|
Name |
Accession |
Description |
Interval |
E-value |
| Uds1 |
pfam15456 |
Up-regulated During Septation; Uds1 is a domain family is found mostly in fungi, and is ... |
99-232 |
2.18e-39 |
|
Up-regulated During Septation; Uds1 is a domain family is found mostly in fungi, and is typically between 120 and 138 amino acids in length. The GO annotation for the S.pombe protein describes the protein as barrier septum assembly involved in cell cycle cytokinesis, GO:0071937. Many of the uncharacterized members are listed as being involucrin repeat proteins, but this can not be substantiated.
Pssm-ID: 434730 [Multi-domain] Cd Length: 119 Bit Score: 141.53 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 99 LLVETAVGDSLGYEILSFEELEALKKERTALTSKMEAVGQKLALETKMRDAAQSLSRLNakrrgsngervhgrsFSRSSQ 178
Cdd:pfam15456 1 LLVETALLDSQEFEILSFEEVEELKKELRALDSRLEYLRRKLALETKLRDAARSLHRLY---------------SSYLRS 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 407920239 179 TSNGSNPDSSAKSEAEYTASAQKCDNLSRELWQMERRYRQIDNQLLRHTAGILQ 232
Cdd:pfam15456 66 PRNSKFSESLLKAEEELAESDRKIDELAQELEKLENRRAEVRRRLLEHTAAVLQ 119
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
558-806 |
4.17e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELnEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIA 637
Cdd:COG1196 248 LEELEAELEELEAELAEL-EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 638 ELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAanpEVKRELE 717
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---ELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 718 ELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLE 797
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
....*....
gi 407920239 798 AQLSDEKMR 806
Cdd:COG1196 484 EELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-879 |
1.39e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 563 SILRRQIKQQRE-LneKSDAEKEEEFMRLRSEIDRLRHQLHAN---------SGDSDALQTAEERVAQLEAALSEAQGEA 632
Cdd:COG1196 192 EDILGELERQLEpL--ERQAEKAERYRELKEELKELEAELLLLklreleaelEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 633 DT---KIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAan 709
Cdd:COG1196 270 EElrlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 710 pEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTL 789
Cdd:COG1196 348 -EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 790 REKIESLEAQLSDEKMRwlgikspaaiptpgpngtpgmVLAETTSTKVLREEFRKMMRETRAEAIKALRAEQDERKRLEQ 869
Cdd:COG1196 427 EEALAELEEEEEEEEEA---------------------LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330
....*....|
gi 407920239 870 ILRQLKREQL 879
Cdd:COG1196 486 LAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-876 |
3.04e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 567 RQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAA 646
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 647 KASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEVKRELEELAKVNAE- 725
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEd 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 726 ---LTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMtkvnvesEKEREGLESVIDTLREKIESLEAQLSD 802
Cdd:TIGR02168 854 iesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL-------SEELRELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407920239 803 EKMRWLGIKspaaiptpgpngtpgMVLAETTSTkvLREEFRKMMRETRAEAIKALRAEQDERKRLEQILRQLKR 876
Cdd:TIGR02168 927 LELRLEGLE---------------VRIDNLQER--LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
566-804 |
5.46e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 566 RRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEA 645
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 646 AKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAEldgaygtRAQRAADIAanpEVKRELEELAKVNAE 725
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-------AAELAAQLE---ELEEAEEALLERLER 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407920239 726 LTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLSDEK 804
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-877 |
4.98e-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: 73.18 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 560 EKQSILRRQIKQQRELNEKsDAEKEEEFMRLRSEIDRLRHQLHANSgdsdaLQTAEERVAQLEAALSEAQGE---ADTKI 636
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRR-EREKAERYQALLKEKREYEGYELLKE-----KEALERQKEAIERQLASLEEElekLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 637 AELNQSLEAAKASEAEVARTIEQK-EEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADI----AANPE 711
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdkllAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 712 VKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKvnvesekEREGLESVIDTLRE 791
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR-------EINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 792 KIESLEAQLSDEKMRWLGIKspAAIPTpgpngtpgmvLAETTSTKVLR----EEFRKMMRETRAEAIKALRAEQDERKRL 867
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIE--AKINE----------LEEEKEDKALEikkqEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330
....*....|
gi 407920239 868 EQILRQLKRE 877
Cdd:TIGR02169 482 EKELSKLQRE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
558-800 |
5.42e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILR----RQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLhansgdsdalQTAEERVAQLEAALSEAQG--- 630
Cdd:COG1196 222 LKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAEL----------EELRLELEELELELEEAQAeey 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 631 EADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAygtRAQRAADIAANP 710
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 711 EVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLR 790
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250
....*....|
gi 407920239 791 EKIESLEAQL 800
Cdd:COG1196 449 EEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-794 |
1.17e-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: 68.93 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 439 AENQINYVEDALYAIEQSQQGLLTQLDEARNaDTSELTAYWKEQATEYEKVCESLwemirtGHEEARQRKLQRRRVLEAD 518
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISALRKDL------ARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 519 PDAVSDLGEMSPDEDPMPEEFTLSRFSTQVQDMYRRASGLKEKQSILRRQIkqqRELNEKSDAEKEEeFMRLRSEIDRLR 598
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL---DELRAELTLLNEE-AANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 599 HQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEV 678
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 679 VRLQTELTMAKAELdGAYGTRAQRA-ADIAanpEVKRELEELAKVNAEltsEVARLTEAHAAAARSAKDVAEREKMLREE 757
Cdd:TIGR02168 911 SELRRELEELREKL-AQLELRLEGLeVRID---NLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 407920239 758 L----RDTISEFEEMTKVNVESEKEREGLESVIDTLREKIE 794
Cdd:TIGR02168 984 LgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-800 |
1.91e-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: 68.16 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELNEKSDAEKEEefmrLRSEIDRLRHQLHAnsgdsdalqtAEERVAQLEAALSEAQGEadtkIA 637
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQE----LEEKLEELRLEVSE----------LEEEIEELQKELYALANE----IS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 638 ELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYG----TRAQRAADIAANPEVK 713
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAeleeLEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 714 RELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNV-----ESEKEREGLESVIDT 788
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeleELEEELEELQEELER 458
|
250
....*....|..
gi 407920239 789 LREKIESLEAQL 800
Cdd:TIGR02168 459 LEEALEELREEL 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
552-797 |
5.46e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 552 YRRASGLKEKQSILRRQIKQQRELNEKSDAEKE---EEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEA 628
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 629 QGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAEldgayGTRAQRAADIAA 708
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS-----KLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 709 NPEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDT 788
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
....*....
gi 407920239 789 LREKIESLE 797
Cdd:TIGR02169 894 LEAQLRELE 902
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
541-797 |
3.64e-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: 63.93 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 541 LSRFSTQVQDMYRRASGLKEKQSILRRQIKQ-QRELNEKSD--AEKEEEFMRLRSEIDRLRHQLH----------ANSGD 607
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQeiENVKSELKELEARIEELEEDLHkleealndleARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 608 S------DALQTAEERVAQLEAALSEAQGE----------ADTKIAELNQSLEAAKASEAEVARTIE-------QKEEEL 664
Cdd:TIGR02169 791 SripeiqAELSKLEEEVSRIEARLREIEQKlnrltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeELEEEL 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 665 AKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANP----EVKRELEELAKVNAELTSEVARLTEAHAAA 740
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407920239 741 ARSAKDVAEREKMLrEELRD-------TISEFEEMTKVNVESEKEREGLESVIDTLREKIESLE 797
Cdd:TIGR02169 951 LSLEDVQAELQRVE-EEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
584-799 |
4.20e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 584 EEEFMRLRSEIDRLrHQLHansgdsDALQTAEERVAQLE--AALSEAQGEADTKIAELNQSLEAAKASEAEvaRTIEQKE 661
Cdd:COG4913 224 FEAADALVEHFDDL-ERAH------EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 662 EELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQ----RAADIAAnpEVKRELEELAKVNAELTSEVARLTEAH 737
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLER--EIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407920239 738 AAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQ 799
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-800 |
2.14e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 555 ASGLKEKQSILRRQIKQQRELNEKSDaEKEEEFMRLRSEIDRLRHQLhansgdsdalQTAEERVAQLEAALSEAQGEADT 634
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIE-ELQKELYALANEISRLEQQK----------QILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 635 KIAELNQSLEAAKASEAEVART---IEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANpe 711
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 712 vKRELEELAKVNAELTSEVARLTEAHAAAARSA--KDVAEREKM---LREELRDTISEFEEMTKVNVESEKEREGLESVI 786
Cdd:TIGR02168 406 -EARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEEleeLQEELERLEEALEELREELEEAEQALDAAEREL 484
|
250
....*....|....
gi 407920239 787 DTLREKIESLEAQL 800
Cdd:TIGR02168 485 AQLQARLDSLERLQ 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
616-877 |
3.59e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 616 ERVAQLEAALSEAQG--------EADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTM 687
Cdd:TIGR02168 213 ERYKELKAELRELELallvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 688 AKAELDGAYG----TRAQRAADIAANPEVKRELEELAKVNAELTSEVARLTEahaaaarSAKDVAEREKMLREELRDTIS 763
Cdd:TIGR02168 293 LANEISRLEQqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEE-------KLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 764 EFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLS----------DEKMRWLGIKSPAAIPTPGPNgtpgmvLAETT 833
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearlerleDRRERLQQEIEELLKKLEEAE------LKELQ 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 407920239 834 STKVLREEFRKMMRETRAEAIKALRAEQDERKRLEQILRQLKRE 877
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
485-796 |
5.44e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 485 EYEKVCESLWEMIRTGHEEARQRKLQRRRVLEADPDAVSDLGEMSPDEDPMPEEF-TLSRFSTQVQDMYRRASGLKEKQS 563
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLaRLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 564 ILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSL 643
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 644 EAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADI-AANPEVKRELEELAKV 722
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELrELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407920239 723 NAELTSEVARLTEAHAaaarsakDVAEREKMLREELRDTiseFEEMTKVNVESEKEREGLESVIDTLREKIESL 796
Cdd:TIGR02168 921 REKLAQLELRLEGLEV-------RIDNLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
540-767 |
6.76e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 540 TLSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRElnEKSDAEKEEEfmRLRSEIDRLRHQLhanSGDSDALQTAEERVA 619
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEE--RRRELEERLE--ELEEELAELEEEL---EELEEELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 620 QLEAALSEAQGEadtkIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTR 699
Cdd:COG1196 348 EAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407920239 700 AQRAADIAanpEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEE 767
Cdd:COG1196 424 EELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
481-812 |
7.55e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 481 EQATEYEKVCESLWEMIRTgHEEARQRKLQRRRVL-------EADPDAVSDLGEMSPDEDPMPEEfTLSRFSTQVQDMYR 553
Cdd:PRK02224 265 ETIAETEREREELAEEVRD-LRERLEELEEERDDLlaeagldDADAEAVEARREELEDRDEELRD-RLEECRVAAQAHNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 554 RASGLKEKQSILRRQIKQQRELNEKSDAEKE---EEFMRLRSEIDRLRHQLHANS---GDSD-ALQTAEERVAQLEAALS 626
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEearEAVEDRREEIEELEEEIEELRerfGDAPvDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 627 EAQG----------EADTKIAELNQSLEAAKASE-------AEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAK 689
Cdd:PRK02224 423 ELREreaeleatlrTARERVEEAEALLEAGKCPEcgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 690 --AELDGAYGTRAQRAADIAANPEVKRE--------LEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELR 759
Cdd:PRK02224 503 dlVEAEDRIERLEERREDLEELIAERREtieekrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 407920239 760 DTISEFEEMTKVnVESEKEREGLESVIDTLREKIESLeAQLSDEKMRWLGIKS 812
Cdd:PRK02224 583 ELKERIESLERI-RTLLAAIADAEDEIERLREKREAL-AELNDERRERLAEKR 633
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
608-801 |
8.27e-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: 58.62 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 608 SDALQTAEERVAQLEAALSEAQGEAD---TKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTE 684
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 685 LTMAKAE----LDGAYGTRAQRAADIAANPE-----------VKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAE 749
Cdd:COG4942 99 LEAQKEElaelLRALYRLGRQPPLALLLSPEdfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 407920239 750 REKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLS 801
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
610-806 |
1.44e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 610 ALQTAEERVAQLEAALSEAQGEadtkIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAK 689
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 690 AELDGAYGTRAQRAADIAA------------------------------------NPEVKRELEELAKVNAELTSEVARL 733
Cdd:COG4942 90 KEIAELRAELEAQKEELAEllralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407920239 734 TEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLSDEKMR 806
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
452-873 |
1.61e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 452 AIEQSQQGLLTQLDEARNADTSELTAYWKEQATEYEKVCESLWEMIRTGHEEARQRKlQRRRVLEADPDAVSDLGEMS-- 529
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAee 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 530 ---PDEDPMPEEFTLSRFSTQVQDMYRRASGLKEKQSILRrqiKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSG 606
Cdd:PTZ00121 1365 kaeAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK---KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 607 DSdalQTAEErvAQLEAALSEAQGEADTKIAELNQSLEAAK-ASEAEVARTIEQKEEELAKTDKELRELEgEVVRLQTEL 685
Cdd:PTZ00121 1442 EA---KKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAA-EAKKKADEA 1515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 686 TMA--KAELDGAYGTRAQRAADIAANPEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLR--EELR-- 759
Cdd:PTZ00121 1516 KKAeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARie 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 760 DTISEFEEMTKVNVE----SEKEREGLESV--IDTLREKIESLEAQLSDEKMRWLGIKSpaaiptpgpngtpgmvlaETT 833
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEeakkAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKK------------------AEE 1657
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 407920239 834 STKVLREEFRKMMRETRAEAIKALRAEQDERKRLEQILRQ 873
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
569-800 |
6.13e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 569 IKQQRELNeKSDAEKEEEFmrLRSEIDRLRHQLhansgdsdalQTAEERVAQLEA-----ALSEAQGEADTKIAELNQSL 643
Cdd:COG3206 162 LEQNLELR-REEARKALEF--LEEQLPELRKEL----------EEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 644 EAAKASEAEVARTIEQKEEELAKTDKELRELEG--EVVRLQTELTMAKAELDGAygtrAQRAADiaANPEVKRELEELAK 721
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAEL----SARYTP--NHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407920239 722 VNAELTSEVARLTEAHAAAarsakdvAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQL 800
Cdd:COG3206 303 LRAQLQQEAQRILASLEAE-------LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-802 |
7.62e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 567 RQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAA 646
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 647 KASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAygtRAQRAADIAANPEVKRELEELAKVNAEL 726
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL---NAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407920239 727 TSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLSD 802
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
615-802 |
1.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 615 EERVAQLEAALSEAQGEADTKIAELNQSLEAAkasEAEVARTIEQK-----EEELAKTDKELRELEGEVVRLQTELTMAK 689
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA---EAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 690 AELD---GAYGTRAQRAADIAANPEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRdtisefe 766
Cdd:COG3206 240 ARLAalrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ------- 312
|
170 180 190
....*....|....*....|....*....|....*.
gi 407920239 767 emtKVNVESEKEREGLESVIDTLREKIESLEAQLSD 802
Cdd:COG3206 313 ---RILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
609-764 |
5.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 609 DALQTAEERVAQLEAALSEAQ---GEADTKIAELNQSLEAAKASE---------AEVARTIEQKEEELA---KTDKELRE 673
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELErldASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 674 LEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAanpEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKM 753
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELE---QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170
....*....|.
gi 407920239 754 LREELRDTISE 764
Cdd:COG4913 767 LRENLEERIDA 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
634-887 |
7.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 634 TKIAELNQSLEAAKASEAEvartIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELD--GAYGTRAQRAADIAANPE 711
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 712 VKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREK-MLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLR 790
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 791 EKIESLEAQLSDEKMRW---------------LGIKSPAAIPTPGPNGTPGMVLAETTSTKVLREEFRKMMRETRAEAIK 855
Cdd:COG4717 227 EELEQLENELEAAALEErlkearlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270
....*....|....*....|....*....|..
gi 407920239 856 ALRAEQDERKRLEQILRQLKREQLPPPKSPKS 887
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-878 |
7.82e-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: 53.14 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 630 GEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELtmakaeldgaygtraqraadiaan 709
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL------------------------ 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 710 PEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTL 789
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 790 REKIESLEAQLSDEKMRwlgikspAAIPTPGPNGTPGMVLAETTSTKVLREEFRKM-------------MRETRAEAIKA 856
Cdd:TIGR02168 802 REALDELRAELTLLNEE-------AANLRERLESLERRIAATERRLEDLEEQIEELsedieslaaeieeLEELIEELESE 874
|
250 260
....*....|....*....|..
gi 407920239 857 LRAEQDERKRLEQILRQLKREQ 878
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSEL 896
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
562-764 |
8.95e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 562 QSILRRQIKQQRELNEKSDAEKEE----EFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIA 637
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPElnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 638 ELN--------QSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAAdiaan 709
Cdd:COG4717 124 LLQllplyqelEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA----- 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 407920239 710 pevkRELEELAKVNAELTSEVARLTEAHAAAARSAKDVaeREKMLREELRDTISE 764
Cdd:COG4717 199 ----EELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKE 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
630-802 |
9.88e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 630 GEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAygtraqraadiaan 709
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-------------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 710 PEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLRE------ELRDTISEFEEMTKVNVESEKEREGLE 783
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170
....*....|....*....
gi 407920239 784 SVIDTLREKIESLEAQLSD 802
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKE 332
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
611-794 |
1.26e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 611 LQTAEERVAQLEaalseaqgeadTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKA 690
Cdd:COG1579 12 LQELDSELDRLE-----------HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 691 ELDGAYGTRAQRAadiaanpeVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTK 770
Cdd:COG1579 81 QLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|....
gi 407920239 771 vnvESEKEREGLESVIDTLREKIE 794
Cdd:COG1579 153 ---ELEAELEELEAEREELAAKIP 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
465-804 |
1.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 465 DEARNADTSELTAYWKEQATEYEKVCESlwemiRTGHEEARQRKLQRRRVLEADPDAvsDLGEMSPDEDPMPEEFTLSRF 544
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEE-----AKKADEAKKKAEEAKKADEAKKKA--EEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 545 STQVQDMYRRASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEErVAQLEaa 624
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE-AKKAE-- 1590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 625 lsEAQGEADTKIAELNQSLEAAKASEAEVARTIEQ---KEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQ 701
Cdd:PTZ00121 1591 --EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 702 RAADIAANPEVKRELEELAKVNAELT---SEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEF---EEMTKVNVES 775
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAkkeAEEDKKKAEE 1748
|
330 340
....*....|....*....|....*....
gi 407920239 776 EKEREGLESVIDTLREKIESLEAQLSDEK 804
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
558-800 |
1.84e-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: 51.94 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELNEKSDAE---KEEEFMRLRSEIDRLRHQlhaNSGDSDALQTAEERVAQLEAALSEAqgeaDT 634
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQikkLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNL----DN 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 635 KIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKEL-------RELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIA 707
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 708 anpEVKRELEE---------LAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFE--EMTKVNVE-- 774
Cdd:TIGR04523 542 ---DLEDELNKddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEekEKKISSLEke 618
|
250 260
....*....|....*....|....*....
gi 407920239 775 ---SEKEREGLESVIDTLREKIESLEAQL 800
Cdd:TIGR04523 619 lekAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
553-887 |
2.05e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 553 RRASGLKEKQSILRRQIKQQRELNEKSDAE----KEEEfmrLRSEIDRLRHQLHANSgDSDALQTAEERVAQLEAALSEA 628
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADeakkKAEE---AKKKADEAKKAAEAKK-KADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 629 QGEADT--KIAELNQSLEAAKASE---AEVARTIEQKEEELAKTDKELRELE----------GEVVRLQTELTMAKAELD 693
Cdd:PTZ00121 1533 AKKADEakKAEEKKKADELKKAEElkkAEEKKKAEEAKKAEEDKNMALRKAEeakkaeeariEEVMKLYEEEKKMKAEEA 1612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 694 GAYGTRAQRAADIAANPEVKRELEELAKVNAE---LTSEVARLTEAHAAAARSAKDVAEREKMLREELRDtiSEFEEMTK 770
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKA 1690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 771 VNVESEKEREglesvidtlREKIESLEAQLSDEKMRWLGIKSpaaiptpgpngtpgmvlaETTSTKVLREEFRKMMRETR 850
Cdd:PTZ00121 1691 AEALKKEAEE---------AKKAEELKKKEAEEKKKAEELKK------------------AEEENKIKAEEAKKEAEEDK 1743
|
330 340 350
....*....|....*....|....*....|....*..
gi 407920239 851 AEAiKALRAEQDERKRLEQILRQLKREQLPPPKSPKS 887
Cdd:PTZ00121 1744 KKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
568-868 |
2.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 568 QIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADtkiaELNQSLEAAK 647
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 648 ASEAEVARTIEQKEEELAKTDKELRElEGEVVRLQTELTMAKAELDGAygtRAQRAADIAANPEVKRELEELAKVNAELT 727
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKA---EAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 728 SEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGlesviDTLREKIEslEAQLSDE-KMR 806
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA-----DEAKKKAE--EAKKADEaKKK 1452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407920239 807 WLGIKSPAAIPTPGPNGTPGMVLAETTSTKVLREEFRKMMRETRAEAIKALRAEQDERKRLE 868
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
538-803 |
2.22e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 538 EFTLSRFSTQVQDMYRRASGLKEKQS----ILRRQIKQQRELNE-KSDAEKEEEFMRLRSEIDRLRHQLHANSGDS---- 608
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEErleeLKKKLKELEKRLEElEERHELYEEAKAKKEELERLKKRLTGLTPEKleke 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 609 -DALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVAR-----TIEQKEEELAKTDKELRELEGEVVRLQ 682
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelTEEHRKELLEEYTAELKRIEKELKEIE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 683 TELTMAKAELDGAYGTRAqRAADIAANPEVKREL----EELAKVNAELTSEVARLTEAhaaaarsakdVAEREKMLREEL 758
Cdd:PRK03918 473 EKERKLRKELRELEKVLK-KESELIKLKELAEQLkeleEKLKKYNLEELEKKAEEYEK----------LKEKLIKLKGEI 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 407920239 759 RDTISEFEEMTkvnvESEKEREGLESVIDTLREKIESLEAQLSDE 803
Cdd:PRK03918 542 KSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-882 |
3.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 369 AEVAANIEEKLDYLDQGLRDIEAEQSNLRTQKATsgMDDRLESINNQLFQLVSRAPREGADEFPpppQE----GAENQIN 444
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEE--LELELEEAQAEEYELLAELARLEQDIAR---LEerrrELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 445 YVEDALYAIEQSQQGLLTQLDEARnADTSELTAYWKEQATEYEKVCESLWEMIRTGHEEARQRKLQRRRVLEADPDAVSD 524
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELE-EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 525 LGEMSPDEDpmpEEFTLSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHAN 604
Cdd:COG1196 399 AAQLEELEE---AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 605 SGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTE 684
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 685 LTMAKAELDGAYGTRAQRAADIAANPEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISE 764
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 765 FEEMTKVNVESEKEREGLESVID----TLREKIESLEAQLSDEKMRWLGIKSPAAIptpgpngtpgmvLAETTSTKVLRE 840
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAggslTGGSRRELLAALLEAEAELEELAERLAEE------------ELELEEALLAEE 703
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 407920239 841 EFRKMMRETRAEAIKALRAEQDERKRLEQILRQLKREQLPPP 882
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
541-806 |
4.94e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 541 LSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRELnEKSDAEKEEEFMRLRSEIDRLRHQLhANSGDSDaLQTAEERVAQ 620
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL-KKKLAELEKKLDELEEELAELLKEL-EELGFES-VEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 621 LEAALSEAQGEADTKiaelnQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTmakaeldgaygtra 700
Cdd:PRK03918 597 LEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-------------- 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 701 qraadiaanpevKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELrdtisefEEMTKVNVESEKERE 780
Cdd:PRK03918 658 ------------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-------EEREKAKKELEKLEK 718
|
250 260
....*....|....*....|....*.
gi 407920239 781 GLESVIDtLREKIESLEAQLSDEKMR 806
Cdd:PRK03918 719 ALERVEE-LREKVKKYKALLKERALS 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
547-719 |
9.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 547 QVQDMYRRASGLKEKQSILRRQIKQQRELNEKSDAEKEeeFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALS 626
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 627 EAQ---GEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKEL----------RELEGEVVR-LQTELTMAKAEL 692
Cdd:COG4913 703 ELEeelDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaaalgDAVERELREnLEERIDALRARL 782
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 407920239 693 DGAYG--TRAQRA-------------ADIAANPEVKRELEEL 719
Cdd:COG4913 783 NRAEEelERAMRAfnrewpaetadldADLESLPEYLALLDRL 824
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
547-760 |
1.18e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 547 QVQDMYRRASGLKEKQSILRRQIKQQRELNEKSD--AEKEEEFMRLRSEIDRLRHQLHANSGDS--DALQTAEERVAQLE 622
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIELLEPIRELAEryAAARERLAELEYLRAALRLWFAQRRLELleAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 623 AALSEAQ---GEADTKIAELNQSLEAAKaseaevARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAygtr 699
Cdd:COG4913 309 AELERLEarlDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---- 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407920239 700 aqrAADIAANpevKRELEELAkvnAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRD 760
Cdd:COG4913 379 ---AEEFAAL---RAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
565-708 |
1.34e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 565 LRRQIKQ-QRELNEKSD--AEKEEEFMRLRSEIDRLRHQLHANSGDsdaLQTAEERVAQLEAALSEAQG----EADTK-I 636
Cdd:COG1579 22 LEHRLKElPAELAELEDelAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGNVRNnkeyEALQKeI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407920239 637 AELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAA 708
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
631-804 |
1.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 631 EADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANP 710
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 711 EVKRELEEL--AKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDT 788
Cdd:COG3883 100 GSVSYLDVLlgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170
....*....|....*.
gi 407920239 789 LREKIESLEAQLSDEK 804
Cdd:COG3883 180 QEALLAQLSAEEAAAE 195
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
558-797 |
1.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELNEKSDaEKEEEFMRLRSEIDRLRHQL-HANSGDSDALQTAEERVAQLEAALSEAQGEAD--- 633
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKELtNSESENSEKQRELEEKQNEIEKLKKENQSYKQeik 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 634 ---TKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTE---LTMAKAELDGAYGTRAQRAADIA 707
Cdd:TIGR04523 388 nleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEikdLTNQDSVKELIIKNLDNTRESLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 708 ANPEV--------KRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLR---EELRDTISEFE------EMTK 770
Cdd:TIGR04523 468 TQLKVlsrsinkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKekiEKLESEKKEKEskisdlEDEL 547
|
250 260
....*....|....*....|....*..
gi 407920239 771 VNVESEKEREGLESVIDTLREKIESLE 797
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKNKEIEELK 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
562-735 |
2.15e-05 |
|
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: 47.84 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 562 QSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHAnsgDSDALQTAEERVAQLEAALSEAQGE---ADTKIAE 638
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAALARRIRALEQELAALEAElaeLEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 639 LNQSLEAAKASEAEV------------------------------------------ARTIEQKEEELAKTDKELRELEG 676
Cdd:COG4942 95 LRAELEAQKEELAELlralyrlgrqpplalllspedfldavrrlqylkylaparreqAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 677 EVVRLQTELTMAKAELDGAYGTRAQRAADIAAN-PEVKRELEELAKVNAELTSEVARLTE 735
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKElAELAAELAELQQEAEELEALIARLEA 234
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
568-685 |
3.86e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 568 QIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHA--NSGDSDALQ----TAEERVAQLEAALSEAQGEADTKIAELNQ 641
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQkeieSLKRRISDLEDEILELMERIEELEEELAE 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 407920239 642 SLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTEL 685
Cdd:COG1579 129 LEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-800 |
4.53e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 327 LKSVDKRLEDLNDRLRQLIIQANPDANKEYDAgpkHRADAGGAEVAANIEEKLDYLDQGLRDIEAEQSNLRTQKATSgmD 406
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEEL---EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA--E 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 407 DRLESINNQLFQLVSRAPREGADEfppppqEGAENQINYVEDALYAIEQSQQGLLTQLDE---ARNADTSELTAYWKEQA 483
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQL------EELEEAEEALLERLERLEEELEELEEALAEleeEEEEEEEALEEAAEEEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 484 TEYEKVCESLWEMIRTGHEEARQRKLQRRRVLEADPDAVSDLGEMSPDEDPmpEEFTLSRFSTQVQDMYRRASGLKekqS 563
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY--EGFLEGVKAALLLAGLRGLAGAV---A 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 564 ILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDA----LQTAEERVAQLEAALSEAQGEADTKIAEL 639
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 640 NQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPE-------- 711
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAeleelaer 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 712 VKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLRE 791
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
....*....
gi 407920239 792 KIESLEAQL 800
Cdd:COG1196 768 ELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
553-806 |
5.47e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 553 RRASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRhqlhanSGDSDALQTAEERVAQLEAALSEAQGEA 632
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR------TLVAARLEAALRRAVTLAGRLREVTLEG 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 633 DTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEV 712
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 713 KRELEELAKVNAELTSEVArltEAHAAAARSAKDVAEREKMLREELRD-------TISEFEEMTKVNVESEKEREGLESV 785
Cdd:COG1196 734 REELLEELLEEEELLEEEA---LEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEA 810
|
250 260
....*....|....*....|.
gi 407920239 786 IDTLREKIESLeaqlsDEKMR 806
Cdd:COG1196 811 RETLEEAIEEI-----DRETR 826
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
505-693 |
6.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 505 RQRKLQRRRVLEADpDAVSDL----GEMSPDEDPMPEEFTLSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRelNEKSD 580
Cdd:COG3206 182 EQLPELRKELEEAE-AALEEFrqknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP--DALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 581 AEKEEEFMRLRSEIDRLRHQLHANSG----DSDALQTAEERVAQLEAALseaQGEADTKIAELNQSLEAAKASEAEVART 656
Cdd:COG3206 259 LLQSPVIQQLRAQLAELEAELAELSArytpNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190
....*....|....*....|....*....|....*..
gi 407920239 657 IEQKEEELaktdKELRELEGEVVRLQTELTMAKAELD 693
Cdd:COG3206 336 LAQLEARL----AELPELEAELRRLEREVEVARELYE 368
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
553-814 |
7.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 553 RRASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRlrhqlhansgdSDALQTAEErVAQLEAAlseAQGEA 632
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-----------AEELRKAED-ARKAEAA---RKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 633 DTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRElegEVVRLQTELTMAK-AELDGAYGTRAQRAADIAANPE 711
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN---EEIRKFEEARMAHfARRQAAIKAEEARKADELKKAE 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 712 VKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRdtiSEFEEMTKVNVESEKEREGLESVIDTLRE 791
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
250 260
....*....|....*....|...
gi 407920239 792 KIESLEAQLSDEKMRWLGIKSPA 814
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKA 1387
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
558-807 |
8.12e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQ-QRELNEKSDA--EKEEEFMRLRSEIDRLRHQLHANSGDsdaLQTAEERVAQLEAALSEAQgeadT 634
Cdd:TIGR04523 223 LKKQNNQLKDNIEKkQQEINEKTTEisNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQLNQLK----S 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 635 KIAELNQslEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAanpEVKR 714
Cdd:TIGR04523 296 EISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE---EKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 715 ELEELAKVNAELTSEVARLT--------------------EAHAAAARSAKDVAERE-KMLREELRDTISEFEEMTKVNV 773
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLEsqindleskiqnqeklnqqkDEQIKKLQQEKELLEKEiERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270
....*....|....*....|....*....|....
gi 407920239 774 ESEKEREGLESVIDTLREKIESLEAQLSDEKMRW 807
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
554-800 |
1.29e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.48 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 554 RASGLKEKQSILRRQIKQQRELNEKSDAEK-EEEFMRLRSEIDRLRHQLHANSgdsDALQTAEERVAQLEAalseaqgea 632
Cdd:pfam03528 139 RESAEREIADLRRRLSEGQEEENLEDEMKKaQEDAEKLRSVVMPMEKEIAALK---AKLTEAEDKIKELEA--------- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 633 dTKIAELNQSLEAAKAS----EAEVARTIEQK---EEELAKTDKELRelegEVVRLQTELTMAKAELDGAYgtraQRAAD 705
Cdd:pfam03528 207 -SKMKELNHYLEAEKSCrtdlEMYVAVLNTQKsvlQEDAEKLRKELH----EVCHLLEQERQQHNQLKHTW----QKAND 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 706 IAANPEvKRELEELAKVNAELTSEVARLTEahaaaARSAKDVAEREKMLREELRDTISEFEEMTKV--------NVESEK 777
Cdd:pfam03528 278 QFLESQ-RLLMRDMQRMESVLTSEQLRQVE-----EIKKKDQEEHKRARTHKEKETLKSDREHTVSihavfspaGVETSA 351
|
250 260
....*....|....*....|...
gi 407920239 778 EREGLESVIDTLREKIESLEAQL 800
Cdd:pfam03528 352 PLSNVEEQINSAHGSVHSLDTDV 374
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
425-855 |
1.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 425 REGADEFPPPPQEGAENQINYVEDALYAIEQSQQGLLTQLDEARNADtsELTAYWKEQATEYEKVCESLWEMIRTGHEEA 504
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 505 RQRKLQRrrvLEADPDAVSDLGEMSPDEDPMPEEFTLSrfstqvQDMYRRASGLKEKQSILRRqiKQQRELNEKSDAEKE 584
Cdd:PTZ00121 1587 KKAEEAR---IEEVMKLYEEEKKMKAEEAKKAEEAKIK------AEELKKAEEEKKKVEQLKK--KEAEEKKKAEELKKA 1655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 585 EEFMRLRSEidRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADT------KIAELNQSLEAAKASEAEVARTIE 658
Cdd:PTZ00121 1656 EEENKIKAA--EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelkkKEAEEKKKAEELKKAEEENKIKAE 1733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 659 Q---KEEELAKTDKELRELEGEVVRLQTeltMAKAELDGAYGTRAQRAA---------DIAANPEVKRELEELaKVNAEL 726
Cdd:PTZ00121 1734 EakkEAEEDKKKAEEAKKDEEEKKKIAH---LKKEEEKKAEEIRKEKEAvieeeldeeDEKRRMEVDKKIKDI-FDNFAN 1809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 727 TSEVAR-----LTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLS 801
Cdd:PTZ00121 1810 IIEGGKegnlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 407920239 802 DEKMRWLGIKSPAAIPTPGPNGTpgmvlaETTSTKVLREEFRKM-MRETRAEAIK 855
Cdd:PTZ00121 1890 IEKIDKDDIEREIPNNNMAGKNN------DIIDDKLDKDEYIKRdAEETREEIIK 1938
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
322-802 |
1.42e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 322 MSADTLKSVDKRLEDLNDRLRQLIIQANPDANKEYDAGPKHRADAGGAEVAANI------EEKLDYLDQgLRDIEAEQSN 395
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiqeqarNQNSMYMRQ-LSDLESTVSQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 396 LRTQ--KATSGMDDRLESINNQLFqLVSRAPREGADEFPPPPQEGA--ENQINYVEDALY------AIEQSQQGLLTQLD 465
Cdd:pfam15921 329 LRSElrEAKRMYEDKIEELEKQLV-LANSELTEARTERDQFSQESGnlDDQLQKLLADLHkrekelSLEKEQNKRLWDRD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 466 --------------EARNADTSELTAYWKEQATEYEKVCESLWEMIRtGHEEARQRKLQRRRVLEADPDAVSDLGEMSPD 531
Cdd:pfam15921 408 tgnsitidhlrrelDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ-GKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 532 EDPMPE--EFTLSRFSTQVQDMYRRASGLKEKQSILRRQIKQQreLNEKSDAEKEEEFMR-LRSEIDRLRHQLHANSGDS 608
Cdd:pfam15921 487 KKMTLEssERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK--LQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 609 DALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEaakaseaevARTIEQKEEELA--KTDKELRELEGEVvrlqTELT 686
Cdd:pfam15921 565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN---------DRRLELQEFKILkdKKDAKIRELEARV----SDLE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 687 MAKAELDGAYGTRAQRAADIaanpevKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKM----LREELRDTI 762
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDI------KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQ 705
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 407920239 763 SEFEEM--------------TKVNVESEKEREGLESVIDTLREKIESLEAQLSD 802
Cdd:pfam15921 706 SELEQTrntlksmegsdghaMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN 759
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
553-732 |
1.48e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 553 RRASGLKEKQSILRRQIKQQRELnEKSDAEKEEEFMRLRSEIDRlrhqlhansgdsDALQTAEERvAQLEAALSEAQGEA 632
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEI-AIAQANREAEEAELEQEREI------------ETARIAEAE-AELAKKKAEERREA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 633 DTKIAELNQSLEAAKA-SEAEVARTIE----QKEEELAKTDKELRE--LEGEVV-----RLQTELTMAKAELDGAY---- 696
Cdd:COG2268 258 ETARAEAEAAYEIAEAnAEREVQRQLEiaerEREIELQEKEAEREEaeLEADVRkpaeaEKQAAEAEAEAEAEAIRakgl 337
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 407920239 697 ----GTRAQRAADIAANPEVKRELeeLAKVNAELTSEVAR 732
Cdd:COG2268 338 aeaeGKRALAEAWNKLGDAAILLM--LIEKLPEIAEAAAK 375
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
547-735 |
1.55e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 547 QVQDMYRRASGLKEKQSILRRQIKQQRE--------LNEKSDAE-KEEEFMRLRSEIDRLRH--QLHANSGDSDAL---- 611
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAERAReldllrfqLEELEAAAlQPGEEEELEEERRRLSNaeKLREALQEALEAlsgg 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 612 -QTAEERVAQLEAALSEAQgEADTKIAELNQSLEAAKASEAEVARTIEQKEEEL-------------------------- 664
Cdd:COG0497 239 eGGALDLLGQALRALERLA-EYDPSLAELAERLESALIELEEAASELRRYLDSLefdperleeveerlallrrlarkygv 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 665 ---------AKTDKELRELEG---EVVRLQTELTMAKAELDGAYGT----RAQRAADIAAnpEVKRELEELAKVNAELTS 728
Cdd:COG0497 318 tveellayaEELRAELAELENsdeRLEELEAELAEAEAELLEAAEKlsaaRKKAAKKLEK--AVTAELADLGMPNARFEV 395
|
....*..
gi 407920239 729 EVARLTE 735
Cdd:COG0497 396 EVTPLEE 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
553-676 |
1.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 553 RRASGLKEKQSILRRQIKQQRElnEKSDAEKEEEfmRLRSEIDRLRHQLHANSGD-------------------SDALQT 613
Cdd:COG4913 288 RRLELLEAELEELRAELARLEA--ELERLEARLD--ALREELDELEAQIRGNGGDrleqlereierlereleerERRRAR 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 614 AEERVAQL-------EAALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEG 676
Cdd:COG4913 364 LEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
375-735 |
1.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 375 IEEKLDYLDQGLRDIEAEQSNLRTQKATSGMDDRLESINNQLFQLVSRAPRegadefppppQEGAENQINYVEDALYAIE 454
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE----------LEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 455 QSQQGLLTQLDEARNADTSELTAYWKEQATEYEKVCESLWEM------IRTGHEEARQR--KLQRRRVLEADPDAVSDLG 526
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELeeeleeAQEELEELEEEleQLENELEAAALEERLKEAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 527 -------------------------------------------------EMSPDEDPMPEEFTLSRFSTQVQDMYRRASG 557
Cdd:COG4717 250 lllliaaallallglggsllsliltiagvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSI-----LRRQIKQQRELN-EKSDAEKEEEFMRLRSEIDRLRHQLHANSGDS--------DALQTAEERVAQLEA 623
Cdd:COG4717 330 LPPDLSPeelleLLDRIEELQELLrEAEELEEELQLEELEQEIAALLAEAGVEDEEElraaleqaEEYQELKEELEELEE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 624 ALSEAQGE-----ADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELE--GEVVRLQTELTMAKAELdgAY 696
Cdd:COG4717 410 QLEELLGEleellEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAEL--RE 487
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 407920239 697 GTRAQRAADIAAN--PEVKRELEE--LAKVNAELTSEVARLTE 735
Cdd:COG4717 488 LAEEWAALKLALEllEEAREEYREerLPPVLERASEYFSRLTD 530
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
561-770 |
2.70e-04 |
|
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: 44.63 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 561 KQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSgDSDALQTAEERVAQLEAALSEAQGEADTK----- 635
Cdd:pfam05667 257 RSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFT-HTEKLQFTNEAPAATSSPPTKVETEEELQqqree 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 636 -IAELNQSLEAAKASEAEVAR-------TIEQKEEELAKTDKELRELEGEV-VRLQT--ELTMAK---AELDGAYGTRAQ 701
Cdd:pfam05667 336 eLEELQEQLEDLESSIQELEKeikklesSIKQVEEELEELKEQNEELEKQYkVKKKTldLLPDAEeniAKLQALVDASAQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407920239 702 RAADIAANPEVKR-----ELEELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTK 770
Cdd:pfam05667 416 RLVELAGQWEKHRvplieEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
592-764 |
2.99e-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: 43.37 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 592 SEIDRLRHQLhanSGDSDALQTAEERVAQLEAALSEAQGEadtkIAELNQSLEAAKASEAEVARTIEQKEEEL--AKTDK 669
Cdd:COG1579 17 SELDRLEHRL---KELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 670 ELRELEGEVVRLQTELTMAKAELdgaygtraqraadIAANPEVKRELEELAKVNAELTSEVARLTEAHAAAARSAKDVAE 749
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEI-------------LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*...
gi 407920239 750 REKML---REELRDTISE 764
Cdd:COG1579 157 ELEELeaeREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
541-659 |
3.15e-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: 43.37 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 541 LSRFSTQVQDMYRRASGLKEKQSilrrQIKQQRELNeksDAEKEEEFMRLRSEI--DRLRHQLHANSGDSDALQTAEERV 618
Cdd:COG1579 61 IKRLELEIEEVEARIKKYEEQLG----NVRNNKEYE---ALQKEIESLKRRISDleDEILELMERIEELEEELAELEAEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 407920239 619 AQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQ 659
Cdd:COG1579 134 AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
540-695 |
3.18e-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: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 540 TLSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRE---------------------LNEKSDAEKEEEFMRLRSEIDRLR 598
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 599 HQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEV 678
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
170
....*....|....*..
gi 407920239 679 VRLQTELTMAKAELDGA 695
Cdd:COG4942 230 ARLEAEAAAAAERTPAA 246
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
551-730 |
3.93e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 551 MYRRASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEidrlrhQLHANSGDSDALQTAEERVAQLEAALSEAQG 630
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQ------QRQEARREREELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 631 EADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVV--RLQTELTMAKAELDGAYGTRAQRAADIAA 708
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLlkLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
170 180
....*....|....*....|...
gi 407920239 709 NPEVKRELEELA-KVNAELTSEV 730
Cdd:PRK12705 179 QNILAQAMQRIAsETASDLSVSV 201
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
541-684 |
3.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 541 LSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRELNEKSDAEkeEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQ 620
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407920239 621 LEAALSEAQGEADTK----IAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTE 684
Cdd:COG4717 175 LQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
562-725 |
4.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 562 QSILRRQIKQQRELNEK--SDAEKE-------------EEFMRLRSEIDRLRHQLHANsgdsdaLQTAEERVAQLEAALS 626
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRilEEAKKEaeaikkealleakEEIHKLRNEFEKELRERRNE------LQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 627 EAQGEADTKIAELNQSLEAAKASEaevaRTIEQKEEEL-AKTDKELRELEgEVVRLQTE------LTMAKAELdgaygtR 699
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQ----QELEKKEEELeELIEEQLQELE-RISGLTAEeakeilLEKVEEEA------R 168
|
170 180
....*....|....*....|....*.
gi 407920239 700 AQRAADIaanpevkRELEELAKVNAE 725
Cdd:PRK12704 169 HEAAVLI-------KEIEEEAKEEAD 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
567-804 |
5.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 567 RQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLhanSGDSDALQTAEERVAQLEAALSEAQGEADT---KIAELNQSL 643
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEEL---EELNEQLQAAQAELAQAQEELESLQEEAEElqeELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 644 EAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEVKRELEELAKVN 723
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 724 AELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLSDE 803
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
.
gi 407920239 804 K 804
Cdd:COG4372 285 L 285
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
556-873 |
5.92e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 556 SGLKEKQSILRRQ---IKQQRELNEKSDAEKEEEFMRLRSEIdrlrhqlhansgdsdalqtaEERVAQLEAALSEAQGEA 632
Cdd:pfam15921 281 TGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDL--------------------ESTVSQLRSELREAKRMY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 633 DTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIaanPEV 712
Cdd:pfam15921 341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI---DHL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 713 KRELEelakvnaELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTIsefEEMTKVNVESEKEREGLESVIDTLREK 792
Cdd:pfam15921 418 RRELD-------DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL---EKVSSLTAQLESTKEMLRKVVEELTAK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 793 ---IESLEAQLSD------EKMRwlGIKSPAAIPTPgPNGTPGMVLAETTSTKVLREEFRKMMRETraeaiKALRAEQDE 863
Cdd:pfam15921 488 kmtLESSERTVSDltaslqEKER--AIEATNAEITK-LRSRVDLKLQELQHLKNEGDHLRNVQTEC-----EALKLQMAE 559
|
330
....*....|
gi 407920239 864 RKRLEQILRQ 873
Cdd:pfam15921 560 KDKVIEILRQ 569
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
573-804 |
6.25e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 573 RELNEKSDAEKEEEFMRLRSEIdrlrhqlhansgdsdalqtaEERVAQLEAALSEAQGEADTKI-AELNQSLEAAKASEA 651
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKL--------------------SEALDKLRSYLPKLNPLREEKKkVSVKSLEELIKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 652 ---EVARTIEQKEEELAKTDKELRELEGEVVRLQ--TELTMAKAELDGaYGTRAQRAADIAANPEvKRELEELAKVNAEL 726
Cdd:PRK05771 94 eleKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLG-FKYVSVFVGTVPEDKL-EELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 727 TSE------VARLTEahaaaarsAKDVAEREKMLR--EELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEA 798
Cdd:PRK05771 172 ISTdkgyvyVVVVVL--------KELSDEVEEELKklGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
....*.
gi 407920239 799 QLSDEK 804
Cdd:PRK05771 244 KYLEEL 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
584-879 |
6.57e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 584 EEEFMRLRSEIDRLRHqLH-----ANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASeaevartIE 658
Cdd:pfam12128 247 QQEFNTLESAELRLSH-LHfgyksDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAA-------VA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 659 QKEEELAKTDKELRELEGEVVRlqteltmakaeldgaygtraQRAADIAANPEVKRELEELAKVNAELTSEVARLTEAHA 738
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIE--------------------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 739 AAARSAKDVAEREKMLREELRDTIseFEEMTKVNVESEKEREGLESvidTLREKIESLEAQLSDEKMR------WLGIKS 812
Cdd:pfam12128 379 RRRSKIKEQNNRDIAGIKDKLAKI--REARDRQLAVAEDDLQALES---ELREQLEAGKLEFNEEEYRlksrlgELKLRL 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407920239 813 PAAIPTPgpngtpgmvlaETTSTKVLREEFRKMMRETRAEAIKALRAEQDE----RKRLEQILRQLKREQL 879
Cdd:pfam12128 454 NQATATP-----------ELLLQLENFDERIERAREEQEAANAEVERLQSElrqaRKRRDQASEALRQASR 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
278-798 |
6.75e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 278 DDKDAFDERsLYRSPENLDKLVDALKHGKALTsrpdGLGDVDSPMSADTLKSVDKRLEDLNDRLRQLIIQANpDANKEYD 357
Cdd:PRK02224 272 REREELAEE-VRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 358 agpkhradaGGAEVAANIEEKLDYLDQGLRDIEAEQSNLRTQKATSgmDDRLESINNQLfqlvsrapregadefppppqE 437
Cdd:PRK02224 346 ---------SLREDADDLEERAEELREEAAELESELEEAREAVEDR--REEIEELEEEI--------------------E 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 438 GAENQINYVEDALYAIEQSQQGLLTQLDEARNADTSeltaywkeqateyekvceslwemIRTGHEEARQRKLQRRRVLEA 517
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAE-----------------------LEATLRTARERVEEAEALLEA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 518 D--PDAVSDLGEmSPDEDpmpeefTLSRFSTQVQDMYRRASGLKEKQSILRRQIKQQRELNEksdaekeeefmrLRSEID 595
Cdd:PRK02224 452 GkcPECGQPVEG-SPHVE------TIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE------------AEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 596 RLRhqlhansgdsDALQTAEERVAQLEAALSEAQGEADTK---IAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELR 672
Cdd:PRK02224 513 RLE----------ERREDLEELIAERRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 673 ELEGEVVRLQT--ELTMAKAELDGAYGTRAQRAADIAA-NPEVKRELEELAKVNAELTSEV--ARLTEAHAAAARSAKDV 747
Cdd:PRK02224 583 ELKERIESLERirTLLAAIADAEDEIERLREKREALAElNDERRERLAEKRERKRELEAEFdeARIEEAREDKERAEEYL 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 407920239 748 AEREKMLRE--ELRDTISEFEEMtkvnVESE-KEREGLESVIDTLREKIESLEA 798
Cdd:PRK02224 663 EQVEEKLDElrEERDDLQAEIGA----VENElEELEELRERREALENRVEALEA 712
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
621-808 |
6.84e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 621 LEAALSEAQGEADTKIaelnqsleaakasEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTEltmakaeldgaygtra 700
Cdd:COG2433 378 IEEALEELIEKELPEE-------------EPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE---------------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 701 qraadiaaNPEVKRELEELAKVNAELTSEVARLTEAhaaaarsakdvaEREKMLREElrdtisEFEEMTKVNVESEKERE 780
Cdd:COG2433 429 --------VEELEAELEEKDERIERLERELSEARSE------------ERREIRKDR------EISRLDREIERLERELE 482
|
170 180
....*....|....*....|....*...
gi 407920239 781 GLESVIDTLREKIESLEAQLSDEKMRWL 808
Cdd:COG2433 483 EERERIEELKRKLERLKELWKLEHSGEL 510
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
428-878 |
7.63e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 428 ADEFPPPPQEGAENQINYVEDALYAIEQSQQGL--LTQLDEARNADTSeltayWKEQATEYEKVCESLWEMIRTgHEEAR 505
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHayLTQKREAQEEQLK-----KQQLLKQLRARIEELRAQEAV-LEETQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 506 QRKLQRRRVLEADPDAVSdLGEMSPDEDPMPEEFTlSRFSTQVQDMYRRASGLKEKQSI-----LRRQIKQQRELNEKSd 580
Cdd:TIGR00618 284 ERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQ-SKMRSRAKLLMKRAAHVKQQSSIeeqrrLLQTLHSQEIHIRDA- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 581 AEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAE---LNQSLEAAKASE------- 650
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQelqqrya 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 651 -------AEVARTIEQKEEELAKTDKELRELEGEVVRLQTeLTMAKAELDGAYGTRAQRAADI-------AANPEVKREL 716
Cdd:TIGR00618 441 elcaaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEpcplcgsCIHPNPARQD 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 717 EELAKVNA----ELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREK 792
Cdd:TIGR00618 520 IDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 793 IES---LEAQLSDEKMRWLGIKSPAA----IPTPGPNGTPGMVLAETTSTKVLREEFRKMMREtraeaiKALRAEQDERK 865
Cdd:TIGR00618 600 TEKlseAEDMLACEQHALLRKLQPEQdlqdVRLHLQQCSQELALKLTALHALQLTLTQERVRE------HALSIRVLPKE 673
|
490
....*....|...
gi 407920239 866 RLEQILRQLKREQ 878
Cdd:TIGR00618 674 LLASRQLALQKMQ 686
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
570-805 |
7.74e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 570 KQQRELNEKSDAEKEEEF----MRLRSEIDRLRHQLHANsgdsdalqtaEERVAQLE-AALSEAQGEADTKIAELNQSLE 644
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYalehLNVDKEIQQLEEQLEEN----------LALLENLElDEAEEALEEIEERIDQLYDLLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 645 AAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEVKRELEELAKVNA 724
Cdd:pfam06160 281 KEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 725 ELTSEVARLTEAHAAAARSAKDVAEREKMLRE---ELRDTISEFE-EMTKVNVESEKER-----EGLESVIDTLREKIES 795
Cdd:pfam06160 361 ELQEELEEILEQLEEIEEEQEEFKESLQSLRKdelEAREKLDEFKlELREIKRLVEKSNlpglpESYLDYFFDVSDEIED 440
|
250
....*....|
gi 407920239 796 LEAQLSDEKM 805
Cdd:pfam06160 441 LADELNEVPL 450
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
562-676 |
9.16e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 562 QSILRRQIKQQ--------RELNEKSD--AEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTaeervaqLEAALSEAQGE 631
Cdd:PRK09039 41 QFFLSREISGKdsaldrlnSQIAELADllSLERQGNQDLQDSVANLRASLSAAEAERSRLQA-------LLAELAGAGAA 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 407920239 632 ADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEG 676
Cdd:PRK09039 114 AEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEA 158
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
558-806 |
1.12e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELnEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQ-------- 629
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEEL-ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKkqnnqlkd 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 630 ---------GEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKaeldgaygtrA 700
Cdd:TIGR04523 233 niekkqqeiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN----------N 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 701 QRAADIaaNPEVKRELEELAKVNAELTSEVA-------RLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNV 773
Cdd:TIGR04523 303 QKEQDW--NKELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
250 260 270
....*....|....*....|....*....|....*
gi 407920239 774 ESEKEREGLESVIDTLREKIESLE--AQLSDEKMR 806
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEklNQQKDEQIK 415
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
520-683 |
1.54e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 520 DAVSDLGEMSPDEDPMPEEFTLSRFSTQVQDMYRRASglkekqsILRRQIKQQRELNEKSD---AEKEEEFMRLRSEIDR 596
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEIR-------RLEEQVERLEAEVEELEaelEEKDERIERLERELSE 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 597 LRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKA---SEAEVARTIEQ-KEEELAKTDKELR 672
Cdd:COG2433 453 ARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLehsGELVPVKVVEKfTKEAIRRLEEEYG 532
|
170
....*....|.
gi 407920239 673 ELEGEVVRLQT 683
Cdd:COG2433 533 LKEGDVVYLRD 543
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
555-685 |
1.61e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.57 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 555 ASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLhanSGDSDALQTAEERVAQLEAALSEAQGEADT 634
Cdd:pfam06785 60 ALKEKFEKSFLEEKEAKLTELDAEGFKILEETLEELQSEEERLEEEL---SQKEEELRRLTEENQQLQIQLQQISQDFAE 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 407920239 635 KIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTEL 685
Cdd:pfam06785 137 FRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEI 187
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
579-708 |
1.73e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 579 SDAEKEEEFMRLRSEIDRLRHQLHANSGDS-----DALQTAEERVAQLEA-ALSEAQGEADTKIAELNQSLEAAKA-SEA 651
Cdd:NF041483 649 ARAEGENVAVRLRSEAAAEAERLKSEAQESadrvrAEAAAAAERVGTEAAeALAAAQEEAARRRREAEETLGSARAeADQ 728
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 407920239 652 EVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAA 708
Cdd:NF041483 729 ERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVA 785
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
569-878 |
2.08e-03 |
|
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: 42.03 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 569 IKQQRELNEKSDAEKEEefmrlRSEIDRLRHQlhansgdSDALQTAEERVAQLEAALSEAQGEADTKIA--------ELN 640
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE-----KMEQERLRQE-------KEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 641 QSLEAAKASEAEVARTIEQ-KEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEVKRELEEL 719
Cdd:pfam17380 346 RERELERIRQEERKRELERiRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 720 AKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGLesvIDTLREKIesLEAQ 799
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR---AEEQRRKI--LEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407920239 800 LSDEKMRWLGIKSPAAIPTPGpngtpgmvlAETTSTKVLREEFRKMMRETRAEAIkalraEQDERKRLEQILRQLKREQ 878
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKE---------MEERQKAIYEEERRREAEEERRKQQ-----EMEERRRIQEQMRKATEER 565
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
637-754 |
2.17e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 41.76 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 637 AELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEVKREL 716
Cdd:COG5283 10 KPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRL 89
|
90 100 110
....*....|....*....|....*....|....*....
gi 407920239 717 -EELAKVNAELTSEVARLTEAHAAAARSAKDVAEREKML 754
Cdd:COG5283 90 rSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLA 128
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-770 |
2.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 324 ADTLKSVDKRLEDLNDRLRQLIiqanpDANKEYDAGPKHRADAGGAEVAANIEEKLDYLDQGLRDIEAEQSNLRTQKATS 403
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLE-----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 404 GMDDRLESINNQLFQLVSRAPREgadefppppQEGAENQINYVEDALYAIEQSQQGLLTQLDEARNADTSELTAY--WKE 481
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLL---------LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleAAL 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 482 QATEYEKVCESLWEMIRTGhEEARQRKLQRRRVLEADPDAVSDLGEMSPDEDPMPEEFTLSRFSTQVQDMYRRASGLkek 561
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD--- 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 562 qSILRRQIKQQRELNEKSDAEKEEEfmrlrSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKIAELNQ 641
Cdd:COG1196 621 -TLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 642 SLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELDGAYGTRAQRAADIAANPEVKRELEELAK 721
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407920239 722 -------VN----AELTSEVARLTEAhaaaarsakdVAEREKML--REELRDTISEFEEMTK 770
Cdd:COG1196 775 eiealgpVNllaiEEYEELEERYDFL----------SEQREDLEeaRETLEEAIEEIDRETR 826
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
636-803 |
2.25e-03 |
|
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: 41.98 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 636 IAELNQSLEAAKASEAEVARTIE----------------QKEEELA-----------------------KTDKELRELEG 676
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIErldliidekrqqlerlRREREKAeryqallkekreyegyellkekeALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 677 EVVRLQTELTMAKAELDGAYGTRAQRAADIAA-NPEVKRELEE----LAKVNAELTSEVARLTEAHAAAARSAKDVAERE 751
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 407920239 752 KMLREELRDTISEFEEMTKVNVESEKEREGLESVIDTLREKIESLEAQLSDE 803
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
584-693 |
2.51e-03 |
|
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: 39.92 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 584 EEEFMRLRSEIDRLRHQLHA-----NSGDSDALQTAEERVAQLEAALSEAQ---GEADTKIAELNQSLEAAKASEAEVAR 655
Cdd:pfam08614 20 EAENAKLQSEPESVLPSTSSsklskASPQSASIQSLEQLLAQLREELAELYrsrGELAQRLVDLNEELQELEKKLREDER 99
|
90 100 110
....*....|....*....|....*....|....*...
gi 407920239 656 TIEQKEEELAKTDKELRELEGEVVRLQTELTMAKAELD 693
Cdd:pfam08614 100 RLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELV 137
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
608-708 |
2.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 608 SDALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTM 687
Cdd:COG3883 128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|.
gi 407920239 688 AKAELDGAYGTRAQRAADIAA 708
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
558-674 |
2.90e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELNEK-SDAEKEEEfmRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQGEADTKI 636
Cdd:PRK12704 60 LEAKEEIHKLRNEFEKELRERrNELQKLEK--RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 407920239 637 AELNQSLEA--------AKA---------SEAEVARTIEQKEEElAK--TDKELREL 674
Cdd:PRK12704 138 EEQLQELERisgltaeeAKEillekveeeARHEAAVLIKEIEEE-AKeeADKKAKEI 193
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
609-681 |
3.59e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.57 E-value: 3.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407920239 609 DALQTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKAS-----EAEVARTIEQKEEELAK-TDKELRELEGEVVRL 681
Cdd:cd06503 44 KAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEilaeaKEEAERILEQAKAEIEQeKEKALAELRKEVADL 122
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
551-802 |
4.82e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 551 MYRRASGLKEKQSILRRQIKQQRELNEK----SDAEKEEEFMRLRSEIDRLRHQL----HANSGDSDALQTAEERVAQLE 622
Cdd:PLN02939 37 ARRRGFSSQQKKKRGKNIAPKQRSSNSKlqsnTDENGQLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 623 AALSEAQGEADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTMAkaeldgayGTRAQR 702
Cdd:PLN02939 117 TNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSET--------DARIKL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 703 AADIAANPEVKRELeeLAKVNAELTSEVARLTEAHAAAARSAKDVAEREKMLREE---LRDTISEFEEMTKVNVESEKER 779
Cdd:PLN02939 189 AAQEKIHVEILEEQ--LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDiqfLKAELIEVAETEERVFKLEKER 266
|
250 260
....*....|....*....|...
gi 407920239 780 EGLESvidTLREkiesLEAQLSD 802
Cdd:PLN02939 267 SLLDA---SLRE----LESKFIV 282
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
581-733 |
7.47e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 38.04 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 581 AEKEEEFMRLRSEIDRLRHQLHANSGDSDALqTAEERVAQLEAALSEAQGEADTKIAELNQSLEAAKASEAEVA------ 654
Cdd:pfam17098 14 AEKEQEIQELKAQLQDLKQSLQPPSSQLRSL-LLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKFTPDSTTgkrlma 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 655 --RTIEQKEEELAKTdkelrELEGEVVRLQTELtmakaeldgaygtRAQRaadiAANPEVKRELEELAKVNAELTSEVAR 732
Cdd:pfam17098 93 kcRLLQQENEELGRQ-----LSEGRIAKLEIEL-------------ALQK----KVVEELKKSLEELDEFLIELDEELEG 150
|
.
gi 407920239 733 L 733
Cdd:pfam17098 151 L 151
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
611-871 |
8.22e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 611 LQTAEERVAQLEAALSEAQGE---ADTKIAELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELTM 687
Cdd:COG4372 54 LEQAREELEQLEEELEQARSEleqLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 688 AKAELDGAYGTRAQRAADI-AANPEVKRELEELAKV--------NAELTSEVARLTEAHAAAARSAKDVAEREKMLREEL 758
Cdd:COG4372 134 LEAQIAELQSEIAEREEELkELEEQLESLQEELAALeqelqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 759 RDTISEFEEmtKVNVESEKEREGLESVIDTLREKIESLEAQLSDEKMRWLGIKSPAAIPTPGPNGTPGMVLAETTSTKVL 838
Cdd:COG4372 214 RELAEELLE--AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
250 260 270
....*....|....*....|....*....|...
gi 407920239 839 REEFRKMMRETRAEAIKALRAEQDERKRLEQIL 871
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
558-802 |
8.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 558 LKEKQSILRRQIKQQRELNEKSdAEKEEEFMRLRSEIDRLRHQLhanSGDSDALQTAEERVAQLEAALSEAQG---EADT 634
Cdd:pfam01576 196 LKKEEKGRQELEKAKRKLEGES-TDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETAQKNNALKkirELEA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 635 KIAELNQSLEAAKASEaevartieqkeeelAKTDKELRELEGEVVRLQTEL------TMAKAELdgaygtRAQRAADIAa 708
Cdd:pfam01576 272 QISELQEDLESERAAR--------------NKAEKQRRDLGEELEALKTELedtldtTAAQQEL------RSKREQEVT- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 709 npEVKRELEELAKVN----AEL----TSEVARLTEAHAAAARSAKDVAEREKMLREELRDTISEFEEMTKVNVESEKERE 780
Cdd:pfam01576 331 --ELKKALEEETRSHeaqlQEMrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRK 408
|
250 260
....*....|....*....|..
gi 407920239 781 GLESVIDTLREKIESLEAQLSD 802
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAE 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
502-811 |
8.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 502 EEARQRKLQRRRVLEADPDAVSDLGEMSPDEDPMPEEFTLSRfSTQVQDMYRRASGLKEKQSILRRQIKQQRElnEKSDA 581
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-EEELQDLAEELEELQQRLAELEEELEEAQE--ELEEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 582 EKEEEFMRLRSEIDRLRHQLHAN-------------SGDSDALQTAEERVAQLEAA-----------LSEAQGEADTKIA 637
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKASLGKEAE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 638 ELNQSLEAAKASEAEVARTIEQKEEELAKTDKELRELEGEVVRLQTELT-----MAKAELDGAYGTRAQRAADIAANPE- 711
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaeelEEELQLEELEQEIAALLAEAGVEDEe 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 712 -------VKRELEELAKVNAELTSEVARLTEAHAAAARS--AKDVAEREKMLREELRDTISEFEEMTKVNVESEKEREGL 782
Cdd:COG4717 386 elraaleQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
330 340 350
....*....|....*....|....*....|.
gi 407920239 783 ES--VIDTLREKIESLEAQLSDEKMRWLGIK 811
Cdd:COG4717 466 EEdgELAELLQELEELKAELRELAEEWAALK 496
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
555-802 |
8.98e-03 |
|
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: 39.74 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 555 ASGLKEKQSILRRQIKQQRELNEKSDAEKEEEFMRLRSEIDRLRHQLHANSGDSDALQTAEERVAQLEAALSEAQG---- 630
Cdd:pfam09731 175 ISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElvas 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 631 -------EADTKIAELNQSL-EAAKASEAEVARTIEQKEEELAKTDKELRELEGEV-VRLQTELTMAKAELDGAygtraq 701
Cdd:pfam09731 255 erivfqqELVSIFPDIIPVLkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREeKHIERALEKQKEELDKL------ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407920239 702 rAADIAANPEVKRELEElAKVNAELTSEVARLTEAHAAA--ARSAKDVAEREKMLREELRDTISEFEEMTKVNVES--EK 777
Cdd:pfam09731 329 -AEELSARLEEVRAADE-AQLRLEFEREREEIRESYEEKlrTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkvEE 406
|
250 260
....*....|....*....|....*
gi 407920239 778 EREGLESVIDTLREKIESLEAQLSD 802
Cdd:pfam09731 407 ERAGRLLKLNELLANLKGLEKATSS 431
|
|
| |
