|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
468-668 |
9.72e-77 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 244.52 E-value: 9.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 468 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPAC- 546
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 547 ------------------LKPALTPVDLVEPQEAlasCESDEAKMRRQAgvaaaaslvsvdgevdaggEGGTRALRREVG 608
Cdd:pfam06818 81 eaellrekvgkleeevsgLREALSDVSPSGYESV---YESDEAKEQRQE-------------------EADLGSLRREVE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 609 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 668
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-643 |
1.80e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGKLQQVArRAQRAQQGLQLQVLRLQQ 428
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 429 DKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 509 EGRA---SLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpaltpvDLVEPQEALASCESDEAKMRRQAGVAAAASL 585
Cdd:COG1196 397 ELAAqleELEEAEEALLERLERLEEELEELEEALAEL------------EEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128117 586 VSVDGEVDAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVI 643
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-673 |
8.54e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEVAALR-RSLEQSEAAVAQVLEERQKAWERELAELRQgCSGKLQQVARRAQRAQQglqlqvlrlqqDK 430
Cdd:COG1196 216 RELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELEL-----------EL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 431 KQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 510
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 511 RASLREKEEQLLSLRDSFGSKQAslelsegelppaclkpaltpvDLVEPQEALASCESDEAKMRRQAGVAAAASLvsvdg 590
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAE---------------------ELLEALRAAAELAAQLEELEEAEEALLERLE----- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 591 evdaggeggtrALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 670
Cdd:COG1196 418 -----------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
...
gi 1940128117 671 GAA 673
Cdd:COG1196 487 AEA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-644 |
1.19e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEERLWEKEQEVAALRRSLEQSEAA---VAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAqqglqlqvlr 425
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEAlleAEAELAEAEEELEELAEELLE----ALRAAAELAAQL---------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 426 lqqdkKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRS 505
Cdd:COG1196 403 -----EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 506 QLREGRASLREKEEQLLSLrdsfgskQASLELSEGELPPAclKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAASL 585
Cdd:COG1196 478 ALAELLEELAEAAARLLLL-------LEAEADYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940128117 586 VSVDGEVDAGGEGGTRALRRE------------VGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 644
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-671 |
2.10e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQ 427
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 428 QdKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:TIGR02168 762 E-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 508 REGRASLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpALTPVDLVEPQEALASCESDEAKMRRQagvaaaasLVS 587
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEE--------LRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 588 VDGEVDAgGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEkekVIEYQKQLQLSYVEMYQRNQQLERRL 667
Cdd:TIGR02168 906 LESKRSE-LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEARRRLKRLENKI 981
|
....
gi 1940128117 668 RERG 671
Cdd:TIGR02168 982 KELG 985
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-640 |
3.22e-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: 60.46 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVaQVLEERQKAWERELAELRQgcsgKLQQVARraqraqqglqlqvlrlq 427
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRE----RLANLER----------------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 428 qDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:TIGR02168 317 -QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 508 REGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPACLKpaLTPVDLVEPQEALASCESDEAKMRRQagvaaaasLVS 587
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEA--------LEE 465
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1940128117 588 VDGEVDAgGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKE 640
Cdd:TIGR02168 466 LREELEE-AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-528 |
2.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 406
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 407 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEEtkWEVCQKAGEISLLKQQL 486
Cdd:COG4913 689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1940128117 487 KdsQADVSQKLSEIV-GLRSQLREGRASLREKEEQLLSLRDSF 528
Cdd:COG4913 756 A--AALGDAVERELReNLEERIDALRARLNRAEEELERAMRAF 796
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-524 |
7.90e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRaqqglqlqvlrlqqDK 430
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLEL----EIEEVEARIKK--------------YE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 431 KQL-----QEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRS 505
Cdd:COG1579 80 EQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|
gi 1940128117 506 QLREGRASLREK-EEQLLSL 524
Cdd:COG1579 160 ELEAEREELAAKiPPELLAL 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-673 |
2.21e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWE--RELAELRQgcsgKLQQVARRAQRAQQGLQLQvlrlqqd 429
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPlyQELEALEA----ELAELPERLEELEERLEEL------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 430 kKQLQEEAAQLIRQREELEDKVA-ACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:COG4717 159 -RELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 509 EGRASLREKEEQ----LLSLRDSFGSKQASLELSEGELPP---------ACLKPALTPVDLVEPQEALASCESDEAKMRR 575
Cdd:COG4717 238 AAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 576 QAGVAAAASLVSVDGEVDAGG-------EGGTRALRREVGRLQAELAAERRARERQ------GASFAEERRVWLEEKEKV 642
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEEllelldrIEELQELLREAEELEEELQLEELEQEIAallaeaGVEDEEELRAALEQAEEY 397
|
330 340 350
....*....|....*....|....*....|.
gi 1940128117 643 IEYQKQLQlsyvemyQRNQQLERRLRERGAA 673
Cdd:COG4717 398 QELKEELE-------ELEEQLEELLGELEEL 421
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
372-523 |
4.07e-07 |
|
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: 53.11 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 372 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAAQLIRQREELEDKV 451
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 452 AAcqKEQA-DFLPRMEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464
|
170
....*....|....*...
gi 1940128117 509 EGRASLREKEE---QLLS 523
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
351-540 |
4.64e-07 |
|
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: 53.53 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLqlqvlrlqqdk 430
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRA----ELEEVDKEFAETRDEL----------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 431 KQLQEEAAQLIRQREEL---------------------EDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDS 489
Cdd:TIGR02169 388 KDYREKLEKLKREINELkreldrlqeelqrlseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1940128117 490 QADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRD-SFGSKQASLELSEG 540
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErVRGGRAVEEVLKAS 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-668 |
1.08e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 344 PPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRqgcsgklqqvarraqraqqglqlqv 423
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA-SRKIGEIE------------------------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 424 lrlqQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQklSEIVGL 503
Cdd:TIGR02169 723 ----KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 504 RSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAA 583
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 584 ------SLVSVDGEVDAgGEGGTRALRREVGRL--QAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVE 655
Cdd:TIGR02169 877 lrdlesRLGDLKKERDE-LEAQLRELERKIEELeaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
330
....*....|...
gi 1940128117 656 MYQRNQQLERRLR 668
Cdd:TIGR02169 956 VQAELQRVEEEIR 968
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
351-673 |
4.26e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQK-AWERELAELRQGCSGKLQQVArraqraqqglqlqVLRLQQD 429
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAERYQALLKEKREYE-------------GYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 430 KKQLQEEAAQLIRQREELEDKVAACQK-----------------------------EQADFLPRMEETKWEVCQKAGEIS 480
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEeiselekrleeieqlleelnkkikdlgeeEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 481 LLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQ 560
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 561 EAL-------------ASCESDEAKMRRQAGVAAAASLvsvdgevdAGGEGGTRALRREVGRLQAELAAERRARERQGAS 627
Cdd:TIGR02169 392 EKLeklkreinelkreLDRLQEELQRLSEELADLNAAI--------AGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1940128117 628 FAEERRVWLEEKEKVIEYQK---QLQLSYVEMYQRNQQLERRLRERGAA 673
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKelsKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-546 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVL---R 425
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlglP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 426 LQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADflprmeetkwevcqkageislLKQQLKDSQADVSQKLSEIvglrS 505
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAE---------------------AEAALRDLRRELRELEAEI----A 429
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1940128117 506 QLREGRASLrekEEQLLSLRDSFgskQASLELSEGELPPAC 546
Cdd:COG4913 430 SLERRKSNI---PARLLALRDAL---AEALGLDEAELPFVG 464
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
347-699 |
1.24e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 347 PSALIqeLEERLWEKEQEVAALrrsLEQSEAAVAQVLEERQK------AWERELAELRQGCsGKLQQVARRAQRAQQGLQ 420
Cdd:pfam07888 27 PRAEL--LQNRLEECLQERAEL---LQAQEAANRQREKEKERykrdreQWERQRRELESRV-AELKEELRQSREKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 421 LQVLRLQQDKKQLQEEAAQLIRQRE-------ELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADV 493
Cdd:pfam07888 101 EKYKELSASSEELSEEKDALLAQRAahearirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 494 SQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQasLELSEGELPPACLKPALTpvDLVEPQEALASCESDEAKM 573
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEALLE--ELRSLQERLNASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 574 RRQAGVAAA-------------------------ASLVSVDGEVDAGGEGGT------------RALRREVGRLQAELAA 616
Cdd:pfam07888 257 GEELSSMAAqrdrtqaelhqarlqaaqltlqladASLALREGRARWAQERETlqqsaeadkdriEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 617 ERRARERQGASFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQRNQQLERRLRERGAAGGSSTPTPQ 682
Cdd:pfam07888 337 ERMEREKLEVELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTS 416
|
410
....*....|....*..
gi 1940128117 683 HGEEKKAWTPSRLERIE 699
Cdd:pfam07888 417 TERPDSPLSDSEDENPE 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-669 |
1.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEVAALRRSLEQSEAAVAQV--LEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQD 429
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 430 KKQLQEEAAQLIRQREELEDKVAACQKEQADFlpRMEETKWEVCQKAGEIS--LLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAA--ALEERLKEARLLLLIAAalLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 508 --------REGRASLREKEEQLLSLRDSFGSKQASLE--LSEGELPPAcLKPALTPV---DLVEPQEALASCESDEAKMR 574
Cdd:COG4717 286 lallflllAREKASLGKEAEELQALPALEELEEEELEelLAALGLPPD-LSPEELLElldRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 575 RQAGVAAAASLVsvdGEVDAGGEGGTRALRREVGRLQaELAAERRARERQGASFAEERRVWLEE------KEKVIEYQKQ 648
Cdd:COG4717 365 LEELEQEIAALL---AEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEAldeeelEEELEELEEE 440
|
330 340
....*....|....*....|....
gi 1940128117 649 LQL---SYVEMYQRNQQLERRLRE 669
Cdd:COG4717 441 LEEleeELEELREELAELEAELEQ 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-669 |
1.46e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 428
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 429 DKKQLQEEAAQLIRQREELEDKVAAcQKEQADFLPRM-----EETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGL 503
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 504 RSQLREGRASL----REKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQAGV 579
Cdd:COG1196 566 LKAAKAGRATFlpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 580 AAAASL---VSVDGEVDAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEM 656
Cdd:COG1196 646 LREVTLegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1940128117 657 YQRN---------------------------------QQLERRLRE 669
Cdd:COG1196 726 LEEQleaereelleelleeeelleeealeelpeppdlEELERELER 771
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-543 |
1.55e-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: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 339 FAACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQG 418
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALAR----RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 419 LQLQvlrlqqdKKQLQEEAAQLIRQREELEDKVAACQK--------------EQADFLPRMEETKWEVCQKAGEIsllkQ 484
Cdd:COG4942 85 LAEL-------EKEIAELRAELEAQKEELAELLRALYRlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQA----E 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1940128117 485 QLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELP 543
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-512 |
3.05e-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: 46.68 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGcSGKLQQVARRA---QRAQQGLQLQVLRLQ 427
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS-PEDFLDAVRRLqylKYLAPARREQAEELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 428 QDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 1940128117 508 REGRA 512
Cdd:COG4942 237 AAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-672 |
4.18e-05 |
|
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: 46.97 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 368 LRRSLE----QSEAAvaqvleERQKAWERELAELRQGCSGKLQQVARRAQRAQQGlqlqvlrlqqDKKQLQEEAAQLIRQ 443
Cdd:TIGR02168 198 LERQLKslerQAEKA------ERYKELKAELRELELALLVLRLEELREELEELQE----------ELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 444 R-------EELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLRE 516
Cdd:TIGR02168 262 LqeleeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 517 KEEQLLSLRDSFGSKQASLELSEGELPPACLKpaltpvdLVEPQEALASCESDEAKMRRQAGvAAAASLVSVDGEVDAGG 596
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESR-------LEELEEQLETLRSKVAQLELQIA-SLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128117 597 EGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRERGA 672
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
351-653 |
4.78e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWER------ELAELRQGCSGKLQQVARRAQRAqqglqlqvL 424
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEleelneQLQAAQAELAQAQEELESLQEEA--------E 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 425 RLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLkdSQADVSQKLSEIVGLR 504
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 505 SQLREGRASLREKEEQLLSLRDSF-GSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAA 583
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPrELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1940128117 584 SLVSVDGEVDAGGEGGTRA--LRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSY 653
Cdd:COG4372 270 EKDTEEEELEIAALELEALeeAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-679 |
6.06e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQGC------SGKLQQVAR---RAQRAQQGLQL 421
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEAR-LEAAEEEVDSLKSQLADYQQALdvqqtrAIQYQQAVQaleKARALCGLPDL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 422 QVLRLQQDKKQLQEEAAQLIRQREELEDKV-----AACQKEQADFLprmeetkweVCQKAGEISLL------KQQLKD-- 488
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLsvadaARRQFEKAYEL---------VCKIAGEVERSqawqtaRELLRRyr 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 489 SQADVSQKLSeivGLRSQLREGRASLREKEEqLLSLRDSFgSKQASLELSEGELPPACLKPALTPVDlvEPQEALASCES 568
Cdd:COG3096 506 SQQALAQRLQ---QLRAQLAELEQRLRQQQN-AERLLEEF-CQRIGQQLDAAEELEELLAELEAQLE--ELEEQAAEAVE 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 569 DEAKMRRQagvaaaaslvsvdgevdaggEGGTRALRREVGR-----LQAELAAERrARERQGASFAEERRVwLEEKEKVI 643
Cdd:COG3096 579 QRSELRQQ--------------------LEQLRARIKELAArapawLAAQDALER-LREQSGEALADSQEV-TAAMQQLL 636
|
330 340 350
....*....|....*....|....*....|....*.
gi 1940128117 644 EYQKQLQLSYVEMYQRNQQLERRLRERGAAGGSSTP 679
Cdd:COG3096 637 EREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
355-673 |
1.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 355 EERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWE-------RELAELRQGCSGKLQQVARRAQ---------RAQQG 418
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarkaeevRKAEELRKAEDARKAEAARKAEeerkaeearKAEDA 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 419 LQLQVLRLQQDKKQLQEEA--AQLIRQREELEDKVAAcqkEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQK 496
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRKFEEA---RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 497 LSEIVGLRSQLREGRAS--LREKEEQLLSLRDSFgSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMR 574
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKAdeAKKKAEEAKKKADAA-KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 575 RQAGVAAAAslvsvdgEVDAGGEGGTRA--LRREVGRLQAELAAERRARERQGAsfAEERRVWLEEKEKVIEYQKQLQL- 651
Cdd:PTZ00121 1380 ADAAKKKAE-------EKKKADEAKKKAeeDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAk 1450
|
330 340
....*....|....*....|..
gi 1940128117 652 SYVEMYQRNQQLERRLRERGAA 673
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKA 1472
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
429-684 |
1.78e-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: 44.37 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 429 DKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 509 EGRASLREkeeqllSLRDSFGSKQASlelsegelPPACLKPALTPVDLVEPQEALAS-CESDEAKMRRQAgvAAAASLVS 587
Cdd:COG4942 101 AQKEELAE------LLRALYRLGRQP--------PLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELR--ADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 588 VDGEVDAGGEGgTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERRL 667
Cdd:COG4942 165 LRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEA 236
|
250
....*....|....*..
gi 1940128117 668 RERGAAGGSSTPTPQHG 684
Cdd:COG4942 237 AAAAERTPAAGFAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-522 |
2.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 350 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 429
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 430 KKQLQEEAAQLIRQREELEDKVAACQ--KEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170
....*....|....*
gi 1940128117 508 REgrasLREKEEQLL 522
Cdd:PRK03918 341 EE----LKKKLKELE 351
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
432-670 |
2.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 432 QLQEEAAQLIRQREELEDKVAACQK-EQADFlprmEETKWEVCQKagEISLLKQQLKDSQADvSQKLSEivgLRSQLREG 510
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRlAEYSW----DEIDVASAER--EIAELEAELERLDAS-SDDLAA---LEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 511 RASLREKEEQLLSLRDSFGSKQASLELSEGELppACLKPALTPVDLVEPQEALASCEsdeaKMRRQAGVAAAASlvsvdg 590
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEEL--DELQDRLEAAEDLARLELRALLE----ERFAAALGDAVER------ 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 591 EVDAGGEGGTRALRREVGRLQAELaaeRRARERQGASFAEERRVWLEEKEKVIEYQKQL-QLSYVEMYQRNQQLERRLRE 669
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEYLALLdRLEEDGLPEYEERFKELLNE 842
|
.
gi 1940128117 670 R 670
Cdd:COG4913 843 N 843
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
352-524 |
4.37e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERlweKEQEVAALRRSLE-QSEAAVAQVLEERQK---AWERELAELRQGCSGK----------------LQQVARR 411
Cdd:pfam01576 319 QELRSK---REQEVTELKKALEeETRSHEAQLQEMRQKhtqALEELTEQLEQAKRNKanlekakqalesenaeLQAELRT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 412 AQRAQQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQA 491
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1940128117 492 ----DVSQKLS----------EIVGLRSQLREGRASLREKEEQLLSL 524
Cdd:pfam01576 476 llqeETRQKLNlstrlrqledERNSLQEQLEEEEEAKRNVERQLSTL 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
434-669 |
4.64e-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: 43.21 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 434 QEEAAQLIRQREELEDKVAACQKEQAdflprmeetkwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRAS 513
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA--------------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 514 LREKEEQLLSLRDSFGSKQASLelsegelppACLKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAAslvsvdgEVD 593
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEEL---------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-------PAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128117 594 AGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRE 669
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
355-670 |
6.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 355 EERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWE-RELAELRQGCSGKLQQVARRAQRaqqgLQLQVLRLQQDKKQL 433
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEE----DKNMALRKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 434 QEEAAQLIRQREELEDKVAACQKEQADflprMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRAS 513
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAE----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 514 LREKEEQllslrdsfgSKQASLELSEGElppaclkpaltpVDLVEPQEALAScESDEAKmrrqagvaAAASLVSVDGEVD 593
Cdd:PTZ00121 1666 EAKKAEE---------DKKKAEEAKKAE------------EDEKKAAEALKK-EAEEAK--------KAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128117 594 AGGEGGTRAlrREVGRLQAELAAERRARERQGasfAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQ-LERRLRER 670
Cdd:PTZ00121 1716 KKAEELKKA--EEENKIKAEEAKKEAEEDKKK---AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEE 1788
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-641 |
9.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAV--------------------AQVLEERQKAWERELAELRQgcsgKLQQVAR 410
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLeeleeerddllaeaglddadAEAVEARREELEDRDEELRD----RLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 411 RAQRAqqglQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQ 490
Cdd:PRK02224 336 AAQAH----NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 491 ADVSQKLSEIVGLRSQLREGRASLREKEEQLlslrdsfgsKQASLELSEGELpPACLKpaltPVDLVEPQEALASCESDE 570
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERV---------EEAEALLEAGKC-PECGQ----PVEGSPHVETIEEDRERV 477
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940128117 571 AKMRRQAGvAAAASLVSVDGEVDAGGEGGTRALRREVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 641
Cdd:PRK02224 478 EELEAELE-DLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET---IEEKRERAEELRE 544
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
344-447 |
1.32e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 344 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 421
Cdd:PRK11448 137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100
....*....|....*....|....*.
gi 1940128117 422 QVLRLQQDKKQLQEEAAQLIRQREEL 447
Cdd:PRK11448 210 TSQERKQKRKEITDQAAKRLELSEEE 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
362-524 |
1.51e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 362 EQEVAALRRSLEQSEAAVAQ--------VLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQQDKKQL 433
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEfrqknglvDLSEEAKLLLQQLSELES----QLAEARAELAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 434 QE-----EAAQLIRQREELEDKVAACQKEQADFLPRMEETKwevcqkaGEISLLKQQLKDSQADVSQKL-SEIVGLRSQL 507
Cdd:COG3206 257 PEllqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALR-------AQIAALRAQLQQEAQRILASLeAELEALQARE 329
|
170
....*....|....*..
gi 1940128117 508 REGRASLREKEEQLLSL 524
Cdd:COG3206 330 ASLQAQLAQLEARLAEL 346
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-649 |
2.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERElAELRQGCSgKLQQVARRAQRAQQGLQLQVLRLQQDK 430
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-AELEATLR-TARERVEEAEALLEAGKCPECGQPVEG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 431 KQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKwEVCQKAGEISLLKQQLKDSQADVSQKlseivglrsqlreg 510
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAER-------------- 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 511 RASLREKEEQLLSLRDsfgsKQASLElSEGELPPACLKPALTPVDlvEPQEALASCESD--EAKMRRQAGVAAAASLVSV 588
Cdd:PRK02224 529 RETIEEKRERAEELRE----RAAELE-AEAEEKREAAAEAEEEAE--EAREEVAELNSKlaELKERIESLERIRTLLAAI 601
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1940128117 589 DgevDAGGEGGTRALRR----EVGRLQAELAAERRARERQGASFAEERRV--WLEEKEKVIEYQKQL 649
Cdd:PRK02224 602 A---DAEDEIERLREKRealaELNDERRERLAEKRERKRELEAEFDEARIeeAREDKERAEEYLEQV 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-457 |
2.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 346 SPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLR 425
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQD----RLEAAEDLARLELRALLEERFA 756
|
90 100 110
....*....|....*....|....*....|..
gi 1940128117 426 LQQDKKQLQEEAAQLIRQREELEDKVAACQKE 457
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
351-664 |
2.58e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAalrrSLEQSEAAVAQVLEERQkawerelaELRQGcsgKLQQVARRAQRAQQGLQLQVLRLQQDK 430
Cdd:COG5185 231 IEEALKGFQDPESELE----DLAQTSDKLEKLVEQNT--------DLRLE---KLGENAESSKRLNENANNLIKQFENTK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 431 KQLQE-EAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRsQLRE 509
Cdd:COG5185 296 EKIAEyTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 510 GRASLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpaltpvdLVEPQEALASCESDEAKMRRQagVAAAASLVSVD 589
Cdd:COG5185 375 SSEELDSFKDTIESTKESLDEIPQNQRGYAQEI-------------LATLEDTLKAADRQIEELQRQ--IEQATSSNEEV 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1940128117 590 GE-VDAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEE-KEKVIEYQKQLQLSYVEMyqrNQQLE 664
Cdd:COG5185 440 SKlLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQiESRVSTLKATLEKLRAKL---ERQLE 513
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
349-545 |
2.70e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWER-------------------ELAELRQGCSGKLQQVA 409
Cdd:COG5185 322 EAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENivgevelsksseeldsfkdTIESTKESLDEIPQNQR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 410 RRAQRAQQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRM-EETKWEVCQKAGEISL-LKQQLK 487
Cdd:COG5185 402 GYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAdEESQSRLEEAYDEINRsVRSKKE 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128117 488 DSQADVSQKLSEIVGLRSQLREGRASLrekEEQLLSLRDSFGSKQASLELSEGELPPA 545
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKL---ERQLEGVRSKLDQVAESLKDFMRARGYA 536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
351-541 |
2.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLE-----ERQKAWERELAELRQGCSGKLQQVaRRAQRAQQGLQLQVLR 425
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklyEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 426 LQQDKKQLQE--EAAQLIRQREELEDKVAACQKEQADFLPRMEETKwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGL 503
Cdd:PTZ00121 1642 EAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
170 180 190
....*....|....*....|....*....|....*...
gi 1940128117 504 RSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGE 541
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
602-670 |
2.71e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 2.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940128117 602 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 670
Cdd:smart00935 29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-542 |
3.01e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEvaalRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGklqqvaRRAQRAQQGLQLQVLRLQQDKK 431
Cdd:PRK02224 237 DEADEVLEEHEER----REELETLEAEIED-LRETIAETEREREELAEEVRD------LRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 432 QLQEEAAQLirQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGR 511
Cdd:PRK02224 306 DADAEAVEA--RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
170 180 190
....*....|....*....|....*....|.
gi 1940128117 512 ASLREKEEQLLSLRDSFGSKQASLELSEGEL 542
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
352-553 |
4.44e-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: 40.49 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawERELAELRQGCSGKLQQVAR-RAQRAQQGLQLQVLRLQQDK 430
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERlRQQEEERKRKKLELEKEKRD 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 431 KQLQEEAAQLIRQREELEDKVAACQKEQADflpRMEETKWEVCQKAgeISLLKQQLKDSQADVSQK-LSEIVGLRSQLR- 508
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKR---KLLEKEMEERQKA--IYEEERRREAEEERRKQQeMEERRRIQEQMRk 560
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1940128117 509 --EGRASLREKEEQLLSLRDSFGSKQASLELsEGELPPACLKPALTP 553
Cdd:pfam17380 561 atEERSRLEAMEREREMMRQIVESEKARAEY-EATTPITTIKPIYRP 606
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
429-667 |
4.44e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 429 DKKQLQEEAAQLIRQR-EELEDKVAACQKEQADFLprmeetkwevcQKAGEISLlkqqlkDSQADVSqkLSEIVGLRSQL 507
Cdd:COG3206 168 LRREEARKALEFLEEQlPELRKELEEAEAALEEFR-----------QKNGLVDL------SEEAKLL--LQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 508 REGRASLREKEEQLLSLrdsfgskQASLELSEGELPPACLKPALTpvdlvEPQEALASCESDEAKMRRQAGvAAAASLVS 587
Cdd:COG3206 229 AEARAELAEAEARLAAL-------RAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYT-PNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 588 VDGEVDAggegGTRALRREVGRLQAELAAERRARERQGASFAEErrvwLEEKEKVIEYQKQLQLSYVEMyQRNQQLERRL 667
Cdd:COG3206 296 LRAQIAA----LRAQLQQEAQRILASLEAELEALQAREASLQAQ----LAQLEARLAELPELEAELRRL-EREVEVAREL 366
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
352-621 |
4.54e-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: 40.54 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEVAALRRSLEQsEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARraqraqqglqlqvlrLQQDKK 431
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEE-DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK---------------LEKTKN 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 432 QLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQL--KDSQA-DVSQKLSEIVGLRSQLR 508
Cdd:pfam01576 577 RLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAreKETRAlSLARALEEALEAKEELE 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 509 EGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPAClkpALTPVDLVEPQEALASCEsdEAKMRRQAGVAAAASLVSV 588
Cdd:pfam01576 657 RTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV---EEMKTQLEELEDELQATE--DAKLRLEVNMQALKAQFER 731
|
250 260 270
....*....|....*....|....*....|....
gi 1940128117 589 DGEV-DAGGEGGTRALRREVGRLQAELAAERRAR 621
Cdd:pfam01576 732 DLQArDEQGEEKRRQLVKQVRELEAELEDERKQR 765
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
352-536 |
4.77e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 352 QELEERLWEKEQEVAALRRSLEQ----SEAAVAQVLE------------ERQKAWERELAELRQGCSGKLQQVARRAQRA 415
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQklsvAQAAHSQFEQayqlvrkiagevSRSEAWDVARELLRRLREQRHLAEQLQQLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 416 QQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEislLKQQLKDSQADVSQ 495
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA---LRQQLEQLQARIQR 597
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940128117 496 ----------------KLSEIVGL----RSQLREGRASLREKEEQLLSLRDSFGSKQASLE 536
Cdd:PRK04863 598 laarapawlaaqdalaRLREQSGEefedSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-651 |
5.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 349 ALIQELEER---LWEKEQEVAALRRSLEQSEAAVAQVLEERQKA-----------WERELAELRQGCSGKLQQVARRAQR 414
Cdd:PRK03918 391 KELEELEKAkeeIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 415 AQQGLQLQVLRLQQDKKQLQEEaAQLIRQRE------ELEDKVAACQKEQADFLPR-MEETKWEVCQKAGEISLLKQQLK 487
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKE-SELIKLKElaeqlkELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 488 dsqadvsqklsEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQAS----LELSEGELPPA-----CLKPAltPVDLVE 558
Cdd:PRK03918 550 -----------KLEELKKKLAELEKKLDELEEELAELLKELEELGFEsveeLEERLKELEPFyneylELKDA--EKELER 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 559 PQEALASCEsDEAKMRRQAGVAAAASLVSVDGEVDAGG-----------EGGTRALRREVGRLQAELAAERRARErQGAS 627
Cdd:PRK03918 617 EEKELKKLE-EELDKAFEELAETEKRLEELRKELEELEkkyseeeyeelREEYLELSRELAGLRAELEELEKRRE-EIKK 694
|
330 340
....*....|....*....|....
gi 1940128117 628 FAEERRvwlEEKEKVIEYQKQLQL 651
Cdd:PRK03918 695 TLEKLK---EELEEREKAKKELEK 715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
348-513 |
6.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAvaqvLEERQKAWERELAEL-RQGCSGK--------------------LQ 406
Cdd:COG3883 50 NEEYNELQAELEALQAEIDKLQAEIAEAEAE----IEERREELGERARALyRSGGSVSyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 407 QVARRAQRAQQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQL 486
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
170 180
....*....|....*....|....*..
gi 1940128117 487 KDSQADVSQKLSEIVGLRSQLREGRAS 513
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
351-694 |
6.41e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 351 IQELEERLwekeQEVAALRRSLEQSEAAVAQVLE-------------ERQKAWERELAELRQGCSgklQQVARRAQRAqq 417
Cdd:PRK10246 313 IEEVNTRL----QSTMALRARIRHHAAKQSAELQaqqqslntwlaehDRFRQWNNELAGWRAQFS---QQTSDREQLR-- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 418 glqlqvlrlqqdkkQLQEEAAQLIRQREEL--------EDKVAACQKEQADFLPrmeeTKWEVCQKAGEISLLKQQLKDS 489
Cdd:PRK10246 384 --------------QWQQQLTHAEQKLNALpaitltltADEVAAALAQHAEQRP----LRQRLVALHGQIVPQQKRLAQL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 490 QADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQ--ASLELSEGELPP--------ACLKPALtpvdlvep 559
Cdd:PRK10246 446 QVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEAriKDLEAQRAQLQAgqpcplcgSTSHPAV-------- 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 560 qEALASCESDEAKMRRQAgvaaaaslvsVDGEVDAGGEGGTrALRrevGRLQAeLAAERRARERQGASFAEERRV----- 634
Cdd:PRK10246 518 -EAYQALEPGVNQSRLDA----------LEKEVKKLGEEGA-ALR---GQLDA-LTKQLQRDESEAQSLRQEEQAltqqw 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 635 -------------------WLEEKEkviEYQKQL-QLSYVEMYQR------------NQQLE-RRLRERGAAGGSSTPTP 681
Cdd:PRK10246 582 qavcaslnitlqpqddiqpWLDAQE---EHERQLrLLSQRHELQGqiaahnqqiiqyQQQIEqRQQQLLTALAGYALTLP 658
|
410
....*....|...
gi 1940128117 682 QHGEEkKAWTPSR 694
Cdd:PRK10246 659 QEDEE-ASWLATR 670
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
350-458 |
8.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 350 LIQELEE---RLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQgcsgklqqvarRAQRAQqglqlqvlrl 426
Cdd:PRK00409 521 LIASLEElerELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK-----------EAQQAI---------- 579
|
90 100 110
....*....|....*....|....*....|..
gi 1940128117 427 qqdkKQLQEEAAQLIRQREELEDKVAACQKEQ 458
Cdd:PRK00409 580 ----KEAKKEADEIIKELRQLQKGGYASVKAH 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-536 |
8.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 344 PPSPSALIQELEE---RLWEKEQEVAALRRSLEQSEAAVAQVlEERQKAWEReLAELRQGcsgKLQQVARRAQRAQQGLQ 420
Cdd:COG4913 220 EPDTFEAADALVEhfdDLERAHEALEDAREQIELLEPIRELA-ERYAAARER-LAELEYL---RAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128117 421 LQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADflprmeetkwevcQKAGEISLLKQQLKDSQADVSQKLSEI 500
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1940128117 501 VGLRSQLR-------EGRASLREKEEQLLSLRDSFGSKQASLE 536
Cdd:COG4913 362 ARLEALLAalglplpASAEEFAALRAEAAALLEALEEELEALE 404
|
|
| |
