|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-602 |
1.75e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 368 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAE 447
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 448 LLQQVEEvasLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQD 527
Cdd:COG1196 391 ALRAAAE---LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024452934 528 TQRTLARREDELAVCKAELAFKEELVKAMKQAQArnrrNHSPRAGGVQPEPQAPLKDRSWATGRAEVERPGQEWA 602
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEA----DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
357-567 |
1.78e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 357 WLQRELSQWHA-AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQ 435
Cdd:COG1196 236 ELEAELEELEAeLEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 436 QKAASSRKHIAELLQQ----VEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKL 511
Cdd:COG1196 316 ERLEELEEELAELEEEleelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024452934 512 QQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRNH 567
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
360-565 |
7.84e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 360 RELSQWHAAAH---AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQ 436
Cdd:COG1196 223 KELEAELLLLKlreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 437 KAASSRKHIAELLQQVEEvasLKAELAQVQRKIGHNlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSS 516
Cdd:COG1196 303 DIARLEERRRELEERLEE---LEEELAELEEELEEL-------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452934 517 QVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-564 |
6.91e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 352 RELAVWLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTI 431
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 432 HDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQrkighnlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKL 511
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEE-------------EEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024452934 512 QQLSSQVQYWQQLHQDTQRTLARREDELAVcKAELAFKEELVKAMKQAQARNR 564
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-566 |
9.94e-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: 75.10 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKArEMQNLQQlsRHRQTIHDLQQKAASSRKHIAEL 448
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE-EYAELKE--ELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 449 LQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELK--KQQKAQEQSR----QEAYSFQE-KLQQLSSQVQYW 521
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEkedkALEIKKQEwKLEQLAADLSKY 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024452934 522 QQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRN 566
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-570 |
1.06e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 368 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAE 447
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 448 LLQQVEEvasLKAELAQVQRKIGhnlpllcHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQD 527
Cdd:TIGR02168 773 AEEELAE---AEAEIEELEAQIE-------QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024452934 528 TQRTLARREDELAVCKAELA--------FKEELVKAMKQAQARNRRNHSPR 570
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEeleelieeLESELEALLNERASLEEALALLR 893
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-565 |
4.53e-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: 68.25 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 362 LSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASS 441
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 442 RKHIAELLQQVEEVASLKAELAQVQR-----------KIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAysfQEK 510
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL---EAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024452934 511 LQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-561 |
1.33e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQtihDLQQKAASSRKHIAELLQQ 451
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---DLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRT 531
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190
....*....|....*....|....*....|
gi 2024452934 532 LARREDELAVCKAELAFKEELVKAMKQAQA 561
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
362-529 |
1.69e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 362 LSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQ-QQEVLAATKAREMQNL-QQLSRHRQTIHDLQQKAA 439
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElREELEKLEKLLQLLPLyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 440 SSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEER-QQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQV 518
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|.
gi 2024452934 519 QYWQQLHQDTQ 529
Cdd:COG4717 230 EQLENELEAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-565 |
1.05e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 376 QKSQEQLQALEEQLRAqkeqnqtLQRSLAQQQEVLAATKArEMQNLQQLSRHRQTIHDL---QQKAASSRKHIAELLQQV 452
Cdd:COG4913 606 FDNRAKLAALEAELAE-------LEEELAEAEERLEALEA-ELDALQERREALQRLAEYswdEIDVASAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 453 EEVASLKAELAQVQRKIGHNlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRT- 531
Cdd:COG4913 678 ERLDASSDDLAALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAl 750
|
170 180 190
....*....|....*....|....*....|....
gi 2024452934 532 LARREDELAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
369-540 |
3.17e-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: 59.39 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAatkaREMQNLQQLSRHRQ---------------TIHD 433
Cdd:COG4942 65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA----ELLRALYRLGRQPPlalllspedfldavrRLQY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 434 LQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIghnLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQ 513
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAEL---EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*..
gi 2024452934 514 LSSQVQYWQQLHQDTQRTLARREDELA 540
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
357-562 |
3.83e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 357 WLQRELSQwhaaahAKQELQKSQEQLQA---------LEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRH 427
Cdd:COG3206 179 FLEEQLPE------LRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 428 RQTIHDLQQKAAssrkhIAELLQQVEEvasLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQ-QKAQEQSRQEAYS 506
Cdd:COG3206 253 PDALPELLQSPV-----IQQLRAQLAE---LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 507 FQEKLQQLSSQVqywQQLHQDTQRtLARREDELAVCKAELAFKEE----LVKAMKQAQAR 562
Cdd:COG3206 325 LQAREASLQAQL---AQLEARLAE-LPELEAELRRLEREVEVARElyesLLQRLEEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-565 |
7.35e-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: 59.30 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 371 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKArEMQNL-QQLSRHRQTIHDLQQKAASSRKHIAELL 449
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-EISRLeQQKQILRERLANLERQLEELEAQLEELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 450 QQV----EEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLH 525
Cdd:TIGR02168 330 SKLdelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452934 526 QDTQRTLARREDE---LAVCKAELAFKE------ELVKAMKQAQARNRR 565
Cdd:TIGR02168 410 ERLEDRRERLQQEieeLLKKLEEAELKElqaeleELEEELEELQEELER 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
352-561 |
1.30e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 352 RELAVWLQreLSQWHAAAHAKQELQKsqeQLQALEEQLRAQKEQNQTLQRSLAQQQEVLA--ATKAREMQNLQQLsRHRQ 429
Cdd:TIGR02169 221 REYEGYEL--LKEKEALERQKEAIER---QLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQL-RVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 430 TIHDLQQKAASSRKHIAELLQQVEEVA-----------SLKAELAQVQRKIGHNLPLLCHYEEERQQLHREL-KKQQKAQ 497
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEerlakleaeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELeDLRAELE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 498 EQS------RQEAYSFQEKLQQLSSQvqywqqlHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQA 561
Cdd:TIGR02169 375 EVDkefaetRDELKDYREKLEKLKRE-------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-565 |
1.89e-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: 57.08 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 382 LQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEvasLKAE 461
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---LEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 462 LAQVQRKIghnlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQ---RTLARREDE 538
Cdd:COG4942 92 IAELRAEL----------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReqaEELRADLAE 161
|
170 180
....*....|....*....|....*..
gi 2024452934 539 LAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERA 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-565 |
1.91e-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: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 351 CRELAVWLQRELSQWHAAAHAKQELQKSQEQLQA-----------LEEQLRAQKEQNQTLQRSLAQQQEVLAatkaremQ 419
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKelyalaneisrLEQQKQILRERLANLERQLEELEAQLE-------E 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 420 NLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKighnlpllchYEEERQQLHRELK--KQQKAQ 497
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE----------LEEQLETLRSKVAqlELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 498 EQSRQEAYSfqEKLQQLSSQVQYWQQ------------LHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:TIGR02168 398 LNNEIERLE--ARLERLEDRRERLQQeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
360-550 |
2.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 360 RELSQWHAA---AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLA----ATKAREMQ------NLQQLSR 426
Cdd:PRK03918 443 RELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelAEQLKELEeklkkyNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 427 HRQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIgHNLpllchyEEERQQLHRELKkqqkaqEQSRQEAYS 506
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DEL------EEELAELLKELE------ELGFESVEE 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452934 507 FQEKLQQLSSQVQYWQQLhQDTQRTLARREDELAVCKAEL--AFKE 550
Cdd:PRK03918 590 LEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELdkAFEE 634
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
371-558 |
4.19e-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: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 371 AKQELQKSQEQLQALeEQLRAQKEQNQTLQRSLAQQQEVLAA----TKAREMQNLQQ-LSRHRQTIHDLQQKAASSRKHI 445
Cdd:COG4913 240 AHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwFAQRRLELLEAeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 446 AELLQQVEE------------VASLKAELAQVQRKIghnlpllchyeEERQQLHRELKKQ-QKAQEQSRQEAYSFQEKLQ 512
Cdd:COG4913 319 DALREELDEleaqirgnggdrLEQLEREIERLEREL-----------EERERRRARLEALlAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452934 513 QLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 558
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-553 |
6.47e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQN-LQQLSRHRQTIHDLQQ 436
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 437 KAASSRKHIAELLQQVE----EVASLKAELAQVQRKIGHNLPLLchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQ 512
Cdd:COG4913 353 ELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEAL---EEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024452934 513 QL-SSQVQYWQQLHQdtqrtlARRE--DELAVCKAELAFKEELV 553
Cdd:COG4913 430 SLeRRKSNIPARLLA------LRDAlaEALGLDEAELPFVGELI 467
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
371-563 |
1.85e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 371 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKaremQNLQQLSRhrqtihDLQQKAASSRKHIAELLQ 450
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE----EELEELNE------QLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 451 QVEEVASLKAELAQVQrkighnlpllchyeEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQR 530
Cdd:COG4372 106 LQEEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190
....*....|....*....|....*....|...
gi 2024452934 531 TLARREDELAVCKAELAFKEELVKAMKQAQARN 563
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-552 |
6.79e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 370 HAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELL 449
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 450 QQVEEVA----SLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKK-QQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQL 524
Cdd:COG4372 122 KERQDLEqqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAlEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180
....*....|....*....|....*...
gi 2024452934 525 HQDTQRTLARREDELAVCKAELAFKEEL 552
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-540 |
9.67e-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: 52.38 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 359 QRELSQwhAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQevlAATKAREMQNLQ-QLSRHR-------QT 430
Cdd:TIGR02169 746 LSSLEQ--EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR---IPEIQAELSKLEeEVSRIEarlreieQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 431 IHDLQQKAASSRKHIAELLQQVEEV----ASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEAYS 506
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
170 180 190
....*....|....*....|....*....|....
gi 2024452934 507 FQEKLQQLSSQVQYWQQLHQDTQRTLARREDELA 540
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-565 |
1.10e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 373 QELQKsqeQLQALEEQlRAQKEQNQTLQRSLAQQQEVLAATKAREMQnlQQLSRHRQTIHDLQqkaassrkhiAELLQQV 452
Cdd:COG1196 196 GELER---QLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELE--AELEELEAELEELE----------AELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 453 EEVASLKAELAQVQRKIghnlpllchyEEERQQLHR-------------ELKKQQKAQEQSRQEAysfQEKLQQLSSQVQ 519
Cdd:COG1196 260 AELAELEAELEELRLEL----------EELELELEEaqaeeyellaelaRLEQDIARLEERRREL---EERLEELEEELA 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452934 520 YWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
352-537 |
1.22e-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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 352 RELAVWLQRELSQWHAAAH-AKQELQKSQEQLQALEEQLRAQKEQNQT---LQRSLAQQQEVLAATKARemqnLQQLSRH 427
Cdd:pfam05557 103 REVISCLKNELSELRRQIQrAELELQSTNSELEELQERLDLLKAKASEaeqLRQNLEKQQSSLAEAEQR----IKELEFE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 428 RQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLlchyEEERQQLHRELKKQQKAQEqsrqEAYSF 507
Cdd:pfam05557 179 IQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLL----KEEVEDLKRKLEREEKYRE----EAATL 250
|
170 180 190
....*....|....*....|....*....|
gi 2024452934 508 QEKLQQLSSQVQYWQQLHQDTQRTLARRED 537
Cdd:pfam05557 251 ELEKEKLEQELQSWVKLAQDTGLNLRSPED 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
380-562 |
2.13e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 380 EQLQALEEQLRAQKEQNQTLQRSLAQQQEvlaatKAREMQNLQQLsrhrqtIHDLQQKAASSRKHIaELLQQVEEVASLK 459
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAE------LEELREELEKLEKLL-QLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 460 AELAQVQRKighnlplLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLS----SQVQYWQQLHQDTQRTLARR 535
Cdd:COG4717 139 AELAELPER-------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAEL 211
|
170 180
....*....|....*....|....*..
gi 2024452934 536 EDELAVCKAELAFKEELVKAMKQAQAR 562
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
373-475 |
3.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 373 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSR----HRQTIHDLQQKAASSRKHIAEL 448
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKelaeLAAELAELQQEAEELEALIARL 232
|
90 100
....*....|....*....|....*..
gi 2024452934 449 LQQVEEVASLKAELAQVQRKIGHNLPL 475
Cdd:COG4942 233 EAEAAAAAERTPAAGFAALKGKLPWPV 259
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
366-504 |
3.63e-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: 48.77 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 366 HAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQT--IHDLQQKAASSRK 443
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024452934 444 HIAEL----LQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQEA 504
Cdd:COG1579 104 RISDLedeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
372-565 |
4.37e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQ----------TLQRSLA-----QQQEVLaaTKAREMQNLQQLSRHRQTIHDLqQ 436
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAelnkaggsidKLRKEIErlewrQQTEVL--SPEEEKELVEKIKELEKELEKA-K 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 437 KAASSRKHIAELLQQVEEvasLKAELAQVQRKIGhnlpllcHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSS 516
Cdd:COG1340 154 KALEKNEKLKELRAELKE---LRKEAEEIHKKIK-------ELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452934 517 QVQYWQQLHQDTQRTLARREDELavcKAELAFKEELVKAMKQAQARNRR 565
Cdd:COG1340 224 KADELHEEIIELQKELRELRKEL---KKLRKKQRALKREKEKEELEEKA 269
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
369-512 |
5.07e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQL----QALEEQLRAQKEQNQTLQrSLAQQQEVLAATKAREMQNLQQlsRHRQTIHDLQQKAAssrkh 444
Cdd:PRK00409 505 EEAKKLIGEDKEKLneliASLEELERELEQKAEEAE-ALLKEAEKLKEELEEKKEKLQE--EEDKLLEEAEKEAQ----- 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024452934 445 iaellqqvEEVASLKAELAQVQRKIGHnLPLLCHYEEERQQL---HRELKKQQKAQEQSRQEAYSFQEKLQ 512
Cdd:PRK00409 577 --------QAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELieaRKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-514 |
8.76e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKE-------------QNQTLQRSLAQQQEVLAATKARemqnLQQL 424
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllplyqELEALEAELAELPERLEELEER----LEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 425 SRHRQTIHDLQQKAASSRKHIAELLQQV-----EEVASLKAELAQVQRKIGhnlpllcHYEEERQQLHRELK--KQQKAQ 497
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLA-------ELEEELEEAQEELEelEEELEQ 231
|
170
....*....|....*..
gi 2024452934 498 EQSRQEAYSFQEKLQQL 514
Cdd:COG4717 232 LENELEAAALEERLKEA 248
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
372-600 |
1.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKhiAELLQQ 451
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--ADEAKK 1490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQlhRELKKQQ---------KAQEQSRQEAYSFQEKLQQLSSQVQYWQ 522
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEeakkadeakKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 523 QLHQDTQRTLARREDELAVcKAELAFKEELV------KAMKQAQARNRRNHSPRAGGVQPEPQAPLKDRSWATGRAEVER 596
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAK-KAEEARIEEVMklyeeeKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
....
gi 2024452934 597 PGQE 600
Cdd:PTZ00121 1648 KAEE 1651
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
372-516 |
1.56e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLaATKAREMQNL-QQLSRHRQTIHDLQQKAASSRKHIAEL-- 448
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK-ELLEKEIERLkETIIKNNSEIKDLTNQDSVKELIIKNLdn 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 449 -----LQQVE----EVASLKAELAQVQRKIghnlpllchyeEERQQLHRELKKQQKAQEQS----RQEAYSFQEKLQQLS 515
Cdd:TIGR04523 462 treslETQLKvlsrSINKIKQNLEQKQKEL-----------KSKEKELKKLNEEKKELEEKvkdlTKKISSLKEKIEKLE 530
|
.
gi 2024452934 516 S 516
Cdd:TIGR04523 531 S 531
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
372-558 |
1.68e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDL-QQKAASSRKHIAELLQ 450
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 451 QVEE-VASLKAELAQVQRKIGH------NLP-LLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQ 522
Cdd:TIGR04523 318 NQEKkLEEIQNQISQNNKIISQlneqisQLKkELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024452934 523 QLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 558
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
369-551 |
3.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAel 448
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA-- 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 449 LQQVEEVAslKAELAQVQRkighnlpLLCHYEEERQQLHRELKKQQKAQ---EQSRQEaysfqEKLQQLSSQVQYWQQLH 525
Cdd:PTZ00121 1580 LRKAEEAK--KAEEARIEE-------VMKLYEEEKKMKAEEAKKAEEAKikaEELKKA-----EEEKKKVEQLKKKEAEE 1645
|
170 180
....*....|....*....|....*.
gi 2024452934 526 QDTQRTLARREDELAVCKAELAFKEE 551
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
358-454 |
3.47e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQwhAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQ--QQEVLAATKA-----REMQNLQQLSRHRQT 430
Cdd:PRK00409 528 LERELEQ--KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeaQQAIKEAKKEadeiiKELRQLQKGGYASVK 605
|
90 100
....*....|....*....|....
gi 2024452934 431 IHDLQQKaassRKHIAELLQQVEE 454
Cdd:PRK00409 606 AHELIEA----RKRLNKANEKKEK 625
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
374-460 |
3.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 374 ELQKSQEQLQALEEQLRAQKEQN----QTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELL 449
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRIlaslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
90
....*....|.
gi 2024452934 450 QQVEEVASLKA 460
Cdd:COG3206 372 QRLEEARLAEA 382
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
373-466 |
4.08e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 373 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKArEMQNLQQL--------SRHRQTIHDLQQKAASSRKH 444
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEA-ERSRLQALlaelagagAAAEGRAGELAQELDSEKQV 131
|
90 100
....*....|....*....|....*.
gi 2024452934 445 IAELLQQVE----EVASLKAELAQVQ 466
Cdd:PRK09039 132 SARALAQVEllnqQIAALRRQLAALE 157
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
358-540 |
4.23e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQ-WHAAAHAKQELQKSQEQLQALE-----EQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTI 431
Cdd:PRK10246 255 LQQEASRrQQALQQALAAEEKAQPQLAALSlaqpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 432 HDLQQKAASSRKHIAELLQQVE-------EVASLKAELAQVQRKIGHNLPLLCHYEEERQQLH--------------REL 490
Cdd:PRK10246 335 AKQSAELQAQQQSLNTWLAEHDrfrqwnnELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNalpaitltltadevAAA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024452934 491 KKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRTLARREDELA 540
Cdd:PRK10246 415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
224-531 |
5.17e-05 |
|
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: 46.56 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 224 TEQLEQVTVQAGSKHHRKKWAIKEHQCWAQNMSSTGHRTTKEEAQGRRQCHQAALSQAAQvparSLAAQSHPQHKEEQLW 303
Cdd:pfam05667 195 TAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAE----QLRSAALAGTEATSGA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 304 PCAGSTMQRTEEQPCSCARSSTQHPADSSIVEPQAPQVAAESSCGHACRELAVWLQRELSQwhaaaHAKQELQKSQEQLQ 383
Cdd:pfam05667 271 SRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQ-----QREEELEELQEQLE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 384 ALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASsrkhIAELLQQVEEVASLKAELA 463
Cdd:pfam05667 346 DLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEEN----IAKLQALVDASAQRLVELA 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024452934 464 QVQRKigHNLPLLCHYEEERQQL-HRELKKQQKAQE---------QSRQEAYSFQEKLQQLSSQVqywQQLHQDTQRT 531
Cdd:pfam05667 422 GQWEK--HRVPLIEEYRALKEAKsNKEDESQRKLEEikelrekikEVAEEAKQKEELYKQLVAEY---ERLPKDVSRS 494
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
374-562 |
5.44e-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: 45.30 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 374 ELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVE 453
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 454 EVASLKaelaqvqrkighnlpllchyeeERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVqywqqlhQDTQRTLA 533
Cdd:COG1579 84 NVRNNK----------------------EYEALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELA 134
|
170 180 190
....*....|....*....|....*....|
gi 2024452934 534 RREDELAVCKAEL-AFKEELVKAMKQAQAR 562
Cdd:COG1579 135 ELEAELEEKKAELdEELAELEAELEELEAE 164
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
374-562 |
5.53e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.25 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 374 ELQKSQEQLQALEEQLRAQ-KEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQV 452
Cdd:pfam03528 19 EFYRLKQQLEAEFNQKRAKfKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQEAIDEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 453 -----EEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRqeaYSFQEKLQQLSSQVQYWQQLHQD 527
Cdd:pfam03528 99 ksqwqEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRR---LSEGQEEENLEDEMKKAQEDAEK 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2024452934 528 TQRTLARREDELAVCKAELAFKEELVKAMKQAQAR 562
Cdd:pfam03528 176 LRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMK 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-577 |
5.57e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQrslaQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQ 451
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEEVASLKaELAQVQRKIghnlpllchyEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQywqqlhqdTQRT 531
Cdd:PRK03918 282 VKELKELK-EKAEEYIKL----------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE--------RLEE 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024452934 532 LARREDELAVCKAELAFKEELVKAMKQAQARNRRnHSPRAGGVQPE 577
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGLTPE 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-570 |
6.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 352 RELAVWLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREmQNLQQLSRHRQTI 431
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 432 HDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHY---------EEERQQLHRELKKQQKAQEQSRQ 502
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdeeelEEELEELEEELEELEEELEELRE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 503 EAYSFQEKLQQLSSQVQYWQQLHQ--DTQRTLARREDELAVCKAelafkeeLVKAMKQAQARNRRNHSPR 570
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQEleELKAELRELAEEWAALKL-------ALELLEEAREEYREERLPP 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-564 |
9.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 349 HACRELAVwLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHR 428
Cdd:COG4913 648 EALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 429 QtihdlQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKighnlpllCHYEEERQQLHRELKKQQKAQEQSRQEAYS-- 506
Cdd:COG4913 727 E-----ELDELQDRLEAAEDLARLELRALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEELERam 793
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024452934 507 ------FQEKLQQLSSQV----QYWQQLHQDTQRTLARREDEL--AVCKAELAFKEELVKAMKQA--QARNR 564
Cdd:COG4913 794 rafnreWPAETADLDADLeslpEYLALLDRLEEDGLPEYEERFkeLLNENSIEFVADLLSKLRRAirEIKER 865
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
372-505 |
1.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAremqnlqqlsrhrqtihDLQQKAASSRKHIAELLQQ 451
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ-----------------ELEKKEEELEELIEEQLQE 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEEVASLKAE------LAQVQRKIghnlpllchyEEERQQLHRELKkqQKAQEQSRQEAY 505
Cdd:PRK12704 144 LERISGLTAEeakeilLEKVEEEA----------RHEAAVLIKEIE--EEAKEEADKKAK 191
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
357-565 |
1.09e-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: 45.73 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 357 WLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQtlQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQ 436
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 437 KAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNlpllcHYEEERQQLHRELKKQQKAQeqsRQEAYSFQEKLQQLSS 516
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI-----RDAHEVATSIREISCQQHTL---TQHIHTLQQQKTTLTQ 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452934 517 QVQYWQQLHQDTQRTLARREDELAvckAELAFKEELVKAMKQAQARNRR 565
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTS---AFRDLQGQLAHAKKQQELQQRY 439
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
371-559 |
1.87e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 371 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLaqQQEVLAATKAREM--QNLQQLSRHRQTIHDLQQKAASSRKHIAEL 448
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQV--KELREEAQELREKrdELNEKVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 449 LQQVEEVASLKAELAQVQRKIGH--------NLPLlchyEEERQ------QLHRELKKQQKAQEQS-------------R 501
Cdd:COG1340 98 RKELAELNKAGGSIDKLRKEIERlewrqqteVLSP----EEEKElvekikELEKELEKAKKALEKNeklkelraelkelR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024452934 502 QEAYSFQEKLQQLSSQVqywQQLHQDTQrTLARREDELavcKAEL-AFKEELVKAMKQA 559
Cdd:COG1340 174 KEAEEIHKKIKELAEEA---QELHEEMI-ELYKEADEL---RKEAdELHKEIVEAQEKA 225
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
373-523 |
2.06e-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: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 373 QELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNL-QQLSRHRQTIhdlqqkaassRKHIAELLQQ 451
Cdd:COG5185 370 VELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAdRQIEELQRQI----------EQATSSNEEV 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024452934 452 VEEVASLKAELAQVQRKIGHNLPLlcHYEEERQQLHRELkkqqkaqeqsRQEAYSFQEKLQQLSSQVQYWQQ 523
Cdd:COG5185 440 SKLLNELISELNKVMREADEESQS--RLEEAYDEINRSV----------RSKKEDLNEELTQIESRVSTLKA 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
378-632 |
2.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 378 SQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEVAS 457
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 458 ---------------LKAE--------LAQVQRKIGHNLPLLCHYEEERQQL---HRELKKQQKAQEQSRQEAYSFQEKL 511
Cdd:COG3883 94 alyrsggsvsyldvlLGSEsfsdfldrLSALSKIADADADLLEELKADKAELeakKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 512 QQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRNHSPRAGGVQPEPQAPLKDRSWATGR 591
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2024452934 592 AEVERPGQEWANCRAKTNKGGGGGSVETLHASHTSACSNSS 632
Cdd:COG3883 254 AAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
358-526 |
2.29e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQWHAAAHAKQelQKSQEQLQALeeqlraqkeqNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQK 437
Cdd:TIGR00618 716 YDREFNEIENASSSLG--SDLAAREDAL----------NQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 438 AASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCH-YEEERQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSS 516
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
170
....*....|
gi 2024452934 517 QVQYWQQLHQ 526
Cdd:TIGR00618 864 LTQEQAKIIQ 873
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
369-610 |
2.38e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTihdlqQKAASSRKHI--- 445
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA-----KKAEAARKAEevr 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 446 -AELLQQVEEVASLK-AELAQVQRKIGHnlplLCHYEEER--QQLHRELKKQQKAQEQSRQEAYSFQEKLQQL-SSQVQY 520
Cdd:PTZ00121 1189 kAEELRKAEDARKAEaARKAEEERKAEE----ARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFeEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 521 WQQLHQDTQRTLARREDEL----AVCKAELAFKEELVKamKQAQARNRRNHSPRAGGVQPEPQAPLKDRSWATGRAEVER 596
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELkkaeEKKKADEAKKAEEKK--KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
250
....*....|....
gi 2024452934 597 PGQEWANCRAKTNK 610
Cdd:PTZ00121 1343 KAAEAAKAEAEAAA 1356
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
374-558 |
2.48e-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: 44.71 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 374 ELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATK-----AREMQNLQQ-----LSRHRQTIHDLQQKAASSRK 443
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKqfekiAEELKGKEQeliflLQAREKEIHDLEIQLTAIKT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 444 HIAELLQQVEEvasLKAELAQVQRKighNLPLLCHYE----------EERQQLHRELKKQQ-------KAQEQSRQEAYS 506
Cdd:pfam05483 465 SEEHYLKEVED---LKTELEKEKLK---NIELTAHCDklllenkeltQEASDMTLELKKHQediinckKQEERMLKQIEN 538
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024452934 507 FQEKLQQLSSQVQY----WQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 558
Cdd:pfam05483 539 LEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
354-561 |
3.08e-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: 44.25 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 354 LAVWLQRELSQWHaaahakQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQ----EVLAATKAREMQNLQQLSRHRQ 429
Cdd:pfam05701 213 AALAREQDKLNWE------KELKQAEEELQRLNQQLLSAKDLKSKLETASALLLdlkaELAAYMESKLKEEADGEGNEKK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 430 TIHDLQQKAASSRKHIAELLQQVE----EVASL--------------KAELAQVQRKIGHNLPLLCHYEEERQQLHRELK 491
Cdd:pfam05701 287 TSTSIQAALASAKKELEEVKANIEkakdEVNCLrvaaaslrselekeKAELASLRQREGMASIAVSSLEAELNRTKSEIA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024452934 492 KQQKAQEQSRQEAYSFQEKLQQlssqvqywqqlhqdtqrtlARREDELAVCKAELAfKEELVKA---MKQAQA 561
Cdd:pfam05701 367 LVQAKEKEAREKMVELPKQLQQ-------------------AAQEAEEAKSLAQAA-REELRKAkeeAEQAKA 419
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
368-565 |
3.27e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 368 AAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAAT--KAREMQNlqqlsrhrqTIHDLQQKAASSRKHI 445
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrKLRETQN---------TLNQLNKQIDELNASI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 446 AEL-LQQVEEVASLKAELAQVQRKIGHN-LPLLCHYEE----ER-------------------QQLHRELKKQQKAQEQS 500
Cdd:PRK11637 113 AKLeQQQAAQERLLAAQLDAAFRQGEHTgLQLILSGEEsqrgERilayfgylnqarqetiaelKQTREELAAQKAELEEK 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024452934 501 RQEAysfQEKLQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELA--------FKEELVKAMKQAQARNRR 565
Cdd:PRK11637 193 QSQQ---KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSelranesrLRDSIARAEREAKARAER 262
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-469 |
3.29e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 367 AAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAAS-SRKHI 445
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElLEEEA 752
|
90 100
....*....|....*....|....
gi 2024452934 446 AELLQQVEEVASLKAELAQVQRKI 469
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREI 776
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-562 |
3.54e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 351 CRELAVWLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKaremqnlQQLSRHRQT 430
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR-------ERAEELRER 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 431 IHDLQQKAASSRKHIAELLQQVEE----VASLKAELAQVQ------RKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQS 500
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALAELNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 501 RQEAYSFQEKLQQLSSQV----------------QYWQQLHQDTQRTLARRED---ELAVCKAELAFKEELVKAMKQAQA 561
Cdd:PRK02224 626 RERLAEKRERKRELEAEFdearieearedkeraeEYLEQVEEKLDELREERDDlqaEIGAVENELEELEELRERREALEN 705
|
.
gi 2024452934 562 R 562
Cdd:PRK02224 706 R 706
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
372-562 |
3.76e-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: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTlQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKaassrkhIAELLQQ 451
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRELERIRQEE-------IAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEEVASLKAELAQVQRKIGHNLPLLCHY---EEERQ----QLHRELKKQQKAQEQSRQ-EAYSFQEKLQQLSSQVQYWQQ 523
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVkilEEERQrkiqQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQ 456
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024452934 524 LHQDTQRTLARREDELAVCKAELAfKEELVKAMKQAQAR 562
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 ... |
377-546 |
4.69e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 377 KSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEvLAATKAREMQNLQ-----QLSRHRQTIHDLQQKAASSrkhIAELLQQ 451
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELEDTLDTTAAQQE-LRSKREQEVTELKkaleeETRSHEAQLQEMRQKHTQA---LEELTEQ 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEEVASLKAELAQVQRKIghnlpllchyEEERQQLHRELKKQQKAQEQSRQeaysfqeKLQQLSSQVQYWQQLHQDTQRT 531
Cdd:pfam01576 365 LEQAKRNKANLEKAKQAL----------ESENAELQAELRTLQQAKQDSEH-------KRKKLEGQLQELQARLSESERQ 427
|
170
....*....|....*
gi 2024452934 532 LARREDELAVCKAEL 546
Cdd:pfam01576 428 RAELAEKLSKLQSEL 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
446-569 |
5.62e-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: 42.83 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 446 AELLQQVEEVASLKAELAQVQRKIghnlpllchyeeerQQLHRELKKQQKAQEQSRQEAYSFQEKLQQLSSQVQYWQQLH 525
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEI--------------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024452934 526 QDTQRTLARREDELAVCKAELAFKEELVKAMKQAQARNRRNHSP 569
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL 122
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
358-564 |
6.74e-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: 43.40 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQWHAAAHAKQELQK-------SQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQ-------- 422
Cdd:COG3096 408 QQTRAIQYQQAVQALEKARAlcglpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiage 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 423 ------------QLSRHRQTIHDLQQkAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHREL 490
Cdd:COG3096 488 versqawqtareLLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 491 KKQQKAQEQSRQEAYSFQEKLQQLSSQVqywQQLHQ------DTQRTLARREDElavCKAELAFKEELVKAMKQAQARNR 564
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLEQLRARI---KELAArapawlAAQDALERLREQ---SGEALADSQEVTAAMQQLLERER 640
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
357-516 |
7.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 357 WLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQkeqnQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQ 436
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ----QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 437 KAASSRKHIAELLQQVEEVASLKAELAQvQRKIGHNL-PLLCHYEEE--------------RQQLHRELKKQQKAQEQSR 501
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAA-RAPAWLAAqDALARLREQsgeefedsqdvteyMQQLLERERELTVERDELA 651
|
170
....*....|....*
gi 2024452934 502 QEAYSFQEKLQQLSS 516
Cdd:PRK04863 652 ARKQALDEEIERLSQ 666
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
372-558 |
1.30e-03 |
|
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: 41.17 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQL-----RAQKEQNQ--TLQRSLAQQQEVLAATKAREMQNLQQLS----------RHRQTIHDL 434
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLeeaekRAEKAEAEvaALNRRIQLLEEELERTEERLAEALEKLEeaekaadeseRGRKVLENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 435 QQK----------AASSRKHIAE-LLQQVEEVAS----LKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQ 499
Cdd:pfam00261 87 ALKdeekmeileaQLKEAKEIAEeADRKYEEVARklvvVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024452934 500 SRQEAYSFQEKLQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAELAFKEELVKAMKQ 558
Cdd:pfam00261 167 ASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
372-525 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKeqnQTLQRSLAQQQEVlaatkAREMQNLQQ--LSRHRQTIHDLQQKAASSRKHIAELL 449
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRK---DALEEELRQLKQL-----EDELEDCDPteLDRAKEKLKKLLQEIMIKVKKLEELE 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024452934 450 QQVEEvasLKAELAQVQRKIghnlpllchyeeerQQLHRELKKQQKAQEQSRQeaYSFQEkLQQLSSQVQYWQQLH 525
Cdd:smart00787 232 EELQE---LESKIEDLTNKK--------------SELNTEIAEAEKKLEQCRG--FTFKE-IEKLKEQLKLLQSLT 287
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
400-546 |
1.93e-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: 41.86 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 400 QRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHY 479
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024452934 480 EEERQQLHRELKKQ-----------QKAQEQSRQEAYSfqekLQQLSSQVQywQQLHQDTQRTLARreDELAVCKAEL 546
Cdd:COG3096 587 LEQLRARIKELAARapawlaaqdalERLREQSGEALAD----SQEVTAAMQ--QLLEREREATVER--DELAARKQAL 656
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
371-462 |
2.17e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 371 AKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAAtkaremqnlqQLSRHRQTIHDLQQKAASSRKHIAELLQ 450
Cdd:pfam00038 215 AKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL----------QLADYQELISELEAELQETRQEMARQLR 284
|
90
....*....|..
gi 2024452934 451 QVEEVASLKAEL 462
Cdd:pfam00038 285 EYQELLNVKLAL 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
372-467 |
2.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSR-----HRQTIhdLQQKAASSRKHIA 446
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGltaeeAKEIL--LEKVEEEARHEAA 172
|
90 100
....*....|....*....|....*...
gi 2024452934 447 ELLQQVEEVASLKAE------LAQ-VQR 467
Cdd:PRK12704 173 VLIKEIEEEAKEEADkkakeiLAQaIQR 200
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
359-565 |
2.67e-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: 40.67 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 359 QRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREmqnlQQLSRHRQTIHDLQQKA 438
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE----REIARLRAQQEKAQDEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 439 ASSRKHIAELLQQVEEVASLKAELAQVQRKIGHNLPLLCHYEEERQQLHRELKKQQKAQEQSRQ---EAYSFQEKLQQLS 515
Cdd:pfam13868 201 AERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFErmlRKQAEDEEIEQEE 280
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024452934 516 SQVQywQQLHQDTQRTLAR--REDELAVCKAELAFKEELVKAMKQAQARNRR 565
Cdd:pfam13868 281 AEKR--RMKRLEHRRELEKqiEEREEQRAAEREEELEEGERLREEEAERRER 330
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
358-456 |
2.79e-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: 39.43 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQWhaaahaKQELQKSQEQLQALEEQLRAQK-----EQNQTLQRSLAQQQevlaatkaremQNLQQLSRHRQTih 432
Cdd:COG2825 48 LEKEFKKR------QAELQKLEKELQALQEKLQKEAatlseEERQKKERELQKKQ-----------QELQRKQQEAQQ-- 108
|
90 100
....*....|....*....|....*
gi 2024452934 433 DLQQKAASSRKHIAELLQQ-VEEVA 456
Cdd:COG2825 109 DLQKRQQELLQPILEKIQKaIKEVA 133
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
358-438 |
2.79e-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: 39.50 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQwhaAAHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQevlaatkaREMQNLqqLSRHRQTIHDLQQK 437
Cdd:pfam13851 73 LRKQLEN---YEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVE--------RERDEL--YDKFEAAIQDVQQK 139
|
.
gi 2024452934 438 A 438
Cdd:pfam13851 140 T 140
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
369-518 |
2.89e-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: 40.90 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQLQALeeqlraQKEQNQTLQRSLAQQQEVLaatKAREMQNLQQLSRHR-QTIHDLQQKAASSRKHIAE 447
Cdd:pfam09731 290 AHAHREIDQLSKKLAEL------KKREEKHIERALEKQKEEL---DKLAEELSARLEEVRaADEAQLRLEFEREREEIRE 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024452934 448 LLQQveevaSLKAELAQvQRKIgHNLPLLCHYEEERQQLHRELkkQQKAQEQSRQEAYSFQEKLQQLSSQV 518
Cdd:pfam09731 361 SYEE-----KLRTELER-QAEA-HEEHLKDVLVEQEIELQREF--LQDIKEKVEEERAGRLLKLNELLANL 422
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
369-469 |
2.97e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 369 AHAKQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQ---EVLAATKAREMQnLQQLSRHRQtihdLQQKAASSRKHI 445
Cdd:COG2268 240 AEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREvqrQLEIAEREREIE-LQEKEAERE----EAELEADVRKPA 314
|
90 100 110
....*....|....*....|....*....|..
gi 2024452934 446 AELLQQVEEVASLKAE--------LAQVQRKI 469
Cdd:COG2268 315 EAEKQAAEAEAEAEAEairakglaEAEGKRAL 346
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
358-526 |
3.64e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 358 LQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQNQTL------QRSLAQQQEVL--------AATKARE------ 417
Cdd:COG0497 160 YREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAalqpgeEEELEEERRRLsnaeklreALQEALEalsgge 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 418 ----------MQNLQQLSRHRQTIHDLQQKAASSRKHIAEL-----------------LQQVEE----VASLK------- 459
Cdd:COG0497 240 ggaldllgqaLRALERLAEYDPSLAELAERLESALIELEEAaselrryldslefdperLEEVEErlalLRRLArkygvtv 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024452934 460 AELAQVQRKIGHNLPLLCHYEEERQQLHRELKK-----QQKAQE--QSRQEAysfqekLQQLSSQVQywQQLHQ 526
Cdd:COG0497 320 EELLAYAEELRAELAELENSDERLEELEAELAEaeaelLEAAEKlsAARKKA------AKKLEKAVT--AELAD 385
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
346-457 |
3.93e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 346 SCGHACRELAVWLQRELS-QWHAAA-------HAKQELQKSQEQLQALEEQLRAQ---KEQNQTLQRSLAQQQEVLAATK 414
Cdd:PRK11448 107 MGLKLAFRLAVWFHRTYGkDWDFKPgpfvppeDPENLLHALQQEVLTLKQQLELQareKAQSQALAEAQQQELVALEGLA 186
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024452934 415 AREMQNLQQLSRHRQTIhdLQQKAASSRKHIAELLQQVEEVAS 457
Cdd:PRK11448 187 AELEEKQQELEAQLEQL--QEKAAETSQERKQKRKEITDQAAK 227
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
371-566 |
5.81e-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: 39.52 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 371 AKQELQKSQEQLQALEEQLRAQKEQNQtlQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASsRKHIAELLQ 450
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-EREIARLRA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 451 QVEEVASLKAELAQVQRKighnlplLCHYEEERQQLHRELKKQQKAQEQSRQEAYSFQEklqqlssqvqywQQLHQDTQR 530
Cdd:pfam13868 192 QQEKAQDEKAERDELRAK-------LYQEEQERKERQKEREEAEKKARQRQELQQAREE------------QIELKERRL 252
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024452934 531 TLARREDELAVCKAELAFKEELVKAMKQAQARNRRN 566
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
370-546 |
7.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 370 HAKQELQKSQEQLQALEEQLRAQKEQNQTLQR-----------SLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKA 438
Cdd:PRK04863 848 ELERALADHESQEQQQRSQLEQAKEGLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIV 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 439 ASSR---KHIAELLQQVEEVASLKAELAQ--------VQRKigHNLPllchYEE------ERQQLHRELKKQQKAQEQSR 501
Cdd:PRK04863 928 SVLQsdpEQFEQLKQDYQQAQQTQRDAKQqafaltevVQRR--AHFS----YEDaaemlaKNSDLNEKLRQRLEQAEQER 1001
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024452934 502 QEAysfQEKLQQLSSQVQYWQQLHQDTQRTLARREDELAVCKAEL 546
Cdd:PRK04863 1002 TRA---REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
367-504 |
7.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 367 AAAHAKQELQKSQEQLQALEEQLRAQKEqnqtLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIA 446
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNE----FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024452934 447 ELLQQVEEVASLKAELAQVQRKIGHNLPLLCHyEEERQQLHRELKKQQKAQ---------EQSRQEA 504
Cdd:PRK12704 121 QKQQELEKKEEELEELIEEQLQELERISGLTA-EEAKEILLEKVEEEARHEaavlikeieEEAKEEA 186
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
372-456 |
8.80e-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: 37.18 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEqnqTLQRSLAQQQEVLAATKAREMQNLQQLSRhrqtiHDLQQKAASSRKHIAELLQQ 451
Cdd:smart00935 31 QAELEKLEKELQKLKEKLQKDAA---TLSEAAREKKEKELQKKVQEFQRKQQKLQ-----QDLQKRQQEELQKILDKINK 102
|
....*.
gi 2024452934 452 -VEEVA 456
Cdd:smart00935 103 aIKEVA 108
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
372-566 |
8.94e-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: 38.55 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 372 KQELQKSQEQLQALEEQLRAQKEQNQTLQRSLAQQQEVLAATKAREMQNLQQLSRHRQTIHDLQQKAASSRKHIAELLQQ 451
Cdd:pfam06008 25 TKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 452 VEE---------VASLKAELAQVQRKIGhnlpllchyeeerQQLHRELKKQQKAQEQSRQEAysfqeklQQLSSQVQYWQ 522
Cdd:pfam06008 105 VATlgendfalpSSDLSRMLAEAQRMLG-------------EIRSRDFGTQLQNAEAELKAA-------QDLLSRIQTWF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024452934 523 QLHQDTQRTLARR-EDELAVCKAELAFKEELVKA----MKQAQARNRRN 566
Cdd:pfam06008 165 QSPQEENKALANAlRDSLAEYEAKLSDLRELLREaaakTRDANRLNLAN 213
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
362-504 |
8.95e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 362 LSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQnqtlQRSLAQQQEVLAATKAREMQNLQqlsrhrqtihdlQQKAASS 441
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQ----ERLKQLEKERLAAQEQKKQAEEA------------AKQAALK 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024452934 442 RKHIAELLQQVEEVASLKAELAQVQrkighnlpllchYEEERQQLHRELKKQQKAQEQSRQEA 504
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKR------------AAAAAKKAAAEAKKKAEAEAAKKAAA 181
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
357-535 |
9.11e-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: 39.44 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 357 WLQRELSQWHAAAHAKQELQKSQEQLQALEEQLRAQKEQ--NQTLQRSLAQQqevlAATKAREmqNLQQLSRHRQTIHDL 434
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEleKASREETFART----ALKNARL--DLRRLFDEKQSEKDK 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024452934 435 QQKAASSRKHIAEllqqvEEVASLKAELAQVQRKIGHNLPllchyEEERQQLHRELKKQQKAQE----QSRQEAYSFQEK 510
Cdd:pfam12128 669 KNKALAERKDSAN-----ERLNSLEAQLKQLDKKHQAWLE-----EQKEQKREARTEKQAYWQVvegaLDAQLALLKAAI 738
|
170 180
....*....|....*....|....*
gi 2024452934 511 LQQLSSQVQYWQQLHQDTQRTLARR 535
Cdd:pfam12128 739 AARRSGAKAELKALETWYKRDLASL 763
|
|
| |
