590 QNITVRLQD---LTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKL-TALHALQLTLTQERVREHA 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 813 LASAKDEhLQQYQEVCAQRDAYQQKLVQLQEKCLALqAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMN 892
Cdd:TIGR00618 665 LSIRVLP-KELLASRQLALQKMQSEKEQLTYWKEML-AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
330
....*....|
gi 150010552 893 QVFQSLRREF 902
Cdd:TIGR00618 743 QSLKELMHQA 752
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
614-781 |
8.36e-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: 57.63 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 614 EKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMtahQKKETELQMqlteslketdlLRGQLTKVQAK 693
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEIEE-----------VEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 694 LSELQETSE-QA-QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 771
Cdd:COG1579 82 LGNVRNNKEyEAlQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 150010552 772 LDKLRQLLKK 781
Cdd:COG1579 162 EAEREELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
582-870 |
8.89e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 582 LEKSNRIEEQNDKISELIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQaRVLHAEQEKA 639
Cdd:PRK03918 100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLG-EVIKEIKRRI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 640 KVTEELAAATAQVshlqlkmtahQKKETELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSE---QAQSKFK 709
Cdd:PRK03918 179 ERLEKFIKRTENI----------EELIKEKEKELEEVLREINEisselpeLREELEKLEKEVKELEELKEeieELEKELE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 710 SEKQNRKQLELKVTSLEEELTDLRVEKESLEKNlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRvstdqa 789
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 790 aaEQLSLVQAELQtQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQ---QKLVQLQEkclaLQAQITALTKQN-EQHI 863
Cdd:PRK03918 321 --EEINGIEERIK-ELEEKEERLeeLKKKLKELEKRLEELEERHELYEeakAKKEELER----LKKRLTGLTPEKlEKEL 393
|
....*..
gi 150010552 864 KELEKNK 870
Cdd:PRK03918 394 EELEKAK 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
510-775 |
9.53e-09 |
|
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: 60.08 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 510 TEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSmsvtmetsmIMSNIQRIIQENERLKQEILEKSNRIE 589
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE---------LEEDLSSLEQEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 590 EQNDKISEL------------------IERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 651
Cdd:TIGR02169 769 ELEEDLHKLeealndlearlshsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 -------VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 724
Cdd:TIGR02169 849 iksiekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 725 LEEELTDL----RVEKESLEKNLSERKKKSAQERSQAE---------------EEIDEIRKSYQEELDKL 775
Cdd:TIGR02169 929 LEEELSEIedpkGEDEEIPEEELSLEDVQAELQRVEEEiralepvnmlaiqeyEEVLKRLDELKEKRAKL 998
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-801 |
1.01e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLK--QEILEKsnrIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqtaTENTQARVLHAEQEKAK 640
Cdd:COG4913 223 TFEAADALVEHFDDLEraHEALED---AREQIELLEPIRELAERYAAARERLAELE-------YLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQ-AKLSELQETSEQAQSKFKSEKQNRKQLE 719
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDE-------LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 720 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQL------LKKTRVSTDQ----- 788
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeiasLERRKSNIPArllal 445
|
250
....*....|....*
gi 150010552 789 --AAAEQLSLVQAEL 801
Cdd:COG4913 446 rdALAEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
563-805 |
1.15e-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: 58.62 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVlhaEQEKAKVT 642
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 643 EELAAA--TAQVSHLQLKMTAHQKKETELQMQLTESLKETDllRGQLTKVQAKLSELQetseqaqskfksekQNRKQLEL 720
Cdd:COG4942 108 ELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELA--------------ALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 721 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEElDKLRQLLKKTRVSTDQAAAEQLSLVQAE 800
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 150010552 801 LQTQW 805
Cdd:COG4942 251 LKGKL 255
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
595-903 |
1.23e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 595 ISELIERNQRYvEQSNLMMEK-------RNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKET 667
Cdd:pfam01576 189 ISDLEERLKKE-EKGRQELEKakrklegESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 668 ELQMQLTESLKETDLLRGQLTKV-----------QAKLSELQET--SEQAQSKFKSEKQN-----RKQLELKVTSLEEEL 729
Cdd:pfam01576 268 ELEAQISELQEDLESERAARNKAekqrrdlgeelEALKTELEDTldTTAAQQELRSKREQevtelKKALEEETRSHEAQL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 730 TDLRVE------------------KESLEKNL----SERKKKSAQERS--QAEEEIDEIRKSYQEELDKLRQLLKKT-RV 784
Cdd:pfam01576 348 QEMRQKhtqaleelteqleqakrnKANLEKAKqaleSENAELQAELRTlqQAKQDSEHKRKKLEGQLQELQARLSESeRQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 785 STDqaAAEQLSLVQAELQT------QWEAKCEHLL--ASAKDEHLQQYQEVCA----QRDAYQQKLVQLQEKCLALQAQI 852
Cdd:pfam01576 428 RAE--LAEKLSKLQSELESvssllnEAEGKNIKLSkdVSSLESQLQDTQELLQeetrQKLNLSTRLRQLEDERNSLQEQL 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 150010552 853 -------TALTKQNEQHIKELEKNKSQMSGvEAAASDPSEKVKKIMNQVFQSLRREFE 903
Cdd:pfam01576 506 eeeeeakRNVERQLSTLQAQLSDMKKKLEE-DAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
658-803 |
1.48e-08 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 56.07 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 658 KMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskFKSEKQNRKQLELKVTSLEEELTDLRVEKE 737
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 738 SLEknlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtRVstdQAAAEQLSLVQAELQT 803
Cdd:pfam13851 110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
578-870 |
1.88e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 578 KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE---ELAAATAQVSH 654
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsRVDLKLQELQH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 655 LQLKMTAHQKKETE---LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ-SKFKSEKQ-NRKQLEL--------- 720
Cdd:pfam15921 536 LKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELqefkilkdk 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 721 ---KVTSLEEELTDLRVEKESLEKNLSER---KKKSAQERSQAEEEIDEIR---KSYQEELDKLRQLLK---KTRVSTDQ 788
Cdd:pfam15921 616 kdaKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRnelNSLSEDYEVLKRNFRnksEEMETTTN 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 789 AAAEQLSLVQAEL-QTQWEAKC-EHLLASAKDEHLQQYQEVCAQR---DAYQQKLVQLQEkclalqaqitALTKQN-EQH 862
Cdd:pfam15921 696 KLKMQLKSAQSELeQTRNTLKSmEGSDGHAMKVAMGMQKQITAKRgqiDALQSKIQFLEE----------AMTNANkEKH 765
|
....*...
gi 150010552 863 IKELEKNK 870
Cdd:pfam15921 766 FLKEEKNK 773
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
641-893 |
2.09e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 720
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 721 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQ----ERSQ------AEEE---IDEIRKsYQEELDKLRQLLKKTR-VST 786
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLRKEierlEWRQqtevlsPEEEkelVEKIKE-LEKELEKAKKALEKNEkLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 787 DQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEHLQQYQ---EVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI 863
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKeadELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270
....*....|....*....|....*....|..
gi 150010552 864 KELE--KNKSQMSGVEAAASDPSEKVKKIMNQ 893
Cdd:COG1340 244 KELKklRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
514-914 |
2.12e-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: 58.83 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 514 QHNTEIRMAVSKVADKMDHLMTKVE-ELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQN 592
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELtKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 593 DKISELIERNQRYVEQSNLMMEKRNNSLQTatENTQARVLHAEQEKAKVTEELAaataqvshlqlkmtahQKKETELQMQ 672
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEA--EELLADRVQEAQDKINEELKLL----------------KQKIDEEEEE 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 673 LTESLKEtdllrgQLTKVQAKLSELQETSEQAQSKFKSEKQ-NRKQLELKVTSLEEELTdlrvEKESLEKNLSERKKKSA 751
Cdd:pfam02463 752 EEKSRLK------KEEKEEEKSELSLKEKELAEEREKTEKLkVEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQ 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 752 QERSQAEEEIDEIRKSYQEEL--DKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvca 829
Cdd:pfam02463 822 LLIEQEEKIKEEELEELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE--- 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 830 qrdayQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQ---MSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE 906
Cdd:pfam02463 899 -----KKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEpeeLLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
....*...
gi 150010552 907 SYNGRTIL 914
Cdd:pfam02463 974 KVNLMAIE 981
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
625-853 |
3.43e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 625 ENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKE--TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 702
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 703 QAQSKFKSEKQNRKQL--ELKVTSLEEELTDLRVEKESLEKNLSERkkksAQERSQAEEEIDEIRKSYQEELDKLRQLLk 780
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQRILASL- 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150010552 781 KTRVSTDQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEkcLALQAQIT 853
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALT 384
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
636-807 |
3.57e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 636 QEKAKVTEELAAATAQVSHL--QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQ 713
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELeeELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 714 NRKQLElkvtSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 793
Cdd:COG4717 161 LEEELE----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170
....*....|....
gi 150010552 794 LSLVQAELQTQWEA 807
Cdd:COG4717 237 EAAALEERLKEARL 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
555-793 |
3.59e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.46 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 555 SVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA 634
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 635 EQEKaKVTEELAAATAQVSHLQLKMTAHQKKETELQ----MQLTESL---KETDL------LRGQLTKVQAKL---SELQ 698
Cdd:COG1340 85 EKLN-ELREELDELRKELAELNKAGGSIDKLRKEIErlewRQQTEVLspeEEKELvekikeLEKELEKAKKALeknEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 699 ETSEQAQSKFKSEKQNRKQLE----------LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsY 768
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKelaeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE-L 242
|
250 260
....*....|....*....|....*
gi 150010552 769 QEELDKLRQLLKKTRVSTDQAAAEQ 793
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEE 267
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-913 |
3.69e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 573 ENERLKQEILEKSN--RIEEQNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQARVLHAEQEKAKVTE--ELAA 647
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEakKKAE 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 648 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-----------RK 716
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaeekKK 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 717 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE---------EIDEIRKSyQEELDKLRQLLKKtrvSTD 787
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakkkaeeakKADEAKKK-AEEAKKAEEAKKK---AEE 1468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 788 QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvcAQRDAyqQKLVQLQEKCLALQAQITALTKQNEQHIKELE 867
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE--AKKKA--DEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 150010552 868 KNKSQmSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTI 913
Cdd:PTZ00121 1545 KKKAD-ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
566-905 |
4.70e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 566 NIQRIIQE----NERLKQEILEKSN---RIEEQNDKISELIErnqryvEQSNLMMEKRnnSLQTATENTQARVLHAEQEK 638
Cdd:PRK03918 166 NLGEVIKEikrrIERLEKFIKRTENieeLIKEKEKELEEVLR------EINEISSELP--ELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 639 akvtEELAAATAQVshlqLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ--AQSKFKSEKQNRK 716
Cdd:PRK03918 238 ----EEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 717 QlelkvtSLEEELTDLRVEKESLEKNLSERKKKSAqERSQAEEEIDEIRKSYQE------ELDKLRQLLKKTRVSTDQAA 790
Cdd:PRK03918 310 R------EIEKRLSRLEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 791 AEQLSLVQAELQTQWEAKCEHLLASAK-DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaltkqnEQHIKEL-EK 868
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------EEHRKELlEE 456
|
330 340 350
....*....|....*....|....*....|....*..
gi 150010552 869 NKSQMSGVEaaasdpsEKVKKIMNQVFQSLRREFELE 905
Cdd:PRK03918 457 YTAELKRIE-------KELKEIEEKERKLRKELRELE 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
645-871 |
4.74e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 645 LAAATAQVSHLQLKMTAHQKKETELQmQLtESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsekqnrkqlELKVTS 724
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE-QI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 725 LEEELTDLRVEKESLEknlsERKKKSAQERSQAEEEIDEIRKSYQE----ELDKLRQLLKktrvstdqAAAEQLSLVQAE 800
Cdd:COG4913 293 LEAELEELRAELARLE----AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIE--------RLERELEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150010552 801 LQtQWEAKCEHL---LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH---IKELEKNKS 871
Cdd:COG4913 361 RA-RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLERRKS 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
634-832 |
6.13e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 634 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKfksEKQ 713
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 714 NRKQLElKVTSlEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDEIRKSY---QEELDKLRQLLKKTRVSTDQAA 790
Cdd:COG1579 78 YEEQLG-NVRN-NKEYEALQKEIESLKRRISDLED----EILELMERIEELEEELaelEAELAELEAELEEKKAELDEEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 150010552 791 AEqlslVQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRD 832
Cdd:COG1579 152 AE----LEAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
656-867 |
6.43e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 656 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFkseKQNRKQLE---------------- 719
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKL---RQAQAELEalkddndeetretlst 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 720 LKVTSLEEELTDLRVEKESLEKNLSERKK-----KSAQERSQAeeEIDEirksYQEELDKLRQLLKKTRVSTDQAAAEQL 794
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSqlvslQTQPERAQA--ALYA----NSQRLQQIRNLLKGGKVGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 795 SLVQAELQtqweakcehlLASAKDEHLQQ-----------YQevcAQRDAYQQKLVQLQEKCLALQAQITA-LTKQNEQH 862
Cdd:PRK11281 195 VLLQAEQA----------LLNAQNDLQRKslegntqlqdlLQ---KQRDYLTARIQRLEHQLQLLQEAINSkRLTLSEKT 261
|
....*
gi 150010552 863 IKELE 867
Cdd:PRK11281 262 VQEAQ 266
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
575-887 |
7.06e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSN-----RIEEQNDKISELIERNQRYVEQSNLMMEKRNN--SLQTATENTQARVLHAEQEKAKVTEELAA 647
Cdd:PRK02224 190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEadEVLEEHEERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 648 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 720
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 721 KVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQ------EELDKLRQLLKKTRvstdQAAA 791
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREER----DELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 792 EQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQE----VCAQRDaYQQKLVQLQEKCLALQAQITALTKQNEQhIKE 865
Cdd:PRK02224 426 EREAELEATLRTARErvEEAEALLEAGKCPECGQPVEgsphVETIEE-DRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
330 340
....*....|....*....|..
gi 150010552 866 LEKNKSQMSGVEAAASDPSEKV 887
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELI 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
663-906 |
8.56e-08 |
|
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: 56.99 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 663 QKKETELQMQLTEslkeTDLLRGQ--LTKVQAKLSELQETSEQAQsKFKSEKQNRKQLELKVTsleeeLTDLRVEKESLE 740
Cdd:TIGR02168 173 RRKETERKLERTR----ENLDRLEdiLNELERQLKSLERQAEKAE-RYKELKAELRELELALL-----VLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 741 KNLSErKKKSAQERSQAEEEIDEirksYQEELDKLRqlLKKTRVSTDQAAAeqlslvQAELQTQWEAKcehllaSAKDEH 820
Cdd:TIGR02168 243 ELQEE-LKEAEEELEELTAELQE----LEEKLEELR--LEVSELEEEIEEL------QKELYALANEI------SRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 821 LQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRR 900
Cdd:TIGR02168 304 KQILRE----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
....*.
gi 150010552 901 EFELEE 906
Cdd:TIGR02168 374 LEELEE 379
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
655-879 |
8.81e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 55.31 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 655 LQLKMTAHQKKETELQMQLtESLKETDL--LRGQL-------TKVQAKLSELQETSEQAQSKFKSEKQNRkqlelkvTSL 725
Cdd:pfam00038 30 LETKISELRQKKGAEPSRL-YSLYEKEIedLRRQLdtltverARLQLELDNLRLAAEDFRQKYEDELNLR-------TSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 726 EEELTDLR--VEKESLEKNLSERKKKSAQErsqaeeEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQA--EL 801
Cdd:pfam00038 102 ENDLVGLRkdLDEATLARVDLEAKIESLKE------ELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 802 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRD-------AYQQKLVQLQEKCLALQAQITALTKQN-----------EQHI 863
Cdd:pfam00038 176 RAQYEEIAAKNREEAEEWYQSKLEELQQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKaslerqlaeteERYE 255
|
250
....*....|....*.
gi 150010552 864 KELEKNKSQMSGVEAA 879
Cdd:pfam00038 256 LQLADYQELISELEAE 271
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
579-777 |
9.74e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 579 QEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLK 658
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-----------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 659 MTAHqKKETELQmQLTeslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvTSLEEELTDLRVEKES 738
Cdd:COG1579 82 LGNV-RNNKEYE-ALQ---KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 150010552 739 LEKNLSERKKksaqERSQAEEEIDE-IRKSYqeelDKLRQ 777
Cdd:COG1579 154 LEAELEELEA----EREELAAKIPPeLLALY----ERIRK 185
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
571-906 |
1.84e-07 |
|
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: 54.54 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 571 IQENERLKQEILEKSNRIEEqndkiseliernqryveqsnlMMEKRNnslqtatENTQARVLHAEQEKAKVTEELAAAta 650
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDE---------------------MMEEER-------ERALEEEEEKEEERKEERKRYRQE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 651 qvshLQLKMTAHQKKEtelQMQLTESLKETDLLRGQLTKVQAKlselqetsEQAQSKFKSEKQNRKQLELKVTSleeELT 730
Cdd:pfam13868 78 ----LEEQIEEREQKR---QEEYEEKLQEREQMDEIVERIQEE--------DQAEAEEKLEKQRQLREEIDEFN---EEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 731 DLRVEKESLEKNLSERK-----KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVstDQAAAEQL--SLVQAELQT 803
Cdd:pfam13868 140 AEWKELEKEEEREEDERileylKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELraKLYQEEQER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 804 QW-------EAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQhiKELEKNKSQMSGV 876
Cdd:pfam13868 218 KErqkereeAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE--KRRMKRLEHRREL 295
|
330 340 350
....*....|....*....|....*....|
gi 150010552 877 EAAASDPSEKVKKIMNQVFQSLRREFELEE 906
Cdd:pfam13868 296 EKQIEEREEQRAAEREEELEEGERLREEEA 325
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
571-905 |
2.36e-07 |
|
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: 54.15 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 571 IQENE----RLKQEIL------EKSNRIEEQNDKISELIERNQRYveqsNLMMEKRNnslqtatENTQARVLHAEQEKAK 640
Cdd:pfam13868 1 LRENSdelrELNSKLLaakcnkERDAQIAEKKRIKAEEKEEERRL----DEMMEEER-------ERALEEEEEKEEERKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEELAAAtaqvshLQLKMTAHQKKEtelQMQLTESLKETDLLRGQLTKVQAKlselqetsEQAQSKFKSEKQNRKQLEL 720
Cdd:pfam13868 70 ERKRYRQE------LEEQIEEREQKR---QEEYEEKLQEREQMDEIVERIQEE--------DQAEAEEKLEKQRQLREEI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 721 KVTSleeELTDLRVEKESLEKNLSERK-----KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVstDQAAAEQL- 794
Cdd:pfam13868 133 DEFN---EEQAEWKELEKEEEREEDERileylKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELr 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 795 -SLVQAELQTQW-------EAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQhiKEL 866
Cdd:pfam13868 208 aKLYQEEQERKErqkereeAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE--KRR 285
|
330 340 350
....*....|....*....|....*....|....*....
gi 150010552 867 EKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 905
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-783 |
2.73e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQaRVLHAEQEKAKVTEELA 646
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK-EEELEEQKLKDELESKE 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 647 AATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ-SKFKSEKQNRKQLELKVTSL 725
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEeNNKEEEEERNKRLLLAKEEL 972
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 150010552 726 EEEltDLRVEKESLEKNLSERKKKSAQERsqAEEEIDEIRksyQEELDKLRQLLKKTR 783
Cdd:pfam02463 973 GKV--NLMAIEEFEEKEERYNKDELEKER--LEEEKKKLI---RAIIEETCQRLKEFL 1023
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-906 |
2.97e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILE-----KSNRIEEQNDKisELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 641
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEeaagsRLKRKKKEALK--KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 TEELAAATAQVSHLQlkmtahqkketelqmqlteslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKqLELK 721
Cdd:pfam02463 222 EEEYLLYLDYLKLNE---------------------ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK-EEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 722 VTSLEEE---LTDLRVEKESLE-------KNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA 791
Cdd:pfam02463 280 EKKLQEEelkLLAKEEEELKSEllklerrKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 792 EQLSLVQAELQTQWEAKCEHLLASA-------KDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK 864
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESErlssaakLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 150010552 865 ELEKNKSQMSGVEAaasDPSEKVKKIMNQVFQSLRREFELEE 906
Cdd:pfam02463 440 ELKQGKLTEEKEEL---EKQELKLLKDELELKKSEDLLKETQ 478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-888 |
3.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELA--A 647
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAEEAKKADEAKkkA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 648 ATAQVSHLQLKMTAHQKKETElQMQLTESLKETDLLRGQLTKVQA----------KLSELQETSE--QAQSKFKSEkQNR 715
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKAdeakkaeekkKADELKKAEElkKAEEKKKAE-EAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 716 KQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEE---IDEIRKSyQEELDKLRQLLKKTRVSTDQA 789
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEevmKLYEEEKKMKAEEAKKAEEAkikAEELKKA-EEEKKKVEQLKKKEAEEKKKA 1649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 790 -----AAEQLSLVQAELQTQWEA---KCEHLLASAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNE- 860
Cdd:PTZ00121 1650 eelkkAEEENKIKAAEEAKKAEEdkkKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEe 1727
|
330 340 350
....*....|....*....|....*....|....
gi 150010552 861 ------QHIKELEKNKSQmsgVEAAASDPSEKVK 888
Cdd:PTZ00121 1728 nkikaeEAKKEAEEDKKK---AEEAKKDEEEKKK 1758
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
572-906 |
3.87e-07 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 54.53 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 651
Cdd:pfam15964 367 RQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMD 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHL------QLKMTAHQKKETELQMQ--LTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVT 723
Cdd:pfam15964 447 VTKVcgemryQLNQTKMKKDEAEKEHReyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 724 SLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyqeeldkLRQLLKKTRVSTDQAAAEQLSLV--QAEL 801
Cdd:pfam15964 527 ESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQE--------------LTQKMQQMEAQHDKTVNEQYSLLtsQNTF 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 802 QTQWEAKCeHLLASAKDEHLQQYQEVCAQrdaYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAAS 881
Cdd:pfam15964 593 IAKLKEEC-CTLAKKLEEITQKSRSEVEQ---LSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQ 668
|
330 340
....*....|....*....|....*
gi 150010552 882 DPSEKVKKIMNQVFQSLRREFELEE 906
Cdd:pfam15964 669 ATAQQLVQLLSKQNQLFKERQNLTE 693
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
625-911 |
3.99e-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: 54.80 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 625 ENTQARvlhaEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQL---TESLKETDLLRGQL-----------TKV 690
Cdd:pfam01576 5 EEMQAK----EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLaarkqeleeilHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 691 QAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN----------LSERKKKSAQERSQAEEE 760
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKikkleedillLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 761 IDEIRKSYQEELDKLRQLLKktrvstdqaaaeqlslvqaeLQTQWEAKCEHLLASAKDEHlQQYQEVCAQRDAYQQKLVQ 840
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSK--------------------LKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 841 LQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQsLRREFELEESYNGR 911
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE-LQEDLESERAARNK 289
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
634-885 |
4.32e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 634 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQET-SEQAQSKFKSEK 712
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 713 QNrKQLELKVTSleEELTDLrVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtrVSTDQAAAE 792
Cdd:COG3883 101 SV-SYLDVLLGS--ESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE--LEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 793 QLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQ 872
Cdd:COG3883 175 AQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|...
gi 150010552 873 MSGVEAAASDPSE 885
Cdd:COG3883 247 AGAGAAGAAGAAA 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
672-886 |
4.36e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 672 QLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERkKKSA 751
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 752 QERSQAEEEIDEI--RKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDEHLQQYQEVCA 829
Cdd:COG3883 96 YRSGGSVSYLDVLlgSESFSDFLDRLSAL--SKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 150010552 830 QRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEK 886
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
578-868 |
6.09e-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: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 578 KQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATENtQARVLHAEQEKAKVTEELAAATAQVSHLQL 657
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 658 kmtahQKKETELQMQLTEslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL---ELKVTSLEEELTDLRV 734
Cdd:COG3096 376 -----QLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 735 EKESLEKNLSERKkksaQERSQAEEEIDEIRKSYQ------------EELDKLRQLLKKTRVSTDQAA-----------A 791
Cdd:COG3096 449 KEQQATEEVLELE----QKLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQrlqqlraqlaeL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 792 EQLSLVQAELQTQWEAKCEHL---LASAKD-EHLQQYQEvcAQRDAYQQKLVQLQEKCLALQAQitalTKQNEQHIKELE 867
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIgqqLDAAEElEELLAELE--AQLEELEEQAAEAVEQRSELRQQ----LEQLRARIKELA 598
|
.
gi 150010552 868 K 868
Cdd:COG3096 599 A 599
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
575-746 |
1.06e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENtqarvlhaeqekakvtEELAAATAQ 651
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQLGNVRNN----------------KEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQskfksekqnrKQLELKVTSLEEELTD 731
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKK----------AELDEELAELEAELEE 160
|
170
....*....|....*
gi 150010552 732 LRVEKESLEKNLSER 746
Cdd:COG1579 161 LEAEREELAAKIPPE 175
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
530-865 |
1.12e-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: 52.59 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 530 MDHLMTKVEELQKHSAGNSML--IPSMSVtmetsmimsnIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE 607
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLlvVPRAEL----------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 608 QSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQmQLTESLKETDLLRgql 687
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 688 tkvQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSER----------------KKKSA 751
Cdd:pfam07888 149 ---ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRdtqvlqlqdtittltqKLTTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 752 QERSQAEEEIDEIRKSYQEEL-------DKLRQLLKKTRVSTDQAAAE----------------QLSLVQAELQTQWEAK 808
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLnaserkvEGLGEELSSMAAQRDRTQAElhqarlqaaqltlqlaDASLALREGRARWAQE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 809 CEHLLASAKDEH---------LQQYQEVCAQRDAYQQKL------------VQLQEKCLALQ---AQITALTKQNEQHIK 864
Cdd:pfam07888 306 RETLQQSAEADKdrieklsaeLQRLEERLQEERMEREKLevelgrekdcnrVQLSESRRELQelkASLRVAQKEKEQLQA 385
|
.
gi 150010552 865 E 865
Cdd:pfam07888 386 E 386
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
608-894 |
1.30e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 608 QSNLMMEKRNNSLQTATENTQARvlHAEQEkakvtEELAAATAQVSHLQLKMT----AHQKKETELQMQLTESLKEtdll 683
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREK--QAAAE-----EQLVQANGELEKASREETfartALKNARLDLRRLFDEKQSE---- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 684 rgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL-SERKKKSAQ-------ERS 755
Cdd:pfam12128 666 --KDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVeGALDAQLALlkaaiaaRRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 756 QAEEEIDEIRKSYQEELDKLrqllkktrvSTDQAAAEQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQEvcaQRDA 833
Cdd:pfam12128 744 GAKAELKALETWYKRDLASL---------GVDPDVIAKLKREIRTLERKIEriAVRRQEVLRYFDWYQETWLQ---RRPR 811
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 834 YQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 894
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
568-882 |
1.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 568 QRIIQENERLKQEILEKSNRIEEQNDKISE---------------------LIERN------------------------ 602
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAEterereelaeevrdlrerleeLEEERddllaeaglddadaeavearreel 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 603 -------QRYVEQSNLMMEKRNNSLQTATEN------------TQARVLHAEQEKAKvtEELAAATAQVSHLQLKMTAHQ 663
Cdd:PRK02224 320 edrdeelRDRLEECRVAAQAHNEEAESLREDaddleeraeelrEEAAELESELEEAR--EAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 664 KKETELQMQL------TESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEK-----QNRK---------QLELKV 722
Cdd:PRK02224 398 ERFGDAPVDLgnaedfLEELREErDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEgsphvetieEDRERV 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 723 TSLEEELTDLRVEKESLEK----------------NLSERKKKSAQERSQAEEEIDEiRKSYQEELDKLRQLLKKTRVST 786
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEErleraedlveaedrieRLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAEAEEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 787 DQAAAEQLSLVQAELQTQweAKCEHLLASAKD--EHLQQYQEVCAQRDAYQQKLVQLQEKclalQAQITALTKQNEQHIK 864
Cdd:PRK02224 557 REAAAEAEEEAEEAREEV--AELNSKLAELKEriESLERIRTLLAAIADAEDEIERLREK----REALAELNDERRERLA 630
|
410 420
....*....|....*....|....
gi 150010552 865 ELEKNKSQMSG------VEAAASD 882
Cdd:PRK02224 631 EKRERKRELEAefdearIEEARED 654
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
567-928 |
1.40e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.83 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEI-------LEKSNRIEEQNDKISEL-IERNQRYVEQSNLM-------MEKRNNSLQTATENTQARV 631
Cdd:pfam07111 68 ISRQLQELRRLEEEVrllretsLQQKMRLEAQAMELDALaVAEKAGQAEAEGLRaalagaeMVRKNLEEGSQRELEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 632 LHAEQEKAKVT---EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLsELQET-------- 700
Cdd:pfam07111 148 LHQEQLSSLTQaheEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEEL-EAQVTlveslrky 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 701 -SEQAQSKFKSE--KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam07111 227 vGEQVPPEVHSQtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 778 LLKKTRvstDQAAAEQLSLVQAELQTQWEAK-CEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALT 856
Cdd:pfam07111 307 LLNRWR---EKVFALMVQLKAQDLEHRDSVKqLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 857 KQNEQHIKELEKNKS---QMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE--SYNGR---TILGTIMNTIKMVTLQL 928
Cdd:pfam07111 384 RAQEARRRQQQQTASaeeQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNrlSYAVRkvhTIKGLMARKVALAQLRQ 463
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
668-865 |
1.51e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.38 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 668 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtSLEEEL-------TDLRVEKESLE 740
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENfrletarDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 741 KNLSERK------KKSAQERSQAEEEIDEIRKS-------------YQEELDKLRQLLKKTRVSTDQAAaeqlSLVQAEL 801
Cdd:pfam05622 94 KEVLELQhrneelTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNA----EYMQRTL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150010552 802 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKE 865
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIE 233
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
515-793 |
1.75e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.60 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 515 HNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSN---------IQRIIQENERLKQEILEKS 585
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNqarlqaledLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 586 NRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTahQKK 665
Cdd:PLN02939 177 MRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELI--EVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 666 ETELQMQLTEslKETDLLRGQLTKVQAKLSELQE--------------------------TSEQAQSKFKSEKQNRkQLE 719
Cdd:PLN02939 254 ETEERVFKLE--KERSLLDASLRELESKFIVAQEdvsklsplqydcwwekvenlqdlldrATNQVEKAALVLDQNQ-DLR 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 720 LKVTSLEEELTDLRVEKESLEK-NLSERKKKSAQERSQA-EEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 793
Cdd:PLN02939 331 DKVDKLEASLKEANVSKFSSYKvELLQQKLKLLEERLQAsDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
585-885 |
1.81e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.60 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 585 SNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENT----QARvLHAEQEKAKVTEELAAATAQVSHLQLKMT 660
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnQAR-LQALEDLEKILTEKEALQGKINILEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 661 ahqkkETELQMQLTESLK-ETDLLRGQLTKVQAKLSELQETSEQAqskfksekqnrkqlelkVTSLEEELTDLRVEKESL 739
Cdd:PLN02939 181 -----ETDARIKLAAQEKiHVEILEEQLEKLRNELLIRGATEGLC-----------------VHSLSKELDVLKEENMLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 740 EKNLSERKkksaqersqaeEEIDEIRKSYQE--ELDKLRQLLKKT------RVSTDQAAAEQLSLVQAELqtqWEAKCE- 810
Cdd:PLN02939 239 KDDIQFLK-----------AELIEVAETEERvfKLEKERSLLDASlrelesKFIVAQEDVSKLSPLQYDC---WWEKVEn 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 811 --HLLASAKD--EH----LQQYQEV--------------------CAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH 862
Cdd:PLN02939 305 lqDLLDRATNqvEKaalvLDQNQDLrdkvdkleaslkeanvskfsSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
|
330 340 350
....*....|....*....|....*....|
gi 150010552 863 IKELE------KNKSQMSGVEAAASD-PSE 885
Cdd:PLN02939 385 IKEFQdtlsklKEESKKRSLEHPADDmPSE 414
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
566-805 |
2.00e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 566 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERN-----QRY----VEQSNLMMEKRNNSLQTATE-----NTQARV 631
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLstlsLRQLESRLAQTLDQLQNAQNdlaeyNSQLVS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 632 LHAEQEKAKVteELAAATAQVSHL--QLKMTAHQKKET--ELQMQLTESLKETDLLRGQLTKVQAKLSELQETsEQAQSK 707
Cdd:PRK11281 154 LQTQPERAQA--ALYANSQRLQQIrnLLKGGKVGGKALrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDL-LQKQRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 708 FKSEKQNRkqlelkvtsLEEELTDLRvekESL-EKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVST 786
Cdd:PRK11281 231 YLTARIQR---------LEHQLQLLQ---EAInSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKAT 298
|
250 260
....*....|....*....|
gi 150010552 787 DQAAaeqlSLVQAELQT-QW 805
Cdd:PRK11281 299 EKLN----TLTQQNLRVkNW 314
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
693-812 |
2.16e-06 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 48.45 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 693 KLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV-------EKESLEKNLSERKKK---SAQERSQA----- 757
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHknqqleeEVEKLEEQLKEAKEKaeeSEKLKTNNenltr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150010552 758 -----EEEIDEIRKSYQEELDKLRQllkktrvsTDQAAAEQLSLVQAELQT--QWEAKCEHL 812
Cdd:pfam12718 81 kiqllEEELEESDKRLKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
572-903 |
2.19e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 651
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHL--QLKMTAHQKKETE-----LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 724
Cdd:pfam01576 498 RNSLqeQLEEEEEAKRNVErqlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 725 LEEELTDLRVEKESLEKNLS--ERKKKS---------------AQERSQAE------------------------EEIDE 763
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSnlEKKQKKfdqmlaeekaisaryAEERDRAEaeareketralslaraleealeakEELER 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 764 IRKSYQEELDKL----------RQLLKKTRVSTDQAAAE---QLSLVQAELQTQWEAK--CEHLLASAKDEHLQQYQevc 828
Cdd:pfam01576 658 TNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEmktQLEELEDELQATEDAKlrLEVNMQALKAQFERDLQ--- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 829 AQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI---KELEKN-KSQMSGVEAAASDPSEKVK--KIMNQVFQSLRREF 902
Cdd:pfam01576 735 ARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakKKLELDlKELEAQIDAANKGREEAVKqlKKLQAQMKDLQREL 814
|
.
gi 150010552 903 E 903
Cdd:pfam01576 815 E 815
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
635-908 |
2.74e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 635 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 714
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 715 RKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQL 794
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 795 SL-VQAELQTQWEAKCehllasakdEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSqm 873
Cdd:TIGR00618 339 SIeEQRRLLQTLHSQE---------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR-- 407
|
250 260 270
....*....|....*....|....*....|....*
gi 150010552 874 sgvEAAASDPSEKVKKIMNQVFQSLRREFELEESY 908
Cdd:TIGR00618 408 ---EQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
593-882 |
2.76e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 593 DKISELIERNQRYVeqSNLMMEKRNNslqtATENTQaRVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQ 672
Cdd:PRK04863 257 DLFKHLITESTNYV--AADYMRHANE----RRVHLE-EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 673 LtESLKEtdllrgQLTKVQaklselqeTSEQAQskfksEKQNRKQLELkvtsleEELTDLRVEKESLEKNLSERKKKSAQ 752
Cdd:PRK04863 330 Y-QAASD------HLNLVQ--------TALRQQ-----EKIERYQADL------EELEERLEEQNEVVEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 753 ERSQAEEEIDEIRK---SYQEELDKLR----------QLLKKTRVSTDQA--AAEQLSLVQAELQTQWEAKCEHLLA--- 814
Cdd:PRK04863 384 RAEAAEEEVDELKSqlaDYQQALDVQQtraiqyqqavQALERAKQLCGLPdlTADNAEDWLEEFQAKEQEATEELLSleq 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 815 ------SAKDEHLQQYQEVCA-----QRDAYQQKLVQL-----QEKCLALQAQitaltkQNEQHIKELEKNKSQMSGVEA 878
Cdd:PRK04863 464 klsvaqAAHSQFEQAYQLVRKiagevSRSEAWDVARELlrrlrEQRHLAEQLQ------QLRMRLSELEQRLRQQQRAER 537
|
....
gi 150010552 879 AASD 882
Cdd:PRK04863 538 LLAE 541
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
643-868 |
3.47e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 643 EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQN 714
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladetlADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 715 RKQLELkvtsLEEELTDLRVEKESLEkNLSERKKKSAQERSQAEEEIDEI-----RK---SYQEEL----------DKLR 776
Cdd:COG3096 916 GKALAQ----LEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALsevvqRRphfSYEDAVgllgensdlnEKLR 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 777 QLLK-------KTRVSTDQAAAE--QLSLVQAELQTQWEAKCEhLLASAKDEhLQQY-------QEVCAQ--RDAYQQKL 838
Cdd:COG3096 991 ARLEqaeearrEAREQLRQAQAQysQYNQVLASLKSSRDAKQQ-TLQELEQE-LEELgvqadaeAEERARirRDELHEEL 1068
|
250 260 270
....*....|....*....|....*....|
gi 150010552 839 VQLQEKCLALQAQITALTKQNEQHIKELEK 868
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
656-883 |
3.50e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 49.61 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 656 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL-------------ELKV 722
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeilaSLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 723 TSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAE---EEIDEIRKsyqeELDKLRQLLKKTRVSTDQAAAEQLSLVQA 799
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPEraqQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 800 ELQtqweakcehlLASAKDEHLQQYQEVC--------AQRDAYQQKLVQLQEKCLALQAQItaltkqNEQHIKELEKN-- 869
Cdd:pfam12795 157 ELA----------ALKAQIDMLEQELLSNnnrqdllkARRDLLTLRIQRLEQQLQALQELL------NEKRLQEAEQAva 220
|
250
....*....|....
gi 150010552 870 KSQMSGVEAAASDP 883
Cdd:pfam12795 221 QTEQLAEEAAGDHP 234
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
578-758 |
3.93e-06 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 50.99 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 578 KQEILEKS-NRIEEqndKISELIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARVLHAEQEKAKVTEELAAATAQ 651
Cdd:pfam15066 357 KQQVFVDIiNKLKE---NVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQLELKKIKVN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHLQLK-MTAHQKKETE----LQMQLTESLKETDLLRGQLTKvqaklSELQETSEQAQSKFKSEKQNRKQLELkvtSLE 726
Cdd:pfam15066 428 YVHLQERyITEMQQKNKSvsqcLEMDKTLSKKEEEVERLQQLK-----GELEKATTSALDLLKREKETREQEFL---SLQ 499
|
170 180 190
....*....|....*....|....*....|...
gi 150010552 727 EELTdlRVEKESLEknlsERKK-KSAQERSQAE 758
Cdd:pfam15066 500 EEFQ--KHEKENLE----ERQKlKSRLEKLVAQ 526
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-1011 |
4.05e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 573 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE--ELAAATA 650
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 651 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA-----------KLSELQETSEQ---AQSKFKSEKQNRK 716
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeakkkaeeakKADEAKKKAEEakkAEEAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 717 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE--------EIDEIRKSyqEELDKLRQLLK--KTRVST 786
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaeeakKADEAKKA--EEAKKADEAKKaeEKKKAD 1549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 787 DQAAAEQLSLVQAELQTQWEAKCEH--LLASAKDEHLQQYQEvcaQRDAYQQKLVQLQEKCLALQAQitaltKQNEQHIK 864
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAK-----KAEEAKIK 1621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 865 --ELEKNKSQMSGVEAAASDPSEKVKKImnqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeQEKEESSSE 942
Cdd:PTZ00121 1622 aeELKKAEEEKKKVEQLKKKEAEEKKKA-----EELKKAEE--------------ENKIKAAEEA------KKAEEDKKK 1676
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 943 EEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQV--VEEAVPLPPQALTTSQDGHRRKGD 1011
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
664-779 |
4.14e-06 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 47.25 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 664 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN----RKQL-ELK--VTSLEEELTDLRVEK 736
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLhaedIKALqALReeLNELKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 150010552 737 ESLEKNLSERKKKSAQERSQAEEEIDEIRKSYqEELDKLRQLL 779
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
575-855 |
4.43e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSNRIEEQN---DKISELIERNQRYVEQSNLMMEKRNNSL---QTATENTQARVL---HAEQ--EKAK--- 640
Cdd:PRK04863 351 ERYQADLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIqyqQAVQalERAKqlc 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 ----------------VTEELAAATAQVSHLQLKMTAHQ--KKETELQMQLTESL-----------KETDLLR------- 684
Cdd:PRK04863 431 glpdltadnaedwleeFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIagevsrseawdVARELLRrlreqrh 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 685 --GQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEid 762
Cdd:PRK04863 511 laEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQQ-- 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 763 eirksyQEELDKLRQLLKKTRVS--TDQAAAEQLSlvqaelqtqwEAKCEHLLASAK-DEHLQQYQEvcaQRDAYQQKLV 839
Cdd:PRK04863 588 ------LEQLQARIQRLAARAPAwlAAQDALARLR----------EQSGEEFEDSQDvTEYMQQLLE---RERELTVERD 648
|
330
....*....|....*.
gi 150010552 840 QLQEKCLALQAQITAL 855
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
194-265 |
7.18e-06 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 47.02 E-value: 7.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150010552 194 VEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLrLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVG 265
Cdd:COG1047 1 IEKGDVVTLHYTLKL----EDGEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
688-887 |
7.66e-06 |
|
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: 48.80 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 688 TKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKEsleknlSERKKKSAQeRSQAEEEIDEIRKS 767
Cdd:pfam15397 63 KQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQ-IANLVRQLQQLKDS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 768 YQEELDKLRQLLKKTRvstdqaaaeqlslvqAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLvqlqEKCLA 847
Cdd:pfam15397 136 QQDELDELEEMRRMVL---------------ESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVM----LKEIE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 150010552 848 lqaqitaltkQNEQHIKELEKN----KSQMSGVEAAASDPSEKV 887
Cdd:pfam15397 197 ----------QFREFIDELEEEipklKAEVQQLQAQRQEPREVI 230
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
951-1164 |
9.16e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 951 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 1030
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1031 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1109
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 150010552 1110 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1164
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
511-879 |
1.10e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 511 EARQhntEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEE 590
Cdd:COG3096 289 ELRR---ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 591 QNDKISELIERNQRYVEQSNLmMEKRNNSL-------QTATENTQARVLHAEQ-----EKAK------------VTEELA 646
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEA-AEEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARalcglpdltpenAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 647 AATAQVSHL---------QLKMTAHQKKETELQMQLTESL-----------KETDLLR---------GQLTKVQAKLSEL 697
Cdd:COG3096 445 AFRAKEQQAteevleleqKLSVADAARRQFEKAYELVCKIageversqawqTARELLRryrsqqalaQRLQQLRAQLAEL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 698 QETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEeldkLRQ 777
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE----LAA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 778 LLKKTRVStdQAAAEQLslvqaelqtqweakCEHLlasakDEHLQQYQEVcaqrDAYQQKLVQLQEKCLALQAQITALTK 857
Cdd:COG3096 600 RAPAWLAA--QDALERL--------------REQS-----GEALADSQEV----TAAMQQLLEREREATVERDELAARKQ 654
|
410 420
....*....|....*....|..
gi 150010552 858 QNEQHIKELeknkSQMSGVEAA 879
Cdd:COG3096 655 ALESQIERL----SQPGGAEDP 672
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
571-776 |
1.19e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 571 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATA 650
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 651 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQ------AKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 724
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 150010552 725 LEEELTDLRVEKESLEKNLSERKKKSAQERSQ-AEEEIDEIrksyQEELDKLR 776
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEEAREDKErAEEYLEQV----EEKLDELR 673
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
514-906 |
1.33e-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: 49.66 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 514 QHNTEIRMAVSKVADKMDHLMTKVEELQ-----KHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRI 588
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTEselkkKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 589 EEQNDKISEL----------------IERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLHAEQEKAKVTEELAAATAQV 652
Cdd:TIGR00606 768 EEQETLLGTImpeeesakvcltdvtiMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 653 SHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQlelkVTSLEEELTDL 732
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLEKD 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 733 RVEKESLEKNLSERKKKSAQERSQAEEEIDEI---RKSYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaELQTQWEAKC 809
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQDGKDDYLKQKETELNTVNAQLE----ECEKHQEKIN 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 810 EHLLASAKDEHLQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELekNKSQMSGVEAAASDPSEKVKK 889
Cdd:TIGR00606 998 EDMRLMRQDIDTQKIQE----------RWLQDNLTLRKRENELKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDL 1065
|
410
....*....|....*..
gi 150010552 890 IMNQVFQSLRREFELEE 906
Cdd:TIGR00606 1066 IKRNHVLALGRQKGYEK 1082
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
575-873 |
1.70e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEIleksNRIEEQNDKISELIERNQRYVEQSNLMMekrNNSLQTATEntqarvlhAEQEkakvtEELAAATAQVSH 654
Cdd:PRK04863 789 EQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFI---GSHLAVAFE--------ADPE-----AELRQLNRRRVE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 655 LQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQNRKQLELkvtsLE 726
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LE 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 727 EELTDLRVEKESLEK-----NLSERKKKSAQERSQAEEEIDEIRK--SYQEEL----------DKLRQLLK--------- 780
Cdd:PRK04863 925 PIVSVLQSDPEQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAemlaknsdlnEKLRQRLEqaeqertra 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 781 KTRVSTDQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEhLQQY---------QEVCAQRDAYQQKLVQLQEKCLALQAQ 851
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASLKSSYDAKRQ-MLQELKQE-LQDLgvpadsgaeERARARRDELHARLSANRSRRNQLEKQ 1082
|
330 340
....*....|....*....|....*.
gi 150010552 852 IT----ALTKQNEQhIKELEKNKSQM 873
Cdd:PRK04863 1083 LTfceaEMDNLTKK-LRKLERDYHEM 1107
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
663-854 |
1.81e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.92 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 663 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQ---ETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL 739
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 740 EKNLSERKKKSAQERSQAEEEIDEIRKSYQEE-----------LDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQwEAK 808
Cdd:pfam05622 383 KEQIEELEPKQDSNLAQKIDELQEALRKKDEDmkameerykkyVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEK-DKK 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 809 CEHLLASAKDEHLQQYQE------------VCAQRDAYQQKLVQLQ---EKCLALQAQITA 854
Cdd:pfam05622 462 IEHLERDFEKSKLQREQEeklivtawynmgMALHRKAIEERLAGLSspgQSFLARQRQATN 522
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
634-756 |
2.01e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 45.32 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 634 AEQEKAKVTEELAAATAQVSHLQLKM--------TAHQKKETELQMQlTESLKETDLLRGQLTKVQAKLSELQETSEQAQ 705
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLekqaeiarEAQQNYERELVLH-AEDIKALQALREELNELKAEIAELKAEAESAK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 150010552 706 SKFKSEKQnrkqlelkvtSLEEEltdlrveKESLEKNLSERKKKSAQERSQ 756
Cdd:pfam07926 85 AELEESEE----------SWEEQ-------KKELEKELSELEKRIEDLNEQ 118
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
576-868 |
2.23e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 576 RLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAataqvshl 655
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 656 qlkmtahqkketeLQMQLTESLKETDLLRGQLT------KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 729
Cdd:pfam15905 127 -------------LEKQLLELTRVNELLKAKFSedgtqkKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 730 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRK--SYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaeLQTQWEA 807
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITElsCVSEQVEKYKLDIAQLEELLKEKNDEIES-----LKQSLEE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 808 KCEHLLASAKD--EHLQQYQEvcaqrdAYQQKLVQLQEKCLALQAQITALTK---QNEQHIKELEK 868
Cdd:pfam15905 269 KEQELSKQIKDlnEKCKLLES------EKEELLREYEEKEQTLNAELEELKEkltLEEQEHQKLQQ 328
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
575-781 |
2.26e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 46.59 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSNRIEEQNDKISELIErnqryveqsnlmmekrnnslqtatENTQARVLHAEQEKAkvteelaaataqVSH 654
Cdd:pfam05010 11 EKARNEIEEKELEINELKAKYEELRR------------------------ENLEMRKIVAEFEKT------------IAQ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 655 LqlkMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEeltdlRV 734
Cdd:pfam05010 55 M---IEEKQKQKELEHAEIQKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA-----RI 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 150010552 735 EKEslEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 781
Cdd:pfam05010 127 KKE--EQRYQALKAHAEEKLDQANEEIAQVRSKAKAETAALQASLRK 171
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
518-783 |
2.99e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 518 EIRMAVSKVADKMDHLMTKVEELQKHSAG--NSM--LIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQND 593
Cdd:TIGR01612 1115 KIKDDIKNLDQKIDHHIKALEEIKKKSENyiDEIkaQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 594 KISELIErnqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAtaqvshlqlkMTAHQKKETELQMQL 673
Cdd:TIGR01612 1195 LLNEIAE-----IEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKA----------MEAYIEDLDEIKEKS 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 674 TESLKETdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE------LKVTSLEEELTDLRVEKESLEKNLSERK 747
Cdd:TIGR01612 1260 PEIENEM----GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISdireksLKIIEDFSEESDINDIKKELQKNLLDAQ 1335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 748 KKSAQ-------------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 783
Cdd:TIGR01612 1336 KHNSDinlylneianiynilklnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
567-808 |
4.45e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELA 646
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ--------AQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 647 AATAQVSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQEtsEQAQSKFKSEKQNRKQLELKVTSLE 726
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 727 EELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE 806
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
..
gi 150010552 807 AK 808
Cdd:COG4372 284 EL 285
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
631-800 |
4.89e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 47.56 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 631 VLHAEQEKAKVTEELAAATAQvshlQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkVQAKlSELQETSEQAQSKFKS 710
Cdd:PRK00106 21 LISIKMKSAKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 711 EKQNRKQLELKVT----SL---EEELTDLRVEKESLEKNLSErKKKSAQERsqaEEEIDEIRKSYQEELDKLRQLlkktr 783
Cdd:PRK00106 95 ERQELKQIESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL----- 165
|
170
....*....|....*..
gi 150010552 784 vstDQAAAEQLSLVQAE 800
Cdd:PRK00106 166 ---SQAEAREIILAETE 179
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
569-775 |
5.22e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 45.67 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 569 RIIQENERLKQEILEKSNRIEEQN-DKI----SELIERNQRYVEQSNLMMEkrnnslqtatentqarvlhAEQEKAKVTE 643
Cdd:pfam13851 1 ELMKNHEKAFNEIKNYYNDITRNNlELIkslkEEIAELKKKEERNEKLMSE-------------------IQQENKRLTE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 644 ELAAATAQVSHLQLKMTAHQK----------KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQS--KFKSE 711
Cdd:pfam13851 62 PLQKAQEEVEELRKQLENYEKdkqslknlkaRLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQdvQQKTG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150010552 712 KQNRkQLELKVTSLEEELtdlrvekESLEKNLSERKKKS---AQERSQAEEEIDEIRKSYQEELDKL 775
Cdd:pfam13851 142 LKNL-LLEKKLQALGETL-------EKKEAQLNEVLAAAnldPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
681-826 |
5.89e-05 |
|
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: 47.25 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 681 DLLRGQLTK-----VQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE--LTDLRVEKESLEKNLSERKK----K 749
Cdd:pfam15709 336 DRLRAERAEmrrleVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQrlqlQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 750 SAQERSQAEEEidEIRKSYQEeldkLRQllKKTRVSTDQAAAEQLSlvQAELQTQWEAKCEHLLASAKD---EHLQQYQE 826
Cdd:pfam15709 416 AAQERARQQQE--EFRRKLQE----LQR--KKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEerlEYQRQKQE 485
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
696-899 |
5.93e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 696 ELQETSEQ-AQSKFKSEKQNR--KQLELKVTSL---------EEELTDLRVEKESLEKNLSERKKKSAQERSQAEeeide 763
Cdd:COG3096 793 ERDELAEQyAKASFDVQKLQRlhQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD----- 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 764 irkSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAK------CEHLlaSAKDEHLQQYQEVCAQRDAYQQK 837
Cdd:COG3096 868 ---QLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQafiqqhGKAL--AQLEPLVAVLQSDPEQFEQLQAD 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 838 LVQLQEKCLALQAQITALTK--QNEQHI------------KEL-EKNKSQMSGVEAAASDPSEKVKKI------MNQVFQ 896
Cdd:COG3096 943 YLQAKEQQRRLKQQIFALSEvvQRRPHFsyedavgllgenSDLnEKLRARLEQAEEARREAREQLRQAqaqysqYNQVLA 1022
|
...
gi 150010552 897 SLR 899
Cdd:COG3096 1023 SLK 1025
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
582-777 |
5.94e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 582 LEKSNRIEEQND----KISELIERNQRYVEQSNLMMEK-----RNNSLQTATENTQARV------LHAEQEKAKVTEELA 646
Cdd:pfam00038 17 IDKVRFLEQQNKlletKISELRQKKGAEPSRLYSLYEKeiedlRRQLDTLTVERARLQLeldnlrLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 647 -----------------AATAQVSHLQLKMTA-----------HQKKETELQMQLTES--LKETDLLRGQ-LTKV----- 690
Cdd:pfam00038 97 lrtsaendlvglrkdldEATLARVDLEAKIESlkeelaflkknHEEEVRELQAQVSDTqvNVEMDAARKLdLTSAlaeir 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 691 ------------------QAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQ 752
Cdd:pfam00038 177 aqyeeiaaknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
|
250 260
....*....|....*....|....*
gi 150010552 753 ERSQAEEEIDEIrksyQEELDKLRQ 777
Cdd:pfam00038 257 QLADYQELISEL----EAELQETRQ 277
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
569-880 |
6.39e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 569 RIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkrnnsLQTATENtQARVLHAEQEKAKV------- 641
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD-----VKTICEQ-EARIKDLEAQRAQLqagqpcp 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 ----TEELAAATAQVshlqLKMTAHQKKETELQMQLTESLKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSEKQNRKQ 717
Cdd:PRK10246 508 lcgsTSHPAVEAYQA----LEPGVNQSRLDALEKEVKKLGEEGAALRGQL---DALTKQLQRDESEAQSLRQEEQALTQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 718 LELKVTSL------EEELTDLRVEKESLEKNL---SERKKKSAQERSQAEEEIdeirkSYQEELDKLRQLLkktrvsTDQ 788
Cdd:PRK10246 581 WQAVCASLnitlqpQDDIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQQII-----QYQQQIEQRQQQL------LTA 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 789 AAAEQLSLVQAELQTQWeakcehllASAKDEHLQQYQEVCAQRDAYQQKLVQLQ-------------------------- 842
Cdd:PRK10246 650 LAGYALTLPQEDEEASW--------LATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetvaldnwrq 721
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 150010552 843 --EKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAA 880
Cdd:PRK10246 722 vhEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAS 761
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
684-897 |
7.77e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 684 RGQLTKVQAKLSELQETSEQAQSKfksEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDE 763
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRK---ALFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 764 IRKSYQEELDKLRQllkktrvstdqaAAEQLSLVQaelqtqweakcehllasakdehlQQYQEVCAQRDAYQQKLVQLQE 843
Cdd:COG4372 85 LNEQLQAAQAELAQ------------AQEELESLQ-----------------------EEAEELQEELEELQKERQDLEQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 150010552 844 KCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQS 897
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
580-754 |
8.28e-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: 46.98 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 580 EILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaeqeKAKVTEELAAataqvsHLQLKM 659
Cdd:pfam05911 664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKS-----QLQESEQLIA------ELRSEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 660 TAHQKK----ETELQMQlTESLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTdlRVE 735
Cdd:pfam05911 733 ASLKESnslaETQLKCM-AESYEDLET---RLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNE 806
|
170 180
....*....|....*....|
gi 150010552 736 KESLEKNL-SERKKKSAQER 754
Cdd:pfam05911 807 KKESSNCDaDQEDKKLQQEK 826
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
569-862 |
8.69e-05 |
|
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: 46.66 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 569 RIIQ-ENERLKQEILEKSNRIEEQNdKISELIERNQRYVEqsnlmmekRNNSLQTATENTQARvLHAEQEKAKVTEELAA 647
Cdd:pfam05557 10 RLSQlQNEKKQMELEHKRARIELEK-KASALKRQLDRESD--------RNQELQKRIRLLEKR-EAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 648 ATAQ----VSHLQLKMTAHQKKETELQMQLTESLKE--TDLLRGQLtKVQAKLSELQETSEQ---AQSKFKSEKQNRKQL 718
Cdd:pfam05557 80 LKKKyleaLNKKLNEKESQLADAREVISCLKNELSElrRQIQRAEL-ELQSTNSELEELQERldlLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 719 ELKVTSL---EEELTDLRVEKESLEKNLSERKKKSAQ---------ERSQAEEEIDEIRKS------YQEELDKLRQLLK 780
Cdd:pfam05557 159 EKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSElaripelekELERLREHNKHLNENienkllLKEEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 781 KTRVSTDQAAAEQLSL--VQAELQtQWE----AKCEHL----LASAKDEHLQQYQEVCAQRD--------AYQQKLVQLQ 842
Cdd:pfam05557 239 REEKYREEAATLELEKekLEQELQ-SWVklaqDTGLNLrspeDLSRRIEQLQQREIVLKEENssltssarQLEKARRELE 317
|
330 340
....*....|....*....|
gi 150010552 843 EKCLALQAQITALTKQNEQH 862
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRH 337
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
631-885 |
8.74e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.67 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 631 VLHAEQEKAKVTE--ELAAATAQVSHLQLKmtahqKKETELQMQLTE-SLKETDLLRGQLTKVQAKLSELQEtsEQAQSK 707
Cdd:pfam09731 235 VEKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 708 fkseKQNRKQLELKVTSLEEELTDLRVE-KESLEKNLSERKKksaQERSQAEEEIDEIRKSYQEELdklrqllkktrvst 786
Cdd:pfam09731 308 ----KREEKHIERALEKQKEELDKLAEElSARLEEVRAADEA---QLRLEFEREREEIRESYEEKL-------------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 787 dqaaaeqlslvQAELQTQWEAKCEHLlasaKDEHLQQYQEvcaqrdayqqklvqLQEKclALQAQITALTKQNEQHIKEL 866
Cdd:pfam09731 367 -----------RTELERQAEAHEEHL----KDVLVEQEIE--------------LQRE--FLQDIKEKVEEERAGRLLKL 415
|
250
....*....|....*....
gi 150010552 867 EKNKSQMSGVEAAASDPSE 885
Cdd:pfam09731 416 NELLANLKGLEKATSSHSE 434
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
597-775 |
8.81e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 44.54 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 597 ELIERNQRYVEQSNLMmEKRNNSLQTATEN-TQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE 675
Cdd:pfam08614 4 ELIDAYNRLLDRTALL-EAENAKLQSEPESvLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 676 slketdllrgqltkVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL-------TDLRVEKESLekNLserkk 748
Cdd:pfam08614 83 --------------LNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELrekrklnQDLQDELVAL--QL----- 141
|
170 180
....*....|....*....|....*..
gi 150010552 749 ksaqERSQAEEEIDEIRKSYQEELDKL 775
Cdd:pfam08614 142 ----QLNMAEEKLRKLEKENRELVERW 164
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
650-814 |
9.48e-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: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 650 AQVSHLQLKMTAHQK-KETELQMQLTESLKETDL-LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE---LKVTS 724
Cdd:TIGR00606 187 ALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 725 LEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR-------KSYQEELDKLRQLLKKTRVSTDQAAAEQLSLV 797
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYhnhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170
....*....|....*....
gi 150010552 798 --QAELQTQWEAKCEHLLA 814
Cdd:TIGR00606 347 veQGRLQLQADRHQEHIRA 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
563-759 |
9.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQT--ATENTQARVLHAeqe 637
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRsgGSVSYLDVLLGS--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 638 kakvtEELAAATAQVSHLQlKMTAHQKKETELQMQLTESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 716
Cdd:COG3883 112 -----ESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 150010552 717 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 759
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
635-894 |
1.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 635 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 714
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 715 RKQLELKVTSLEEELTDlrvEKESLEKNLSERKKKSaQERSQAEEEIDEIRK---SYQEELDKL-RQLLKKTRVSTD--- 787
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKE---NKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKqkeELENELNLLeKEKLNIQKNIDKikn 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 788 QAAAEQLSLVQAELQTQweakcEHLLASAKDEHL-QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKEL 866
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQ-----KNKSLESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260
....*....|....*....|....*...
gi 150010552 867 EKNKSQMSGVEAAASDPSEKVKKIMNQV 894
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
511-1004 |
1.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEK---SNR 587
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 588 IEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ-LKMTAHQKKE 666
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 667 TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE---------QAQSKFKSEK-----QNRKQLELKVTSLEEELTDL 732
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkkadeakKAEEAKKADEakkaeEAKKADEAKKAEEKKKADEL 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 733 RVEKE---SLEKNLSERKKKSAQERSQAE---EEIDEIRKSYQEELDKLRQLLKKTRvsTDQAAAEQLSLVQAE--LQTQ 804
Cdd:PTZ00121 1552 KKAEElkkAEEKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMK--AEEAKKAEEAKIKAEelKKAE 1629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 805 WEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK---ELEKNKSQMSGVEAAAS 881
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKKAEELKK 1709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 882 DPSEKVKKImnqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeqekeeSSSEEEEEKAEERPRRPSQEQSA 961
Cdd:PTZ00121 1710 KEAEEKKKA-----EELKKAEE--------------ENKIKAEEAK-----------KEAEEDKKKAEEAKKDEEEKKKI 1759
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 150010552 962 SASSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQD 1004
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
706-893 |
1.18e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 706 SKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsYQEELDKLRQLLKKTRVS 785
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 786 TDQaAAEQLSLVQAELQtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLV-------QLQEKCLALQAQITALTKQ 858
Cdd:COG1340 80 RDE-LNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVEKIKELEKELEKAKKA 155
|
170 180 190
....*....|....*....|....*....|....*
gi 150010552 859 NEQHiKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 893
Cdd:COG1340 156 LEKN-EKLKELRAELKELRKEAEEIHKKIKELAEE 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-777 |
1.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 565 SNIQRIiqenERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNL--------MMEKRNNSLQTATENTQAR------ 630
Cdd:COG4913 607 DNRAKL----AALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeysWDEIDVASAEREIAELEAElerlda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 631 ----VLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESlkETDLLRGQLTKVQAKLSELQETSEQAQS 706
Cdd:COG4913 683 ssddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 707 KfKSEKQNRKQLELKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIDEIRkSYQEELDKLRQ 777
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAE---EELERAMRAFNREWPAETADLDADLESLP-EYLALLDRLEE 826
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
703-889 |
1.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 703 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEeynELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 780 K---KTRVSTD-----------QAAAEQLSLV-------QAELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQQKL 838
Cdd:COG3883 93 RalyRSGGSVSyldvllgsesfSDFLDRLSALskiadadADLLEELKADKAE--LEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 150010552 839 VQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKK 889
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
650-857 |
1.28e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 46.38 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 650 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKvtsLEEEl 729
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR---LKAE- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 730 tdlRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQllKKTRVSTdqaaaeQLSLVQAELQTQwEAKC 809
Cdd:pfam09726 478 ---QEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQ--RKRELES------EIKKLTHDIKLK-EEQI 545
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 150010552 810 EHLLASAKDehLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 857
Cdd:pfam09726 546 RELEIKVQE--LRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETR 591
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
567-777 |
1.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEE 644
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---AEEKREaaAEAEEEAEEAREEVAELNSKLAELKER 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 645 L-------------AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkvQAKLSELQETSEQAqskfkse 711
Cdd:PRK02224 588 IeslerirtllaaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERA------- 658
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150010552 712 KQNRKQLELKVTSLEEELTDLRVE----KESLE--KNLSERKKKSAQERSQAE---EEIDEIRKSYQEELDKLRQ 777
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEigavENELEelEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQ 733
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
579-917 |
1.38e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 579 QEILEKSNRIEEQNDKISElIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLK 658
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLAC-IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS--AQR 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 659 MTAHQKKETELQMQLTE--SLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 736
Cdd:COG5022 877 VELAERQLQELKIDVKSisSLKLVNL---ELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 737 ESLEKNLSERK--KKSAQERS----QAEEEIDEIRKSyQEELDKLRQLLKKTRVSTD--QAAAEQLSLVQAELQTQWEAk 808
Cdd:COG5022 954 PELNKLHEVESklKETSEEYEdllkKSTILVREGNKA-NSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSA- 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 809 cEHLLASAKDEhLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaLTKQNEQHIKELEKNKSQMSGVEAA--------A 880
Cdd:COG5022 1032 -SKIISSESTE-LSILKPLQKLKGLLLLENNQLQARYKALKLRRE-NSLLDDKQLYQLESTENLLKTINVKdlevtnrnL 1108
|
330 340 350
....*....|....*....|....*....|....*..
gi 150010552 881 SDPSEKVKKImnqVFQSLRREFELEESYNGRTILGTI 917
Cdd:COG5022 1109 VKPANVLQFI---VAQMIKLNLLQEISKFLSQLVNTL 1142
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
657-782 |
1.38e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 45.10 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 657 LKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSekqnrkqLELKVTSLEEELTDLRVEK 736
Cdd:COG4026 121 LKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKK-------LREENSILEEEFDNIKSEY 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 150010552 737 ESLEKNLSERKKKSAQERSQAEEEIDEIrksYQEELDKLRQLLKKT 782
Cdd:COG4026 194 SDLKSRFEELLKKRLLEVFSLEELWKEL---FPEELPEEDFIYFAT 236
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
571-871 |
1.56e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 571 IQENE-RLKQEILEKSNRIEEQNDKISELIERNQryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAT 649
Cdd:TIGR00606 370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 650 AQVSHLQLKMtahQKKETELQmQLTESLKETDLLRGQLTKVQAKLSELQETS--EQAQSKFKSEKQNRKQLELKVTSLEE 727
Cdd:TIGR00606 447 EILEKKQEEL---KFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 728 ELTDLRVEKESLEKNLSERKKKsaqerSQAEEEIDEIRKSYQEEL--------------DKLRQLLKKTRVSTDQAAAEQ 793
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDK-----MDKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 794 LSLVQAE-LQTQWEAKCEhllasAKDEHLQQYQ----EVCAQRDaYQQKLVQLQ---EKCLALQAQITALTKQNEQHIKE 865
Cdd:TIGR00606 598 KELASLEqNKNHINNELE-----SKEEQLSSYEdklfDVCGSQD-EESDLERLKeeiEKSSKQRAMLAGATAVYSQFITQ 671
|
....*..
gi 150010552 866 L-EKNKS 871
Cdd:TIGR00606 672 LtDENQS 678
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
670-903 |
1.60e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 670 QMQLT-ESLKETDLLRGQLTKVQA-KLSELQETSEQA-----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKn 742
Cdd:PRK04778 55 KLNLTgQSEEKFEEWRQKWDEIVTnSLPDIEEQLFEAeelndKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLE- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 743 lSErkKKSAQERSQAEEEIDEIRK-------SYQEELDKLRQLLKKTRVSTDQ-----------AAAEQLSLVQAELqTQ 804
Cdd:PRK04778 134 -SE--EKNREEVEQLKDLYRELRKsllanrfSFGPALDELEKQLENLEEEFSQfveltesgdyvEAREILDQLEEEL-AA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 805 WEAKCEH---LLASAKDEHLQQYQEVcaqRDAYQQKLVQ---LQEkcLALQAQITALTKQ---NEQHIKELEknksqmsg 875
Cdd:PRK04778 210 LEQIMEEipeLLKELQTELPDQLQEL---KAGYRELVEEgyhLDH--LDIEKEIQDLKEQideNLALLEELD-------- 276
|
250 260 270
....*....|....*....|....*....|.
gi 150010552 876 VEAAasdpSEKVKKI---MNQVFQSLRREFE 903
Cdd:PRK04778 277 LDEA----EEKNEEIqerIDQLYDILEREVK 303
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
663-870 |
1.66e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.87 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 663 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqskfksEKQNRKQLELKVTslEEELTDLRVEKESLEKN 742
Cdd:pfam03528 7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKE--------EDLKRQNAVLQEA--QVELDALQNQLALARAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 743 LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE------AKCEHLLASA 816
Cdd:pfam03528 77 MENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYREsaereiADLRRRLSEG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 817 KDEHLQQYQEVCAQRDAYQQKLV--QLQEKCLALQAQITaltkQNEQHIKELEKNK 870
Cdd:pfam03528 157 QEEENLEDEMKKAQEDAEKLRSVvmPMEKEIAALKAKLT----EAEDKIKELEASK 208
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
563-794 |
1.71e-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: 45.62 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRI---IQEN----ERLKQEILEKSNR-IEEQNDKISELIER----------NQRYVEQSNLMMEKRNNSLQTAT 624
Cdd:pfam06160 235 VDKEIQQLeeqLEENlallENLELDEAEEALEeIEERIDQLYDLLEKevdakkyvekNLPEIEDYLEHAEEQNKELKEEL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 625 ENTQARVLHAEQEKAKV---TEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQets 701
Cdd:pfam06160 315 ERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILE-------QLEEIEEEQEEFK--- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 702 EQAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEE-------IDEIRKSYQEE 771
Cdd:pfam06160 385 ESLQSLRKDELEAREKLDEFKLELRE--IKRLVEKSnlpGLPESYLDYFFDVSDEIEDLADElnevplnMDEVNRLLDEA 462
|
250 260
....*....|....*....|....
gi 150010552 772 LDKLRQLLKKTRVSTDQAA-AEQL 794
Cdd:pfam06160 463 QDDVDTLYEKTEELIDNATlAEQL 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-772 |
1.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEILEKS-NRIEEQNDKISELIERNQRYVEQSNlmMEKRNNSLQTATENTQARVLHAEQEKAKV 641
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD--AEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 TEELAAATAQVSHLQLKMTahQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqsKFKSEKQNRKQLELK 721
Cdd:PRK03918 639 EKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE----KLKEELEEREKAKKE 712
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 150010552 722 VTSLEEELTDLRVEKESLeknlserKKKSAQERSQAEEEIDEIRKSYQEEL 772
Cdd:PRK03918 713 LEKLEKALERVEELREKV-------KKYKALLKERALSKVGEIASEIFEEL 756
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
640-858 |
2.07e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 640 KVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKS--------- 710
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKElaeaiknli 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 711 ----------EKQNRKQLELKVTSLEEELTDL-RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:pfam06008 96 dnikeinekvATLGENDFALPSSDLSRMLAEAqRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150010552 780 KKTRvstdqaaaEQLSLVQAELQTQWEAKCEHLLASAKDEHLQqyQEVCAQRDAYQQKLVQLQEkclaLQAQITALTKQ 858
Cdd:pfam06008 176 NALR--------DSLAEYEAKLSDLRELLREAAAKTRDANRLN--LANQANLREFQRKKEEVSE----QKNQLEETLKT 240
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
713-890 |
2.22e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 713 QNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDK-LRQLLKKTRVSTDQAAA 791
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYASVKA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 792 EQLSLVQAELQTQWEAKCEHLLASAKDEH-LQQYQEVcaqrdayqqKLVQLQEKclalqAQITALTKQNE---Q------ 861
Cdd:PRK00409 607 HELIEARKRLNKANEKKEKKKKKQKEKQEeLKVGDEV---------KYLSLGQK-----GEVLSIPDDKEaivQagimkm 672
|
170 180 190
....*....|....*....|....*....|.
gi 150010552 862 --HIKELEKNKSQmsgveaaasdPSEKVKKI 890
Cdd:PRK00409 673 kvPLSDLEKIQKP----------KKKKKKKP 693
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
563-759 |
2.25e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKI---SELIERNQRYVEQSNLMMEKRNNSLqtaTENTQARVLHAEQEKA 639
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARR 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 640 KVTEELAAATAQVSH----LQLKMTAHQKKETELQmQLTESLKETDllrgqltkVQAKlselQETSEQAQSKfKSEKQNR 715
Cdd:COG3096 1002 EAREQLRQAQAQYSQynqvLASLKSSRDAKQQTLQ-ELEQELEELG--------VQAD----AEAEERARIR-RDELHEE 1067
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 150010552 716 -KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 759
Cdd:COG3096 1068 lSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
675-783 |
2.27e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 675 ESLKEtdLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNR-KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQE 753
Cdd:COG2433 376 LSIEE--ALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453
|
90 100 110
....*....|....*....|....*....|..
gi 150010552 754 RSQAEEEIDEIRK--SYQEELDKLRQLLKKTR 783
Cdd:COG2433 454 RSEERREIRKDREisRLDREIERLERELEEER 485
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
307-495 |
3.06e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.14 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 307 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 386
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 387 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 465
Cdd:pfam03154 260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321
|
170 180 190
....*....|....*....|....*....|..
gi 150010552 466 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 495
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
511-874 |
3.37e-04 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 44.83 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMlipsmsvtmetsmimsNIQRIIQENERLKQEILEKSN---- 586
Cdd:COG4477 101 KAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNRE----------------EIEELKEKYRELRKTLLAHRHsfgp 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 587 ---RIEEQNDKISELIERNQRYVEQSNlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTA 661
Cdd:COG4477 165 aaeELEKQLEELEPEFEEFEELTESGD-YLEAREilEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 662 ------HQKKETELQmQLTESLKET--DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLR 733
Cdd:COG4477 244 qgyvleHLNIEKEIE-QLEEQLKEAleLLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 734 VEKESLEknlserkkksaqersqaeEEIDEIRKSYQ---EELDKLRQLLKktrvstdqaaaeQLSLVQAELQTqweakce 810
Cdd:COG4477 323 EQNRELK------------------EEIDRVQQSYRlneNELEKVRNLEK------------QIEELEKRYDE------- 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150010552 811 hlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKqNEQHIKE-LEKNKSQMS 874
Cdd:COG4477 366 --IDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRK-DELEAREkLDELKKKLR 427
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
567-840 |
3.39e-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: 44.14 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERN--QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvtEE 644
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE--DE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 645 LAAATAQVSHLQLKMTAHQKKETELQMQlteslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 724
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKE-----REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 725 LEEELtDLRvekESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 804
Cdd:pfam13868 231 ARQRQ-ELQ---QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR 306
|
250 260 270
....*....|....*....|....*....|....*.
gi 150010552 805 WEAKcehllasakdEHLQQYQEVCAQRDAYQQKLVQ 840
Cdd:pfam13868 307 AAER----------EEELEEGERLREEEAERRERIE 332
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
588-804 |
3.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 588 IEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ--LKMTAHQKK 665
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 666 ETELQMQLTESLKE----TDLLRG-----QLTKVQAKL----SELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 732
Cdd:COG3883 97 RSGGSVSYLDVLLGsesfSDFLDRlsalsKIADADADLleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150010552 733 RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 804
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
572-909 |
3.84e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QENERLKQEILEKSNRIEEQNDKISELIERN----QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAA 647
Cdd:PTZ00440 560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 648 ATAQVSHLQLKMTA--HQKKETE-LQMQLTESLKETDLLR-----------GQLTKVQAKLSELQETSEQAQ-SKFKSEK 712
Cdd:PTZ00440 640 LLDELSHFLDDHKYlyHEAKSKEdLQTLLNTSKNEYEKLEfmksdnidniiKNLKKELQNLLSLKENIIKKQlNNIEQDI 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 713 QNR-KQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQ 788
Cdd:PTZ00440 720 SNSlNQYTIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISND 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 789 AAA--EQLSLVQAELQTqWEAKCEHLLASA--KDEHLQQYQEVCAQRDAyQQKLVQLQEKCLALQAQITALTKQNEQHIK 864
Cdd:PTZ00440 800 INIlkENKKNNQDLLNS-YNILIQKLEAHTekNDEELKQLLQKFPTEDE-NLNLKELEKEFNENNQIVDNIIKDIENMNK 877
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 150010552 865 ELEKNKSQMSGVEAAASDPS--EKVKKIMNQVFQSLRREFELEESYN 909
Cdd:PTZ00440 878 NINIIKTLNIAINRSNSNKQlvEHLLNNKIDLKNKLEQHMKIINTDN 924
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
663-784 |
4.63e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 663 QKKETELQMQLTESLKETDLLRGQ-LTKVQAKLSELQETSEQAQSKFKSEKQnrkqLELKVTSLEEELTDLRVEKESLEK 741
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 742 NLSERKKKSAQERSQAEEEIDE--------------IRKSYQEELDKLRQL---LKKtRV 784
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
|
|
| NST1 |
pfam13945 |
Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly ... |
602-772 |
4.75e-04 |
|
Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly or indirectly, in the salt sensitivity of some cellular functions in yeast. It does this without affecting sodium accumulation. It negatively affects salt-tolerance through an interaction with the splicing factor Msl1p. This interaction stresses the importance of efficient RNA processing under salt stress conditions.
Pssm-ID: 372833 Cd Length: 186 Bit Score: 42.57 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 602 NQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQkkeTELQMQLTESLKETD 681
Cdd:pfam13945 6 NNNSQNQQQNQHDNNTVDHHSQVNSSKRKSKKKKKKKNRNGSNNNNDESSTSQSTPSPFAIT---TSSTRPVSNNPPLSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 682 LLRGQLTKVQAKLSELQETSEQaqskfkSEKQNRKQLELKVTslEEELTDL-RVEKESLEKNLSERKKKS------AQER 754
Cdd:pfam13945 83 SAASRSAHKNNKDRSIWNTSTQ------EERENIKEFWLSLG--EEERRSLvKVEKEAVLKKMKEQQKHScsctvcGRKR 154
|
170
....*....|....*...
gi 150010552 755 SQAEEEIDEIRKSYQEEL 772
Cdd:pfam13945 155 TAIEEELEVLYDAYYEEL 172
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
509-781 |
4.80e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNS----MLIPSMSVTMETSMIMSNIQRIIQENERLKQEI-LE 583
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELaLK 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 584 KSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARV-------------LHAEQEKAK-----VTEEL 645
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcqtlLRELETHIEeydreFNEIE 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 646 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRkQLELKVTSL 725
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA--HFNNNEEVTAALQTGAELSHLAAEIQFFNR-LREEDTHLL 801
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 726 EEELTDLRVEKESLEKNLSERKKKSAQERSQAEE----------EIDEIRKSYQEELDKLRQLLKK 781
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSrleeksatlgEITHQLLKYEECSKQLAQLTQE 867
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
502-746 |
4.85e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 502 GDMASFLMTEARQHNTEIRMavskVADKMDHLMTKV-------EELQKHSAGNsmlipsmsVTMETSMIMSN---IQRII 571
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQT----LDMKIDHIQQQIktynkniEEQRKKNGEN--------IARKQNKYDELveeAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QENERLKQEILEKSNRIEEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTATENtqarvLHAEQEK-AKVT 642
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 643 EELAAATAQVSHLQLKMTAHQKKE---TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQnrkqle 719
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE------ 379
|
250 260
....*....|....*....|....*..
gi 150010552 720 lKVTSLEEELTDLRVEKESLEKNLSER 746
Cdd:PHA02562 380 -ELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
523-771 |
5.12e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 523 VSKVADKMDHLMTKVEELQ----KHSAGNSMLIPSMSVTMETSMIMSNIQ--------------RIIQENERL------K 578
Cdd:PTZ00440 2317 VKLYIENITHLLNRINTLIndldNYQDENYGKDKNIELNNENNSYIIKTKekinnlkeefskllKNIKRNNTLcnnnniK 2396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 579 QEILEKSNRIEEQNDKISELIERNQRYV-------EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 651
Cdd:PTZ00440 2397 DFISNIGKSVETIKQRFSSNLPEKEKLHqieenlnEIKNIMNETKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDL 2476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 652 VSHLqlkmTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-RKQLELKVTSLEE--- 727
Cdd:PTZ00440 2477 IENV----TSHNEKIKSELLIINDALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYiINELESHVSKLNElls 2552
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 728 ----ELTDL----------------RVEKESLEKNLSERKKKSAQERSQAEEEI--DEIRKSYQEE 771
Cdd:PTZ00440 2553 yidnEIKELeneklkllekakieesRKERERIESETQEDNTDEEQINRQQQERLqkEEEQKAYSQE 2618
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
565-786 |
5.51e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 565 SNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnLMMEKRNNSLQTATENTQARVLHAEQEK-----A 639
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE--LVEEAKTIKAEIEELTDELLNLVMDIEDpsaalN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 640 KVTEELAAATAQVSHLQLKMTAHQK----------------KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ 703
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 704 A---QSKFKSEKQNRKQLELKVTSLE---EELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDeirksyqeELDKLRQ 777
Cdd:PHA02562 339 LlelKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY--------HRGIVTD 410
|
....*....
gi 150010552 778 LLKKTRVST 786
Cdd:PHA02562 411 LLKDSGIKA 419
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
563-794 |
6.28e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQENERLKQEI-------LEKSNR-IEEQNDKISELIERN---QRYVEQSN-------LMMEKRNNSLQTAT 624
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLeeldldeAEEKNEeIQERIDQLYDILEREvkaRKYVEKNSdtlpdflEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 625 ENTQA--RVLHAEQEKAK-VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQETs 701
Cdd:PRK04778 334 DRVKQsyTLNESELESVRqLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILK-------QLEEIEKEQEKLSEM- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 702 eqAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEEIDEIR---KSYQEELDK- 774
Cdd:PRK04778 406 --LQGLRKDELEAREKLERYRNKLHE--IKRYLEKSnlpGLPEDYLEMFFEVSDEIEALAEELEEKPinmEAVNRLLEEa 481
|
250 260
....*....|....*....|....
gi 150010552 775 ---LRQLLKKTRVSTDQAA-AEQL 794
Cdd:PRK04778 482 tedVETLEEETEELVENATlTEQL 505
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
642-777 |
6.45e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 40.65 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 TEELAAATAQVSHLQLKMTAHQKKetelqmqlTESLK--ETDLlrgqltkvqAKLSELQETSEQAQSKFKSEKQNRKQLE 719
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAK--------IDALQvvEKDL---------RSCIKLLEEIEAELAKLEEAKKKLKELR 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 150010552 720 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQ 777
Cdd:pfam18595 64 DALEEKEIELRELERREERLQRQLENAQEKLERLREQAEEKREAA----QARLEELRE 117
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
952-1121 |
6.61e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 952 PRRPSQeqsasassgqPQAPLNRERPESPMVP--SEQVVEEAVPLPPQALTTSQDGHRRKGDSEAE-----ALSEIKDGS 1024
Cdd:PTZ00449 633 PKRPPP----------PQRPSSPERPEGPKIIksPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKEtkttvVLDESFESI 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1025 LPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNP--SGKVCVREVAPDGPLQESSTRL----SL 1098
Cdd:PTZ00449 703 LKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADTPLPDILAEEfkeeDI 782
|
170 180
....*....|....*....|....*
gi 150010552 1099 TSDPEEGDPLALGPESPGE--PQPP 1121
Cdd:PTZ00449 783 HAETGEPDEAMKRPDSPSEheDKPP 807
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
665-905 |
7.11e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 665 KETELQMQLTESLKEtdllRGQLTKVQAKLSELQETSEQAQSKFKSE-KQNRKQLELKVTSLEEELTDLRVEKESLEknl 743
Cdd:pfam07888 28 RAELLQNRLEECLQE----RAELLQAQEAANRQREKEKERYKRDREQwERQRRELESRVAELKEELRQSREKHEELE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 744 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEaKCEHLLASAKDEHlqq 823
Cdd:pfam07888 101 -EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDI-----KTLTQRVLERETELERMKE-RAKKAGAQRKEEE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 824 yqevcAQRDAYQQKLVQLQEKCLALQaqitaltkqneqhiKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 903
Cdd:pfam07888 171 -----AERKQLQAKLQQTEEELRSLS--------------KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
..
gi 150010552 904 LE 905
Cdd:pfam07888 232 NE 233
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
502-865 |
7.19e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 502 GDMASFLMTEARQH--------NTEIRMAVS-KVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMimsniQRIIQ 572
Cdd:PRK10246 156 GQFAAFLNAKPKERaelleeltGTEIYGQISaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASL-----QVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 573 ENERL--KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLH------AEQEKA----- 639
Cdd:PRK10246 231 EEKQLltAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRphweriQEQSAAlahtr 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 640 ----KVTEELAAATAQVSHL-QLKMTAHQKKETELQmQLTESLKETDLLR-------------GQLTKVQAKLSELQETS 701
Cdd:PRK10246 311 qqieEVNTRLQSTMALRARIrHHAAKQSAELQAQQQ-SLNTWLAEHDRFRqwnnelagwraqfSQQTSDREQLRQWQQQL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 702 EQAQSKFKS-----------------EKQNRKQ-LELKVTSLEEELTDLRVEKESLEKNLSerkkKSAQERSQAEEEIDE 763
Cdd:PRK10246 390 THAEQKLNAlpaitltltadevaaalAQHAEQRpLRQRLVALHGQIVPQQKRLAQLQVAIQ----NVTQEQTQRNAALNE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 764 IRKSYQEeldKLRQLLKKTRVSTDQAAAEQLSLVQAELQTqweAKCEHLLASAKDEHLQQYQEVC-----AQRDAYQQKL 838
Cdd:PRK10246 466 MRQRYKE---KTQQLADVKTICEQEARIKDLEAQRAQLQA---GQPCPLCGSTSHPAVEAYQALEpgvnqSRLDALEKEV 539
|
410 420
....*....|....*....|....*..
gi 150010552 839 VQLQEKCLALQAQITALTKQNEQHIKE 865
Cdd:PRK10246 540 KKLGEEGAALRGQLDALTKQLQRDESE 566
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
558-868 |
8.68e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 558 METSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER-NQRYVEQSNLMMEKRnNSLQTATENTQARVLHAEQ 636
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQlKDLYRELRKSLLANR-FSFGPALDELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 637 EKAKVTEElaaaTAQVSHLQLKMTAHQKKETELQM-QLTESLKEtdLLRGQLTKVQAKLSELQETSEQAqskfksEKQNR 715
Cdd:PRK04778 180 EFSQFVEL----TESGDYVEAREILDQLEEELAALeQIMEEIPE--LLKELQTELPDQLQELKAGYREL------VEEGY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 716 KqleLKVTSLEEELTDLRVEKESLEKNLSERKKKSAQER-SQAEEEIDEI----------RKSYQEELDKLRQLLKKTRV 784
Cdd:PRK04778 248 H---LDHLDIEKEIQDLKEQIDENLALLEELDLDEAEEKnEEIQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 785 STDQAAAEQLSLVQA------ELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQqklvQLQEKCLALQAQITALTKQ 858
Cdd:PRK04778 325 QNKELKEEIDRVKQSytlnesELESVRQLEKQ--LESLEKQYDEITERIAEQEIAYS----ELQEELEEILKQLEEIEKE 398
|
330
....*....|...
gi 150010552 859 NEQ---HIKELEK 868
Cdd:PRK04778 399 QEKlseMLQGLRK 411
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
968-1204 |
9.57e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 968 PQAPLNRERPESPMVPSEQVVEeavPLPPQALTTSQDghrrkgdseAEALSEIKDGSLPPELscipshrvlgPPTSIPPE 1047
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGE---PVHPRMLTWIRG---------LEELASDDAGDPPPPL----------PPAAPPAA 2563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1048 PlgpvsmdsecEESLAASPMAAKPDNPSgkVCVREVAPDGPLQESSTRLSLT---SDPEEGDPLALGPESPGEPQPPQLK 1124
Cdd:PHA03247 2564 P----------DRSVPPPRPAPRPSEPA--VTSRARRPDAPPQSARPRAPVDdrgDPRGPAPPSPLPPDTHAPDPPPPSP 2631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1125 KDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLS-GDEEDELFKGATLKALRPKAQPeeededeVSMKGRPPPT 1203
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRRRAARPTVGS-------LTSLADPPPP 2704
|
.
gi 150010552 1204 P 1204
Cdd:PHA03247 2705 P 2705
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
689-868 |
9.67e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 41.42 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 689 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEIRKS 767
Cdd:pfam10368 1 SPEEKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELYEEIIELGMDEFDEIKKLSDEALENVEEREELlEKEKESIEEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 768 YqEELDKLRQLLKKTRvstDQAAAEQLSLVQAELQTQWEAkceHllasakDEHLQQYQE-VCAQRDAY---QQKLVQLQE 843
Cdd:pfam10368 81 K-EEFKKIKEIIEEIE---DEELKKEAEELIDAMEERYEA---Y------DELYDAYKKaLELDKELYemlKDEDLTLEE 147
|
170 180
....*....|....*....|....*
gi 150010552 844 kclaLQAQITALTKQNEQHIKELEK 868
Cdd:pfam10368 148 ----LQEQIEKINESYEEVKEANEQ 168
|
|
| AmmeMemoSam_B |
TIGR04336 |
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain ... |
1014-1072 |
9.96e-04 |
|
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain family as the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility). Members of the present family occur as part of a three gene system with an uncharacterized radical SAM enzyme and a homolog of the mammalian protein AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Memo in humans has protein-protein interaction activity with binding of phosphorylated Try, but members of this family may be active as enzymes, as suggested by homology to a class of nonheme iron dioxygenases.
Pssm-ID: 275135 [Multi-domain] Cd Length: 269 Bit Score: 42.56 E-value: 9.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 1014 AEALSEIKDGslPPELSCI--PSHRVLGPPTSIPPE-----PLGPVSMDSECEESLAASPMAAKPD 1072
Cdd:TIGR04336 55 AHAYAALKKG--RPETVVLlgPNHTGYGSGIALPPEgswetPLGDVPVDEELAEELLEHSPIIELD 118
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
568-892 |
1.05e-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: 43.30 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 568 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQT-------ATENTQARVLHAEQEKAK 640
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLAnrfsygpAIDELEKQLAEIEEEFSQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEElaaaTAQVSHLQLKMTAHQ-KKETElqmQLTESLKET-DLLRGQLTKVQAKLSELQETSEQAQskfksekqnRKQL 718
Cdd:pfam06160 165 FEEL----TESGDYLEAREVLEKlEEETD---ALEELMEDIpPLYEELKTELPDQLEELKEGYREME---------EEGY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 719 ELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEI----------RKSYQEELDKLRQLLKKTRVSTD 787
Cdd:pfam06160 229 ALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEiEERIDQLydllekevdaKKYVEKNLPEIEDYLEHAEEQNK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 788 QAAAEQLSLVQA-ELQTQWEAKCEHLlasakDEHLQ----QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH 862
Cdd:pfam06160 309 ELKEELERVQQSyTLNENELERVRGL-----EKQLEelekRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEF 383
|
330 340 350
....*....|....*....|....*....|
gi 150010552 863 IKELEknksQMSGVEAAASDPSEKVKKIMN 892
Cdd:pfam06160 384 KESLQ----SLRKDELEAREKLDEFKLELR 409
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1024-1204 |
1.12e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1024 SLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPE 1103
Cdd:PHA03307 92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1104 EGDPLALGPES---PGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPShhSQRSSLSGDEEDELfkgatlkal 1180
Cdd:PHA03307 172 AALPLSSPEETaraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR--SAADDAGASSSDSS--------- 240
|
170 180
....*....|....*....|....
gi 150010552 1181 rpKAQPEEEDEDEVSMKGRPPPTP 1204
Cdd:PHA03307 241 --SSESSGCGWGPENECPLPRPAP 262
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
727-858 |
1.12e-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: 40.31 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 727 EELTDLRVEKESLEKNLS--ERKKKSAQERSQAEEEI-DEIRKSYQEELdklrqLLKKTRVSTDQAAAEQLSLVQAELQt 803
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAAdaEAQLQKLQEDLEKQAEIaREAQQNYEREL-----VLHAEDIKALQALREELNELKAEIA- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 150010552 804 QWEAKCEhllaSAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 858
Cdd:pfam07926 75 ELKAEAE----SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
620-903 |
1.22e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 620 LQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLKMTAHQKKeTELQMQLTESLKETDLLRGQLTKVQAK-LSELQ 698
Cdd:NF041483 224 LNAASTQAQEATDHAEQLRSSTAAESDQARRQAA--ELSRAAEQRM-QEAEEALREARAEAEKVVAEAKEAAAKqLASAE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 699 ETSEQAQSKFKSE-----KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAeeEIDEIRKSYQEELD 773
Cdd:NF041483 301 SANEQRTRTAKEEiarlvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAA--QLAKAARTAEEVLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 774 KLRQLLKktrvSTDQAAAEQLSLVQAELqtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQIT 853
Cdd:NF041483 379 KASEDAK----ATTRAAAEEAERIRREA----EAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAE 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150010552 854 AL---------------TKQNEQHIKE--------LEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 903
Cdd:NF041483 451 QLraeavaegerirgeaRREAVQQIEEaartaeelLTKAKADADELRSTATAESERVRTEAIERATTLRRQAE 523
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
577-715 |
1.25e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 577 LKQEILEKSNRIEEQNDKISELIERnqryveqsnLMMEKRNN-SLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHL 655
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADL---------LSLERQGNqDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 656 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsEKQNR 715
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAK 173
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
655-807 |
1.26e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 655 LQLKMTAHQKKETELQMQLTESLKE-TDLLRGQLTKVQAKLSELQEtseqAQSKFKSE-KQNRKQLELKVTSLEEELTD- 731
Cdd:cd22656 97 LELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVD----KLTDFENQtEKDQTALETLEKALKDLLTDe 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 732 -LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRqllKKTRVSTD-QAAAEQLSLVQA---------- 799
Cdd:cd22656 173 gGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLA---AALRLIADlTAADTDLDNLLAligpaipale 249
|
....*...
gi 150010552 800 ELQTQWEA 807
Cdd:cd22656 250 KLQGAWQA 257
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
510-851 |
1.50e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 510 TEARQhnTEIRMAVSKVAdKMDHLMTKVEELQKHSAGNSMLIPS--------MSVTMETSMIMSN-IQRIIQENERLKQE 580
Cdd:pfam10174 228 TKALQ--TVIEMKDTKIS-SLERNIRDLEDEVQMLKTNGLLHTEdreeeikqMEVYKSHSKFMKNkIDQLKQELSKKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 581 ILEKSNRIEEQNDKISElierNQRYVE---QSNLMMEKRNNSLQTATENTQARVLHAEQ---EKAK----VTEELAAATA 650
Cdd:pfam10174 305 LLALQTKLETLTNQNSD----CKQHIEvlkESLTAKEQRAAILQTEVDALRLRLEEKESflnKKTKqlqdLTEEKSTLAG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 651 QVSHLQLKMTAHQKKETELQMQLtESLKEtdllrgQLTKVQAKLSELQEtseqaqskfksekqnrkqlelKVTSLEEELT 730
Cdd:pfam10174 381 EIRDLKDMLDVKERKINVLQKKI-ENLQE------QLRDKDKQLAGLKE---------------------RVKSLQTDSS 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 731 DLRVEKESLEKNLSErkKKSAQERSQaeEEIDEIRKSYQEELDKLRQLLKKTRvstdqaaaEQLSLVQAELQTQweakcE 810
Cdd:pfam10174 433 NTDTALTTLEEALSE--KERIIERLK--EQREREDRERLEELESLKKENKDLK--------EKVSALQPELTEK-----E 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 150010552 811 HLLASAKdEHLQQYQEVCAQRDAYQQKL----VQLQEKCLALQAQ 851
Cdd:pfam10174 496 SSLIDLK-EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQ 539
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
628-804 |
1.52e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 628 QARVLHAEQEKAKVTEElAAATAQVshlqlkmtahQKKETELQMQlteslKETDLLRGQLTK-VQAKLSELQETSEQAQS 706
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-AKKEAEA----------IKKEALLEAK-----EEIHKLRNEFEKeLRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 707 KFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKnlserkkksaqersqAEEEIDEIRKSYQEELDKLRQLlkktrvST 786
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEK---------------KEEELEELIEEQLQELERISGL------TA 152
|
170
....*....|....*...
gi 150010552 787 DQAAAEQLSLVQAELQTQ 804
Cdd:PRK12704 153 EEAKEILLEKVEEEARHE 170
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
563-781 |
1.59e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 563 IMSNIQRIIQEnerlKQEILEKSNRIeeQN-DKISELIERNQRYVEQSNLMMEKRNNSLQTAT-ENTQARVLHAEQEKAK 640
Cdd:NF033838 63 VESHLEKILSE----IQKSLDKRKHT--QNvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTkKELDAAFEQFKKDTLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 641 VTEELAAATAQVSHLQLKmtAHQKKETELQMQLTESLKETDLLRGQlTKVQAKLSELQETSEQAQSKFKSEKQnrKQLEL 720
Cdd:NF033838 137 PGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAE-SDVEVKKAELELVKEEAKEPRDEEKI--KQAKA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150010552 721 KVTSLEEELTdlrvekeSLEKNLSERKK--KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 781
Cdd:NF033838 212 KVESKKAEAT-------RLEKIKTDREKaeEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKR 267
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
571-703 |
1.77e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.65 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 571 IQENERLKQEILEKSNRI-EEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE---NTQARVLHAEQEKAK-VTEEL 645
Cdd:pfam10368 27 LVELEKKEQELYEEIIELgMDEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEefkKIKEIIEEIEDEELKkEAEEL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150010552 646 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL----LRGQLTKVQAKLSELQETSEQ 703
Cdd:pfam10368 107 IDAMEERYEAYDELYDAYKKALELDKELYEMLKDEDLtleeLQEQIEKINESYEEVKEANEQ 168
|
|
| tig |
TIGR00115 |
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ... |
178-251 |
1.83e-03 |
|
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]
Pssm-ID: 272913 [Multi-domain] Cd Length: 410 Bit Score: 42.16 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 178 LDAVLSQ--DLIVADGPAVEVGDSLEVAYTGwlfqnHVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 251
Cdd:TIGR00115 131 LERLREQnaTLVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAG 199
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
720-854 |
1.91e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 720 LKVTSLEEELTDLRVEKESLEKnlserkkksaqERSQAEEEIDEirkSYQEELDKLRQLLKKTRvstdqaaaEQLslvqA 799
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 150010552 800 ELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITA 854
Cdd:COG0542 458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
397-491 |
1.94e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 42.76 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 397 QGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQA------PSAALMQVSSLDSHSAVSGN-AQSFQPYAGMQAY 469
Cdd:PRK10263 738 DGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQY 817
|
90 100
....*....|....*....|....
gi 150010552 470 AYPQASAVTSQ--LQPVRPLYPAP 491
Cdd:PRK10263 818 QQPQQPVAPQPqyQQPQQPVAPQP 841
|
|
| WH1 |
smart00461 |
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ... |
70-168 |
1.98e-03 |
|
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.
Pssm-ID: 214674 Cd Length: 106 Bit Score: 38.88 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 70 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 146
Cdd:smart00461 3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82
|
90 100
....*....|....*....|..
gi 150010552 147 RQnWSIMFESEKAAVEFNKQVC 168
Cdd:smart00461 83 CV-YGLNFASEEEAKKFRKKVL 103
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
564-867 |
2.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 564 MSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSlqtatENTQARVLHAEQEKAKVTE 643
Cdd:PRK01156 182 ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL-----KSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 644 ELAAATAQVSHLQLKMTAHQKKETELqMQLT---------------------ESLKET-DLLRGQLTKVQA---KLSELQ 698
Cdd:PRK01156 257 EIKTAESDLSMELEKNNYYKELEERH-MKIIndpvyknrnyindyfkykndiENKKQIlSNIDAEINKYHAiikKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 699 ETSEQAQSKfKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKsaQERSQAeeEIDEIRKSYQEELDKLRQL 778
Cdd:PRK01156 336 KDYNDYIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN--IERMSA--FISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 779 LKKTRVSTDQAAAEqlslvQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQ-------------RDAYQQKLVQLQEKC 845
Cdd:PRK01156 411 LNEINVKLQDISSK-----VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeeksnhiINHYNEKKSRLEEKI 485
|
330 340
....*....|....*....|..
gi 150010552 846 LALQAQITALTKQNEQHIKELE 867
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKE 507
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
626-903 |
2.42e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 626 NTQARVLHAEQEKAK-----VTEELAaataQVSHLQLKMtahqkkETElqmQLTESLKE--TDLLRGQLTKVQAKLSELQ 698
Cdd:pfam06160 7 KIYKEIDELEERKNElmnlpVQEELS----KVKKLNLTG------ETQ---EKFEEWRKkwDDIVTKSLPDIEELLFEAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 699 ETSEQaqSKFKSEKQNRKQLELKVTSLEEELTDLRvekESLeKNLSERKKKSAQERSQAEEEIDEIRKSY---------- 768
Cdd:pfam06160 74 ELNDK--YRFKKAKKALDEIEELLDDIEEDIKQIL---EEL-DELLESEEKNREEVEELKDKYRELRKTLlanrfsygpa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 769 ----QEELDKLRQLLKKTRVSTDQ----AAAEQLSLVQ---AELQTQWEaKCEHLLASAKDEHLQQYQEVcaqRDAYQqk 837
Cdd:pfam06160 148 idelEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEeetDALEELME-DIPPLYEELKTELPDQLEEL---KEGYR-- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010552 838 lvQLQEK-----CLALQAQITALTKQNEQHIKELEKNksQMSGVEAAASDPSEKvkkiMNQVFQSLRREFE 903
Cdd:pfam06160 222 --EMEEEgyaleHLNVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEER----IDQLYDLLEKEVD 284
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
691-777 |
2.67e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 39.52 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 691 QAKLSELQETSEQAQSKFKSEKQNRKQ----LELKVTSLEEELTDLRVEKESLEK-----------NLSERKKKSAQERS 755
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEEenrrleadhvsRLEEKEAELKKEYS 128
|
90 100
....*....|....*....|..
gi 150010552 756 QAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam09744 129 KLHERETEVLRKLKEVVDRQRD 150
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
575-872 |
3.08e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENtqarvLHAEQEKAKVT-EELAAATAQVS 653
Cdd:pfam05622 186 ETYKRQVQELHGKLSEESKKADKLEFEYKK--------LEEKLEALQKEKER-----LIIERDTLRETnEELRCAQLQQA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 654 HLQLKMTAHQK-----------------KETELQMQLteslkETDLLR----GQLTKVQAKLSELQETSEQAQSKFksEK 712
Cdd:pfam05622 253 ELSQADALLSPssdpgdnlaaeimpaeiREKLIRLQH-----ENKMLRlgqeGSYRERLTELQQLLEDANRRKNEL--ET 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 713 QNRKQlelkvtslEEELTDLRVEKESLEKNLSERKKK---SAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQA 789
Cdd:pfam05622 326 QNRLA--------NQRILELQQQVEELQKALQEQGSKaedSSLLKQKLEEHLEKLHEA-QSELQKKKEQIEELEPKQDSN 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 790 AAEQLslvqAELQTQWEAKCEHLLASakDEHLQQYQE----VCAQRDAYQQKLVQLQekCLALQAQITALTKQNEQHIKE 865
Cdd:pfam05622 397 LAQKI----DELQEALRKKDEDMKAM--EERYKKYVEkaksVIKTLDPKQNPASPPE--IQALKNQLLEKDKKIEHLERD 468
|
....*..
gi 150010552 866 LEKNKSQ 872
Cdd:pfam05622 469 FEKSKLQ 475
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
572-771 |
3.14e-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: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 572 QENERLKQEILEKSNRIEEqndkisELIERNQRYVEQSNLMMEKRNNS--LQTATENTQARVLHAEQEKAKVTEElaaat 649
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMRE------ELELEQQRRFEEIRLRKQRLEEErqRQEEEERKQRLQLQAAQERARQQQE----- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 650 aqvshlqlkmtAHQKKETELQMQlteslketdllrgqltkvqaklsELQETSEQAQskfkSEKQNRKQLELKVT------ 723
Cdd:pfam15709 427 -----------EFRRKLQELQRK-----------------------KQQEEAERAE----AEKQRQKELEMQLAeeqkrl 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 150010552 724 ---SLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 771
Cdd:pfam15709 469 memAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
528-922 |
3.27e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 528 DKMDHLMTKVEELQKhsagNSMLIPSMSVTMETSMI-MSNIQRIIQENERLKQEILEKSNRIE-----EQNDKI------ 595
Cdd:PTZ00440 863 QIVDNIIKDIENMNK----NINIIKTLNIAINRSNSnKQLVEHLLNNKIDLKNKLEQHMKIINtdniiQKNEKLnllnnl 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 596 ---SELIER--NQRYVEQSNLMMEKRNNSLQTATENTQARV-LHAEQEKAKVTE------ELAAATAQVSHLQLKMTAHQ 663
Cdd:PTZ00440 939 nkeKEKIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNDgTHLEKLDKEKDEwehfksEIDKLNVNYNILNKKIDDLI 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 664 KKETELQMQLTESLKeTDLLRGQLTKVQAKLSELQETSEQAQSKFKSE----------KQNRKQLELKVTSLEEELTDLR 733
Cdd:PTZ00440 1019 KKQHDDIIELIDKLI-KEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIdikkyknpkiKEEIKLLEEKVEALLKKIDENK 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 734 VEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyqeeLDKLRQLLKKTRVSTDQAAAEQLSLVQA-ELQTQWEAKCEHL 812
Cdd:PTZ00440 1098 NKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKS----LEKIYKQMEKTLKELENMNLEDITLNEVnEIEIEYERILIDH 1173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 813 LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL---------TKQNEQHIKELEKNKSQMSGvEAAASDP 883
Cdd:PTZ00440 1174 IVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTfeynayydkATASYENIEELTTEAKGLKG-EANRSTN 1252
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 884 SEKVKKIMNQVFQSLRRE-----------------FELEESYNGRTILGTIMNTIK 922
Cdd:PTZ00440 1253 VDELKEIKLQVFSYLQQVikennkmenalheiknmYEFLISIDSEKILKEILNSTK 1308
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
564-781 |
3.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 564 MSNIQRIIQENERLKQEILEKsnRIEEQNDKISEL------IERNQRYVEQsnlmMEKRNNSLQTATEN---TQARVLHA 634
Cdd:PRK04863 874 LSALNRLLPRLNLLADETLAD--RVEEIREQLDEAeeakrfVQQHGNALAQ----LEPIVSVLQSDPEQfeqLKQDYQQA 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 635 EQEKAKVTEELAAATAQVSHLqlkmtAHQKKETELQMqLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKF------ 708
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVVQRR-----AHFSYEDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqv 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 709 ----KSEKQNRKQLelkVTSLEEELTDLRVE-KESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQ---EELDKLRQLLK 780
Cdd:PRK04863 1022 laslKSSYDAKRQM---LQELKQELQDLGVPaDSGAEERARARRDELHARLSANRSRRNQLEKQLTfceAEMDNLTKKLR 1098
|
.
gi 150010552 781 K 781
Cdd:PRK04863 1099 K 1099
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
753-868 |
3.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 753 ERSQAEEEIDEIRKSYqEELDKLRQLLKKTRVSTD------------QAAAEQLSLVQAELQT--QWEA-KCEHLLASAK 817
Cdd:COG4913 219 EEPDTFEAADALVEHF-DDLERAHEALEDAREQIEllepirelaeryAAARERLAELEYLRAAlrLWFAqRRLELLEAEL 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 150010552 818 DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQ--------ITALTKQNEQHIKELEK 868
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEE 356
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
577-800 |
3.77e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 577 LKQEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATentqaRVLHAEQEK-AKVTEELAAATAQVSHL 655
Cdd:PRK11637 52 IQQDIAAKEKSVRQQQQQRASLLAQ-----------LKKQEEAISQAS-----RKLRETQNTlNQLNKQIDELNASIAKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 656 -------------QLKMTAHQKKETELQMQLT--ESLKETDLLR--GQLTKV-QAKLSELQETSEQAQskfksekQNRKQ 717
Cdd:PRK11637 116 eqqqaaqerllaaQLDAAFRQGEHTGLQLILSgeESQRGERILAyfGYLNQArQETIAELKQTREELA-------AQKAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 718 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyQEELDKLRQllKKTRVSTDQAAAEQLSLV 797
Cdd:PRK11637 189 LEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD--------QQQLSELRA--NESRLRDSIARAEREAKA 258
|
...
gi 150010552 798 QAE 800
Cdd:PRK11637 259 RAE 261
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
726-812 |
4.28e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 40.04 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 726 EEELTDLRVEKEslEKNLSERKKKSAQERSQAEEEiDEIRKsyqEELDKLRQLLKKTRvstdqAAAEQLSLVqAELQTQW 805
Cdd:pfam15927 5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72
|
....*....
gi 150010552 806 E--AKCEHL 812
Cdd:pfam15927 73 EryMRCDGL 81
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
603-903 |
4.42e-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: 41.31 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 603 QRYVEQSNLmmeKRNNSLQTATENtQARVLHAEQEKAKVTEELAAATaqvshlQLKMTAHQKKEtELQMQLTESLKETDL 682
Cdd:pfam01576 811 QRELEEARA---SRDEILAQSKES-EKKLKNLEAELLQLQEDLAASE------RARRQAQQERD-ELADEIASGASGKSA 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 683 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTdlrvekesleknlSERK--KKSAQERSQAEEE 760
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA-------------AERStsQKSESARQQLERQ 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 761 IDEIRKSYQEELDKLRQLLKKTrvstdqAAAEQLSLVQAELQTQWEAKcEHLLASakdehlqqyqevcaqrdayqqKLVQ 840
Cdd:pfam01576 947 NKELKAKLQEMEGTVKSKFKSS------IAALEAKIAQLEEQLEQESR-ERQAAN---------------------KLVR 998
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150010552 841 LQEKCLA-LQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKiMNQVFQSLRREFE 903
Cdd:pfam01576 999 RTEKKLKeVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR-ANAARRKLQRELD 1061
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
634-907 |
4.51e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 634 AEQEKAKVTEELAAATAQVSHLQLKMtahQKKETELQmqltESLKETDLLRGQLTKVQAKLSElqETSEQAQSKFKSEKQ 713
Cdd:pfam05701 61 AEAAKAQVLEELESTKRLIEELKLNL---ERAQTEEA----QAKQDSELAKLRVEEMEQGIAD--EASVAAKAQLEVAKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 714 NRKQLELKVTSLEEELTDLRVEKESL--EKNLSERKkksAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA 791
Cdd:pfam05701 132 RHAAAVAELKSVKEELESLRKEYASLvsERDIAIKR---AEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 792 EQLSLVQAELQ--TQWEAKCEHllasAKDEHLQQYQEVCAQRDaYQQKLVQLQEKCLALQAQITALT--KQNEQHIKELE 867
Cdd:pfam05701 209 HRIGAALAREQdkLNWEKELKQ----AEEELQRLNQQLLSAKD-LKSKLETASALLLDLKAELAAYMesKLKEEADGEGN 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 150010552 868 KNKSQMSGVEAAASDPSE--KVK----------KIMNQVFQSLRREFELEES 907
Cdd:pfam05701 284 EKKTSTSIQAALASAKKEleEVKaniekakdevNCLRVAAASLRSELEKEKA 335
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
533-776 |
4.81e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 533 LMTKVEELQKHSAGNSMLIPSMSVTMETSMIM---SNIQRIIQENERLKQEILEKSN-------RIEEQNDKISELIERN 602
Cdd:COG5022 919 LIENLEFKTELIARLKKLLNNIDLEEGPSIEYvklPELNKLHEVESKLKETSEEYEDllkkstiLVREGNKANSELKNFK 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 603 QRYVEQS-NLM-----------MEKRNNSLQTA-----TENTQARVLHAEQE-KAKVTEELAAATAQVSHLQL-KMTAHQ 663
Cdd:COG5022 999 KELAELSkQYGalqestkqlkeLPVEVAELQSAskiisSESTELSILKPLQKlKGLLLLENNQLQARYKALKLrRENSLL 1078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 664 KKETELQMQLTESL-KETDLLRGQLTKVQ-AKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLE-----EELTDLRVEK 736
Cdd:COG5022 1079 DDKQLYQLESTENLlKTINVKDLEVTNRNlVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEpvfqkLSVLQLELDG 1158
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 150010552 737 ESLEKNLSERKKKSA-----QERSQAEEEIDEIRKSYQEELDKLR 776
Cdd:COG5022 1159 LFWEANLEALPSPPPfaalsEKRLYQSALYDEKSKLSSSEVNDLK 1203
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
514-710 |
4.83e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.03 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 514 QHNTEIRMAVSKVADKMDHLMTKVEE---LQKHSAgnsmlipsmsvTMETSmimsniqriIQENERLKQEILEK----SN 586
Cdd:pfam15665 22 AHEEEIQQILAETREKILQYKSKIGEeldLKRRIQ-----------TLEES---------LEQHERMKRQALTEfeqyKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 587 RIEEQNDKISEliERNQRYVEQSNLMMEKRNNSLQTATENTQARVlHAEQEKAKVTEELAAATAQ-VSHLQLKMTAHQKK 665
Cdd:pfam15665 82 RVEERELKAEA--EHRQRVVELSREVEEAKRAFEEKLESFEQLQA-QFEQEKRKALEELRAKHRQeIQELLTTQRAQSAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 150010552 666 ETELQMQLTESLK-ETDLLRGQLTKVQAKLSELQETSEQAQSKFKS 710
Cdd:pfam15665 159 SLAEQEKLEELHKaELESLRKEVEDLRKEKKKLAEEYEQKLSKAQA 204
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
678-764 |
4.87e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 678 KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL-EKNLSE--RKKKSAQER 754
Cdd:TIGR04320 254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATaqAALANAEAR 333
|
90
....*....|.
gi 150010552 755 -SQAEEEIDEI 764
Cdd:TIGR04320 334 lAKAKEALANL 344
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
575-821 |
5.03e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 575 ERLKQEI-LEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVlhaEQEKAKVTEELAAATAQVS 653
Cdd:PRK05771 34 EDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV---EEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 654 HLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA------KLSELQETSEQAQSKFKSEKQNRK-----QLELKV 722
Cdd:PRK05771 111 ELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVyvvvvVLKELS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 723 TSLEEELTDLRVEKESLEknlseRKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdqaaaEQLSLVQAELQ 802
Cdd:PRK05771 191 DEVEEELKKLGFERLELE-----EEGTPSELIREIKEELEEIEKERESLLEELKELAKKY---------LEELLALYEYL 256
|
250
....*....|....*....
gi 150010552 803 TQWEAKCEHLLASAKDEHL 821
Cdd:PRK05771 257 EIELERAEALSKFLKTDKT 275
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
951-1121 |
5.56e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 951 RPRRPSQEQSASASSGQPQAPLNRERPesPMVPSEQVVEEAVPLPPQAlttSQDGHRRKGDSEAEALSEIKDGSLPPELS 1030
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTR--PAVASLSESRESLPSPWDP---ADPPAAVLAPAAALPPAASPAGPLPPPTS 2833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 1031 CIPSHRVLGPPTSIPPEPL-GPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPdgPLQESSTRLSLTSDPEEGDPla 1109
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLgGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQPERPP-- 2909
|
170
....*....|..
gi 150010552 1110 lGPESPGEPQPP 1121
Cdd:PHA03247 2910 -QPQAPPPPQPQ 2920
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
689-866 |
5.88e-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: 39.17 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 689 KVQAKLSELQETSEQAQSKFKSEKQNrkqlelKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIdeirksy 768
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQE------LVDRLEKETEALR---ERLQKDLEEVRAKLEPYLEELQAKL------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 769 QEELDKLRQLLK------KTRVSTD-QAAAEQLSLVQAELQTQWEAKCEHLLAsakdeHLQQYQEvcAQRDAYQQKLVQL 841
Cdd:pfam01442 65 GQNVEELRQRLEpyteelRKRLNADaEELQEKLAPYGEELRERLEQNVDALRA-----RLAPYAE--ELRQKLAERLEEL 137
|
170 180
....*....|....*....|....*
gi 150010552 842 QEKclaLQAQITALTKQNEQHIKEL 866
Cdd:pfam01442 138 KES---LAPYAEEVQAQLSQRLQEL 159
|
|
| Tig |
COG0544 |
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ... |
186-251 |
6.02e-03 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440310 [Multi-domain] Cd Length: 424 Bit Score: 40.50 E-value: 6.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 186 LIVADGPAvEVGDSLEVAYTGWlfqnhVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 251
Cdd:COG0544 151 LVPVERAA-EEGDRVTIDFEGT-----IDGEEFEGGKAED--YSLELGSGSFIPGFEEQLVGMKAG 208
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
675-905 |
6.12e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.72 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 675 ESLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKsekqnrkqlelkvtsleEELTDLRVEKESLEKNLsERKKKSAQEr 754
Cdd:pfam17078 13 DALTKTNL---QLTVQSQNLLSKLEIAQQKESKFL-----------------ENLASLKHENDNLSSML-NRKERRLKD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 755 sqAEEEIDEIRKSYQE---ELDKLRQLLKKTRvSTDQAAAEQLSLVQAelqtQWEAkcehLLASakdehlQQYQevcaqR 831
Cdd:pfam17078 71 --LEDQLSELKNSYEElteSNKQLKKRLENSS-ASETTLEAELERLQI----QYDA----LVDS------QNEY-----K 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 832 DAYQQKLVQLQEkclALQAQITALTKQNEQHI-------KELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFEL 904
Cdd:pfam17078 129 DHYQQEINTLQE---SLEDLKLENEKQLENYQqrissndKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDL 205
|
.
gi 150010552 905 E 905
Cdd:pfam17078 206 P 206
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
640-812 |
6.16e-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: 39.17 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 640 KVTEELAAATAQVSHLQLKMTAHQKketELQMQLTeslKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSE-KQNRKQL 718
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQ---ELVDRLE---KETEALRERL---QKDLEEVRAKLEPYLEELQAKlGQNVEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 719 ELKVTSLEEELTD-LRVEKESLEKNLSErkkKSAQERSQAEEEIDEIRKSYQEELDKLRQL-------LKKTRVSTDQAA 790
Cdd:pfam01442 72 RQRLEPYTEELRKrLNADAEELQEKLAP---YGEELRERLEQNVDALRARLAPYAEELRQKlaerleeLKESLAPYAEEV 148
|
170 180
....*....|....*....|..
gi 150010552 791 AEQLSLVQAELQTQWEAKCEHL 812
Cdd:pfam01442 149 QAQLSQRLQELREKLEPQAEDL 170
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
689-912 |
6.21e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.21 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 689 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELT--DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEiRK 766
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-RK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 767 SYQEELDKLRQLLKKTRVSTDQAAAEqlslvQAELQTQWEAKcehllasAKDEHLQQYQEVCAQRDAYQQKL---VQLQE 843
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAE-----EAKKKAEAEAK-------AKAEAEAKAKAEEAKAKAEAAKAkaaAEAAA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150010552 844 KCLALQAQITALTKQ------NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRT 912
Cdd:TIGR02794 212 KAEAEAAAAAAAEAErkadeaELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFRGKT 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
668-781 |
6.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 668 ELQMQLTESLKETDLLRGQltkVQAKLSELQETSEQAQSKFKSEKQNRKQlelkvtSLEEELTDLRVEKESLEKNLSERK 747
Cdd:PRK00409 527 ELERELEQKAEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEK------EAQQAIKEAKKEADEIIKELRQLQ 597
|
90 100 110
....*....|....*....|....*....|....
gi 150010552 748 KKsaQERSQAEEEIDEIRKSYQEELDKLRQLLKK 781
Cdd:PRK00409 598 KG--GYASVKAHELIEARKRLNKANEKKEKKKKK 629
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
511-813 |
6.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSA---GNSMlIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNR 587
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlnGQSV-CPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 588 IEEQNDKISELIERN--------QRYVEQSNLMMEKRNNslQTATENTQARVLHAEQEKAKVTEELAAAtaqvsHLQLkm 659
Cdd:PRK01156 492 VKDIDEKIVDLKKRKeyleseeiNKSINEYNKIESARAD--LEDIKIKINELKDKHDKYEEIKNRYKSL-----KLED-- 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 660 tAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQnrkQLELKVTSLEEELtdlrvekesl 739
Cdd:PRK01156 563 -LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKS---YIDKSIREIENEA---------- 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 740 ekNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ--------WEAKCEH 811
Cdd:PRK01156 629 --NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDdakanrarLESTIEI 706
|
..
gi 150010552 812 LL 813
Cdd:PRK01156 707 LR 708
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
668-891 |
7.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 668 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQA----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 743
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENiarkQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 744 SERKKKSAQERSQAeEEIDEIRKSYQE-------------ELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQtqwEAKCE 810
Cdd:PHA02562 258 NKLNTAAAKIKSKI-EQFQKVIKMYEKggvcptctqqiseGPDRITKI--KDKLKELQHSLEKLDTAIDELE---EIMDE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 811 HLLASAKdehlqqYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ---NEQHIKELEKNKSQMSgveaaaSDPSEKV 887
Cdd:PHA02562 332 FNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIV------KTKSELV 399
|
....
gi 150010552 888 KKIM 891
Cdd:PHA02562 400 KEKY 403
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
686-908 |
7.26e-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: 39.35 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 686 QLTKVQAKLSELQETSEQAQSKFKSEK------QNRKQLElKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 759
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDygddleSVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 760 EIDEIRKSYQEeldkLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASakDEHLQQYQEVCAQrdayQQKLV 839
Cdd:cd00176 80 RLEELNQRWEE----LRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEEL----LKKHK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 840 QLQEKCLALQAQITALTKQNEQHIKEleknksQMSGVEAAASDPSEKVKKIMNQVFQSL-RREFELEESY 908
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEE------GHPDADEEIEEKLEELNERWEELLELAeERQKKLEEAL 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
576-775 |
7.32e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 576 RLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaEQEKAKVTEELAAATAQVSHL 655
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL--AGRLREVTLEGEGGSAGGSLT 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 656 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVE 735
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 150010552 736 KESLEKNLSERKKKSAQERSQAEEEIDEIRKsyqeELDKL 775
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLER----EIEAL 779
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
642-826 |
7.74e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.34 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 642 TEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELK 721
Cdd:pfam17078 16 TKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 722 V-------TSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQllkktRVSTDQAAAE-- 792
Cdd:pfam17078 96 LenssaseTTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQ-----RISSNDKDIDtk 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 150010552 793 ---------QLSLVQAELQTQWEAKCEHLLASAK-DEHLQQYQE 826
Cdd:pfam17078 171 ldsynnkfkNLDNIYVNKNNKLLTKLDSLAQLLDlPSWLNLYPE 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-889 |
7.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 573 ENERLKQEILEKSN---RIEE-QNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAA 648
Cdd:PTZ00121 1112 EEARKAEEAKKKAEdarKAEEaRKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 649 TAQVSHLQLKMTAHQKKETELQMQltESLKETDLLRGQLTKvqaKLSELQETSEQAQ--SKFKSEKQNRKQLELKVTSLE 726
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEEERKAE--EARKAEDAKKAEAVK---KAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFA 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 727 EELTDLRVEkeslEKNLSERKKKsAQERSQAeeeiDEIRKSyqEELDKLRQLLKKT----RVSTDQAAAEQLSLVQAELQ 802
Cdd:PTZ00121 1267 RRQAAIKAE----EARKADELKK-AEEKKKA----DEAKKA--EEKKKADEAKKKAeeakKADEAKKKAEEAKKKADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 803 TQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK---ELEKNKSQMSGVEAA 879
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaEEDKKKADELKKAAA 1415
|
330
....*....|
gi 150010552 880 ASDPSEKVKK 889
Cdd:PTZ00121 1416 AKKKADEAKK 1425
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
674-873 |
8.29e-03 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 38.78 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 674 TESLKETDLLRGQLTKVQAKLSELQETSE------QAQSKFKSEKQNRKQLELkvTSLEEELTDLRVEKESLEKNLSERk 747
Cdd:cd16855 4 LEIRQQLEELRQRTQETENDLRNLQQKQEsfviqyQESQKIQAQLQQLQQQPQ--NERIELEQQLQQQKEQLEQLLNAK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 748 kksAQERSQAEEEIDEIrksYQEELDKLRQLLKKtrvstdqaaaeqlslVQAELQTQWEAKcehllasakdehlQQYQEV 827
Cdd:cd16855 81 ---AQELLQLRMELADK---FKKTIQLLSKLQSR---------------VLDEELIQWKRQ-------------QQLAGN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 150010552 828 CAQRDAyqqKLVQLQEKCLALqaqiTALTKQNEQHIKELEKNKSQM 873
Cdd:cd16855 127 GAPFES---NLDTIQEWCESL----AEIIWQNRQQIKRAERLKQKL 165
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
702-777 |
8.93e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 8.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150010552 702 EQAQSKFKSEKQNRKQlelKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam03938 18 KAAQAQLEKKFKKRQA---ELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQ 90
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
612-812 |
9.59e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 39.21 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 612 MMEKRNNSLQTATEntqarVLHAEQEKAKVTEELAaataqvshlqlkmtahqKKETELQMQLTESLKETDLLRGqLTKVQ 691
Cdd:cd07651 10 IQTRIKDSLRTLEE-----LRSFYKERASIEEEYA-----------------KRLEKLSRKSLGGSEEGGLKNS-LDTLR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010552 692 aklselQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKES-LEKNLserKKKSAQE------RSQAEEEIDEI 764
Cdd:cd07651 67 ------LETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQShMEKLL---KKKQDQEkylekaREKYEADCSKI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150010552 765 rKSYQ--------EELDKLRQLLKKTRVSTD------QAAAEQLSLVQAELQTQWEAKCEHL 812
Cdd:cd07651 138 -NSYTlqsqltwgKELEKNNAKLNKAQSSINssrrdyQNAVKALRELNEIWNREWKAALDDF 198
|
|
| |
