|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
192-285 |
3.18e-28 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 109.21 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 192 AVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACAAGSEGVIGW 271
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 1242862604 272 TQPTDSILVFEVEV 285
Cdd:pfam00254 80 VIPPNATLVFEVEL 93
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
183-285 |
3.19e-26 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 103.72 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 183 QDLVAAEGPAVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACA 262
Cdd:COG0545 4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....*.
gi 1242862604 263 ---AGSEGVIgwtqPTDSILVFEVEV 285
Cdd:COG0545 80 ygeRGAGGVI----PPNSTLVFEVEL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
561-875 |
6.34e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 561 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATA 638
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEelAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 639 QVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 718
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 719 DLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEakcE 798
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEE-EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR---L 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 799 QLLASARDEHLQQYREVCAQRDAHQQK-----LALLQDECLALQAQIAA---------FTEQKEHMQRLEKTKSQAPAGR 864
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRglagaVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAIEYLKAAKAGR 573
|
330
....*....|.
gi 1242862604 865 AAADPSEKVKK 875
Cdd:COG1196 574 ATFLPLDKIRA 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-882 |
2.24e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 564 NIQR---IIQE-NERLKQelLEKSSRIEEQNDKISDliERNQRYVEQSNLMMEKRNNSLQTAtENTQAKVTEELAAATAQ 639
Cdd:COG1196 187 NLERledILGElERQLEP--LERQAEKAERYRELKE--ELKELEAELLLLKLRELEAELEEL-EAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 640 VSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTD 719
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 720 LRAEKTSLEKNLSERKKK---SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQsqwEAK 796
Cdd:COG1196 342 LEEELEEAEEELEEAEAElaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 797 CEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKI 876
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
....*.
gi 1242862604 877 MNQVFQ 882
Cdd:COG1196 499 AEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
564-857 |
3.91e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 564 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATEntqakVTEELAAATAQVSHL 643
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-----LEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 644 QLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEK--------------QSRRQLELK 709
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaaterrledleEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 710 VTSLEEELTDLRAEKTSLEKNL---SERKKKSAQERCQAEAEMDEIR---KSHQEELDRLRQLLKKARvstdqAAAEQLT 783
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSeelRELESKRSELRRELEELR-----EKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 784 LAQAELQSQWEAKCEQLLASAR---DEHLQQYREVCAQRDAHQQKLALLQDECLAL----QAQIAAFTEQKEHMQRLEKT 856
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYDFLTAQ 1008
|
.
gi 1242862604 857 K 857
Cdd:TIGR02168 1009 K 1009
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
531-847 |
4.62e-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: 73.95 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 531 LMTKVEELQKHSSgnsMLLPSMSV-TMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNL 609
Cdd:TIGR02169 693 LQSELRRIENRLD---ELSQELSDaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 610 MMEKRNNsLQTATENTQA--------KVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD 681
Cdd:TIGR02169 770 LEEDLHK-LEEALNDLEArlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 682 LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKsaqeRCQAEAEMDEIRKsHQEELD 761
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRK-RLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 762 RLRQLLKKARVSTDQAAAEQLTLAQAELQ-SQWEAKCEQLLASARD------EHLQQYREVCAQRDAHQQKLALLQDECL 834
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELSlEDVQAELQRVEEEIRAlepvnmLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
330
....*....|...
gi 1242862604 835 ALQAQIAAFTEQK 847
Cdd:TIGR02169 1004 AILERIEEYEKKK 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
576-860 |
2.36e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 576 KQELLEKSSRIEEQNDKISDLIERnqryveqsnlmMEKRNNSLQTatentQAKVTEELAAATAQVSHLQL-----KMTAH 650
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNE-----------LERQLKSLER-----QAEKAERYKELKAELRELELallvlRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 651 QKKETELQLQLTDNLKETDLLRGHVTRLQADLSELR-------EASEQTQTKFKS--------------EKQSRRQLELK 709
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYAlaneisrleqqkqiLRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 710 VTSLEEELTDLRAEKTSLEKNLSERKKK--SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKA--RVSTDQAAAE-QLTL 784
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLElQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 785 AQAELQSQwEAKCEQLlaSARDEHLQQYRE------VCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKS 858
Cdd:TIGR02168 398 LNNEIERL-EARLERL--EDRRERLQQEIEellkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
..
gi 1242862604 859 QA 860
Cdd:TIGR02168 475 QA 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-895 |
2.07e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 651 QKKETELQL--------QLTDNLKEtdlLRGHVTRLQA-------------------------DLSELREASEQTQTKFK 697
Cdd:TIGR02168 173 RRKETERKLertrenldRLEDILNE---LERQLKSLERqaekaerykelkaelrelelallvlRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 698 SEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK-----SAQERCQAEAEMDEIRKSH----QEELDRLRQLLK 768
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEISRLEQQKQILRERLANlerqLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 769 KARVsTDQAAAEQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQ 846
Cdd:TIGR02168 330 SKLD-ELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1242862604 847 KEHMQ-RLEKTKSQAPAGRAAADPSEKvKKIMNQVFQSLRGEFELEESYD 895
Cdd:TIGR02168 409 LERLEdRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEELQEELE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
649-875 |
5.12e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 649 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 728
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 729 KNLSERKKK------SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELQSQWEAKCEQL-- 800
Cdd:COG4942 97 AELEAQKEElaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERae 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 801 LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 875
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
566-788 |
1.76e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 566 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKrnnslqtaTENTQAKVTEELAAATAQVSHLQL 645
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED--------AEERLAKLEAEIDKLLAEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 646 KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTK---FKSEKQS-----------RRQLELKVT 711
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKlekLKREINElkreldrlqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 712 SLEEELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSH---QEELDRLRQLLKKARVSTDQAAAEQLTLA 785
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEeekEDKALEIKKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
...
gi 1242862604 786 QAE 788
Cdd:TIGR02169 504 ERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
627-821 |
2.08e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 627 AKVTEELAAATAQVSHLQLKMTAHQKKETELQ--LQLTDNLKETDLLRGHVTRLQADLSELREASeqtqTKFKSEKQSRR 704
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASS----DDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 705 QLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELD-RLRQLLKKARVstdQAAAEQLT 783
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEeRFAAALGDAVE---RELRENLE 772
|
170 180 190
....*....|....*....|....*....|....*...
gi 1242862604 784 LAQAELQSQwEAKCEQLLASARDEHLQQYREVCAQRDA 821
Cdd:COG4913 773 ERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDA 809
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-776 |
6.86e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 561 IMSNIQRIIQENERLKQELLEkssrIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTaTENTQAKVTEELAAATAQV 640
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-LKDEQNKIKKQLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 641 --SHLQLKMTAHQKKETELQLQLTDNLKETDLLRghvtRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 718
Cdd:TIGR04523 277 eqNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK----ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 719 DLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDrLRQLLKKARVSTDQ 776
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQ 409
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
507-768 |
9.34e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 507 MTEARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSvtMETSMIMSNIQRIIQENERLKQELLEKSSRI 586
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR--KDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 587 EEQNDKISDL------IERNQRYVEQSNLMMEKRNNSLQTATENTQAKVT------------------------------ 630
Cdd:TIGR02168 764 EELEERLEEAeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaanlrerleslerriaaterrledl 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 631 -EELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELK 709
Cdd:TIGR02168 844 eEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1242862604 710 VTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLK 768
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
515-789 |
1.78e-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: 62.38 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 515 TEIRMAVNKVADKMDHLMTKVEELQKhssgnsmllpsmsvtmETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKIS 594
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 595 DLIERNQRyveqsnlmMEKRNNSLQTATENTQAKVTE---ELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLL 671
Cdd:TIGR02168 334 ELAEELAE--------LEEKLEELKEELESLEAELEEleaELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 672 RGHVTRLQADLSELREasEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEknlsERKKKSAQERCQAEAEMDE 751
Cdd:TIGR02168 406 EARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLE----EALEELREELEEAEQALDA 479
|
250 260 270
....*....|....*....|....*....|....*....
gi 1242862604 752 IRKSHQEELDRLRQLLK-KARVSTDQAAAEQLTLAQAEL 789
Cdd:TIGR02168 480 AERELAQLQARLDSLERlQENLEGFSEGVKALLKNQSGL 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
570-793 |
3.34e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 570 QENERLKQELLEKSSRIEEQNDKISDL---IERNQRYVEQSNLMMEKRNNSLQtATENTQAKVTEELAAATAQVSHLQLK 646
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 647 MTAHQKKETEL--QLQLTDNLKETDLLRG---------HVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEE 715
Cdd:COG4942 99 LEAQKEELAELlrALYRLGRQPPLALLLSpedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 716 ELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQW 793
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
512-758 |
6.74e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 512 QHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGnsmllpsmsVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQND 591
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINE---------KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 592 KISDLIER-NQRYVEQSNLMMEKRnnslqtatENTQAKVTEELaaataqvshlqlkmTAHQKKETELQLQLTDNLKETDL 670
Cdd:TIGR04523 282 KIKELEKQlNQLKSEISDLNNQKE--------QDWNKELKSEL--------------KNQEKKLEEIQNQISQNNKIISQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 671 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQ---AEA 747
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikkLQQ 419
|
250
....*....|.
gi 1242862604 748 EMDEIRKSHQE 758
Cdd:TIGR04523 420 EKELLEKEIER 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
571-815 |
7.44e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEkssRIEEQNDKISDL---IERNQRYVEQSNL-MMEKRNNSLQTATENTQakvtEELAAATAQVSHLQLK 646
Cdd:COG4913 245 EDAREQIELLE---PIRELAERYAAArerLAELEYLRAALRLwFAQRRLELLEAELEELR----AELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 647 MTAHQKKETELQLQLTDNlkETDLLrghvTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTS 726
Cdd:COG4913 318 LDALREELDELEAQIRGN--GGDRL----EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 727 LEKNLSERKKKSAQERCQAEAEMDEIRKSHQE---ELDRLRQL-------LKKARvstdQAAAEQLTLAQAEL------- 789
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELREleaEIASLERRksniparLLALR----DALAEALGLDEAELpfvgeli 467
|
250 260 270
....*....|....*....|....*....|....*..
gi 1242862604 790 -----QSQWEAKCEQLLASAR------DEHLQQYREV 815
Cdd:COG4913 468 evrpeEERWRGAIERVLGGFAltllvpPEHYAAALRW 504
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
616-869 |
1.29e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.54 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 616 NSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETE-LQLQLTDNLKETdllrghvTRLQADLSELReASEQTQT 694
Cdd:PRK11281 43 AQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKL-------RQAQAELEALK-DDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 695 KFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSerKKKSAQERCQaeAEMDEirksHQEELDRLRQLLKKARVST 774
Cdd:PRK11281 115 RETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV--SLQTQPERAQ--AALYA----NSQRLQQIRNLLKGGKVGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 775 DQAAAEQLTLAQAELQSqWEAKCE---QLLASArdEHLQQYREvcAQRDAHQQKLALLQDECLALQAQIAA--FTEQKEH 849
Cdd:PRK11281 187 KALRPSQRVLLQAEQAL-LNAQNDlqrKSLEGN--TQLQDLLQ--KQRDYLTARIQRLEHQLQLLQEAINSkrLTLSEKT 261
|
250 260
....*....|....*....|
gi 1242862604 850 MQRLEktkSQAPAGRAAADP 869
Cdd:PRK11281 262 VQEAQ---SQDEAARIQANP 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-842 |
1.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 565 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERnqryveqsnlmmekrnnslqtatentqakvtEELAAATAQVSHLQ 644
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQER-------------------------------REALQRLAEYSWDE 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 645 LKMTAHQKKETELQLQLtDNLKETDllrGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEK 724
Cdd:COG4913 661 IDVASAEREIAELEAEL-ERLDASS---DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 725 TSLEKNLSERKKKSAQERCQAEAEmDEIRKSHQEELDRLRQLLKKARvstdQAAAEQLTLAQAELQSQWEAKCEQLLASA 804
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALG-DAVERELRENLEERIDALRARL----NRAEEELERAMRAFNREWPAETADLDADL 811
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1242862604 805 RDehLQQYREVCAQ--RD---AHQQKLALLQDEC-----LALQAQIAA 842
Cdd:COG4913 812 ES--LPEYLALLDRleEDglpEYEERFKELLNENsiefvADLLSKLRR 857
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
564-855 |
1.87e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 564 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRnNSLQTATENTQAKVTEELAAATAQVSHL 643
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 644 QLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD------------------------------------------ 681
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallallglggsllsliltiagvlflvlg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 682 -----LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAeKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSH 756
Cdd:COG4717 285 llallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 757 QEE--LDRLRQLLKKARVSTD-------------QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDA 821
Cdd:COG4717 364 QLEelEQEIAALLAEAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
330 340 350
....*....|....*....|....*....|....
gi 1242862604 822 HQQKLALLQDECLALQAQIAAFTEQKEHMQRLEK 855
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
566-819 |
2.69e-08 |
|
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: 58.21 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 566 QRIIQENERLKQELlEKSSRIEEQNDKISDLIERNQR-YVEQSNLMMEkRNNSL------QTATENTQAKvTEELAAATA 638
Cdd:pfam17380 299 ERLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQAAiYAEQERMAME-RERELerirqeERKRELERIR-QEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 639 QVSHLQ-LKMTAHQKK----------------ETELQLQLTDNLKETDLLRGHVTRL-QADLSELREASEQTQTKFKSEK 700
Cdd:pfam17380 376 RMRELErLQMERQQKNervrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 701 QSRRQlelKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQAAAE 780
Cdd:pfam17380 456 QERQQ---QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQKAIYE 531
|
250 260 270
....*....|....*....|....*....|....*....
gi 1242862604 781 QLTLAQAELQSQWEAKCEQllasaRDEHLQQYREVCAQR 819
Cdd:pfam17380 532 EERRREAEEERRKQQEMEE-----RRRIQEQMRKATEER 565
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
193-250 |
3.08e-08 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 53.57 E-value: 3.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 193 VETGDSLEVAYTGWLLQnhvlGQVFDSTANkDKPLRLKLGSGKVVKGLEDGLLGMKKG 250
Cdd:COG1047 1 IEKGDVVTLHYTLKLED----GEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVG 53
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
518-859 |
3.27e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.06 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 518 RMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSM--IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISD 595
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKqvLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 596 LIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVtEELAAATAQVSHLQLKMtahQKKETELQLQLTDNLKEtdllRGHV 675
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKA-APLAAHIKAVTQIEQQA---QRIHTELQSKMRSRAKL----LMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 676 TRLQADLSELREASEQTQTKFKSEKQSRRQlelkvtslEEELTDLRAEKtSLEKNLSERKKKSAQERCQAEaemdEIRKS 755
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDA--------HEVATSIREIS-CQQHTLTQHIHTLQQQKTTLT----QKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 756 HQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYRevcaQRDAHQQKLALLQDECLA 835
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK----LEKIHLQESAQSLKEREQ 473
|
330 340
....*....|....*....|....*....
gi 1242862604 836 LQAQIAAFTEQ-----KEHMQRLEKTKSQ 859
Cdd:TIGR00618 474 QLQTKEQIHLQetrkkAVVLARLLELQEE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-798 |
3.69e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 563 SNIQRIIQENErlkQELLEKSSRIEEQNDKISDLIERnQRYVEQSNLMMEKRNNSLqTATENTQAKVTEELAAATAQVSH 642
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI-EELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 643 LQlKMTAHQKKETElqlQLTDNLKETDLLRGHVTRLQAdLSELREaseqtqtKFKSEKqsrRQLELKVTSLEEELTDLRA 722
Cdd:PRK03918 264 LE-ERIEELKKEIE---ELEEKVKELKELKEKAEEYIK-LSEFYE-------EYLDEL---REIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862604 723 EKTSLEKnLSERKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCE 798
Cdd:PRK03918 329 RIKELEE-KEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
569-872 |
3.81e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 57.66 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 569 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVE----QSNLMMEKRN---NSLQTATENTQAKVTEELAAATAQVS 641
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 642 HLQLKmtaHQKKETELQLQLTDNLKETDllrGHVTRLQADLSELREASEQTQTKFKSEKqSRRQLELKVTSLEEELTDLR 721
Cdd:COG5185 311 TESLE---EQLAAAEAEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEI-ENIVGEVELSKSSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 722 AEKTSLEKNLSErKKKSAQERCQ--AEAEMDEIrKSHQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELQSQWEAKCEQ 799
Cdd:COG5185 384 DTIESTKESLDE-IPQNQRGYAQeiLATLEDTL-KAADRQIEELQRQIEQA-TSSNEEVSKLLNELISELNKVMREADEE 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242862604 800 LLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQR-LEKTKSQAPAGRAAADPSEK 872
Cdd:COG5185 461 SQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE---KLRAKLERqLEGVRSKLDQVAESLKDFMR 531
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
190-308 |
4.02e-08 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 55.92 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 190 GPAVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSgkVVKGLEDGLLGMKKGGKRLIITPSACAAGSEGVI 269
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLID----GKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
|
90 100 110
....*....|....*....|....*....|....*....
gi 1242862604 270 GWtqPTDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 308
Cdd:PRK10902 232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
569-854 |
4.22e-08 |
|
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: 56.47 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 569 IQENERLKQELLEKSSRIEEQndkisdliernqryveqsnlMMEKRNNSLQTATENTQAKVTEELAAATAqvshLQLKMT 648
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEM--------------------MEEERERALEEEEEKEEERKEERKRYRQE----LEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 649 AHQKKETELQLQLtdnLKETDLLRGHVTRLQA-DLSELRE-ASEQTQT-----KFKSEKQSRRQLELKvtslEEELTDLR 721
Cdd:pfam13868 84 EREQKRQEEYEEK---LQEREQMDEIVERIQEeDQAEAEEkLEKQRQLreeidEFNEEQAEWKELEKE----EEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 722 AEKTSLEKNLSERKKksaqercqaEAEMDEIRKSHQEELDRLRQLLKKARvsTDQAAAEQL--TLAQAELQSQWEAK--- 796
Cdd:pfam13868 157 ILEYLKEKAEREEER---------EAEREEIEEEKEREIARLRAQQEKAQ--DEKAERDELraKLYQEEQERKERQKere 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 797 -------CEQLLASARDEHL---QQYREVCAQRDAHQQKLALLQdecLALQAQIAAFTEQKEHMQRLE 854
Cdd:pfam13868 226 eaekkarQRQELQQAREEQIelkERRLAEEAEREEEEFERMLRK---QAEDEEIEQEEAEKRRMKRLE 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
575-795 |
5.18e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 575 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATEnTQAKVTEELAAATAQVSHLQlkmtaHQKKE 654
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELR-----EELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 655 TELQLQLTDNLKETDLLRGHVTRLQADLSELREaseqtqtkfksEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSER 734
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEE-----------RLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242862604 735 KKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEA 795
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-788 |
9.06e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 573 ERLKQELLEKSSRIEEQNDKisdliernqRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQVSHLQLKMTAHQK 652
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEA 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 653 KETELQLQLTDNLKETDLLRGHVTRLQADLSE-------LREASEQT-----QTKFKSEKQSRRQLELKVTSLEEELTDL 720
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaeeLKKAEEENkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242862604 721 RAEKTSLEKNLSER-KKKSAQERCQAEaemdEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAE 788
Cdd:PTZ00121 1693 ALKKEAEEAKKAEElKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE 1755
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
571-874 |
9.94e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQA---KVTEELAAATAQVSHLQLKM 647
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 648 TAHQ-KKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEqtqTKFKSEkQSRRQLELKVTSlEEELTDLRAEKTS 726
Cdd:PTZ00121 1392 KADEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE---AKKKAE-EAKKADEAKKKA-EEAKKAEEAKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 727 LEKNLSERKKKSAQERCQAE--AEMDEIRKSHQEELDRLRQLLKKA---RVSTDQAAAEQLTLAQAELQSQWEAKCEQLL 801
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 802 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK--EHMQRLEKTKSQAPAGRAAADPSEKVK 874
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
631-839 |
1.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 631 EELAAATAQVSHLQLKMTAHQK-KETELQLQLTDNLKEtdllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELK 709
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERyAAARERLAELEYLRA----ALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 710 VTSLEEELTDLRAEktsLEKNLSERKKKSAQERCQAEAEMDEIrkshQEELDRLRQLLKKARVSTDQAAAEQltlaqAEL 789
Cdd:COG4913 318 LDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEEF-----AAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1242862604 790 QSQWEAKCEQLlASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQ 839
Cdd:COG4913 386 RAEAAALLEAL-EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
660-867 |
1.65e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 660 QLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLE--LKVTSLEEELTDLRAEKTSLEKNLsERKKK 737
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERL-EELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 738 SAQERCQAEAEMDEIRkshqEELDRLRQLLKKARVSTDQAAAEQLTlaqaelqsqweakceqllasardEHLQQYREVCA 817
Cdd:COG4717 154 RLEELRELEEELEELE----AELAELQEELEELLEQLSLATEEELQ-----------------------DLAEELEELQQ 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1242862604 818 QRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 867
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
679-895 |
1.75e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 679 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKK--KSAQERCQAEAEMDEIRKSH 756
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 757 QEELDRLRQLLKKARVSTDQAAAE------QLTLAQAELQSQWEAKCEQlLASARDEHLQQYREVCAQR---DAHQQKLA 827
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEaeaeieELEAQIEQLKEELKALREA-LDELRAELTLLNEEAANLRerlESLERRIA 834
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 828 LLQDECLALQAQIAaftEQKEHMQRLEktKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYD 895
Cdd:TIGR02168 835 ATERRLEDLEEQIE---ELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
648-820 |
1.94e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 648 TAHQKKETELQLQLTDNlkETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSL 727
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 728 EKNLSE----------RKKKSAQERCQAEAE------MDEI------RKSHQEELDRLRQLLKKARVSTDQAAAEqltlA 785
Cdd:COG1579 79 EEQLGNvrnnkeyealQKEIESLKRRISDLEdeilelMERIeeleeeLAELEAELAELEAELEEKKAELDEELAE----L 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1242862604 786 QAELQSQwEAKCEQLLASARDEHLQQYREVCAQRD 820
Cdd:COG1579 155 EAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
570-860 |
2.14e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 570 QENERLKQELLEKSSRIEEQNDKISDLIERNQryveqsnlmmEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTA 649
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVR----------DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 650 HQKKET-----ELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRaek 724
Cdd:PRK02224 321 DRDEELrdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR--- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 725 tsleknlsERKKKSAQERCQAEAEMDEIRkshqEELDRLRQLLKKARVSTdQAAAEQLTLAQAELQSQWEAKCEQLLA-S 803
Cdd:PRK02224 398 --------ERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATL-RTARERVEEAEALLEAGKCPECGQPVEgS 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862604 804 ARDEHLQQYREvcaQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQA 860
Cdd:PRK02224 465 PHVETIEEDRE---RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
527-860 |
2.76e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.12 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 527 KMDHLMTKVEELQKHSSgnsmllpsMSVTMETSMIMsnIQRIIQEnerlkqeLLEKSSRIEEQNDKISDL---IERNQRY 603
Cdd:pfam15921 449 QMAAIQGKNESLEKVSS--------LTAQLESTKEM--LRKVVEE-------LTAKKMTLESSERTVSDLtasLQEKERA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 604 VEQSNLMMEKRNNSLQTATENTQAKVTEE--LAAATAQVSHLQLKMtAHQKKETELQLQLTDNLkeTDLLRGH---VTRL 678
Cdd:pfam15921 512 IEATNAEITKLRSRVDLKLQELQHLKNEGdhLRNVQTECEALKLQM-AEKDKVIEILRQQIENM--TQLVGQHgrtAGAM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 679 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSER---KKKSAQERCQAeaeMDEIRKS 755
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQL---LNEVKTS 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 756 HQE--ELDRLRQLLKKarvsTDQAAAEQLTLAQAELQSQweakceqlLASARDEhLQQYREVCAQ---RDAHQQKLAL-L 829
Cdd:pfam15921 666 RNElnSLSEDYEVLKR----NFRNKSEEMETTTNKLKMQ--------LKSAQSE-LEQTRNTLKSmegSDGHAMKVAMgM 732
|
330 340 350
....*....|....*....|....*....|.
gi 1242862604 830 QDECLALQAQIAAFTEQkehMQRLEKTKSQA 860
Cdd:pfam15921 733 QKQITAKRGQIDALQSK---IQFLEEAMTNA 760
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
570-768 |
2.93e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 570 QENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQSNLMMEKRNNSLQTATENTQAKVTEElaaaTAQVSHLQLKMTA 649
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEE----TRQKLNLSTRLRQ 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 650 HQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELR----------EASEQTQTKFKSEKQSRRQ-----------LEL 708
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKkkleedagtlEALEEGKKRLQRELEALTQqleekaaaydkLEK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 709 KVTSLEEELTDL-------RAEKTSLEKN-------LSERKKKSAQ---ERCQAEAEMDEIR-------------KSHQE 758
Cdd:pfam01576 574 TKNRLQQELDDLlvdldhqRQLVSNLEKKqkkfdqmLAEEKAISARyaeERDRAEAEAREKEtralslaraleeaLEAKE 653
|
250
....*....|
gi 1242862604 759 ELDRLRQLLK 768
Cdd:pfam01576 654 ELERTNKQLR 663
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
567-832 |
3.81e-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: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 567 RIIQENERLKQELLEKSSRIEEQNDK--------------ISDLIERNQRYvEQSNLMMEKrnnsLQTATENTQAKVTEE 632
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKakslsklknkheamISDLEERLKKE-EKGRQELEK----AKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 633 LAAATAQVSHLQLKMtahQKKETELQLQLTDNLKET---DLLRGHVTRLQADLSELREASEQT-QTKFKSEKQsRRQLEL 708
Cdd:pfam01576 224 IAELQAQIAELRAQL---AKKEEELQAALARLEEETaqkNNALKKIRELEAQISELQEDLESErAARNKAEKQ-RRDLGE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 709 KVTSLEEELTD----------LRAEKtslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLL---KKARVS-- 773
Cdd:pfam01576 300 ELEALKTELEDtldttaaqqeLRSKR---EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLeqaKRNKANle 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 774 -TDQAAAEQLTLAQAELQSQWEAKCE-----QLLASARDEHLQQYREVCAQRDAHQQKLALLQDE 832
Cdd:pfam01576 377 kAKQALESENAELQAELRTLQQAKQDsehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSE 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
652-936 |
3.82e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 652 KKETELQLQLT-DNLKE-TDLLRGhvtrLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEK 729
Cdd:COG1196 174 KEEAERKLEATeENLERlEDILGE----LERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 730 NLSERKKKSAQ-ERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEH 808
Cdd:COG1196 249 EELEAELEELEaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 809 LQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQkehmqRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEF 888
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1242862604 889 ELEESydggtiLRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLR 936
Cdd:COG1196 404 ELEEA------EEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
506-894 |
6.82e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 506 LMTEARQHNTEIRMAVNKVADKMDHLMTKVE-ELQKHSSGNSMLLPSMSvtmETSMIMSNIQRIIQENeRLKQELLEKSS 584
Cdd:pfam05483 202 LRVQAENARLEMHFKLKEDHEKIQHLEEEYKkEINDKEKQVSLLLIQIT---EKENKMKDLTFLLEES-RDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 585 RIEEQNDKisDLIERNQRYVEQsnlmMEKRNNSLQTATeNTQAKVTEELAAAT-----------AQVSHLQLKMTAHQKK 653
Cdd:pfam05483 278 KLQDENLK--ELIEKKDHLTKE----LEDIKMSLQRSM-STQKALEEDLQIATkticqlteekeAQMEELNKAKAAHSFV 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 654 ETELQlQLTDNLKEtdLLRGHVTRLQADLSEL--------REASE-QTQTKFKSEKQSRRQlELKVTSLEEEltDLRAEK 724
Cdd:pfam05483 351 VTEFE-ATTCSLEE--LLRTEQQRLEKNEDQLkiitmelqKKSSElEEMTKFKNNKEVELE-ELKKILAEDE--KLLDEK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 725 TSLEKnLSERKKKSAQERC---QA--------EAEMDEIRKSHQ---EELDRLRQLLKKARVSTDQ--AAAEQLTLAQAE 788
Cdd:pfam05483 425 KQFEK-IAEELKGKEQELIfllQArekeihdlEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIEltAHCDKLLLENKE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 789 LQSQWEAKCEQLLASARD--EHLQQYREVCAQRDAHQQKLALLQDEclaLQAQIAAFTEQKEHMQ-RLEKTKSQAPAGRA 865
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDiiNCKKQEERMLKQIENLEEKEMNLRDE---LESVREEFIQKGDEVKcKLDKSEENARSIEY 580
|
410 420
....*....|....*....|....*....
gi 1242862604 866 AADPSEKVKKIMNQVFQSLRGEFELEESY 894
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
564-790 |
8.47e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 564 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERN-----QRYVEQSNLMMEKRNNSLQTATENTQakvtEELAAATA 638
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ----NDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 639 QVSHLQLK-------MTAHQKKETELQLQLTDNLKETDLLRG-HVTRLQADLS------ELREASEQTQTKFKSEKQSRR 704
Cdd:PRK11281 150 QLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNTQLQDLLQKQR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 705 QL-ELKVTSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAaeqlT 783
Cdd:PRK11281 230 DYlTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLN----T 303
|
....*..
gi 1242862604 784 LAQAELQ 790
Cdd:PRK11281 304 LTQQNLR 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-888 |
1.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 563 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRY--------------VEQSNLMMEKRNNSLQTAtENTQAK 628
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeakakkeelerlkKRLTGLTPEKLEKELEEL-EKAKEE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 629 VTEELAAATAQVSHL------------QLK------------MTAHQKKE-------------------TELQLQLTDNL 665
Cdd:PRK03918 403 IEEEISKITARIGELkkeikelkkaieELKkakgkcpvcgreLTEEHRKElleeytaelkriekelkeiEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 666 KETDLLRGHVTRLQA------------------DLSELREASEQTQT-------------KFKSEKQSRRQLELKVTSLE 714
Cdd:PRK03918 483 RELEKVLKKESELIKlkelaeqlkeleeklkkyNLEELEKKAEEYEKlkekliklkgeikSLKKELEKLEELKKKLAELE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 715 EELTDLRAEKTSLEKNLSERKKKSAQErcqAEAEMDEIRKSHQE---------ELDRLRQLLKKARVSTDQAAAEqLTLA 785
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEE---LEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAET 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 786 QAELQSQwEAKCEQLLASARDEhlqQYREVcaqrdahQQKLALLQDECLALQAQIAAFTEQKEHMQR-LEKTKSQAPAGR 864
Cdd:PRK03918 639 EKRLEEL-RKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKtLEKLKEELEERE 707
|
410 420
....*....|....*....|....
gi 1242862604 865 AAADPSEKVKKIMNQVfQSLRGEF 888
Cdd:PRK03918 708 KAKKELEKLEKALERV-EELREKV 730
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
495-853 |
1.46e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 495 HFQGSGDMMSFLMteaRQHNTEIRMAVNKVADKMDHLmtkvEELQKHSSGNSMLLPSMSvtmetsmiMSNIQRIIQENER 574
Cdd:pfam15921 214 HFRSLGSAISKIL---RELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQH--------QDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 575 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKE 654
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 655 TELQLQLTDNLKETDLLRGHVTRLQADL----SELREASEQTQTKFKSEKQS-------RRQLE---LKVTSLEEELTDL 720
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRLWDRDTGNsitidhlRRELDdrnMEVQRLEALLKAM 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 721 RAE-KTSLEKNLS--ERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKC 797
Cdd:pfam15921 439 KSEcQGQMERQMAaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSDLTASLQEKERAIEATN 516
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 798 EQL--LASARDEHLQQYREVCAQRDAHQQklalLQDECLALQAQIAA-------FTEQKEHMQRL 853
Cdd:pfam15921 517 AEItkLRSRVDLKLQELQHLKNEGDHLRN----VQTECEALKLQMAEkdkvieiLRQQIENMTQL 577
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
612-814 |
1.57e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 612 EKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQ 691
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 692 TQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLK 768
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1242862604 769 KARVSTDQAAAEQLTLAQAELQSQweAKCEQLLASARDEHLQQYRE 814
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRN--AEKEEELAEAEKLIESLPRE 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
651-941 |
2.09e-06 |
|
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: 52.38 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 651 QKKETELQLQLTDNLKETDLLRGHVTRLQadlSELREASEQTqtkfkSEKQSRRQ-LELKVTSLEEELTDL--------- 720
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELS---QELSDASRKI-----GEIEKEIEqLEQEEEKLKERLEELeedlssleq 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 721 -----RAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEqltlAQAELQSqwEA 795
Cdd:TIGR02169 752 eienvKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLNR--LT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 796 KCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQRLEKTKSqapagraaaDPSEKVKK 875
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESRLG---------DLKKERDE 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862604 876 IMNQVFQSLRGEFELEESYDggtILRTIMHTIKmVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQ 941
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIE---KKRKRLSELK-AKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
567-790 |
2.17e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 567 RIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQA------KVTEELAAATAQV 640
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQleeeleQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 641 SHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDL 720
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 721 RAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 790
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
528-852 |
2.20e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 528 MDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmimsnIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQS 607
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLLVVPRAEL--------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 608 NLMMEKRNNSLQTATENTQAKVTE------ELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKetdLLRGHVTRLQAD 681
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEEleekykELSASSEELSEEKDALLAQRAAHEARIRELEEDIK---TLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 682 LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELD 761
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 762 rLRQLLKKARVSTDQAAAEQLTLA----------------QAEL-QSQWEAKCEQLLASARDEHLQQYREVCAQ-RDAHQ 823
Cdd:pfam07888 232 -NEALLEELRSLQERLNASERKVEglgeelssmaaqrdrtQAELhQARLQAAQLTLQLADASLALREGRARWAQeRETLQ 310
|
330 340 350
....*....|....*....|....*....|.
gi 1242862604 824 QKLALLQDECLALQAQIAAFTE--QKEHMQR 852
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQRLEErlQEERMER 341
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
649-842 |
2.31e-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: 50.38 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 649 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSElreaseqtQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 728
Cdd:pfam12795 34 ASKQRAAAYQKALDDAPAELRELRQELAALQAKAEA--------APKEILASLSLEELEQRLLQTSAQLQELQNQLAQLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 729 KNLSERKKKSAQercqAEAEMDEIRKshqeELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQW----EAKCEQLLASA 804
Cdd:pfam12795 106 SQLIELQTRPER----AQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKaqidMLEQELLSNNN 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1242862604 805 RDEHLQqyrevcAQRDAHQQKLALLQDECLALQAQIAA 842
Cdd:pfam12795 178 RQDLLK------ARRDLLTLRIQRLEQQLQALQELLNE 209
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
624-847 |
2.34e-06 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 51.78 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 624 NTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLtdnlketDLLRGHVTRLQADLSELREASEQTQTKFKS----- 698
Cdd:pfam09726 388 NNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQI-------SSLTSLERSLKSELGQLRQENDLLQTKLHNavsak 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 699 --EKQSRRQLELKvtsLEEEltdlRAEKTSLEKNLSERKK-------KSAQERCQAEA---EMDEIRKSHQEELD-RLRQ 765
Cdd:pfam09726 461 qkDKQTVQQLEKR---LKAE----QEARASAEKQLAEEKKrkkeeeaTAARAVALAAAsrgECTESLKQRKRELEsEIKK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 766 LLKKARVSTDQAAaeqltlaqaelqsQWEAKCEQllasardehLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTE 845
Cdd:pfam09726 534 LTHDIKLKEEQIR-------------ELEIKVQE---------LRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETR 591
|
..
gi 1242862604 846 QK 847
Cdd:pfam09726 592 IK 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
627-859 |
2.35e-06 |
|
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: 51.99 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 627 AKVTEELAAATAQVSHLQLKmtahqkkETELQLQLtDNLKETdllRGHVTRLQADLSELR--EASEQTQTKFKSEKQsRR 704
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLI-------IDEKRQQL-ERLRRE---REKAERYQALLKEKReyEGYELLKEKEALERQ-KE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 705 QLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRL----RQLLKKARVSTDQA--A 778
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeaeiASLERSIAEKERELedA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 779 AEQLTLAQAELQSQwEAKCEQLlasarDEHLQQYRevcAQRDAHQQKLALLQDECLALQAQI--------AAFTEQKEHM 850
Cdd:TIGR02169 321 EERLAKLEAEIDKL-LAEIEEL-----EREIEEER---KRRDKLTEEYAELKEELEDLRAELeevdkefaETRDELKDYR 391
|
....*....
gi 1242862604 851 QRLEKTKSQ 859
Cdd:TIGR02169 392 EKLEKLKRE 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
561-734 |
2.65e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 561 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDL----------IERNQRYVEQSNLMMEKRNNSLQTATENtqakvt 630
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteledlekeIKRLELEIEEVEARIKKYEEQLGNVRNN------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 631 EELAAATAQVSHLQLKMTAHQKKETELQLQLtdnlketdllrghvTRLQADLSELREASEQTQTKFKSEKQsrrQLELKV 710
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERI--------------EELEEELAELEAELAELEAELEEKKA---ELDEEL 151
|
170 180
....*....|....*....|....
gi 1242862604 711 TSLEEELTDLRAEKTSLEKNLSER 734
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPE 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
574-894 |
3.51e-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: 51.51 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 574 RLKQELLEKSsriEEQNDKISDLIERNQryVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMtahQKK 653
Cdd:TIGR00618 153 EFAQFLKAKS---KEKKELLMNLFPLDQ--YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 654 ETELQlQLTDNLKETDllrghvtRLQADLSELREASEQTQTKFKSEKQSRRQLElKVTSLEEELtdlraEKTSLEKNLSE 733
Cdd:TIGR00618 225 EKELK-HLREALQQTQ-------QSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVL-----EETQERINRAR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 734 RKKKSAQErcqaEAEMDEIRKSHQEELDRLRQ---LLKKARVSTDQAAAEQLTL-AQAELQSQWEAKCEQLlasaRDEHL 809
Cdd:TIGR00618 291 KAAPLAAH----IKAVTQIEQQAQRIHTELQSkmrSRAKLLMKRAAHVKQQSSIeEQRRLLQTLHSQEIHI----RDAHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 810 QQyrevCAQRDAHQQKLALLQdECLALQAQIAAFTEQkehMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFE 889
Cdd:TIGR00618 363 VA----TSIREISCQQHTLTQ-HIHTLQQQKTTLTQK---LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE 434
|
....*
gi 1242862604 890 LEESY 894
Cdd:TIGR00618 435 LQQRY 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
570-856 |
3.58e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 570 QENERLKQELLEKSSRIEEQNDKISDLIERNQRY-VEQSNLMMEKRNNSLQTATENTQAKVtEELAAATAQVSHLQLKMT 648
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLeKLLQLLPLYQELEALEAELAELPERL-EELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 649 AHQKKETELQLQLTDNLKETDL-LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKT-- 725
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlk 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 726 ----------------------------------------SLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQ 765
Cdd:COG4717 247 earlllliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 766 LL------------------KKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE------HLQQYREVCAQRDA 821
Cdd:COG4717 327 ALglppdlspeellelldriEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraaleQAEEYQELKEELEE 406
|
330 340 350
....*....|....*....|....*....|....*
gi 1242862604 822 HQQKLALLQDECLALqAQIAAFTEQKEHMQRLEKT 856
Cdd:COG4717 407 LEEQLEELLGELEEL-LEALDEEELEEELEELEEE 440
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
623-769 |
3.75e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 623 ENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQT--QTKFKSEK 700
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242862604 701 QSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKK 769
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
563-753 |
3.97e-06 |
|
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: 51.17 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 563 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERN----------QRYVEQSNLMMEKRNNSLQTATENTQAKVTE- 631
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDsvkeliiknlDNTRESLETQLKVLSRSINKIKQNLEQKQKEl 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 632 -----ELAAATAQVSHL------------QLKMTAHQ------KKETELQlQLTDNLKETD------LLRGHVTRLQADL 682
Cdd:TIGR04523 492 kskekELKKLNEEKKELeekvkdltkkisSLKEKIEKlesekkEKESKIS-DLEDELNKDDfelkkeNLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 683 SELRE---ASEQTQTKFK-------SEKQS-RRQLELK---VTSLEEELTDLRAEKTSLE---KNLSERKKKSAQERCQA 745
Cdd:TIGR04523 571 EELKQtqkSLKKKQEEKQelidqkeKEKKDlIKEIEEKekkISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQI 650
|
....*...
gi 1242862604 746 EAEMDEIR 753
Cdd:TIGR04523 651 KETIKEIR 658
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
594-862 |
5.33e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 594 SDLIERNQRYVEQSNLMMEKRNNSLQtATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTdnlketdllrg 673
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 674 hvtRLQADLSELREASEQTQTK--------FKSEKQSRRQLELKVTSLEEELTDLRAektsLEKNLSERKKksaqercqa 745
Cdd:COG4942 87 ---ELEKEIAELRAELEAQKEElaellralYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARRE--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 746 eaEMDEIRKShQEELDRLRQLLKKARvstdqaaaEQLTLAQAELQSQweakcEQLLASARDEHLQQYREVCAQRDAHQQK 825
Cdd:COG4942 151 --QAEELRAD-LAELAALRAELEAER--------AELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAE 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 1242862604 826 LALLQDECLALQAQIAAFteQKEHMQRLEKTKSQAPA 862
Cdd:COG4942 215 LAELQQEAEELEALIARL--EAEAAAAAERTPAAGFA 249
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
571-861 |
5.70e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.41 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAH 650
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTH 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 651 QKKET---ELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSL 727
Cdd:pfam05667 303 TEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 728 EKNLsERKKKSAQERCQAEAEMDEirkshqeeldrLRQLLkkarvstdQAAAEQLtlaqAELQSQWEAKCEQLLasardE 807
Cdd:pfam05667 383 EKQY-KVKKKTLDLLPDAEENIAK-----------LQALV--------DASAQRL----VELAGQWEKHRVPLI-----E 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1242862604 808 HLQQYREVCA-QRDAHQQKLA---LLQDECLalqaQIAAFTEQKEHMQR-LEKTKSQAP 861
Cdd:pfam05667 434 EYRALKEAKSnKEDESQRKLEeikELREKIK----EVAEEAKQKEELYKqLVAEYERLP 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
676-935 |
6.02e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 676 TRLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLseRKKKSAQERCQAEAEMDEIrks 755
Cdd:COG4717 71 KELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 756 hQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE---HLQQYREVCAQRDAHQQKLALLQDE 832
Cdd:COG4717 145 -PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 833 CLALQAQIAAFTEQKEHMQRLE---------------------------------------------------KTKSQAP 861
Cdd:COG4717 222 LEELEEELEQLENELEAAALEErlkearlllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLG 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242862604 862 AGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPL 935
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
676-903 |
1.24e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 676 TRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKkksaQERCQAEAEMDEIrks 755
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 756 hQEELDRLRQLLKKARVSTDQaAAEQLTLAQAELQSqweakceqlLASARDEHLQQYREVCAQRDAHQQKLALLQDECLA 835
Cdd:COG4372 79 -EEELEELNEQLQAAQAELAQ-AQEELESLQEEAEE---------LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 836 LQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTI 903
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
573-871 |
1.30e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 573 ERLKQELLEkssrIEEQNDKISDLIERNQRYVEQSNLMMekrNNSLQTATENTQAkvtEELAAATAQVSHLQLKMTAHQK 652
Cdd:PRK04863 789 EQLRAEREE----LAERYATLSFDVQKLQRLHQAFSRFI---GSHLAVAFEADPE---AELRQLNRRRVELERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 653 KETELQLQLtDNLKET-DLLRGHVTR--------LQADLSELREASEQTQTKFKSEKQSRRQLELkvtsLEEELTDLRAE 723
Cdd:PRK04863 859 QEQQQRSQL-EQAKEGlSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSD 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 724 ktsleknlserkkksaqercqaEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAA---------AEQLTLAQAELQSQWE 794
Cdd:PRK04863 934 ----------------------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSDLNEKLR 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 795 AKCEQlLASARDEHLQQYREVCAQrdaHQQKLALLQDeclaLQAQIAAFTEQ-KEHMQRLEKTKSQAPAG---RAAADPS 870
Cdd:PRK04863 992 QRLEQ-AEQERTRAREQLRQAQAQ---LAQYNQVLAS----LKSSYDAKRQMlQELKQELQDLGVPADSGaeeRARARRD 1063
|
.
gi 1242862604 871 E 871
Cdd:PRK04863 1064 E 1064
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
631-814 |
2.02e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 631 EELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTrlqaDLSELREASEQTQtKFKSEKQSRRQLELKV 710
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE----DEEELRAALEQAE-EYQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 711 TSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 790
Cdd:COG4717 412 EELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|....
gi 1242862604 791 SQWEAKceQLLASARDEHLQQYRE 814
Cdd:COG4717 490 EEWAAL--KLALELLEEAREEYRE 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
571-875 |
2.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATEntqAKVTEELAAATAQVSHLQLKMTAH 650
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 651 QKKETELQLQLTDNLKETDllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKvtslEEELTDLRAEKtsLEKN 730
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEED--KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK----KAEEAKIKAEE--LKKA 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 731 LSERKKKSAQERCQAEA--EMDEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEH 808
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862604 809 LQQYREVcAQRDAHQQKLAllqDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 875
Cdd:PTZ00121 1707 LKKKEAE-EKKKAEELKKA---EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
631-894 |
2.83e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 631 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLR---GHVTRL-QADLSELREASEQTQTKFKSEKQSRRQ 705
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQL-DQLKEQlQLLNkllPQANLLaDETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 706 LELKVTSLEEELTDLRAEKTS---LEKNLSERKKKSAQERCQAEAeMDEI--RKSH-------------QEELDRLRQLL 767
Cdd:COG3096 915 HGKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFA-LSEVvqRRPHfsyedavgllgenSDLNEKLRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 768 KKArvstdQAAAEQLTLAQAELQSQWeAKCEQLLASARdehlqqyrevcAQRDAHQQKLALLQDECLALQAQIAAFTEQK 847
Cdd:COG3096 994 EQA-----EEARREAREQLRQAQAQY-SQYNQVLASLK-----------SSRDAKQQTLQELEQELEELGVQADAEAEER 1056
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1242862604 848 --EHMQRLEktkSQAPAGRAAADPSEKVKKIMNQVFQSLRGEF-ELEESY 894
Cdd:COG3096 1057 arIRRDELH---EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrKAERDY 1103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
557-855 |
3.32e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 557 ETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLqTATENTQAKVTEELAAA 636
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL-HLQQCSQELALKLTALH 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 637 TAQVSHLQLKMTAHQKKETELQLQLTD-NLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEE 715
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKELLAsRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 716 ELTDLRAEKTSLEKNLSERKKKsAQERCQAEAEMDEiRKSHQE-----ELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 790
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQ-ARTVLKARTEAHF-NNNEEVtaalqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE 807
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1242862604 791 SQWEAKCEQLLASARDEHLQQYREVCAQRDA------HQQKLALLQD-ECLALQAQiaAFTEQKEHMQRLEK 855
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksatlGEITHQLLKYeECSKQLAQ--LTQEQAKIIQLSDK 877
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
669-860 |
3.60e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 669 DLLRGHVTRLQADLSELREASEQTQTKFKSE----KQSRRQLE-----LKVTSLEEELTDLRAEKTSLEKNLSERKKKSA 739
Cdd:PRK04778 201 DQLEEELAALEQIMEEIPELLKELQTELPDQlqelKAGYRELVeegyhLDHLDIEKEIQDLKEQIDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 740 QERCQA-EAEMDEI----------RKSHQEELDRLRQLLKKARVSTDQAAAE--------QLTLAQAELQSQWEAKCEQL 800
Cdd:PRK04778 281 EEKNEEiQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsyTLNESELESVRQLEKQLESL 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242862604 801 LAsardehlqQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQ----KEHMQRLEKTKSQA 860
Cdd:PRK04778 361 EK--------QYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEqeklSEMLQGLRKDELEA 416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
739-887 |
3.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 739 AQERCQAEAEMDEIRKS---HQEELDRLRQLLKKARVSTDQAAAEQ-LTLAQAELQsQWEAKCEQLLASARD-EHL-QQY 812
Cdd:COG4913 616 EAELAELEEELAEAEERleaLEAELDALQERREALQRLAEYSWDEIdVASAEREIA-ELEAELERLDASSDDlAALeEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 813 REVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRL--EKTKSQAPAGRAAADP---SEKVKKIMNQVFQSLRGE 887
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleAAEDLARLELRALLEErfaAALGDAVERELRENLEER 774
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
565-793 |
3.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 565 IQRIIQENERLKQELLEKSSR-IEEQNDKISDLIERNQRYVEQsnlmMEKRNNSLQTATENTQakVTEELAAATAQVSHL 643
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEE----FRQKNGLVDLSEEAKL--LLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 644 QLKMTAHQKKETELQLQLTDNLKETDLLRGH--VTRLQADLSELREASEQTQTKFKS---------------EKQSRRQL 706
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPnhpdvialraqiaalRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 707 ELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIrkshQEELDRLRQLLKKArvstdQAAAEQLTLAQ 786
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRL----EREVEVARELYESL-----LQRLEEARLAE 381
|
....*..
gi 1242862604 787 AELQSQW 793
Cdd:COG3206 382 ALTVGNV 388
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
566-793 |
3.77e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 566 QRIIQENERLkqelLEKSSRIEEQNDK---ISDLIerNQRYVEQSnlmmEKRNnSLQTATENTQAKVTEELAAATAQVSH 642
Cdd:PRK10929 109 QEILQVSSQL----LEKSRQAQQEQDRareISDSL--SQLPQQQT----EARR-QLNEIERRLQTLGTPNTPLAQAQLTA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 643 LQLKMTAHQKKETELQL-QLTDNLKE------TDLLRGHVTRLQADLSELReaseqTQTKFKSEKQSRRQLElKVTSLEE 715
Cdd:PRK10929 178 LQAESAALKALVDELELaQLSANNRQelarlrSELAKKRSQQLDAYLQALR-----NQLNSQRQREAERALE-STELLAE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 716 ELTDLRAEKTS-LEKN--LSERKKKSAQercqaeaEMDEIrKSHQEeldrlrqllkkarvstdQAAAEQLTLAQA----E 788
Cdd:PRK10929 252 QSGDLPKSIVAqFKINreLSQALNQQAQ-------RMDLI-ASQQR-----------------QAASQTLQVRQAlntlR 306
|
....*
gi 1242862604 789 LQSQW 793
Cdd:PRK10929 307 EQSQW 311
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
589-854 |
4.62e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 589 QNDKISDLIERNQRYVeQSNLMM---EKRNNSLQTAT-ENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTD- 663
Cdd:COG3096 254 DRDLFKHLITEATNYV-AADYMRhanERRELSERALElRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAa 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 664 ----NLKETDL-LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSE----- 733
Cdd:COG3096 333 sdhlNLVQTALrQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVqqtra 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 734 -------RKKKSAQERCQ--------AEAEMDEIRKSHQEELDRLRQLlkKARVSTDQAAAEQLTLAQAELQS------- 791
Cdd:COG3096 413 iqyqqavQALEKARALCGlpdltpenAEDYLAAFRAKEQQATEEVLEL--EQKLSVADAARRQFEKAYELVCKiagever 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 792 --QWEAKCEQLLASARDEHL--------QQYREvcAQRDAHQQKLA--LLQDECLALQAQIAAFTEQKEHMQRLE 854
Cdd:COG3096 491 sqAWQTARELLRRYRSQQALaqrlqqlrAQLAE--LEQRLRQQQNAerLLEEFCQRIGQQLDAAEELEELLAELE 563
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
569-858 |
4.69e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 569 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmmEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMT 648
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 649 AHQKKETELQLQltdnlketdllrghvtrlQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLeEELTDLRAEKTSLE 728
Cdd:PRK02224 545 RAAELEAEAEEK------------------REAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 729 KNLSERkkksaQERCQAEAEMDEIRKSHQEEL-DRLRQL---LKKARVSTDQAAAEQLTLAQAELqsqweakceqllasa 804
Cdd:PRK02224 606 DEIERL-----REKREALAELNDERRERLAEKrERKRELeaeFDEARIEEAREDKERAEEYLEQV--------------- 665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1242862604 805 rDEHLQQYREvcaQRDAhqqklalLQDECLALQAQIAAFTEQKEHMQRLEKTKS 858
Cdd:PRK02224 666 -EEKLDELRE---ERDD-------LQAEIGAVENELEELEELRERREALENRVE 708
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
580-811 |
4.87e-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: 47.44 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 580 LEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvteELAAATAQVSHLQLKmtahqKKETELQL 659
Cdd:pfam09731 201 LAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYK---ELVASERIVFQQELV-----SIFPDIIP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 660 QLT-DNLKETDLLRGHVTRLQADLSELreaSEQTQTKFKSEKQsrrQLELKVTSLEEELTDLRAEktsLEKNLSE-RKKK 737
Cdd:pfam09731 273 VLKeDNLLSNDDLNSLIAHAHREIDQL---SKKLAELKKREEK---HIERALEKQKEELDKLAEE---LSARLEEvRAAD 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242862604 738 SAQERCQAEAEMDEIRKSHQEEldrLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQ 811
Cdd:pfam09731 344 EAQLRLEFEREREEIRESYEEK---LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
553-814 |
5.16e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 553 SVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAK--VT 630
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERdeLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 631 EELAAATAQVSHLQLKMTAHQKKETEL--------QL---QLTDNL---KETDLLRgHVTRLQADLSELREASEQ----- 691
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIdklrkeieRLewrQQTEVLspeEEKELVE-KIKELEKELEKAKKALEKneklk 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 692 -TQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKS---AQERCQAEAEMDEIRKSH---QEELDRLR 764
Cdd:COG1340 164 eLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAdelHKEIVEAQEKADELHEEIielQKELRELR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1242862604 765 QLLKKARvstDQAAAEQLTLAQAELQSQWEAKCEQLLASAR---DEHLQQYRE 814
Cdd:COG1340 244 KELKKLR---KKQRALKREKEKEELEEKAEEIFEKLKKGEKlttEELKLLQKS 293
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
563-807 |
5.19e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 563 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSh 642
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN----LEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 643 lqlKMTAHQKKETELQLQLTDNLketdllrghvtrLQADLSELREASEQTQTKFKSEKQ--SRRQLELK-----VTSLEE 715
Cdd:pfam12128 397 ---DKLAKIREARDRQLAVAEDD------------LQALESELREQLEAGKLEFNEEEYrlKSRLGELKlrlnqATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 716 ELTDLRAEKTSLEknlserKKKSAQERCQAEAEmdeirkSHQEELDRLRQLLKKARVSTDQA--AAEQLTLAQAELQSQW 793
Cdd:pfam12128 462 LLLQLENFDERIE------RAREEQEAANAEVE------RLQSELRQARKRRDQASEALRQAsrRLEERQSALDELELQL 529
|
250
....*....|....
gi 1242862604 794 EAKCEQLLASARDE 807
Cdd:pfam12128 530 FPQAGTLLHFLRKE 543
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
569-918 |
5.48e-05 |
|
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: 47.41 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 569 IQENERLKQE----------LLEKSSRIEEQNDKIS-DLIERNQRYVEQSNLM--MEKRNNSLQTATENTQAKVTEELAA 635
Cdd:pfam05483 140 IQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEyEREETRQVYMDLNNNIekMILAFEELRVQAENARLEMHFKLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 636 ATAQVSHLqlkmtahqkkETELQLQLTDNLKETDLLRGHVTRLQADLSEL-------REASEQTQTKFKSEKQSRRQLEL 708
Cdd:pfam05483 220 DHEKIQHL----------EEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleesRDKANQLEEKTKLQDENLKELIE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 709 KVTSLEEELTDLR-------AEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE------ELD----RLRQLLK--K 769
Cdd:pfam05483 290 KKDHLTKELEDIKmslqrsmSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvvtEFEattcSLEELLRteQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 770 ARVSTDQaaaEQLTLAQAELQSQW-------------EAKCEQLLAS-ARDEHL----QQYREVCAQRDAHQQKLALL-- 829
Cdd:pfam05483 370 QRLEKNE---DQLKIITMELQKKSseleemtkfknnkEVELEELKKIlAEDEKLldekKQFEKIAEELKGKEQELIFLlq 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 830 --QDECLALQAQIAAFTEQKEH-MQRLEKTKSQAPagraaadpSEKVKKI---MNQVFQSLRGEFELEESYDggtilrti 903
Cdd:pfam05483 447 arEKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELE--------KEKLKNIeltAHCDKLLLENKELTQEASD-------- 510
|
410
....*....|....*
gi 1242862604 904 mhtikmVTLQLLNHQ 918
Cdd:pfam05483 511 ------MTLELKKHQ 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
509-814 |
5.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 509 EARQHNTEIRMAVNKVADKMDHLMTKVEELQK---------------------HSSGNSMllpsMSVTMETSMIMSNIQR 567
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrelteEHRKELL----EEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 568 IIQENERLKQELLEKSSRIEEQ-----NDKISDLIERNQRYVEQSNLmmEKrnnsLQTATENTQaKVTEELAAATAQVSH 642
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNL--EE----LEKKAEEYE-KLKEKLIKLKGEIKS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 643 L--QLKMTAHQKKETELQLQLTDNLKE--TDLLR-------GHVTRLQADLSELREASEQ------TQTKFKSEKQSRRQ 705
Cdd:PRK03918 544 LkkELEKLEELKKKLAELEKKLDELEEelAELLKeleelgfESVEELEERLKELEPFYNEylelkdAEKELEREEKELKK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 706 LELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQErcqaeaEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAAA--E 780
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLElsrELAGLRAELEELEKRREEIKKtlE 697
|
330 340 350
....*....|....*....|....*....|....*
gi 1242862604 781 QLtlaQAELQSQWEAKCE-QLLASARDEhLQQYRE 814
Cdd:PRK03918 698 KL---KEELEEREKAKKElEKLEKALER-VEELRE 728
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
633-870 |
5.92e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 633 LAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTkfksekqsrrqlelKVTS 712
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 713 LEEELTDLRAEKTSLEKNLSERkKKSAQERCQAEAEMDEI--RKSHQEELDRLrQLLKKArVSTDQAAAEQLTLAQAELQ 790
Cdd:COG3883 70 LQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYLDVLlgSESFSDFLDRL-SALSKI-ADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 791 SQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAAD 868
Cdd:COG3883 147 AKKAELEAKLaeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 1242862604 869 PS 870
Cdd:COG3883 227 AA 228
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
646-791 |
6.81e-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: 45.28 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 646 KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkFKSEKQSRRQLELKVTSLEEELTDLRAEKt 725
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEH- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862604 726 sleKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKaRVstdQAAAEQLTLAQAELQS 791
Cdd:pfam13851 109 ---EVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
557-811 |
8.86e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 557 ETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNnslqtatENTQAKVTEELAAA 636
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI-------LEYLKEKAEREEER 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 637 TAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRghVTRLQADLSE-----LREASEQTQTKFKSEKQSRR-QLELKV 710
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELR--AKLYQEEQERkerqkEREEAEKKARQRQELQQAREeQIELKE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 711 TSLEEELTDLRAEKtslEKNLSERKKKSAQERCQAEAEMdEIRKSHQEELDRLRQLLKKARvstdqAAAEQLTLAQAELQ 790
Cdd:pfam13868 250 RRLAEEAEREEEEF---ERMLRKQAEDEEIEQEEAEKRR-MKRLEHRRELEKQIEEREEQR-----AAEREEELEEGERL 320
|
250 260
....*....|....*....|.
gi 1242862604 791 SQWEAKCEQLLASARDEHLQQ 811
Cdd:pfam13868 321 REEEAERRERIEEERQKKLKE 341
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
521-724 |
9.69e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 521 VNKVADKMDHLMTKVEELQKHSSGNSML---LPSMSVTMETSM---IMSNIQRIIQ-ENERLKQELLEKSSRIEEQNDKI 593
Cdd:COG5022 894 ISSLKLVNLELESEIIELKKSLSSDLIEnleFKTELIARLKKLlnnIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEY 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 594 SDLIERNQRYVEQSNLMMEKRNNSLQTATEntQAKVTEELAAATAQVSHLQLKMTAHQK--------KETELQLQLTDNL 665
Cdd:COG5022 974 EDLLKKSTILVREGNKANSELKNFKKELAE--LSKQYGALQESTKQLKELPVEVAELQSaskiisseSTELSILKPLQKL 1051
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1242862604 666 KETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEK 724
Cdd:COG5022 1052 KGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVK 1110
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
573-886 |
1.03e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 573 ERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMmEKRNNSLQTATENTQAkvteelAAATAQVSHLQLKMTAHQK 652
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLADYQQ------ALDVQQTRAIQYQQAVQAL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 653 KETELQLQLTDnlKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQ----LELkVTSLEEELTDLRAEKTSLE 728
Cdd:COG3096 423 EKARALCGLPD--LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQfekaYEL-VCKIAGEVERSQAWQTARE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 729 KNLSERKKKSAQERCQA-EAEMDEIRK--SHQEELDRLRQLLKKaRVSTDQAAAEQLTLAQAELQSQweakceqllasaR 805
Cdd:COG3096 500 LLRRYRSQQALAQRLQQlRAQLAELEQrlRQQQNAERLLEEFCQ-RIGQQLDAAEELEELLAELEAQ------------L 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 806 DEHLQQYREVCAQRDAHQQKLAllqdeclALQAQIAAFTeqkehmqrlektkSQAPAGRAAADPSEKVKKIMNQVFQSLR 885
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLE-------QLRARIKELA-------------ARAPAWLAAQDALERLREQSGEALADSQ 626
|
.
gi 1242862604 886 G 886
Cdd:COG3096 627 E 627
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
569-802 |
1.13e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 569 IQENE-RLKQELLEKSSRIEEQNDKISDLIERNQryvEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKM 647
Cdd:TIGR00606 370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 648 TAHQKKETELQL------QLTDNLKETDLLRGHVTRLQADLSELREAS--EQTQTKFKSEKQSRRQLELKVTSLEEELTD 719
Cdd:TIGR00606 447 EILEKKQEELKFvikelqQLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 720 LRAEKTSLEKNLSERKKKSaqercQAEAEMDEIRKSHQEEL--------------DRLRQLLKKARVSTDQAAAEQLTLA 785
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKM-----DKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLNKELA 601
|
250 260
....*....|....*....|..
gi 1242862604 786 QAE-----LQSQWEAKCEQLLA 802
Cdd:TIGR00606 602 SLEqnknhINNELESKEEQLSS 623
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
509-737 |
1.27e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 509 EARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmiMSNIQRIIQENERLKQELLEKSSRIEE 588
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL-----VEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 589 QNDKISDLierNQRYVEQSNLM--------MEKRNNSLQTATEN---TQAKVTEelaaATAQVSHLQLKMTA---HQKKE 654
Cdd:PHA02562 253 PSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQiseGPDRITK----IKDKLKELQHSLEKldtAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 655 TELQLQLTDNLKEtdllrghVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSER 734
Cdd:PHA02562 326 EEIMDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1242862604 735 KKK 737
Cdd:PHA02562 399 VKE 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-795 |
1.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 619 QTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREA---------- 688
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 689 ------------------------------SEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKS 738
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862604 739 AQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEA 795
Cdd:COG3883 178 AEQE-ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
934-1119 |
1.47e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 934 PLRPSLEQPGPATPGMPPAPPSGETQEAPEvlpeqvvgettPLPLQALPTPENGAQTrkgePAEAEVPSEIKDSSLPPQP 1013
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGA-----------GEPSGAVPQPWLGALV----PGRVAVPRFRVPQPAPSRE 2987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 1014 AGIPA-HRVLGPPTSIPPKPPGPVTMDSESEEMLAADQRTVQPNgllgeEHVREVATDGLLQGNSRRLSL-TPDPEKGEP 1091
Cdd:PHA03247 2988 APASStPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPP-----DDTEDSDADSLFDSDSERSDLeALDPLPPEP 3062
|
170 180
....*....|....*....|....*....
gi 1242862604 1092 PalDPESQGGEAQPPECKQAEDVSSS-GP 1119
Cdd:PHA03247 3063 H--DPFAHEPDPATPEAGARESPSSQfGP 3089
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
671-838 |
1.57e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 671 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMD 750
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 751 EIRKshqeeldRLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALL 829
Cdd:COG3096 589 QLRA-------RIKELAARAPAwLAAQDALERL-----REQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQAL 656
|
....*....
gi 1242862604 830 QDECLALQA 838
Cdd:COG3096 657 ESQIERLSQ 665
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
565-859 |
1.82e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 565 IQRIIQENERLKQELLEKssrieeqndkisDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQvshLQ 644
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEE------------KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR--EEIDEFNEE---QA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 645 LKMTAHQKKETELQLQLTDNLKEtdllrghvtrlQADLSELREASEQTQTKFKSEKQSR-RQLELKVTSLEEELTDLRAE 723
Cdd:pfam13868 141 EWKELEKEEEREEDERILEYLKE-----------KAEREEEREAEREEIEEEKEREIARlRAQQEKAQDEKAERDELRAK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 724 KTsLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELdRLRQLLKKARVSTDQAAAEQLTLAQAELQSQweakcEQLLAS 803
Cdd:pfam13868 210 LY-QEEQERKERQKEREEAEKKARQRQELQQAREEQI-ELKERRLAEEAEREEEEFERMLRKQAEDEEI-----EQEEAE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1242862604 804 ARDEHLQQYR-EVCAQ-RDAHQQKLALLQDEclaLQAQIAAFTEQKEHMQRLEKTKSQ 859
Cdd:pfam13868 283 KRRMKRLEHRrELEKQiEEREEQRAAEREEE---LEEGERLREEEAERRERIEEERQK 337
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
580-768 |
1.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 580 LEKSSRIEEQNDKISDLIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQA---------K 628
Cdd:PRK03918 100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLGEvikeikrriE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 629 VTEELAAATAQVSHLqLKmtaHQKKETELQLQ----LTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRR 704
Cdd:PRK03918 180 RLEKFIKRTENIEEL-IK---EKEKELEEVLReineISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242862604 705 QLELKVTSLEEELTDLRAEKTSLEKNLSERK--KKSAQERCQAEAEMDEIRKSHQE---ELDRLRQLLK 768
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREiekRLSRLEEEIN 324
|
|
| Tig |
COG0544 |
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ... |
185-250 |
2.06e-04 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440310 [Multi-domain] Cd Length: 424 Bit Score: 45.12 E-value: 2.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862604 185 LVAAEGPAvETGDSLEVAYTGWllqnhVLGQVFDSTANKDKPLrlKLGSGKVVKGLEDGLLGMKKG 250
Cdd:COG0544 151 LVPVERAA-EEGDRVTIDFEGT-----IDGEEFEGGKAEDYSL--ELGSGSFIPGFEEQLVGMKAG 208
|
|
| tig |
TIGR00115 |
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ... |
185-255 |
2.11e-04 |
|
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]
Pssm-ID: 272913 [Multi-domain] Cd Length: 410 Bit Score: 45.24 E-value: 2.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242862604 185 LVAAEGPAVETGDSLEVAYTGwllqnHVLGQVFDSTANKDkpLRLKLGSGKVVKGLEDGLLGMKKGGKRLI 255
Cdd:TIGR00115 141 LVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAGEEKEI 204
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
531-816 |
2.35e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 531 LMTKVEELQK----HSSGNSmllpsmSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQndkiSDLIERNQRYVeq 606
Cdd:pfam05557 281 LSRRIEQLQQreivLKEENS------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH----KALVRRLQRRV-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 607 snLMMEKRNNSLQTATEN-----TQAKVTEELAAATAQVSHLQLKMTAHQkkeTELQLQLTDNLKETDLLRGHVTRLQAD 681
Cdd:pfam05557 349 --LLLTKERDGYRAILESydkelTMSNYSPQLLERIEEAEDMTQKMQAHN---EEMEAQLSVAEEELGGYKQQAQTLERE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 682 LSELREASEQTQTKFKSEKQSrrQLELKVTSLEEELTDLRAEKTSLEKNLSER---------KKKSAQERCQAEAEMDEI 752
Cdd:pfam05557 424 LQALRQQESLADPSYSKEEVD--SLRRKLETLELERQRLREQKNELEMELERRclqgdydpkKTKVLHLSMNPAAEAYQQ 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862604 753 RKSH----QEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHL--------QQYREVC 816
Cdd:pfam05557 502 RKNQleklQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLkevfqakiQEFRDVC 577
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
576-765 |
2.52e-04 |
|
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: 44.15 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 576 KQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmMEKRNNSLQTATENTQakvtEELAAATAQVSHLQLKMTAHQKKET 655
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAE----LEDELAALEARLEAAK----TELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 656 ELQLQLTD--NLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEktsleknLSE 733
Cdd:COG1579 77 KYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE-------LDE 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1242862604 734 RKKKSAQERCQAEAEMDEIRKSHQEEL----DRLRQ 765
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPELlalyERIRK 185
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
707-855 |
2.75e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 43.35 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 707 ELKVTSLEEELTDL--RAEKTSLE----KNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARvSTDQAAAE 780
Cdd:pfam15619 10 LHKIKELQNELAELqsKLEELRKEnrllKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ-EKERDLER 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 781 QLTLAQAELQSQwEAKCEQLLASARDEHLqqyrevcAQRDAHQQKLALLQDEclaLQaqiaaftEQKEHMQRLEK 855
Cdd:pfam15619 89 KLKEKEAELLRL-RDQLKRLEKLSEDKNL-------AEREELQKKLEQLEAK---LE-------DKDEKIQDLER 145
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
621-806 |
2.80e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 45.23 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 621 ATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEK 700
Cdd:COG5283 32 ALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRLRSSLEQTNRQLERQQQRLARLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 701 QSRRQLelkvTSLEEELTDLRAEKTSLEkNLSERKKKSAQERCQAEAEMDEIRKSHQ-----EELDRLRQLLKKA----R 771
Cdd:COG5283 112 ARQDRL----KAARARLQRLAGAGAAAA-AIGAALAASVKPAIDFEDAMADVAATVDldkssEQFKALGKQARELsaqtP 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1242862604 772 VSTDQAAAEQLTLAQAELQSQweakceQLLASARD 806
Cdd:COG5283 187 QSADDIAAGQAALAQAGVSAE------DILAFTPT 215
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
571-769 |
2.83e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEKSSRI-EEQNDKISDLIERNQRYVEQSN--------LM-----MEKRNNSLQTATENTQAKVTEELAAA 636
Cdd:pfam10174 537 ENQLKKAHNAEEAVRTnPEINDRIRLLEQEVARYKEESGkaqaeverLLgilreVENEKNDKDKKIAELESLTLRQMKEQ 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 637 TAQVSHLQLKMTAHQKKETELqlqLTDNLKETDLLRGHVTRLQadLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEE 716
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQL---LEEARRREDNLADNSQQLQ--LEELMGALEKTRQELDATKARLSSTQQSLAEKDGH 691
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 717 LTDLRAEKtslEKNLSERKKKSAQERCQAEAEMD------EI----RKSHQEEL-------DRLRQLLKK 769
Cdd:pfam10174 692 LTNLRAER---RKQLEEILEMKQEALLAAISEKDaniallELssskKKKTQEEVmalkrekDRLVHQLKQ 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
509-741 |
3.64e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 509 EARQHNTEIRmaVNKVADKMDHLMTKVEELQKhssgnsmllpsmsvtmETSMIMSNIQRIIQENERLKQELLEKSSRIEE 588
Cdd:TIGR02169 321 EERLAKLEAE--IDKLLAEIEELEREIEEERK----------------RRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 589 QNDKISDLIERNQRYVEqsnlmmekRNNSLQTatenTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKET 668
Cdd:TIGR02169 383 TRDELKDYREKLEKLKR--------EINELKR----ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1242862604 669 DLLRGHVTRLQADLSELREASEQTQTKFksekqsrRQLELKVTSLEEELTDLRAEKTSLEKnlSERKKKSAQE 741
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEY-------DRVEKELSKLQRELAEAEAQARASEE--RVRGGRAVEE 514
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
665-769 |
3.77e-04 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 42.22 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 665 LKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQ----LELKVTSLEEELTDLRAEKTSLE---KNLSERKKK 737
Cdd:pfam09744 35 LELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEeenRRLEADHVS 114
|
90 100 110
....*....|....*....|....*....|..
gi 1242862604 738 SAQERcqaEAEMDEIRKSHQEeldRLRQLLKK 769
Cdd:pfam09744 115 RLEEK---EAELKKEYSKLHE---RETEVLRK 140
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
720-893 |
3.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 720 LRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSH------QEELDRLRQLLKKARVSTDQAAAEQLTLAQA-ELQSQ 792
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeyaelQEELEELEEELEELEAELEELREELEKLEKLlQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 793 WE--AKCEQLLASARD------EHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAftEQKEHMQRLEKTKSQAPAGR 864
Cdd:COG4717 131 YQelEALEAELAELPErleeleERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRL 208
|
170 180
....*....|....*....|....*....
gi 1242862604 865 AAADpsEKVKKIMNQVfQSLRGEFELEES 893
Cdd:COG4717 209 AELE--EELEEAQEEL-EELEEELEQLEN 234
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
677-816 |
3.91e-04 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 42.74 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 677 RLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEM------- 749
Cdd:pfam08703 9 RLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAkkrtsdk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 750 -------DEIRKSH-QEELDRLRQL----------LKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARdEHLQQ 811
Cdd:pfam08703 89 aaqerlkKEINNSHiQEVVQSIKQLeekqkrrqekLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEVR-ESVKS 167
|
....*
gi 1242862604 812 YREVC 816
Cdd:pfam08703 168 CLKEG 172
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
623-733 |
4.05e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 623 ENTQAKVTEELAAATAQVSHLQLKM--------TAHQKKETELQLQlTDNLKETDLLRGHVTRLQADLSELREASEQTQT 694
Cdd:pfam07926 7 QSEIKRLKEEAADAEAQLQKLQEDLekqaeiarEAQQNYERELVLH-AEDIKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 1242862604 695 KFKSEKQSrrqlelkvtsLEEELTDLRAEKTSLEKNLSE 733
Cdd:pfam07926 86 ELEESEES----------WEEQKKELEKELSELEKRIED 114
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
579-763 |
4.37e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 579 LLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAAtaqvshlqlkmtahQKKETELQ 658
Cdd:pfam08614 12 LLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAEL--------------YRSRGELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 659 LQLTDnlketdllrghvtrLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEEL-------TDLRAEKTSLEKNL 731
Cdd:pfam08614 78 QRLVD--------------LNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELrekrklnQDLQDELVALQLQL 143
|
170 180 190
....*....|....*....|....*....|..
gi 1242862604 732 SerkkksaqercQAEAEMDEIRKSHQEELDRL 763
Cdd:pfam08614 144 N-----------MAEEKLRKLEKENRELVERW 164
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
518-858 |
4.64e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 518 RMAVNK-----VADKMDHLMTKVEELQK----HSSGNSMLLPSMSVT------METSMIMS--NIQRIIQENERLKQE-- 578
Cdd:pfam10174 54 RISVLKeqyrvTQEENQHLQLTIQALQDelraQRDLNQLLQQDFTTSpvdgedKFSTPELTeeNFRRLQSEHERQAKElf 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 579 LLEKS-----SRIEEQNDKISDLIERNQRYVEqsnlMMEKRNNSlQTATENTQAKvTEELAAATAQVSHLQLKMtahQKK 653
Cdd:pfam10174 134 LLRKTleemeLRIETQKQTLGARDESIKKLLE----MLQSKGLP-KKSGEEDWER-TRRIAEAEMQLGHLEVLL---DQK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 654 ETELQlqltdNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLeeeltdlraeKTSLEKNLSE 733
Cdd:pfam10174 205 EKENI-----HLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQML----------KTNGLLHTED 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 734 RkkksaqercQAEAEMDEIRKSH----QEELDRLRQLL--KKARVSTDQAAAEQLTLAQAElqsqweakCEQllasarde 807
Cdd:pfam10174 270 R---------EEEIKQMEVYKSHskfmKNKIDQLKQELskKESELLALQTKLETLTNQNSD--------CKQ-------- 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 808 HLQQYREVCAqrdAHQQKLALLQDECLALQAQI----AAFTEQKEHMQRLEKTKS 858
Cdd:pfam10174 325 HIEVLKESLT---AKEQRAAILQTEVDALRLRLeekeSFLNKKTKQLQDLTEEKS 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
565-729 |
5.26e-04 |
|
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: 43.98 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 565 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATAQVSH 642
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 643 LQLKMTAHQKKETELQLQLTDNLKETDLLRghvTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRA 722
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEER---AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*..
gi 1242862604 723 EKTSLEK 729
Cdd:COG4942 235 EAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
509-892 |
6.46e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 509 EARQHNTEIRM-AVNKV--ADKMDHLMTKVEELQKHSSGNSMLLPSMSVtmetsmiMSNIQRIIQENERLKQELLEKSsr 585
Cdd:PTZ00121 1216 EARKAEDAKKAeAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAH-------FARRQAAIKAEEARKADELKKA-- 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 586 ieEQNDKISDLIERNQ-RYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDN 664
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEkKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 665 LKETDLLRGHVTRLQADlsELREASEQT----QTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQ 740
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKAD--AAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 741 ERCQAEA--EMDEIRKSHQ-----EELDRLRQLLKKA----RVSTDQAAAEQLTLAQAELQSQWEA--KCEQLLASARDE 807
Cdd:PTZ00121 1443 AKKADEAkkKAEEAKKAEEakkkaEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAkkKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 808 HLQQYREVCAQRDAHQQKLAllQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGE 887
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
....*
gi 1242862604 888 FELEE 892
Cdd:PTZ00121 1601 YEEEK 1605
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
575-796 |
6.54e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 575 LKQELLEKSSRIEEQNDKISDLIERNQryvEQSNLMMEKrNNSLQTaTENTQAKVTEELAAATAQVSHL----------- 643
Cdd:PRK11637 52 IQQDIAAKEKSVRQQQQQRASLLAQLK---KQEEAISQA-SRKLRE-TQNTLNQLNKQIDELNASIAKLeqqqaaqerll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 644 --QLKMTAHQKKETELQLqltdnlketdLLRGHVT----RLQADLSELREASEQTQTKFKsekQSRRQLELKVTSLEEE- 716
Cdd:PRK11637 127 aaQLDAAFRQGEHTGLQL----------ILSGEESqrgeRILAYFGYLNQARQETIAELK---QTREELAAQKAELEEKq 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 717 ------LTDLRAEKTSLEKNLSERKK------KSAQERCQAEAEMdeirksHQEElDRLRQLLKKARVSTDQAAAEQLTL 784
Cdd:PRK11637 194 sqqktlLYEQQAQQQKLEQARNERKKtltgleSSLQKDQQQLSEL------RANE-SRLRDSIARAEREAKARAEREARE 266
|
250
....*....|..
gi 1242862604 785 AQAELQSQWEAK 796
Cdd:PRK11637 267 AARVRDKQKQAK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
703-852 |
7.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 703 RRQLELKVTSLEEELTDLRAEKTSLEKnlserkkksAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAAA 779
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862604 780 EQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQ-QKLAllqdeclALQAQIAAFTEQKEHMQR 852
Cdd:COG4913 291 ELLEAELEELRAELARLEAELerLEARLDALREELDELEAQIRGNGgDRLE-------QLEREIERLERELEERER 359
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
684-859 |
8.08e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 684 ELREASEQTQTKFKSEKQSRRQLELKVTSLEEELtdlRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKsHQEELDRL 763
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEI---RLRKQRLEEERQRQEEEERKQRLQLQAAQERARQ-QQEEFRRK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 764 RQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYRevcaQRDAHQQKlALLQDECLALQAQIAAF 843
Cdd:pfam15709 432 LQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQR----QKQEAEEK-ARLEAEERRQKEEEAAR 506
|
170
....*....|....*.
gi 1242862604 844 TEQKEHMQRLEKTKSQ 859
Cdd:pfam15709 507 LALEEAMKQAQEQARQ 522
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
679-867 |
8.69e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 679 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEmdEIRKSHQE 758
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA--AAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 759 ELDRLRQLLKKARVSTD-QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAllqdecLALQ 837
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKkKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------EAKA 225
|
170 180 190
....*....|....*....|....*....|
gi 1242862604 838 AQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 867
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
558-890 |
9.48e-04 |
|
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: 43.36 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 558 TSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQSNLMMEKRNnslqtaTENTQAKVteelaaat 637
Cdd:pfam15964 295 TNVHMQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQ----VKQAVQMTEEAN------FEKTKALI-------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 638 aQVSHLQLKMTAHQKK-ETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkfksekqsrrqlelKVTSLEEE 716
Cdd:pfam15964 357 -QCEQLKSELERQKERlEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ-----------------NVAQLEAQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 717 LTDLRAEKTSLEKNLSERKKKSAQErcqaEAEMDEIrkshqeeLDRLRQLLKKARVSTDQAAAEQLTLaQAELQSQWEAK 796
Cdd:pfam15964 419 VEKVTREKNSLVSQLEEAQKQLASQ----EMDVTKV-------CGEMRYQLNQTKMKKDEAEKEHREY-RTKTGRQLEIK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 797 cEQLLASARDEhLQQYREvcaQRDAHQQKLALLQDECLALqAQIAAFTEQKEHMQRLEKTKSQAPAGRAAAdpsekvkki 876
Cdd:pfam15964 487 -DQEIEKLGLE-LSESKQ---RLEQAQQDAARAREECLKL-TELLGESEHQLHLTRLEKESIQQSFSNEAK--------- 551
|
330
....*....|....
gi 1242862604 877 mNQVFQSLRGEFEL 890
Cdd:pfam15964 552 -AQALQAQQREQEL 564
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
505-896 |
9.57e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 505 FLMTearqHNTEIRMAVNKVADKMDHLMTKVEELqKHSSGNSMLLPSMsVTMETSMIMSNIQRIiqENER---------L 575
Cdd:PRK04863 220 YLLP----ENSGVRKAFQDMEAALRENRMTLEAI-RVTQSDRDLFKHL-ITESTNYVAADYMRH--ANERrvhleealeL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 576 KQELLE-KSSRIEEQNDKIS-----DLIERNQRYVEQSNLMMEKRNNSLQTATENTQA--KVTEELAAATAQV-SHLQLK 646
Cdd:PRK04863 292 RRELYTsRRQLAAEQYRLVEmarelAELNEAESDLEQDYQAASDHLNLVQTALRQQEKieRYQADLEELEERLeEQNEVV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 647 MTAHQKKEtELQLQLTDNLKETDllrghvtRLQADLSELREASEQTQTKFKSEKQSRRQLE----------LKVTSLEEE 716
Cdd:PRK04863 372 EEADEQQE-ENEARAEAAEEEVD-------ELKSQLADYQQALDVQQTRAIQYQQAVQALErakqlcglpdLTADNAEDW 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 717 LTDLRA-EKTSLEKNLS-ERKKKSAQE-RCQAEAEMDEIRK-----SHQEELDRLRQLLKKARvsTDQAAAEQLT----- 783
Cdd:PRK04863 444 LEEFQAkEQEATEELLSlEQKLSVAQAaHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLR--EQRHLAEQLQqlrmr 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 784 LAQAELQSQWEAKCEQLLASARDEHLQQYR---EVCAQRDAHQQKLALLQDECLALQAQ-IAAFTEQKEHMQRLEKTKSQ 859
Cdd:PRK04863 522 LSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERrMALRQQLEQLQARIQRLAAR 601
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1242862604 860 APAGRAAADPSEKV-----------KKIMNQVFQSLRGEFELEESYDG 896
Cdd:PRK04863 602 APAWLAAQDALARLreqsgeefedsQDVTEYMQQLLERERELTVERDE 649
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
185-285 |
9.59e-04 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 42.09 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 185 LVAAEGPAVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSgkVVKGLEDGLLGMKKGGKRLIITPSACAAG 264
Cdd:PRK11570 109 LTQGEGAIPARTDRVRVHYTGKLID----GTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYG 182
|
90 100
....*....|....*....|.
gi 1242862604 265 SEGViGWTQPTDSILVFEVEV 285
Cdd:PRK11570 183 ERGA-GASIPPFSTLVFEVEL 202
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
613-848 |
1.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 613 KRNNSLQTATENTQAKVT---EELAAATAQVSHLQLKMTAHQKKETELQlqltdnlketdllrghvtRLQADLSELRE-- 687
Cdd:PRK02224 206 ERLNGLESELAELDEEIEryeEQREQARETRDEADEVLEEHEERREELE------------------TLEAEIEDLREti 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 688 -ASEQTQTKFKSEKQSRRQlelKVTSLEEELTDLRAEktsleknlserkkksaqerCQAEAEMDEIRKSHQEELDR---- 762
Cdd:PRK02224 268 aETEREREELAEEVRDLRE---RLEELEEERDDLLAE-------------------AGLDDADAEAVEARREELEDrdee 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 763 LRQLLKKARVSTDQAA--AEQLTLAQAELQSQWEAKCEQllASARDEHLQQYREVCAQRdahQQKLALLQDECLALQAQI 840
Cdd:PRK02224 326 LRDRLEECRVAAQAHNeeAESLREDADDLEERAEELREE--AAELESELEEAREAVEDR---REEIEELEEEIEELRERF 400
|
....*...
gi 1242862604 841 AAFTEQKE 848
Cdd:PRK02224 401 GDAPVDLG 408
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
571-859 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQ-SNLmmEKRNNSLQTATENTQAKVT---EELAAATAQVSHLQLK 646
Cdd:pfam10174 381 EIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQlAGL--KERVKSLQTDSSNTDTALTtleEALSEKERIIERLKEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 647 mtaHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSE----LREASEQTQTKFKS--EKQSR-RQLELKVTSLEEELTD 719
Cdd:pfam10174 459 ---REREDRERLEELESLKKENKDLKEKVSALQPELTEkessLIDLKEHASSLASSglKKDSKlKSLEIAVEQKKEECSK 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 720 LRAE-KTSLEKNLSERKKKSAQERCQA-EAEM----DEIRKShQEELDRLRQLLKKA---RVSTDQ--AAAEQLTLAQAE 788
Cdd:pfam10174 536 LENQlKKAHNAEEAVRTNPEINDRIRLlEQEVarykEESGKA-QAEVERLLGILREVeneKNDKDKkiAELESLTLRQMK 614
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242862604 789 LQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDEclalqaqiaafteqkEHMQRLEKTKSQ 859
Cdd:pfam10174 615 EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE---------------ELMGALEKTRQE 670
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
515-776 |
1.30e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 515 TEIRMAVNKVADKMDHLMTKVEELQKHSSG-NSMLLPSMSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKI 593
Cdd:TIGR00606 825 QQVNQEKQEKQHELDTVVSKIELNRKLIQDqQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREI 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 594 SDliERNQRY-VEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETE-LQLQLTDNLKETDLL 671
Cdd:TIGR00606 905 KD--AKEQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTV 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 672 RGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVT--SLEEELTDLRAEKTSLEKNLSE-RKKKSAQERCQAEAE 748
Cdd:TIGR00606 983 NAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTlrKRENELKEVEEELKQHLKEMGQmQVLQMKQEHQKLEEN 1062
|
250 260 270
....*....|....*....|....*....|...
gi 1242862604 749 MDEIRKSHQEELDRLRQ-----LLKKARVSTDQ 776
Cdd:TIGR00606 1063 IDLIKRNHVLALGRQKGyekeiKHFKKELREPQ 1095
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
684-788 |
1.39e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.93 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 684 ELREASEQTQTKFKSEKQSRRQLELKVTSLEEELtDLRAEKTSLEKNLSERKKKSAQERC----QAEAEMDEIRKSHQEE 759
Cdd:PRK00106 80 EARKYREEIEQEFKSERQELKQIESRLTERATSL-DRKDENLSSKEKTLESKEQSLTDKSkhidEREEQVEKLEEQKKAE 158
|
90 100
....*....|....*....|....*....
gi 1242862604 760 LDRLRQLlkkarvstDQAAAEQLTLAQAE 788
Cdd:PRK00106 159 LERVAAL--------SQAEAREIILAETE 179
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
576-893 |
1.73e-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: 42.32 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 576 KQELLEKSSRIEEQNDKISDLIERNQRYVEqsnlmmekrnnslqtATENTQAKVTEELAAATAQVSHLQLKMTAHQKKET 655
Cdd:pfam05701 30 RIQTVERRKLVELELEKVQEEIPEYKKQSE---------------AAEAAKAQVLEELESTKRLIEELKLNLERAQTEEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 656 ELQlqltdnlKETDLLRGHVTRLQADLSElrEASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLeknLSERK 735
Cdd:pfam05701 95 QAK-------QDSELAKLRVEEMEQGIAD--EASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASL---VSERD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 736 KkSAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ--SQWEAKCEQLlasarDEHLQ 810
Cdd:pfam05701 163 I-AIKRAEEAVSASKEIEKTVEEltiELIATKESLESAHAAHLEAEEHRIGAALAREQdkLNWEKELKQA-----EEELQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 811 QYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK-----EHMQRLEKTKSQAPAGRAAADPS-EKVK---------- 874
Cdd:pfam05701 237 RLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESKlkeeaDGEGNEKKTSTSIQAALASAKKElEEVKaniekakdev 316
|
330
....*....|....*....
gi 1242862604 875 KIMNQVFQSLRGEFELEES 893
Cdd:pfam05701 317 NCLRVAAASLRSELEKEKA 335
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
571-811 |
1.79e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 571 ENERLKQELLEKSSRIEEQNDkisDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAH 650
Cdd:NF041483 503 ESERVRTEAIERATTLRRQAE---ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTR 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 651 QKKETELQLQ-----LTDNLKETDLLRghvtrlqadlselREASEQTQtKFKSEKQSR-RQLElkvTSLEEELTDLRAEK 724
Cdd:NF041483 580 LHTEAEERLTaaeeaLADARAEAERIR-------------REAAEETE-RLRTEAAERiRTLQ---AQAEQEAERLRTEA 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 725 TS-LEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQwEAKCEQLLAS 803
Cdd:NF041483 643 AAdASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARR-RREAEETLGS 721
|
....*...
gi 1242862604 804 ARDEHLQQ 811
Cdd:NF041483 722 ARAEADQE 729
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
652-887 |
1.82e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 652 KKETELQLQLTDNLKETDLLRGHVtrLQADLSElreaSEQTQTKFKSEKQS--RRQLELKVTSLEEELTDLRAEKTSLE- 728
Cdd:COG5022 823 QKTIKREKKLRETEEVEFSLKAEV--LIQKFGR----SLKAKKRFSLLKKEtiYLQSAQRVELAERQLQELKIDVKSISs 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 729 -KNLSERKKKSAQE-RCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ---WEAKCEQL--L 801
Cdd:COG5022 897 lKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVeskLKETSEEYedL 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 802 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQiaafTEQKEHMQR-------LEKTKSQAPAGRAAADPSEKVK 874
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFKKELAELSKQYGALQES----TKQLKELPVevaelqsASKIISSESTELSILKPLQKLK 1052
|
250
....*....|...
gi 1242862604 875 KIMNQVFQSLRGE 887
Cdd:COG5022 1053 GLLLLENNQLQAR 1065
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
566-795 |
1.82e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 566 QRIIQENERLKQELLEKSSrieeqndkISDLIERNQRYVEQSNLMMEKrnNSLQtatentqakvtEELAAATAQVSHLQl 645
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSG--------VEGLDSSTALTLELEELRQER--DLLR-----------EEIQKLRGQIQQLR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 646 kmtahqkkeTELQlqltdnlkETDllrghvTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKt 725
Cdd:pfam09787 75 ---------TELQ--------ELE------AQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEEL- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862604 726 sleknlsERKKKSAQERCQaeaemdeirkSHQEELDRLR-QLLKKARVSTDQAAAE----QLTLAQAELQSQWEA 795
Cdd:pfam09787 131 -------RRSKATLQSRIK----------DREAEIEKLRnQLTSKSQSSSSQSELEnrlhQLTETLIQKQTMLEA 188
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
694-896 |
1.94e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 694 TKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKksaqercQAEAEMDEIRKSHQEELDRLRQLLKKARVS 773
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA-------ELNQLLRTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 774 TdqaaaeqltlaqaelqsqweAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRL 853
Cdd:pfam12128 317 V--------------------AKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK 376
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1242862604 854 EKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDG 896
Cdd:pfam12128 377 YNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQA 419
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
638-859 |
1.95e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 638 AQVSHLQLKMTAHQK-KETELQLQLTDNLKETDL-LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLE---LKVTS 712
Cdd:TIGR00606 187 ALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 713 LEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ 792
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862604 793 WEAKCEQLLASARDEHLQQYrEVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQ 859
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
741-860 |
2.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 741 ERCQAEAEMDEIrKSHQEELDRLRQLLKKARvstdqaaaeqltlAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRD 820
Cdd:COG4913 219 EEPDTFEAADAL-VEHFDDLERAHEALEDAR-------------EQIELLEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1242862604 821 AHQQKLALLQDECLALQAQIAAFTEQKEhmqRLEKTKSQA 860
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELE---RLEARLDAL 321
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
652-767 |
2.20e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 652 KKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSE--KQSR-----RQLELKVTSLEEELTDLRAEK 724
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvLHAEdikalQALREELNELKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1242862604 725 TSLEKNLSERKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLL 767
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
617-868 |
2.27e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 617 SLQTATEnTQAKVTEELAAATAQVSHLQLKMT--AHQKKETELQLQLTDNLKETDLLRGHvtrlQADLSELREASEQTQT 694
Cdd:pfam12128 612 ALQSARE-KQAAAEEQLVQANGELEKASREETfaRTALKNARLDLRRLFDEKQSEKDKKN----KALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 695 KFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNL-SERKKKSAQ-------ERCQAEAEMDEIRKSHQEELDRLR-Q 765
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVeGALDAQLALlkaaiaaRRSGAKAELKALETWYKRDLASLGvD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 766 LLKKARVSTDQAAAEQlTLAQAelqsqweAKCEQLLASARDEHLQQYREvcaQRDAHQQKLALLQDECLALQAQIAAFTE 845
Cdd:pfam12128 767 PDVIAKLKREIRTLER-KIERI-------AVRRQEVLRYFDWYQETWLQ---RRPRLATQLSNIERAISELQQQLARLIA 835
|
250 260
....*....|....*....|...
gi 1242862604 846 QKEhmQRLEKTKSQAPAGRAAAD 868
Cdd:pfam12128 836 DTK--LRRAKLEMERKASEKQQV 856
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
516-857 |
2.78e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 516 EIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMIMSNIQRIIQENERLKQELLEKSSRI--------- 586
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSdldrtvqqv 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 587 -------EEQNDKISDLIERNQRyveqsnlMMEKRNNSLQTATENTQAKVTEELAAATAqvshlqlkmtahQKKETELQL 659
Cdd:TIGR00606 828 nqekqekQHELDTVVSKIELNRK-------LIQDQQEQIQHLKSKTNELKSEKLQIGTN------------LQRRQQFEE 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 660 QLTDNLKETDLLRGHVTRLQADLSELREASEQTQTK----FKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSE-- 733
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgk 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 734 --RKKKSAQERCQAEAEMDEIRKsHQEeldRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQlLASARDEHLQQ 811
Cdd:TIGR00606 969 ddYLKQKETELNTVNAQLEECEK-HQE---KINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKE-VEEELKQHLKE 1043
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1242862604 812 YRE--VCAQRDAHQQ---KLALLQDECLALQAQIAAFTEQKEHMQRLEKTK 857
Cdd:TIGR00606 1044 MGQmqVLQMKQEHQKleeNIDLIKRNHVLALGRQKGYEKEIKHFKKELREP 1094
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
629-879 |
3.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 629 VTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLEL 708
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 709 KVTSLEEELTDLRAEKTSLEKNLSERKKKsaqercqaEAEMDEIRKSHQ-------------EELDRLRQLLKKARVSTD 775
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKL--------RKEIERLEWRQQtevlspeeekelvEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 776 QAAAEQLTLAQA-ELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQI----AAFTEQKE 848
Cdd:COG1340 158 KNEKLKELRAELkELRKEAEEIHKKIkeLAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAdelhEEIIELQK 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 1242862604 849 HMQRLEKT-----KSQAPAGRAAADPS--EKVKKIMNQ 879
Cdd:COG1340 238 ELRELRKElkklrKKQRALKREKEKEEleEKAEEIFEK 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
630-814 |
3.30e-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: 41.70 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 630 TEELAAATaqvshlQLKMTAHQKKEtELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELK 709
Cdd:pfam01576 846 QEDLAASE------RARRQAQQERD-ELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 710 VTSLEEELTdlrAEKTSLEKNLS-----ERKKKSAQERCQaeaEMD-EIRKSHQEELDRLRQLLKKARVSTDQAAAEQlt 783
Cdd:pfam01576 919 VEQLTTELA---AERSTSQKSESarqqlERQNKELKAKLQ---EMEgTVKSKFKSSIAALEAKIAQLEEQLEQESRER-- 990
|
170 180 190
....*....|....*....|....*....|...
gi 1242862604 784 LAQAELQSQWEAKCEQLLASARDE--HLQQYRE 814
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDErrHADQYKD 1023
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
628-870 |
3.31e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.86 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 628 KVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQtkfksekQSRRQLE 707
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTL-------GHAKELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 708 LKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAE--MDEIRKshqeeldrlRQLLKKARVSTDQAAAEQLTLA 785
Cdd:pfam06008 89 EAIKNLIDNIKEINEKVATLGENDFALPSSDLSRM-LAEAQrmLGEIRS---------RDFGTQLQNAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 786 QA-ELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGR 864
Cdd:pfam06008 159 RIqTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
....*.
gi 1242862604 865 AAADPS 870
Cdd:pfam06008 239 KTARDS 244
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
671-769 |
3.32e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.22 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 671 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQercqaeaemd 750
Cdd:pfam11559 64 LEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAH---------- 133
|
90
....*....|....*....
gi 1242862604 751 EIRKsHQEELDRLRQLLKK 769
Cdd:pfam11559 134 EVKK-RDREIEKLKERLAQ 151
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
731-902 |
3.55e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 39.93 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 731 LSERKKKSAQERCQAEAEMDEIRKSHQEELDRLR-QLLKKARVSTDQAAAEQltLAQAELQSQweakceQLLASARDEHL 809
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKeEILEKAEREAEREKRRI--ISSAELEAR------KELLEAKEELI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 810 QQYREvcaqrdahqqklallqdeclALQAQIAAFTEQKEHMQRLEKT----KSQAPAGRAAADPSEKVKKIMNQVFQSLR 885
Cdd:COG1390 84 EEVFE--------------------EALEKLKNLPKDPEYKELLKKLlkeaAEELGSGDLVVYVNEKDKELLEELLKELK 143
|
170 180
....*....|....*....|.
gi 1242862604 886 GE-FELEE---SYDGGTILRT 902
Cdd:COG1390 144 KKgLEVSEediDILGGVIVES 164
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
214-266 |
3.78e-03 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 39.31 E-value: 3.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1242862604 214 GQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACAAGSE 266
Cdd:PRK15095 22 GSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
302-497 |
4.07e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.68 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 302 SSRDSAAPSPIPASDSLSADPVVTPLPLPLKPGEPGLRsksnslseqlTVNSNPDTVKAKLISRMAKMgQPMLPILPPQl 381
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT----------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 382 dSNDSETEDATVLRGAGQSLVTP-SIQPSLQPaHPVLPQMASQAPQPSGSglQTPSAAlmqavsldshsavsgnaqnfQP 460
Cdd:pfam03154 260 -QVSPQPLPQPSLHGQMPPMPHSlQTGPSHMQ-HPVPPQPFPLTPQSSQS--QVPPGP--------------------SP 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1242862604 461 YAGVQAYAYPQTPSVTSQLQP-----VRPLYPAPLSQaPHFQ 497
Cdd:pfam03154 316 AAPGQSQQRIHTPPSQSQLQSqqpprEQPLPPAPLSM-PHIK 356
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
674-856 |
4.51e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.32 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 674 HVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRaekTSLEKnlsERKKKSAQeRCQAEAEMDEIR 753
Cdd:pfam15397 61 NKKQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLS---TYKDK---EYPVKAVQ-IANLVRQLQQLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 754 KSHQEELDRLRQLLKKARvstdqaaaeqltlaqAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAllqdEC 833
Cdd:pfam15397 134 DSQQDELDELEEMRRMVL---------------ESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVML----KE 194
|
170 180
....*....|....*....|...
gi 1242862604 834 LALQAQIAAftEQKEHMQRLEKT 856
Cdd:pfam15397 195 IEQFREFID--ELEEEIPKLKAE 215
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
682-800 |
4.59e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.82 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 682 LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDL-------RAEKTSLEKNLSERKKK---SAQERCQAEA---- 747
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLthknqqlEEEVEKLEEQLKEAKEKaeeSEKLKTNNENltrk 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1242862604 748 ------EMDEIRKSHQEELDRLRQllkkarvsTDqAAAEQLTLAQAELQS---QWEAKCEQL 800
Cdd:pfam12718 82 iqlleeELEESDKRLKETTEKLRE--------TD-VKAEHLERKVQALEQerdEWEKKYEEL 134
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
591-846 |
5.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 591 DKISDLIERNQRYVEQSN---LMMEKRNNSLQTAteNTQ-AKVTEELAAATAQVSHLQlkmtAHQK-KETELQLqltdnl 665
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAA--HSQfEQAYQLVRKIAGEVSRSE----AWDVaRELLRRL------ 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 666 KETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQA 745
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMAL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 746 EAemdeirksHQEELD-RLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQ 823
Cdd:PRK04863 585 RQ--------QLEQLQaRIQRLAARAPAwLAAQDALARL-----REQSGEEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
250 260
....*....|....*....|...
gi 1242862604 824 QKLALLQDECLALQAQIAAFTEQ 846
Cdd:PRK04863 652 ARKQALDEEIERLSQPGGSEDPR 674
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
569-771 |
6.68e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 569 IQENERLKQEllekssrieeQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTatentqakVTEELAAATAQVSHLQLKMT 648
Cdd:TIGR00606 417 LQSKERLKQE----------QADEIRDEKKGLGRTIELKKEILEKKQEELKF--------VIKELQQLEGSSDRILELDQ 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 649 AHQKKETELQLQLTDNLKETDLLR-GHVTRLQADLSELREASEQTQTKFKSEKQSRRQLEL------------------- 708
Cdd:TIGR00606 479 ELRKAERELSKAEKNSLTETLKKEvKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdkdeqirkiksrh 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 709 --KVTSL------------------------EEELTDLRAEKTSLEKNL----SERKKKSAQERCQAEAEMDEIRKSHQE 758
Cdd:TIGR00606 559 sdELTSLlgyfpnkkqledwlhskskeinqtRDRLAKLNKELASLEQNKnhinNELESKEEQLSSYEDKLFDVCGSQDEE 638
|
250
....*....|....
gi 1242862604 759 -ELDRLRQLLKKAR 771
Cdd:TIGR00606 639 sDLERLKEEIEKSS 652
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
669-771 |
6.90e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 669 DLLRGHVTRLQADLSELREASEQTQTKFKSEKQSR-RQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEA 747
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100
....*....|....*....|....*.
gi 1242862604 748 EMDEIRK--SHQEELDRLRQLLKKAR 771
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEER 485
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
658-790 |
7.05e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.05 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 658 QLQLTDNLKET----DLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTslekNLSE 733
Cdd:pfam10473 5 QLHVLEKLKESerkaDSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLV----TLRS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862604 734 RKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 790
Cdd:pfam10473 81 EKENLTKELQKKQERVSELESLN-SSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
601-859 |
7.67e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 601 QRYVEQSNLMMEKRNNSLQT---ATENTQAKVTEELAAATAQVSHLQLKMTAHQkketelqlqltdnlketdlLRGHVTR 677
Cdd:PRK10246 238 AQQQQQQSLNWLTRLDELQQeasRRQQALQQALAAEEKAQPQLAALSLAQPARQ-------------------LRPHWER 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 678 LQ---ADLSELREASEQTQTKFKSEKQSRRQLElkvTSLEEELTDLRAEKTSLEKNLSE--RKKKSAQERCQAEAEMDEi 752
Cdd:PRK10246 299 IQeqsAALAHTRQQIEEVNTRLQSTMALRARIR---HHAAKQSAELQAQQQSLNTWLAEhdRFRQWNNELAGWRAQFSQ- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 753 RKSHQEELDRLRQLLKKARVSTDQAAAEQLTL-----AQAELQSQWEAKCEQLLASARDEHLQQyrevcaqrdahQQKLA 827
Cdd:PRK10246 375 QTSDREQLRQWQQQLTHAEQKLNALPAITLTLtadevAAALAQHAEQRPLRQRLVALHGQIVPQ-----------QKRLA 443
|
250 260 270
....*....|....*....|....*....|..
gi 1242862604 828 LLQDECLALQAQIAAFTEQKEHMQRLEKTKSQ 859
Cdd:PRK10246 444 QLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQ 475
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
564-867 |
8.86e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 564 NIQRIIQENERLKQELLEKSSRIEEQNDKISD---LIERNQRYVEqsnlmMEKRNNSLQTATENTQAKVTEELAAATAQV 640
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvktICEQEARIKD-----LEAQRAQLQAGQPCPLCGSTSHPAVEAYQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 641 shlqLKMTAHQKKETELQLQLTDNLKETDLLRGHV----TRLQADLSELREAS--EQTQTKFKSEKQSRRQLELKVtslE 714
Cdd:PRK10246 523 ----LEPGVNQSRLDALEKEVKKLGEEGAALRGQLdaltKQLQRDESEAQSLRqeEQALTQQWQAVCASLNITLQP---Q 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 715 EELTDLRAEKTSLEKNLSErkkksAQERCQAEAEMDEirksHQEELDRLRQLLKKARVS-TDQAAAEQLTLAQAELQSQW 793
Cdd:PRK10246 596 DDIQPWLDAQEEHERQLRL-----LSQRHELQGQIAA----HNQQIIQYQQQIEQRQQQlLTALAGYALTLPQEDEEASW 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 794 eakceqllASARDEHLQQYREVCAQRDAHQQKLALLQ----------------------------DECLALQAQIAAFTE 845
Cdd:PRK10246 667 --------LATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetvaldnwrqvhEQCLSLHSQLQTLQQ 738
|
330 340
....*....|....*....|...
gi 1242862604 846 QK-EHMQRLEKTKSQAPAGRAAA 867
Cdd:PRK10246 739 QDvLEAQRLQKAQAQFDTALQAS 761
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
509-759 |
9.17e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 509 EARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEE 588
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 589 QNDKISDL---IERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLkmtAHQKKETELQLQLTDNL 665
Cdd:TIGR00618 702 CQTLLRELethIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE---AHFNNNEEVTAALQTGA 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 666 KETDLLRGHVTR---LQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQER 742
Cdd:TIGR00618 779 ELSHLAAEIQFFnrlREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
250
....*....|....*..
gi 1242862604 743 CQAEAEMDEIRKSHQEE 759
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLS 875
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
302-495 |
9.57e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 302 SSRDSAAPSPIPASDSLSADPVVTPLPLPLKPGEPGlrskSNSLSEQLTVNSNPDTVKAKLISRMAKMGQPMLPILPPQ- 380
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP----PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQr 2682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862604 381 ----------------LDSNDSETEDATVLRGAGQSLVTPSIQPSLQPAHPVLPqmASQAPQPSGSGLQTPSAALMQAvs 444
Cdd:PHA03247 2683 prrraarptvgsltslADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPARPA-- 2758
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1242862604 445 ldSHSAVSGNAQNFQPYAGVQAYAYPQTPSVTSQLQPVRPLYPAPLSQAPH 495
Cdd:PHA03247 2759 --RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807
|
|
| |
