|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-586 |
1.07e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 352 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAE 431
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 432 LLQQVEEvasLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQD 511
Cdd:COG1196 391 ALRAAAE---LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024452938 512 TQRTLARREDELAVCKAELAFKEELVKAMKQAQArnrrNHSPRAGGVQPEPQAPLKDRSWATGRAEVERPGQEWA 586
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEA----DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-551 |
1.20e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 341 WLQRELSQWHA-AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQ 419
Cdd:COG1196 236 ELEAELEELEAeLEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 420 QKAASSRKHIAELLQQ----VEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKL 495
Cdd:COG1196 316 ERLEELEEELAELEEEleelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024452938 496 QQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRNH 551
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-549 |
5.43e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 344 RELSQWHAAAH---AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQ 420
Cdd:COG1196 223 KELEAELLLLKlreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 421 KAASSRKHIAELLQQVEEvasLKAELAQVQRKIGHNlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSS 500
Cdd:COG1196 303 DIARLEERRRELEERLEE---LEEELAELEEELEEL-------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452938 501 QVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
336-548 |
4.37e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 336 RELAVWLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTI 415
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 416 HDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQrkighnlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKL 495
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEE-------------EEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024452938 496 QQLSSQVQYWQQLHQDTQRTLARREDELAVcKAELAFKEELVKAMKQAQARNR 548
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
353-550 |
7.66e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKArEMQNLQQlsRHRQTIHDLQQKAASSRKHIAEL 432
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE-EYAELKE--ELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 433 LQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELK--KQQKAQEQSR----QEAYSFQE-KLQQLSSQVQYW 505
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEkedkALEIKKQEwKLEQLAADLSKY 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024452938 506 QQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRN 550
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-554 |
8.14e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 352 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAE 431
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 432 LLQQVEEvasLKAELAQVQRKIGhnlpllcHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQD 511
Cdd:TIGR02168 773 AEEELAE---AEAEIEELEAQIE-------QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024452938 512 TQRTLARREDELAVCKAELA--------FKEELVKAMKQAQARNRRNHSPR 554
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEeleelieeLESELEALLNERASLEEALALLR 893
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-549 |
2.99e-12 |
|
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: 69.02 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 346 LSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASS 425
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 426 RKHIAELLQQVEEVASLKAELAQVQR-----------KIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAysfQEK 494
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL---EAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024452938 495 LQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
356-545 |
1.13e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQtihDLQQKAASSRKHIAELLQQ 435
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---DLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRT 515
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190
....*....|....*....|....*....|
gi 2024452938 516 LARREDELAVCKAELAFKEELVKAMKQAQA 545
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
346-513 |
1.13e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 346 LSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQ-QQEVLAATKAREMQNL-QQLSRHRQTIHDLQQKAA 423
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElREELEKLEKLLQLLPLyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 424 SSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEER-QQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQV 502
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|.
gi 2024452938 503 QYWQQLHQDTQ 513
Cdd:COG4717 230 EQLENELEAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
360-549 |
7.22e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 360 QKSQEQLQALEEQLRAqkeqnqtLQRSLAQQQEVLAATKArEMQNLQQLSRHRQTIHDL---QQKAASSRKHIAELLQQV 436
Cdd:COG4913 606 FDNRAKLAALEAELAE-------LEEELAEAEERLEALEA-ELDALQERREALQRLAEYswdEIDVASAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 437 EEVASLKAELAQVQRKIGHNlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRT- 515
Cdd:COG4913 678 ERLDASSDDLAALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAl 750
|
170 180 190
....*....|....*....|....*....|....
gi 2024452938 516 LARREDELAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
353-524 |
2.05e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAatkaREMQNLQQLSRHRQ---------------TIHD 417
Cdd:COG4942 65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA----ELLRALYRLGRQPPlalllspedfldavrRLQY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 418 LQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIghnLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQ 497
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAEL---EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*..
gi 2024452938 498 LSSQVQYWQQLHQDTQRTLARREDELA 524
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-546 |
2.63e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.42 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 341 WLQRELSQwhaaahAKQELQKSQEQLQA---------LEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRH 411
Cdd:COG3206 179 FLEEQLPE------LRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 412 RQTIHDLQQKAAssrkhIAELLQQVEEvasLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQ-QKAQEQSRQEAYS 490
Cdd:COG3206 253 PDALPELLQSPV-----IQQLRAQLAE---LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 491 FQEKLQQLSSQVqywQQLHQDTQRtLARREDELAVCKAELAFKEE----LVKAMKQAQAR 546
Cdd:COG3206 325 LQAREASLQAQL---AQLEARLAE-LPELEAELRRLEREVEVARElyesLLQRLEEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-549 |
6.15e-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: 59.69 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 355 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKArEMQNL-QQLSRHRQTIHDLQQKAASSRKHIAELL 433
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-EISRLeQQKQILRERLANLERQLEELEAQLEELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 434 QQV----EEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLH 509
Cdd:TIGR02168 330 SKLdelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452938 510 QDTQRTLARREDE---LAVCKAELAFKE------ELVKAMKQAQARNRR 549
Cdd:TIGR02168 410 ERLEDRRERLQQEieeLLKKLEEAELKElqaeleELEEELEELQEELER 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-545 |
9.65e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 336 RELAVWLQreLSQWHAAAHAKQELQKsqeQLQALEEQLRAQKEQNQTLQRSLAQQQEVLA--ATKAREMQNLQQLsRHRQ 413
Cdd:TIGR02169 221 REYEGYEL--LKEKEALERQKEAIER---QLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQL-RVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 414 TIHDLQQKAASSRKHIAELLQQVEEVA-----------SLKAELAQVQRKIGHNLPLLCHYEEERQQLHREL-KKQQKAQ 481
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEerlakleaeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELeDLRAELE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 482 EQS------RQEAYSFQEKLQQLSSQvqywqqlHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQA 545
Cdd:TIGR02169 375 EVDkefaetRDELKDYREKLEKLKRE-------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
366-549 |
1.31e-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: 57.47 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 366 LQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEvasLKAE 445
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---LEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 446 LAQVQRKIghnlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQ---RTLARREDE 522
Cdd:COG4942 92 IAELRAEL----------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReqaEELRADLAE 161
|
170 180
....*....|....*....|....*..
gi 2024452938 523 LAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERA 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-549 |
1.51e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 335 CRELAVWLQRELSQWHAAAHAKQELQKSQEQLQA-----------LEEQLRAQKEQNQTLQRSLAQQQEVLAatkaremQ 403
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKelyalaneisrLEQQKQILRERLANLERQLEELEAQLE-------E 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 404 NLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKighnlpllchYEEERQQLHRELK--KQQKAQ 481
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE----------LEEQLETLRSKVAqlELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 482 EQSRQEAYSfqEKLQQLSSQVQYWQQ------------LHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:TIGR02168 398 LNNEIERLE--ARLERLEDRRERLQQeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
344-534 |
2.30e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 344 RELSQWHAA---AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLA----ATKAREMQ------NLQQLSR 410
Cdd:PRK03918 443 RELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelAEQLKELEeklkkyNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 411 HRQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIgHNLpllchyEEERQQLHRELKkqqkaqEQSRQEAYS 490
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DEL------EEELAELLKELE------ELGFESVEE 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452938 491 FQEKLQQLSSQVQYWQQLhQDTQRTLARREDELAVCKAEL--AFKE 534
Cdd:PRK03918 590 LEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELdkAFEE 634
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-542 |
2.67e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 355 AKQELQKSQEQLQALeEQLRAQKEQNQTLQRSLAQQQEVLAA----TKAREMQNLQQ-LSRHRQTIHDLQQKAASSRKHI 429
Cdd:COG4913 240 AHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwFAQRRLELLEAeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 430 AELLQQVEE------------VASLKAELAQVQRKIghnlpllchyeEERQQLHRELKKQ-QKAQEQSRQEAYSFQEKLQ 496
Cdd:COG4913 319 DALREELDEleaqirgnggdrLEQLEREIERLEREL-----------EERERRRARLEALlAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452938 497 QLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 542
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-537 |
4.16e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQN-LQQLSRHRQTIHDLQQ 420
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 421 KAASSRKHIAELLQQVE----EVASLKAELAQVQRKIGHNLPLLchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQ 496
Cdd:COG4913 353 ELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEAL---EEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024452938 497 QL-SSQVQYWQQLHQdtqrtlARRE--DELAVCKAELAFKEELV 537
Cdd:COG4913 430 SLeRRKSNIPARLLA------LRDAlaEALGLDEAELPFVGELI 467
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
355-547 |
9.60e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 355 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKaremQNLQQLSRhrqtihDLQQKAASSRKHIAELLQ 434
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE----EELEELNE------QLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 435 QVEEVASLKAELAQVQrkighnlpllchyeEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQR 514
Cdd:COG4372 106 LQEEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190
....*....|....*....|....*....|...
gi 2024452938 515 TLARREDELAVCKAELAFKEELVKAMKQAQARN 547
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
354-536 |
3.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 354 HAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELL 433
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 434 QQVEEVA----SLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKK-QQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQL 508
Cdd:COG4372 122 KERQDLEqqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAlEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180
....*....|....*....|....*...
gi 2024452938 509 HQDTQRTLARREDELAVCKAELAFKEEL 536
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
357-549 |
7.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 357 QELQKsqeQLQALEEQlRAQKEQNQTLQRSLAQQQEVLAATKAREMQnlQQLSRHRQTIHDLQqkaassrkhiAELLQQV 436
Cdd:COG1196 196 GELER---QLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELE--AELEELEAELEELE----------AELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 437 EEVASLKAELAQVQRKIghnlpllchyEEERQQLHR-------------ELKKQQKAQEQSRQEAysfQEKLQQLSSQVQ 503
Cdd:COG1196 260 AELAELEAELEELRLEL----------EELELELEEaqaeeyellaelaRLEQDIARLEERRREL---EERLEELEEELA 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452938 504 YWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-524 |
7.64e-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: 52.76 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 343 QRELSQwhAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQevlAATKAREMQNLQ-QLSRHR-------QT 414
Cdd:TIGR02169 746 LSSLEQ--EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR---IPEIQAELSKLEeEVSRIEarlreieQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 415 IHDLQQKAASSRKHIAELLQQVEEV----ASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYS 490
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
170 180 190
....*....|....*....|....*....|....
gi 2024452938 491 FQEKLQQLSSQVQYWQQLHQDTQRTLARREDELA 524
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
336-521 |
1.01e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 336 RELAVWLQRELSQWHAAAH-AKQELQKSQEQLQALEEQLRAQKEQNQT---LQRSLAQQQEVLAATKARemqnLQQLSRH 411
Cdd:pfam05557 103 REVISCLKNELSELRRQIQrAELELQSTNSELEELQERLDLLKAKASEaeqLRQNLEKQQSSLAEAEQR----IKELEFE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 412 RQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLlchyEEERQQLHRELKKQQKAQEqsrqEAYSF 491
Cdd:pfam05557 179 IQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLL----KEEVEDLKRKLEREEKYRE----EAATL 250
|
170 180 190
....*....|....*....|....*....|
gi 2024452938 492 QEKLQQLSSQVQYWQQLHQDTQRTLARRED 521
Cdd:pfam05557 251 ELEKEKLEQELQSWVKLAQDTGLNLRSPED 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
364-546 |
1.38e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 364 EQLQALEEQLRAQKEQNQTLQRSLAQQQEvlaatKAREMQNLQQLsrhrqtIHDLQQKAASSRKHIaELLQQVEEVASLK 443
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAE------LEELREELEKLEKLL-QLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 444 AELAQVQRKighnlplLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLS----SQVQYWQQLHQDTQRTLARR 519
Cdd:COG4717 139 AELAELPER-------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAEL 211
|
170 180
....*....|....*....|....*..
gi 2024452938 520 EDELAVCKAELAFKEELVKAMKQAQAR 546
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-459 |
2.37e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 357 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSR----HRQTIHDLQQKAASSRKHIAEL 432
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKelaeLAAELAELQQEAEELEALIARL 232
|
90 100
....*....|....*....|....*..
gi 2024452938 433 LQQVEEVASLKAELAQVQRKIGHNLPL 459
Cdd:COG4942 233 EAEAAAAAERTPAAGFAALKGKLPWPV 259
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
350-488 |
2.71e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 350 HAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQT--IHDLQQKAASSRK 427
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024452938 428 HIAEL----LQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEA 488
Cdd:COG1579 104 RISDLedeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
356-549 |
3.40e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQ----------TLQRSLA-----QQQEVLaaTKAREMQNLQQLSRHRQTIHDLqQ 420
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAelnkaggsidKLRKEIErlewrQQTEVL--SPEEEKELVEKIKELEKELEKA-K 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 421 KAASSRKHIAELLQQVEEvasLKAELAQVQRKIGhnlpllcHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSS 500
Cdd:COG1340 154 KALEKNEKLKELRAELKE---LRKEAEEIHKKIK-------ELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452938 501 QVQYWQQLHQDTQRTLARREDELavcKAELAFKEELVKAMKQAQARNRR 549
Cdd:COG1340 224 KADELHEEIIELQKELRELRKEL---KKLRKKQRALKREKEKEELEEKA 269
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
353-496 |
4.88e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQL----QALEEQLRAQKEQNQTLQrSLAQQQEVLAATKAREMQNLQQlsRHRQTIHDLQQKAAssrkh 428
Cdd:PRK00409 505 EEAKKLIGEDKEKLneliASLEELERELEQKAEEAE-ALLKEAEKLKEELEEKKEKLQE--EEDKLLEEAEKEAQ----- 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024452938 429 iaellqqvEEVASLKAELAQVQRKIGHnLPLLCHYEEERQQL---HRELKKQQKAQEQSRQEAYSFQEKLQ 496
Cdd:PRK00409 577 --------QAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELieaRKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-498 |
5.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKE-------------QNQTLQRSLAQQQEVLAATKARemqnLQQL 408
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllplyqELEALEAELAELPERLEELEER----LEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 409 SRHRQTIHDLQQKAASSRKHIAELLQQV-----EEVASLKAELAQVQRKIGhnlpllcHYEEERQQLHRELK--KQQKAQ 481
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLA-------ELEEELEEAQEELEelEEELEQ 231
|
170
....*....|....*..
gi 2024452938 482 EQSRQEAYSFQEKLQQL 498
Cdd:COG4717 232 LENELEAAALEERLKEA 248
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
356-584 |
1.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKhiAELLQQ 435
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--ADEAKK 1490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQlhRELKKQQ---------KAQEQSRQEAYSFQEKLQQLSSQVQYWQ 506
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEeakkadeakKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 507 QLHQDTQRTLARREDELAVcKAELAFKEELV------KAMKQAQARNRRNHSPRAGGVQPEPQAPLKDRSWATGRAEVER 580
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAK-KAEEARIEEVMklyeeeKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
....
gi 2024452938 581 PGQE 584
Cdd:PTZ00121 1648 KAEE 1651
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
356-500 |
1.71e-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: 48.09 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLaATKAREMQNL-QQLSRHRQTIHDLQQKAASSRKHIAEL-- 432
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK-ELLEKEIERLkETIIKNNSEIKDLTNQDSVKELIIKNLdn 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 433 -----LQQVE----EVASLKAELAQVQRKIghnlpllchyeEERQQLHRELKKQQKAQEQS----RQEAYSFQEKLQQLS 499
Cdd:TIGR04523 462 treslETQLKvlsrSINKIKQNLEQKQKEL-----------KSKEKELKKLNEEKKELEEKvkdlTKKISSLKEKIEKLE 530
|
.
gi 2024452938 500 S 500
Cdd:TIGR04523 531 S 531
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
356-542 |
2.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDL-QQKAASSRKHIAELLQ 434
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 435 QVEE-VASLKAELAQVQRKIGH------NLPL-LCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQ 506
Cdd:TIGR04523 318 NQEKkLEEIQNQISQNNKIISQlneqisQLKKeLTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024452938 507 QLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 542
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
342-524 |
2.78e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQ-WHAAAHAKQELQKSQEQLQALE-----EQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTI 415
Cdd:PRK10246 255 LQQEASRrQQALQQALAAEEKAQPQLAALSlaqpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 416 HDLQQKAASSRKHIAELLQQVE-------EVASLKAELAQVQRKIGHNLPLLCHYEEERQQLH--------------REL 474
Cdd:PRK10246 335 AKQSAELQAQQQSLNTWLAEHDrfrqwnnELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNalpaitltltadevAAA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024452938 475 KKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRTLARREDELA 524
Cdd:PRK10246 415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
353-535 |
3.05e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAel 432
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA-- 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 433 LQQVEEVAslKAELAQVQRkighnlpLLCHYEEERQQLHRELKKQQKAQ---EQSRQEaysfqEKLQQLSSQVQYWQQLH 509
Cdd:PTZ00121 1580 LRKAEEAK--KAEEARIEE-------VMKLYEEEKKMKAEEAKKAEEAKikaEELKKA-----EEEKKKVEQLKKKEAEE 1645
|
170 180
....*....|....*....|....*.
gi 2024452938 510 QDTQRTLARREDELAVCKAELAFKEE 535
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
357-450 |
3.18e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 357 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKArEMQNLQQL--------SRHRQTIHDLQQKAASSRKH 428
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEA-ERSRLQALlaelagagAAAEGRAGELAQELDSEKQV 131
|
90 100
....*....|....*....|....*.
gi 2024452938 429 IAELLQQVE----EVASLKAELAQVQ 450
Cdd:PRK09039 132 SARALAQVEllnqQIAALRRQLAALE 157
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
342-438 |
3.23e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQwhAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQ--QQEVLAATKA-----REMQNLQQLSRHRQT 414
Cdd:PRK00409 528 LERELEQ--KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeaQQAIKEAKKEadeiiKELRQLQKGGYASVK 605
|
90 100
....*....|....*....|....
gi 2024452938 415 IHDLQQKaassRKHIAELLQQVEE 438
Cdd:PRK00409 606 AHELIEA----RKRLNKANEKKEK 625
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
358-444 |
3.24e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 358 ELQKSQEQLQALEEQLRAQKEQN----QTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELL 433
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRIlaslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
90
....*....|.
gi 2024452938 434 QQVEEVASLKA 444
Cdd:COG3206 372 QRLEEARLAEA 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
358-546 |
3.96e-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: 45.69 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 358 ELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVE 437
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 438 EVASLKaelaqvqrkighnlpllchyeeERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVqywqqlhQDTQRTLA 517
Cdd:COG1579 84 NVRNNK----------------------EYEALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELA 134
|
170 180 190
....*....|....*....|....*....|
gi 2024452938 518 RREDELAVCKAEL-AFKEELVKAMKQAQAR 546
Cdd:COG1579 135 ELEAELEEKKAELdEELAELEAELEELEAE 164
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
336-554 |
4.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 336 RELAVWLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREmQNLQQLSRHRQTI 415
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 416 HDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHY---------EEERQQLHRELKKQQKAQEQSRQ 486
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdeeelEEELEELEEELEELEEELEELRE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 487 EAYSFQEKLQQLSSQVQYWQQLHQ--DTQRTLARREDELAVCKAelafkeeLVKAMKQAQARNRRNHSPR 554
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQEleELKAELRELAEEWAALKL-------ALELLEEAREEYREERLPP 516
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
358-546 |
4.56e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.64 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 358 ELQKSQEQLQALEEQLRAQ-KEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQV 436
Cdd:pfam03528 19 EFYRLKQQLEAEFNQKRAKfKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQEAIDEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 437 -----EEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRqeaYSFQEKLQQLSSQVQYWQQLHQD 511
Cdd:pfam03528 99 ksqwqEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRR---LSEGQEEENLEDEMKKAQEDAEK 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2024452938 512 TQRTLARREDELAVCKAELAFKEELVKAMKQAQAR 546
Cdd:pfam03528 176 LRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMK 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-561 |
5.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQrslaQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQ 435
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKaELAQVQRKIghnlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQywqqlhqdTQRT 515
Cdd:PRK03918 282 VKELKELK-EKAEEYIKL----------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE--------RLEE 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452938 516 LARREDELAVCKAELAFKEELVKAMKQAQARNRRnHSPRAGGVQPE 561
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGLTPE 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-548 |
7.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 333 HACRELAVwLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHR 412
Cdd:COG4913 648 EALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 413 QtihdlQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKighnlpllCHYEEERQQLHRELKKQQKAQEQSRQEAYS-- 490
Cdd:COG4913 727 E-----ELDELQDRLEAAEDLARLELRALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEELERam 793
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024452938 491 ------FQEKLQQLSSQV----QYWQQLHQDTQRTLARREDEL--AVCKAELAFKEELVKAMKQA--QARNR 548
Cdd:COG4913 794 rafnreWPAETADLDADLeslpEYLALLDRLEEDGLPEYEERFkeLLNENSIEFVADLLSKLRRAirEIKER 865
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
341-549 |
7.54e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 341 WLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQtlQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQ 420
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 421 KAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNlpllcHYEEERQQLHRELKKQQKAQeqsRQEAYSFQEKLQQLSS 500
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI-----RDAHEVATSIREISCQQHTL---TQHIHTLQQQKTTLTQ 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452938 501 QVQYWQQLHQDTQRTLARREDELAvckAELAFKEELVKAMKQAQARNRR 549
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTS---AFRDLQGQLAHAKKQQELQQRY 439
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
356-489 |
9.05e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAremqnlqqlsrhrqtihDLQQKAASSRKHIAELLQQ 435
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ-----------------ELEKKEEELEELIEEQLQE 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKAE------LAQVQRKIghnlpllchyEEERQQLHRELKkqQKAQEQSRQEAY 489
Cdd:PRK12704 144 LERISGLTAEeakeilLEKVEEEA----------RHEAAVLIKEIE--EEAKEEADKKAK 191
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
356-515 |
1.05e-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: 45.40 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASsrkhIAELLQQ 435
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEEN----IAKLQAL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKAELAQVQRKigHNLPLLCHYEEERQQL-HRELKKQQKAQE---------QSRQEAYSFQEKLQQLSSQVqyw 505
Cdd:pfam05667 410 VDASAQRLVELAGQWEK--HRVPLIEEYRALKEAKsNKEDESQRKLEEikelrekikEVAEEAKQKEELYKQLVAEY--- 484
|
170
....*....|
gi 2024452938 506 QQLHQDTQRT 515
Cdd:pfam05667 485 ERLPKDVSRS 494
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
365-616 |
1.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 365 QLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEVAS--- 441
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 442 ------------LKAE--------LAQVQRKIGHNLPLLCHYEEERQQL---HRELKKQQKAQEQSRQEAYSFQEKLQQL 498
Cdd:COG3883 97 rsggsvsyldvlLGSEsfsdfldrLSALSKIADADADLLEELKADKAELeakKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 499 SSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRNHSPRAGGVQPEPQAPLKDRSWATGRAEV 578
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024452938 579 ERPGQEWANCRAKTNKGGGGGSVETLHASHTSACSNSS 616
Cdd:COG3883 257 AAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
342-510 |
1.64e-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: 45.34 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQWHAAAHAKQelQKSQEQLQALeeqlraqkeqNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQK 421
Cdd:TIGR00618 716 YDREFNEIENASSSLG--SDLAAREDAL----------NQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 422 AASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCH-YEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSS 500
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
170
....*....|
gi 2024452938 501 QVQYWQQLHQ 510
Cdd:TIGR00618 864 LTQEQAKIIQ 873
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
355-543 |
1.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 355 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLaqQQEVLAATKAREM--QNLQQLSRHRQTIHDLQQKAASSRKHIAEL 432
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQV--KELREEAQELREKrdELNEKVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 433 LQQVEEVASLKAELAQVQRKIGH--------NLPLlchyEEERQ------QLHRELKKQQKAQEQS-------------R 485
Cdd:COG1340 98 RKELAELNKAGGSIDKLRKEIERlewrqqteVLSP----EEEKElvekikELEKELEKAKKALEKNeklkelraelkelR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024452938 486 QEAYSFQEKLQQLSSQVqywQQLHQDTQrTLARREDELavcKAEL-AFKEELVKAMKQA 543
Cdd:COG1340 174 KEAEEIHKKIKELAEEA---QELHEEMI-ELYKEADEL---RKEAdELHKEIVEAQEKA 225
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
357-507 |
2.00e-04 |
|
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: 44.56 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 357 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNL-QQLSRHRQTIhdlqqkaassRKHIAELLQQ 435
Cdd:COG5185 370 VELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAdRQIEELQRQI----------EQATSSNEEV 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024452938 436 VEEVASLKAELAQVQRKIGHNLPLlcHYEEERQQLHRELkkqqkaqeqsRQEAYSFQEKLQQLSSQVQYWQQ 507
Cdd:COG5185 440 SKLLNELISELNKVMREADEESQS--RLEEAYDEINRSV----------RSKKEDLNEELTQIESRVSTLKA 499
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
338-545 |
2.03e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 338 LAVWLQRELSQWHaaahakQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQ----EVLAATKAREMQNLQQLSRHRQ 413
Cdd:pfam05701 213 AALAREQDKLNWE------KELKQAEEELQRLNQQLLSAKDLKSKLETASALLLdlkaELAAYMESKLKEEADGEGNEKK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 414 TIHDLQQKAASSRKHIAELLQQVE----EVASL--------------KAELAQVQRKIGHNLPLLCHYEEERQQLHRELK 475
Cdd:pfam05701 287 TSTSIQAALASAKKELEEVKANIEkakdEVNCLrvaaaslrselekeKAELASLRQREGMASIAVSSLEAELNRTKSEIA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024452938 476 KQQKAQEQSRQEAYSFQEKLQQlssqvqywqqlhqdtqrtlARREDELAVCKAELAfKEELVKA---MKQAQA 545
Cdd:pfam05701 367 LVQAKEKEAREKMVELPKQLQQ-------------------AAQEAEEAKSLAQAA-REELRKAkeeAEQAKA 419
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
352-549 |
2.13e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 352 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAAT--KAREMQNlqqlsrhrqTIHDLQQKAASSRKHI 429
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrKLRETQN---------TLNQLNKQIDELNASI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 430 AEL-LQQVEEVASLKAELAQVQRKIGHN-LPLLCHYEE----ER-------------------QQLHRELKKQQKAQEQS 484
Cdd:PRK11637 113 AKLeQQQAAQERLLAAQLDAAFRQGEHTgLQLILSGEEsqrgERilayfgylnqarqetiaelKQTREELAAQKAELEEK 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024452938 485 RQEAysfQEKLQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELA--------FKEELVKAMKQAQARNRR 549
Cdd:PRK11637 193 QSQQ---KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSelranesrLRDSIARAEREAKARAER 262
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
353-594 |
2.20e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTihdlqQKAASSRKHI--- 429
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA-----KKAEAARKAEevr 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 430 -AELLQQVEEVASLK-AELAQVQRKIGHnlplLCHYEEER--QQLHRELKKQQKAQEQSRQEAYSFQEKLQQL-SSQVQY 504
Cdd:PTZ00121 1189 kAEELRKAEDARKAEaARKAEEERKAEE----ARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFeEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 505 WQQLHQDTQRTLARREDEL----AVCKAELAFKEELVKamKQAQARNRRNHSPRAGGVQPEPQAPLKDRSWATGRAEVER 580
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELkkaeEKKKADEAKKAEEKK--KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
250
....*....|....
gi 2024452938 581 PGQEWANCRAKTNK 594
Cdd:PTZ00121 1343 KAAEAAKAEAEAAA 1356
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
358-542 |
2.51e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 358 ELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATK-----AREMQNLQQ-----LSRHRQTIHDLQQKAASSRK 427
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKqfekiAEELKGKEQeliflLQAREKEIHDLEIQLTAIKT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 428 HIAELLQQVEEvasLKAELAQVQRKighNLPLLCHYE----------EERQQLHRELKKQQ-------KAQEQSRQEAYS 490
Cdd:pfam05483 465 SEEHYLKEVED---LKTELEKEKLK---NIELTAHCDklllenkeltQEASDMTLELKKHQediinckKQEERMLKQIEN 538
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024452938 491 FQEKLQQLSSQVQY----WQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 542
Cdd:pfam05483 539 LEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
351-453 |
2.74e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 351 AAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAAS-SRKHI 429
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElLEEEA 752
|
90 100
....*....|....*....|....
gi 2024452938 430 AELLQQVEEVASLKAELAQVQRKI 453
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREI 776
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
335-546 |
3.01e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 335 CRELAVWLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKaremqnlQQLSRHRQT 414
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR-------ERAEELRER 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 415 IHDLQQKAASSRKHIAELLQQVEE----VASLKAELAQVQ------RKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQS 484
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALAELNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 485 RQEAYSFQEKLQQLSSQV----------------QYWQQLHQDTQRTLARRED---ELAVCKAELAFKEELVKAMKQAQA 545
Cdd:PRK02224 626 RERLAEKRERKRELEAEFdearieearedkeraeEYLEQVEEKLDELREERDDlqaEIGAVENELEELEELRERREALEN 705
|
.
gi 2024452938 546 R 546
Cdd:PRK02224 706 R 706
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
356-546 |
3.11e-04 |
|
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: 43.96 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTlQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKaassrkhIAELLQQ 435
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRELERIRQEE-------IAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKAELAQVQRKIGHNLPLLCHY---EEERQ----QLHRELKKQQKAQEQSRQ-EAYSFQEKLQQLSSQVQYWQQ 507
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVkilEEERQrkiqQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQ 456
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024452938 508 LHQDTQRTLARREDELAVCKAELAfKEELVKAMKQAQAR 546
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELE-KEKRDRKRAEEQRR 494
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
361-530 |
3.47e-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: 44.01 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 361 KSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEvLAATKAREMQNLQ-----QLSRHRQTIHDLQQKAASSrkhIAELLQQ 435
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELEDTLDTTAAQQE-LRSKREQEVTELKkaleeETRSHEAQLQEMRQKHTQA---LEELTEQ 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEEVASLKAELAQVQRKIghnlpllchyEEERQQLHRELKKQQKAQEQSRQeaysfqeKLQQLSSQVQYWQQLHQDTQRT 515
Cdd:pfam01576 365 LEQAKRNKANLEKAKQAL----------ESENAELQAELRTLQQAKQDSEH-------KRKKLEGQLQELQARLSESERQ 427
|
170
....*....|....*
gi 2024452938 516 LARREDELAVCKAEL 530
Cdd:pfam01576 428 RAELAEKLSKLQSEL 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
430-553 |
4.10e-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: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 430 AELLQQVEEVASLKAELAQVQRKIghnlpllchyeeerQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLH 509
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEI--------------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024452938 510 QDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRNHSP 553
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL 122
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
342-548 |
4.82e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQWHAAAHAKQELQK-------SQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQ-------- 406
Cdd:COG3096 408 QQTRAIQYQQAVQALEKARAlcglpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiage 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 407 ------------QLSRHRQTIHDLQQkAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHREL 474
Cdd:COG3096 488 versqawqtareLLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 475 KKQQKAQEQSRQEAYSFQEKLQQLSSQVqywQQLHQ------DTQRTLARREDElavCKAELAFKEELVKAMKQAQARNR 548
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLEQLRARI---KELAArapawlAAQDALERLREQ---SGEALADSQEVTAAMQQLLERER 640
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
341-500 |
5.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 341 WLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQkeqnQTLQRSLAQQQEVLAATKAREmQNLQQL-SRHRQTIHDLQ 419
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ----QRAERLLAEFCKRLGKNLDDE-DELEQLqEELEARLESLS 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 420 QKAASSRKHIAELLQQVEEVASLKAELAQvQRKIGHNL-PLLCHYEEE--------------RQQLHRELKKQQKAQEQS 484
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA-RAPAWLAAqDALARLREQsgeefedsqdvteyMQQLLERERELTVERDEL 650
|
170
....*....|....*.
gi 2024452938 485 RQEAYSFQEKLQQLSS 500
Cdd:PRK04863 651 AARKQALDEEIERLSQ 666
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
352-544 |
5.58e-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: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 352 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAR---EMQNLQQLSRHRQTIHDLQQKAASSRKH 428
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHlreALQQTQQSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 429 IAELLQQVEEVASLKAELAQVQRKIG---HNLPLLCH------YEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLS 499
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINrarKAAPLAAHikavtqIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024452938 500 SQVQYWQQLHQDTQRtLARREDELAVCKAELAFKEELVKAMKQAQ 544
Cdd:TIGR00618 342 EQRRLLQTLHSQEIH-IRDAHEVATSIREISCQQHTLTQHIHTLQ 385
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
356-542 |
9.71e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQL-----RAQKEQNQ--TLQRSLAQQQEVLAATKAREMQNLQQLS----------RHRQTIHDL 418
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLeeaekRAEKAEAEvaALNRRIQLLEEELERTEERLAEALEKLEeaekaadeseRGRKVLENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 419 QQK----------AASSRKHIAE-LLQQVEEVAS----LKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQ 483
Cdd:pfam00261 87 ALKdeekmeileaQLKEAKEIAEeADRKYEEVARklvvVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024452938 484 SRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 542
Cdd:pfam00261 167 ASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
343-549 |
1.35e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 343 QRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREmqnlQQLSRHRQTIHDLQQKA 422
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE----REIARLRAQQEKAQDEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 423 ASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQ---EAYSFQEKLQQLS 499
Cdd:pfam13868 201 AERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFErmlRKQAEDEEIEQEE 280
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024452938 500 SQVQywQQLHQDTQRTLAR--REDELAVCKAELAFKEELVKAMKQAQARNRR 549
Cdd:pfam13868 281 AEKR--RMKRLEHRRELEKqiEEREEQRAAEREEELEEGERLREEEAERRER 330
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
356-509 |
1.45e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKeqnQTLQRSLAQQQEVlaatkAREMQNLQQ--LSRHRQTIHDLQQKAASSRKHIAELL 433
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRK---DALEEELRQLKQL-----EDELEDCDPteLDRAKEKLKKLLQEIMIKVKKLEELE 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024452938 434 QQVEEvasLKAELAQVQRKIghnlpllchyeeerQQLHRELKKQQKAQEQSRQeaYSFQEkLQQLSSQVQYWQQLH 509
Cdd:smart00787 232 EELQE---LESKIEDLTNKK--------------SELNTEIAEAEKKLEQCRG--FTFKE-IEKLKEQLKLLQSLT 287
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
367-530 |
1.52e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 367 QALEEQLRAQKEQnqtlqRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEVASLKAEL 446
Cdd:COG3096 495 QTARELLRRYRSQ-----QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 447 AQVQRKIGHNLPLLCHYEEERQQLHRELKKQ-----------QKAQEQSRQEAYSfqekLQQLSSQVQywQQLHQDTQRT 515
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalERLREQSGEALAD----SQEVTAAMQ--QLLEREREAT 643
|
170
....*....|....*
gi 2024452938 516 LARreDELAVCKAEL 530
Cdd:COG3096 644 VER--DELAARKQAL 656
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
355-446 |
1.79e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 355 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAAtkaremqnlqQLSRHRQTIHDLQQKAASSRKHIAELLQ 434
Cdd:pfam00038 215 AKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL----------QLADYQELISELEAELQETRQEMARQLR 284
|
90
....*....|..
gi 2024452938 435 QVEEVASLKAEL 446
Cdd:pfam00038 285 EYQELLNVKLAL 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
356-451 |
1.96e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSR-----HRQTIhdLQQKAASSRKHIA 430
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGltaeeAKEIL--LEKVEEEARHEAA 172
|
90 100
....*....|....*....|....*...
gi 2024452938 431 ELLQQVEEVASLKAE------LAQ-VQR 451
Cdd:PRK12704 173 VLIKEIEEEAKEEADkkakeiLAQaIQR 200
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
342-440 |
2.02e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.82 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQWhaaahaKQELQKSQEQLQALEEQLRAQK-----EQNQTLQRSLAQQQevlaatkaremQNLQQLSRHRQTih 416
Cdd:COG2825 48 LEKEFKKR------QAELQKLEKELQALQEKLQKEAatlseEERQKKERELQKKQ-----------QELQRKQQEAQQ-- 108
|
90 100
....*....|....*....|....*
gi 2024452938 417 DLQQKAASSRKHIAELLQQ-VEEVA 440
Cdd:COG2825 109 DLQKRQQELLQPILEKIQKaIKEVA 133
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
353-502 |
2.32e-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: 41.28 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQLQALeeqlraQKEQNQTLQRSLAQQQEVLaatKAREMQNLQQLSRHR-QTIHDLQQKAASSRKHIAE 431
Cdd:pfam09731 290 AHAHREIDQLSKKLAEL------KKREEKHIERALEKQKEEL---DKLAEELSARLEEVRaADEAQLRLEFEREREEIRE 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024452938 432 LLQQveevaSLKAELAQvQRKIgHNLPLLCHYEEERQQLHRELkkQQKAQEQSRQEAYSFQEKLQQLSSQV 502
Cdd:pfam09731 361 SYEE-----KLRTELER-QAEA-HEEHLKDVLVEQEIELQREF--LQDIKEKVEEERAGRLLKLNELLANL 422
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
342-422 |
2.46e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQwhaAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQevlaatkaREMQNLqqLSRHRQTIHDLQQK 421
Cdd:pfam13851 73 LRKQLEN---YEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVE--------RERDEL--YDKFEAAIQDVQQK 139
|
.
gi 2024452938 422 A 422
Cdd:pfam13851 140 T 140
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
353-453 |
2.52e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 353 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQ---EVLAATKAREMQnLQQLSRHRQtihdLQQKAASSRKHI 429
Cdd:COG2268 240 AEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREvqrQLEIAEREREIE-LQEKEAERE----EAELEADVRKPA 314
|
90 100 110
....*....|....*....|....*....|..
gi 2024452938 430 AELLQQVEEVASLKAE--------LAQVQRKI 453
Cdd:COG2268 315 EAEKQAAEAEAEAEAEairakglaEAEGKRAL 346
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
342-510 |
2.76e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 342 LQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTL------QRSLAQQQEVL--------AATKARE------ 401
Cdd:COG0497 160 YREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAalqpgeEEELEEERRRLsnaeklreALQEALEalsgge 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 402 ----------MQNLQQLSRHRQTIHDLQQKAASSRKHIAEL-----------------LQQVEE----VASLK------- 443
Cdd:COG0497 240 ggaldllgqaLRALERLAEYDPSLAELAERLESALIELEEAaselrryldslefdperLEEVEErlalLRRLArkygvtv 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024452938 444 AELAQVQRKIGHNLPLLCHYEEERQQLHRELKK-----QQKAQE--QSRQEAysfqekLQQLSSQVQywQQLHQ 510
Cdd:COG0497 320 EELLAYAEELRAELAELENSDERLEELEAELAEaeaelLEAAEKlsAARKKA------AKKLEKAVT--AELAD 385
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
355-550 |
2.99e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 355 AKQELQKSQEQLQALEEQLRAQKEQNQtlQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASsRKHIAELLQ 434
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-EREIARLRA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 435 QVEEVASLKAELAQVQRKighnlplLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEklqqlssqvqywQQLHQDTQR 514
Cdd:pfam13868 192 QQEKAQDEKAERDELRAK-------LYQEEQERKERQKEREEAEKKARQRQELQQAREE------------QIELKERRL 252
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024452938 515 TLARREDELAVCKAELAFKEELVKAMKQAQARNRRN 550
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
330-441 |
3.64e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 330 SCGHACRELAVWLQRELS-QWHAAA-------HAKQELQKSQEQLQALEEQLRAQ---KEQNQTLQRSLAQQQEVLAATK 398
Cdd:PRK11448 107 MGLKLAFRLAVWFHRTYGkDWDFKPgpfvppeDPENLLHALQQEVLTLKQQLELQareKAQSQALAEAQQQELVALEGLA 186
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024452938 399 AREMQNLQQLSRHRQTIhdLQQKAASSRKHIAELLQQVEEVAS 441
Cdd:PRK11448 187 AELEEKQQELEAQLEQL--QEKAAETSQERKQKRKEITDQAAK 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
354-530 |
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 2024452938 354 HAKQELQKSQEQLQALEEQLRAQKEQNQTLQR-----------SLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKA 422
Cdd:PRK04863 848 ELERALADHESQEQQQRSQLEQAKEGLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIV 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 423 ASSR---KHIAELLQQVEEVASLKAELAQ--------VQRKigHNLPllchYEE------ERQQLHRELKKQQKAQEQSR 485
Cdd:PRK04863 928 SVLQsdpEQFEQLKQDYQQAQQTQRDAKQqafaltevVQRR--AHFS----YEDaaemlaKNSDLNEKLRQRLEQAEQER 1001
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024452938 486 QEAysfQEKLQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAEL 530
Cdd:PRK04863 1002 TRA---REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
356-548 |
5.28e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQlraqkeqnqtlqrslaqqqevLAATKAREMQNLQQLSRHRQTIHDLQQKA--ASS-------R 426
Cdd:COG1842 29 DQAIRDMEEDLVEARQA---------------------LAQVIANQKRLERQLEELEAEAEKWEEKArlALEkgredlaR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 427 KHIAELLQQVEEVASLKAELAQVQRKIGhnlpllcHYEEERQQLHREL--KKQQKAQEQSRQEAYSFQEKLQQLSSQVQY 504
Cdd:COG1842 88 EALERKAELEAQAEALEAQLAQLEEQVE-------KLKEALRQLESKLeeLKAKKDTLKARAKAAKAQEKVNEALSGIDS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024452938 505 wqqlhQDTQRTLAR-------REDELAVcKAELAFKEELVKAMKQAQARNR 548
Cdd:COG1842 161 -----DDATSALERmeekieeMEARAEA-AAELAAGDSLDDELAELEADSE 205
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
346-488 |
5.32e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 346 LSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQnqtlQRSLAQQQEVLAATKAREMQNLQqlsrhrqtihdlQQKAASS 425
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQ----ERLKQLEKERLAAQEQKKQAEEA------------AKQAALK 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024452938 426 RKHIAELLQQVEEVASLKAELAQVQrkighnlpllchYEEERQQLHRELKKQQKAQEQSRQEA 488
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKR------------AAAAAKKAAAEAKKKAEAEAAKKAAA 181
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
356-550 |
6.73e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 38.93 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQ 435
Cdd:pfam06008 25 TKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 436 VEE---------VASLKAELAQVQRKIghnlpllchyeeeRQQLHRELKKQQKAQEQSRQEAysfqeklQQLSSQVQYWQ 506
Cdd:pfam06008 105 VATlgendfalpSSDLSRMLAEAQRML-------------GEIRSRDFGTQLQNAEAELKAA-------QDLLSRIQTWF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452938 507 QLHQDTQRTLARR-EDELAVCKAELAFKEELVKA----MKQAQARNRRN 550
Cdd:pfam06008 165 QSPQEENKALANAlRDSLAEYEAKLSDLRELLREaaakTRDANRLNLAN 213
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
351-488 |
6.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 351 AAAHAKQELQKSQEQLQALEEQLRAQKEqnqtLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIA 430
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNE----FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024452938 431 ELLQQVEEVASLKAELAQVQRKIGHNLPLLCHyEEERQQLHRELKKQQKAQ---------EQSRQEA 488
Cdd:PRK12704 121 QKQQELEKKEEELEELIEEQLQELERISGLTA-EEAKEILLEKVEEEARHEaavlikeieEEAKEEA 186
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
356-440 |
7.03e-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: 37.56 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 356 KQELQKSQEQLQALEEQLRAQKEqnqTLQRSLAQQQEVLAATKAREMQNLQQLSRhrqtiHDLQQKAASSRKHIAELLQQ 435
Cdd:smart00935 31 QAELEKLEKELQKLKEKLQKDAA---TLSEAAREKKEKELQKKVQEFQRKQQKLQ-----QDLQKRQQEELQKILDKINK 102
|
....*.
gi 2024452938 436 -VEEVA 440
Cdd:smart00935 103 aIKEVA 108
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
341-519 |
7.54e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 341 WLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQ--NQTLQRSLAQQqevlAATKAREmqNLQQLSRHRQTIHDL 418
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEleKASREETFART----ALKNARL--DLRRLFDEKQSEKDK 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 419 QQKAASSRKHIAEllqqvEEVASLKAELAQVQRKIGHNLPllchyEEERQQLHRELKKQQKAQE----QSRQEAYSFQEK 494
Cdd:pfam12128 669 KNKALAERKDSAN-----ERLNSLEAQLKQLDKKHQAWLE-----EQKEQKREARTEKQAYWQVvegaLDAQLALLKAAI 738
|
170 180
....*....|....*....|....*
gi 2024452938 495 LQQLSSQVQYWQQLHQDTQRTLARR 519
Cdd:pfam12128 739 AARRSGAKAELKALETWYKRDLASL 763
|
|
| YmcA |
COG4550 |
Cell fate regulator YmcA, YheA/YmcA/DUF963 family (controls sporulation, competence, biofilm ... |
416-498 |
9.14e-03 |
|
Cell fate regulator YmcA, YheA/YmcA/DUF963 family (controls sporulation, competence, biofilm development) [Signal transduction mechanisms];
Pssm-ID: 443614 Cd Length: 135 Bit Score: 37.19 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 416 HDLQQKAassrKHIAELLQQVEEVASLKaelaQVQRKIGHNlpllchyeEERQQLHRELKKQQKaqEQSRQEAYSFQEKL 495
Cdd:COG4550 6 DEILAKA----KELAEMIAETEEVERFK----QAEAKINEN--------QKVQELIAEIKALQK--QAVNFQHYGKPEAL 67
|
...
gi 2024452938 496 QQL 498
Cdd:COG4550 68 KKA 70
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
357-441 |
9.47e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 38.00 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452938 357 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLsrhrqtihdlqqkaaSSRKHIAELLQQV 436
Cdd:COG3167 42 SPQLEELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELLKQL---------------PSKAEVPALLDDI 106
|
....*
gi 2024452938 437 EEVAS 441
Cdd:COG3167 107 SQAAL 111
|
|
| |
