|
Name |
Accession |
Description |
Interval |
E-value |
| Eisosome1 |
pfam12757 |
Eisosome protein 1; Eisosome protein 1 is required for normal formation of eisosomes, large ... |
287-406 |
2.40e-24 |
|
Eisosome protein 1; Eisosome protein 1 is required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Pssm-ID: 432763 [Multi-domain] Cd Length: 125 Bit Score: 98.81 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 287 DAKVLQKALANAESTLRRLDTDATPE----NLFNNRENNLKALAIAQQNSEKRRVN-DGKIDLGGGLFMDPVELNVMAQQ 361
Cdd:pfam12757 1 REALLAAARRNVDARLQDIDEKVYADtgrvPPAMNEEWERKALERAQANSEKRSENyAGKVNIGGGLFMDQEEVDAIAAS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 238031448 362 LVGPVVQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQK 406
Cdd:pfam12757 81 RVQPVLDEIDERAEAQRARDEEIKLDEEERKREKEEWKEREREKK 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-661 |
6.42e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 368 QQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEgekskqfdLIALKQRELD 447
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------ELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 448 GKQNELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARDEELTSLQAERDEEVAplvagLERETGILNELIAEREE 527
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-----EEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 528 LEAsynehhtraeghnnvLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQ 607
Cdd:COG1196 423 LEE---------------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 238031448 608 KLEAERDQLIKKHDDTVAELQDAKLKglqEDKAVNSILPEHLQEDIKDTVSVET 661
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAA---LLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-640 |
9.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 414 EIDKQVRREKLDADK--------EGEKSKQFDLIALKQRELDGKQNELDESVQEDQKIREALVLEKTNLEEKIST----- 480
Cdd:COG1196 197 ELERQLEPLERQAEKaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrlel 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 481 ----EAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLENSETMLSDL 556
Cdd:COG1196 277 eeleLELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 557 DEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLtAQNATLLAQHQKLEAERDQLIKKHDDTVAELQDAKLKGLQ 636
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
....
gi 238031448 637 EDKA 640
Cdd:COG1196 436 EEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
394-633 |
1.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 394 RKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLiALKQRELDGKQNELDESVQEDQKIREALVLEKTN 473
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 474 LEEKISTEAAQRKQARD-------------EELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHT--- 537
Cdd:COG1196 314 LEERLEELEEELAELEEeleeleeeleeleEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEalr 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 538 ---RAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKLEAERD 614
Cdd:COG1196 394 aaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250
....*....|....*....
gi 238031448 615 QLIKKHDDTVAELQDAKLK 633
Cdd:COG1196 474 LLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
379-628 |
2.82e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 379 QQDEQNAQKKLEQKQRKLQYEEELRKQKleEKQNKEIDKQVRR-EKLDADKEGEKSKQFDLIALKQRELDGKQNELDESV 457
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNEL--ERQLKSLERQAEKaERYKELKAELRELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 458 QEDQKIREALVLEKTNLEEKIsteaaqrkqardEELTSLQAERDEEvaplvagLERETGILNELIAEREELEAsynehht 537
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKL------------EELRLEVSELEEE-------IEELQKELYALANEISRLEQ------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 538 RAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKLEAERDQLI 617
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250
....*....|.
gi 238031448 618 KKHDDtVAELQ 628
Cdd:TIGR02168 383 TLRSK-VAQLE 392
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-564 |
5.46e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 367 VQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQREL 446
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 447 DGKQNELDESVQEDQKIREALVLEKTNLEEKISTEAAQrkQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAERE 526
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL--EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180 190
....*....|....*....|....*....|....*...
gi 238031448 527 ELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAAR 564
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-640 |
1.40e-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: 58.53 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 376 LQRQ----QDEQNAQKKLEQKQRKLQYEE-ELRKQKLEEKQNKEIDKQVRREKLDADKEgEKSKQFDlialkqrELDGKQ 450
Cdd:TIGR02168 205 LERQaekaERYKELKAELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQ-ELEEKLE-------ELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 451 NELDESVQEDQKIREALVLEKTNLEEKIsteaaQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEA 530
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQK-----QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 531 SYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEafkkNHETQFASLTAQNATLLAQHQKLE 610
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE----RLEARLERLEDRRERLQQEIEELL 427
|
250 260 270
....*....|....*....|....*....|
gi 238031448 611 AERDQLIKKHDDTVAELQDAKLKGLQEDKA 640
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
373-619 |
1.41e-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: 58.53 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 373 KAALQRQQDEQNAQKKLEQKQRKLQyEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIA---LKQRELDGK 449
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEeaeEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 450 QNELDESVQEDQKIREALVLEKTNLEEKIST--EAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREE 527
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLlnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 528 LEASYNEHHTRAEGHNNVLENSEtmlsdldEQINAARTKLEATKKKAEQVAKDTEAFKKNHEtqfaSLTAQNATLLAQHQ 607
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLE-------EALALLRSELEELSEELRELESKRSELRRELE----ELREKLAQLELRLE 932
|
250
....*....|..
gi 238031448 608 KLEAERDQLIKK 619
Cdd:TIGR02168 933 GLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-589 |
1.77e-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: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 372 SKAALQRQQDEQNAQK-KLEQKQRKLQYEEELRKQKLEEkQNKEIDK-----QVRREKLDADKEGEKSKQFDLIALKQRE 445
Cdd:TIGR02169 238 QKEAIERQLASLEEELeKLTEEISELEKRLEEIEQLLEE-LNKKIKDlgeeeQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 446 LDgkqnELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARdEELTSLQAERD-----------------EEVAPLV 508
Cdd:TIGR02169 317 LE----DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-EEYAELKEELEdlraeleevdkefaetrDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 509 AGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNH 588
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
.
gi 238031448 589 E 589
Cdd:TIGR02169 472 Y 472
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-613 |
9.74e-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: 55.16 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 362 LVGPVVQQIDSKAALQRQQDEqnAQKKLEQKQRKLQyeEELRKQKLEEKQNKEIDKQVrrekldadkegekSKQFDLIAL 441
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ--LQQEIAELEKELA--ALKKEEKALLKQLAALERRI-------------AALARRIRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 442 KQRELDGKQNELDESVQEDQKIREALVLEKTNLEEKISteAAQRKQARDEELTSLQAERdeevaplVAGLERETGILNEL 521
Cdd:COG4942 74 LEQELAALEAELAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPED-------FLDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 522 IAEREELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNAT 601
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|..
gi 238031448 602 LLAQHQKLEAER 613
Cdd:COG4942 225 LEALIARLEAEA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-651 |
3.32e-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: 54.30 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 395 KLQYEEELRKQKLEEKQNKEidKQVRREKLDADKE-GEKSKQFDLIALKQRELDGKQNELDESVQEDQKIREALVLEKTN 473
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRL--DELSQELSDASRKiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 474 LEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLENSETML 553
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 554 SDLDEQINAARTKLEATKKKAEqvakDTEAFKKNHETQFASLTAQNATLLAQHQKLEAERDQLIKKHDDTVAELQDAKLK 633
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKE----ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250
....*....|....*...
gi 238031448 634 gLQEDKAVNSILPEHLQE 651
Cdd:TIGR02169 919 -LSELKAKLEALEEELSE 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-623 |
3.44e-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: 54.30 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 372 SKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQRELDGKQN 451
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 452 ELDESVQEDQKIREAL--VLEKTNLEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELE 529
Cdd:TIGR02169 802 KLEEEVSRIEARLREIeqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 530 ASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNH--------------------- 588
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeelsledvqaelq 961
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 238031448 589 ----------------ETQFASLTAQNATLLAQHQKLEAERDQLIKKHDDT 623
Cdd:TIGR02169 962 rveeeiralepvnmlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
379-609 |
3.66e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 379 QQDEQNAQKKLEQKQRKLQYEEELRKQkLEEKQNKEIDKQVRREKLDADKEGEKSKQFDliALKQRELDGKQNELDESVQ 458
Cdd:PRK11281 62 QQDLEQTLALLDKIDRQKEETEQLKQQ-LAQAPAKLRQAQAELEALKDDNDEETRETLS--TLSLRQLESRLAQTLDQLQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 459 EDQK-IREA---LVLEKTNLE--EKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIA-EREELEAS 531
Cdd:PRK11281 139 NAQNdLAEYnsqLVSLQTQPEraQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDlQRKSLEGN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 532 ------YNEHHTRAEGHNNVLensETMLSDLDEQINAARtkLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNA----T 601
Cdd:PRK11281 219 tqlqdlLQKQRDYLTARIQRL---EHQLQLLQEAINSKR--LTLSEKTVQEAQSQDEAARIQANPLVAQELEINLqlsqR 293
|
....*...
gi 238031448 602 LLAQHQKL 609
Cdd:PRK11281 294 LLKATEKL 301
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-671 |
9.63e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 373 KAALQRQQDEQnaqKKLEQKQR--KLQYEEELRK----QKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQREL 446
Cdd:PTZ00121 1529 KAEEAKKADEA---KKAEEKKKadELKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 447 DGKQNELDEsvQEDQKIREalvlEKTNLEEKISTEAAQRKQARDEELTSLQAERDEevaplvaglERETGILNELIAERE 526
Cdd:PTZ00121 1606 KMKAEEAKK--AEEAKIKA----EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA---------EEENKIKAAEEAKKA 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 527 ELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKknhetqfasLTAQNATLLAQH 606
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK---------IKAEEAKKEAEE 1741
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238031448 607 QKLEAERDQLIKKHDDTVAELQDAKLKGLQE-DKAVNSILPEHL-QEDIKDTVSVETPFDHSKFKFE 671
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELdEEDEKRRMEVDKKIKDIFDNFA 1808
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-631 |
2.31e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 350 MDPVELNV-MAQQLVGPVVQQIDSkaaLQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRR------- 421
Cdd:TIGR02169 179 LEEVEENIeRLDLIIDEKRQQLER---LRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASleeelek 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 422 -----------------------EKLDADKEGE----KSKQFDL---IALKQRELDGKQNEL---DESVQEDQKIREALV 468
Cdd:TIGR02169 256 lteeiselekrleeieqlleelnKKIKDLGEEEqlrvKEKIGELeaeIASLERSIAEKERELedaEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 469 LEKTNLEEKISTEAAQRKQARdEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLEN 548
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLT-EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 549 SETMLSDLdEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKLEAERDQLIKKHDDTVAELQ 628
Cdd:TIGR02169 415 LQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
...
gi 238031448 629 DAK 631
Cdd:TIGR02169 494 EAE 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
354-551 |
2.52e-06 |
|
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: 51.21 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 354 ELNVMAQQLVGPVVQQIDSKAALQRQQDEQNAQ-KKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEK 432
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEElAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 433 SKQFDLiALKQRELDGKQNELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLE 512
Cdd:TIGR02168 386 SKVAQL-ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 238031448 513 RETGILNELIAEREELEASYNEHHTRAEGHNNVLENSET 551
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-655 |
4.80e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 382 EQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVrrEKLDADKEGEKSKQFDLIALKQRELDGKQneldESVQEDQ 461
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEI----KSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 462 KIREALVLEKTNLEEKIsteaaqrkQARDEELTSLQAERDEEVAPLVAGLERETgilneliaerEELEASYNEHhTRAEG 541
Cdd:PRK03918 549 EKLEELKKKLAELEKKL--------DELEEELAELLKELEELGFESVEELEERL----------KELEPFYNEY-LELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 542 HNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNH--------ETQFASLTAQNATLLAQHQKLEAER 613
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyeelREEYLELSRELAGLRAELEELEKRR 689
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 238031448 614 DQLIKKHDDTVAELQDAKlKGLQEDKAVNSILP--EHLQEDIKD 655
Cdd:PRK03918 690 EEIKKTLEKLKEELEERE-KAKKELEKLEKALErvEELREKVKK 732
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-616 |
6.86e-06 |
|
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: 50.06 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 411 QNKEIDKQVRREKLDADKEGEKSKQfdLIALKQrELDGKQNELDESVQEDQKIREALVLEKTNLEekISTEAAQRKQARD 490
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKA--LAELRK-ELEELEEELEQLRKELEELSRQISALRKDLA--RLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 491 EELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEAT 570
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 238031448 571 KKKAEQVAKDTEAFKKNHET----------QFASLTAQNATLLAQHQKLEAERDQL 616
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASL 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-599 |
7.97e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 372 SKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADK---EGEKS-KQFDLIALKQRELD 447
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELkelEARIEeLEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 448 GKQNELDESVQEDQKIREALVLEKTNLEEKIStEAAQRKQARDEELTSLQAERDEEVAPLVAGLEREtgilNELIAEREE 527
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLR-EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI----KSIEKEIEN 858
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238031448 528 LEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQN 599
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
359-500 |
1.06e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 359 AQQLVGPVVQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDK--QVRREKLDADKEGEK-SKQ 435
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKeeNLDRKLELLEKREEElEKK 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238031448 436 FDLIALKQRELDGKQNELDESVQEDQKIRE-----------ALVLEKtnLEEKISTEAAQR-KQArdEELTSLQAER 500
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELErisgltaeeakEILLEK--VEEEARHEAAVLiKEI--EEEAKEEADK 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
400-616 |
1.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 400 EELRKQK-----LEEKQNKEIDKQVRREKLDADKEGEKSKQfdlialKQRELDGKQNELDESVQEDQKIREALvlektnl 474
Cdd:COG4913 245 EDAREQIellepIRELAERYAAARERLAELEYLRAALRLWF------AQRRLELLEAELEELRAELARLEAEL------- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 475 eekisTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHhtraeghnnvlensetmLS 554
Cdd:COG4913 312 -----ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL-----------------LA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238031448 555 DLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKLEAERDQL 616
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-622 |
1.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 276 ERETLSKNTLVDAKVLQKALANAESTLRRLDTDAtpENLFNNRENNLKALAIAQQNSEKRRvndgkidlggglfmdpvel 355
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEEL--SRQISALRKDLARLEAEVEQLEERI------------------- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 356 nvmaqQLVGPVVQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREkLDADKEGEKSKQ 435
Cdd:TIGR02168 750 -----AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 436 FDLIALkQRELDGKQNELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQArdEELTSLQAERDEEVAPLVAGLERET 515
Cdd:TIGR02168 824 ERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 516 GILNELIAEREELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINA-ARTKLEATKKKAEQVAKDTEAFK---KNHETQ 591
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARrrlKRLENK 980
|
330 340 350
....*....|....*....|....*....|.
gi 238031448 592 FASLTAQNATLLAQHQKLEAERDQLIKKHDD 622
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
372-690 |
6.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 372 SKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDAD---KEGEKSKQFDLiALKQRELDG 448
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADE-AKKKAEEAK 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 449 KQNELDESVQEDQKIREAlvleKTNLEEKISTEAAQRK--QARDEELTSLQAERDEEVAPLVAGLERETGILNELiaeRE 526
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEA----KKKAEEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA---KK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 527 ELEASYNEHHTRAEGHNNVLEnsetmLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNA------ 600
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADE-----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeea 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 601 ------TLLAQHQKLEAERdqlIKKHDDtvAELQDAKLKGLQEDKAVNSILPEHLQEDIKDTVSVETPFDHSKFKFEPEP 674
Cdd:PTZ00121 1593 rieevmKLYEEEKKMKAEE---AKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
330
....*....|....*.
gi 238031448 675 FVEESVEQKKPESPKA 690
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKA 1683
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
369-595 |
9.26e-05 |
|
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: 46.32 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 369 QIDSKAALQRQQDEQNAQKKLEQKQRKLQYEE---ELRKQKLEE-------------KQNKEIDKQVRREKLDADKEGEK 432
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvttEAKIKKLEEdillledqnsklsKERKLLEERISEFTSNLAEEEEK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 433 SKQFDLIALKQR----ELDGKQNELDESVQEDQKIREALVLEKTNLEEKISteaaqRKQARDEELTSLQAERDEEVAPLV 508
Cdd:pfam01576 175 AKSLSKLKNKHEamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-----ELQAQIAELRAQLAKKEEELQAAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 509 AGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEAT----------KKKAEQ-- 576
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaqqelRSKREQev 329
|
250 260
....*....|....*....|.
gi 238031448 577 --VAKDTEAFKKNHETQFASL 595
Cdd:pfam01576 330 teLKKALEEETRSHEAQLQEM 350
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
393-661 |
9.99e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 393 QRKLQYEEELRK--QKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQRELDGKQNELDESVQEDQKIREALVLE 470
Cdd:TIGR00606 684 QRVFQTEAELQEfiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 471 KTNLEEK---ISTEAAQRKQARDeeltslqaerdeevaplvagLERETGILNELIAEREELEASYNEHHTRAEGHNNVLE 547
Cdd:TIGR00606 764 KNDIEEQetlLGTIMPEEESAKV--------------------CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 548 NSET--MLSDLDEQINAARTKLEATKKKAEQVAKDTEAFkKNHETQFASLTAQNATLLAQHQKLEAERDQLIKKHDDTVA 625
Cdd:TIGR00606 824 VQQVnqEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-KSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
250 260 270
....*....|....*....|....*....|....*.
gi 238031448 626 ELQDAKlkglQEDKAVNSILPEHLQEDIKDTVSVET 661
Cdd:TIGR00606 903 EIKDAK----EQDSPLETFLEKDQQEKEELISSKET 934
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
452-619 |
1.96e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 452 ELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARDE--ELTSLQAERDEEVAPLVAGLERETGILNELIAEREeLE 529
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEleDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-YE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 530 ASYNEhhtraeghnnvLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKL 609
Cdd:COG1579 93 ALQKE-----------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 238031448 610 EAERDQLIKK 619
Cdd:COG1579 162 EAEREELAAK 171
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
368-618 |
2.84e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 368 QQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRK--QKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQRE 445
Cdd:pfam13868 120 EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 446 LDGKQNELDESVQEDQKIREalvlektnlEEKISTEAAQRKQARDEeltsLQAERDEEVAPLVAGLEREtgilneliAER 525
Cdd:pfam13868 200 KAERDELRAKLYQEEQERKE---------RQKEREEAEKKARQRQE----LQQAREEQIELKERRLAEE--------AER 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 526 EELEAsynehhtraeghnnvlensETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQ 605
Cdd:pfam13868 259 EEEEF-------------------ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGER 319
|
250
....*....|...
gi 238031448 606 HQKLEAERDQLIK 618
Cdd:pfam13868 320 LREEEAERRERIE 332
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
378-650 |
3.23e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 378 RQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEID-KQVRREKLDADKE--GEKSKQFDLIALKQRELDGKQNELD 454
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEeKNALQEQLQAETElcAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 455 ESVQEDQKIREALVLEK-------TNLEEKISTEAAQRKQARDEELT--SLQAERDEEVAPLV---AGLERETGILNELI 522
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKkkmqqhiQDLEEQLDEEEAARQKLQLEKVTteAKIKKLEEDILLLEdqnSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 523 AereELEASYNEHHTRAEGHNNVLENSETMLSDLDEQIN---AARTKLEATKKKAEQVAKDTeafkknhETQFASLTAQN 599
Cdd:pfam01576 162 S---EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDL-------QEQIAELQAQI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 238031448 600 ATLLAQHQKLEAERDQLIKKHDDTVAElQDAKLKGLQEDKAVNSILPEHLQ 650
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQ-KNNALKKIRELEAQISELQEDLE 281
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
383-514 |
3.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 383 QNAQKKLE--QKQRKLQYEEELRKQKLE-EKQNKEIDKQV-RREKLDADKEGEKSKQFDLIALKQRELDGKQNELDESVQ 458
Cdd:PRK12704 45 EEAKKEAEaiKKEALLEAKEEIHKLRNEfEKELRERRNELqKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 238031448 459 E-DQKIREALVLEKTNLE--EKISteAAQRKQARDEELTSLQAERDEEVAPLVAGLERE 514
Cdd:PRK12704 125 ElEKKEEELEELIEEQLQelERIS--GLTAEEAKEILLEKVEEEARHEAAVLIKEIEEE 181
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
371-643 |
3.45e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 371 DSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQnKEIDKQVRREKLDADKEGEKSKqfdLIALKQRELDGKQ 450
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL-KLLAKEEEELKSELLKLERRKV---DDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 451 NELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARDEELTSLQAERDeevapLVAGLERETGILNELIAEREELEA 530
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE-----LLAKKKLESERLSSAAKLKEEELE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 531 synehhTRAEGHNNVLENSEtmLSDLDEQINAARTKLEATKKKAEQvaKDTEAFKKNHETQFASLTAQNATLLAQHQKLE 610
Cdd:pfam02463 399 ------LKSEEEKEAQLLLE--LARQLEDLLKEEKKEELEILEEEE--ESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
250 260 270
....*....|....*....|....*....|...
gi 238031448 611 AERDQLIKKHDDTVAELQDAKLKGLQEDKAVNS 643
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
405-617 |
3.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 405 QKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQRELDGKQNELDESVQEdqkiREALVLEKTNLEEKIST-EAA 483
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE----LEELEAELEELREELEKlEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 484 QRKQARDEELTSLQAERdEEVAPLVAGLERETGILNELIAEREELEASYNEHHTRAEGHNNVLenSETMLSDLdEQINAA 563
Cdd:COG4717 125 LQLLPLYQELEALEAEL-AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEEL-QDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 238031448 564 RTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKLEAERDQLI 617
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
378-647 |
3.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 378 RQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQrELDgkqnELDESV 457
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEA-EIE----DLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 458 QEDQKIREALVLEKTNLEEKISTEAAQRKQARDE-ELTSLQAERDEEvaplvaglEREtgilnELIAEREELEASYNEHH 536
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEaGLDDADAEAVEA--------RRE-----ELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 537 TRAEGHNNVLENSETMLSDLDEQINAARTK---LEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATLLAQHQKLEAER 613
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270
....*....|....*....|....*....|....*.
gi 238031448 614 DQLIKKHDDTVAELQD--AKLKGLQEDKAVNSILPE 647
Cdd:PRK02224 415 EELREERDELREREAEleATLRTARERVEEAEALLE 450
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
377-622 |
3.78e-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: 44.19 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 377 QRQQDEQNAQKKLEQKQRKLQYEE---------ELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQfdliaLKQRELD 447
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERvrehalsirVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ-----TLLRELE 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 448 GKQNELDESVQEDQKIREALvleKTNLEEKISTEAAQRKQARDEELTSLQA-ERDEEVAPLVAGLERETGI-LNELIAE- 524
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSL---GSDLAAREDALNQSLKELMHQARTVLKArTEAHFNNNEEVTAALQTGAeLSHLAAEi 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 525 ---REELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAAR----TKLEATKKKAEQVAKDTEAFKKNHEtQFASLTA 597
Cdd:TIGR00618 788 qffNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEeqflSRLEEKSATLGEITHQLLKYEECSK-QLAQLTQ 866
|
250 260
....*....|....*....|....*
gi 238031448 598 QNATLLAQHQKLEAERDQLIKKHDD 622
Cdd:TIGR00618 867 EQAKIIQLSDKLNGINQIKIQFDGD 891
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
379-550 |
5.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 379 QQDEQNAQKKLEQKQRKLQYEEELRKQkLEEKQNKEIDKQVRREKLDadKEGEKSKQFDLIALKQRELDGKQNELDESVQ 458
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 459 EDQKIREALvlektNLEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHTR 538
Cdd:COG4717 154 RLEELRELE-----EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170
....*....|..
gi 238031448 539 AEGHNNVLENSE 550
Cdd:COG4717 229 LEQLENELEAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-530 |
5.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 366 VVQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQfdlIALKQRE 445
Cdd:COG4913 277 LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE---IERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 446 LDGKQNELDESVQEDQKIREALVLEKTNLEEkISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERetgiLNELIAER 525
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAA-LRAEAAALLEALEEELEALEEALAEAEAALRDLRRE----LRELEAEI 428
|
....*
gi 238031448 526 EELEA 530
Cdd:COG4913 429 ASLER 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
360-619 |
5.88e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 360 QQLVGPVVQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYE-EELRKQKLE-EKQNKEIDKQVRREKLDADKEGEKSKQFD 437
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVlEETQERINRARKAAPLAAHIKAVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 438 LIALKQrELDGKQNELDES-------VQEDQKIREALVLEKTNLEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAG 510
Cdd:TIGR00618 309 AQRIHT-ELQSKMRSRAKLlmkraahVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 511 LERETGILNELIAEREELEasyNEHHTRAEGHNNvlensetmLSDLDEQINAARTKLEATKKKAEQVAKDTeafkknhET 590
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQ---REQATIDTRTSA--------FRDLQGQLAHAKKQQELQQRYAELCAAAI-------TC 449
|
250 260
....*....|....*....|....*....
gi 238031448 591 QFASLTAQNATLLAQHQKLEAERDQLIKK 619
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
367-661 |
5.91e-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: 43.56 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 367 VQQIDSKAALQRQQDEQNAQKK----LEQKQRKLQYEEELRKQKLEEKQNKEIDK---QVRREKLDADKEGEKSKQFDli 439
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKticQLTEEKEAQMEELNKAKAAH-- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 440 ALKQRELDGKQNELDESVQEDQKirealVLEKTNLEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGL-ERETgil 518
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQ-----RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILaEDEK--- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 519 neLIAEREELEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKknhetqfasltAQ 598
Cdd:pfam05483 420 --LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK-----------LK 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238031448 599 NATLLAQHQKLEAERDQLIKKHDDTVAElqdakLKGLQEDKAVNSILPEHLQEDIKDTVSVET 661
Cdd:pfam05483 487 NIELTAHCDKLLLENKELTQEASDMTLE-----LKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
383-613 |
7.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 383 QNAQKKLEQKQRKLQY-EEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQRELDGKQNELD------- 454
Cdd:COG4913 606 FDNRAKLAALEAELAElEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELErldassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 455 ------ESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARdEELTSLQAERDEEVAPLVAGLeretgilneliaeREEL 528
Cdd:COG4913 686 dlaaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAE-EELDELQDRLEAAEDLARLEL-------------RALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 529 EASYNEHHTRaeghnnvlENSETMLSDLDEQINAARTKLEatkKKAEQVAKDTEAFKKNHETQFASLTAQNATL---LAQ 605
Cdd:COG4913 752 EERFAAALGD--------AVERELRENLEERIDALRARLN---RAEEELERAMRAFNREWPAETADLDADLESLpeyLAL 820
|
....*...
gi 238031448 606 HQKLEAER 613
Cdd:COG4913 821 LDRLEEDG 828
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
367-540 |
7.76e-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: 43.19 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 367 VQQIDSKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKqvRREKLDADKEGEKSKQFDliALKQREL 446
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER--KRKKLELEKEKRDRKRAE--EQRRKIL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 447 DGKQNELDESVQEDQKIREALVLEKTNLEEKISTEAaQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAERE 526
Cdd:pfam17380 498 EKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
170
....*....|....
gi 238031448 527 ELEASYNEHHTRAE 540
Cdd:pfam17380 577 MMRQIVESEKARAE 590
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
386-619 |
8.52e-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: 42.80 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 386 QKKLEQKQRKLQYE----EELRKQKleEKQNKEIDKQVRREKLDADKEGEKSKQFDLIALKQRELDGKQNELDESVQEDQ 461
Cdd:pfam17380 281 QKAVSERQQQEKFEkmeqERLRQEK--EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 462 KiREAlvlektnleEKISTEAAQRKQARDEELTSLQAERDEEvaplvagleretgilNELIaeREELEASYNEHHTRAEG 541
Cdd:pfam17380 359 K-REL---------ERIRQEEIAMEISRMRELERLQMERQQK---------------NERV--RQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238031448 542 HNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLTAQNATllAQHQKLEAERDQLIKK 619
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE--RKRKKLELEKEKRDRK 487
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
367-593 |
9.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 367 VQQIDSKAALQRQQDE-----QNAQKKLEQKQRKLQYEEELR--KQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLI 439
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEakkkaEEAKKKADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 440 ALKQRELDgKQNELDESVQEDQKIREALvleKTNLEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILN 519
Cdd:PTZ00121 1384 KKKAEEKK-KADEAKKKAEEDKKKADEL---KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238031448 520 ELIAEREELEASYNEHHTRAEGHNNVLEnsetmlsdldeqinaARTKLEATKKKAEQVAKDTEAFKKNHETQFA 593
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADE---------------AKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
370-476 |
1.20e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 370 IDSKAALQRQQDEQNAQ------------KKLEQKQRKLQYEEELRKQKLEEKQNKEIdKQVRREKLDADKEGEKSKQFD 437
Cdd:PRK00409 522 IASLEELERELEQKAEEaeallkeaeklkEELEEKKEKLQEEEDKLLEEAEKEAQQAI-KEAKKEADEIIKELRQLQKGG 600
|
90 100 110
....*....|....*....|....*....|....*....
gi 238031448 438 LIALKQRELDGKQNELDESVQEDQKIREALVLEKTNLEE 476
Cdd:PRK00409 601 YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-630 |
1.64e-03 |
|
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: 41.67 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 374 AALQRQQDEQNAQKKLEQKQRKLQYEEelrkQKLEEKQNKEIDKQVRREKLDAdkegEKSKQFDLIALKQRELDGKQNEL 453
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 454 DESVQEDQKIREALVLEKTNLEEKISteAAQRKQARDEELTSLQAERdeevaplVAGLERETGILNELIAEREELEasyn 533
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPED-------FLDAVRRLQYLKYLAPARREQA---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 534 ehhtraeghnnvlensetmlsdldEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQFASLtaqnATLLAQHQKLEAER 613
Cdd:COG4942 153 ------------------------EELRADLAELAALRAELEAERAELEALLAELEEERAAL----EALKAERQKLLARL 204
|
250
....*....|....*..
gi 238031448 614 DQLIKKHDDTVAELQDA 630
Cdd:COG4942 205 EKELAELAAELAELQQE 221
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
377-664 |
2.16e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 377 QRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQNKE---------IDKQVRREKLDADKEGEKSKQFDLIALKQRELD 447
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeleeeyllyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 448 GKQNELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQARDEELTSLqaERDEEVAPLVAGLERETGILNELIAEREE 527
Cdd:pfam02463 262 KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV--DDEEKLKESEKEKKKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 528 LEASYNEHHTRAEghnnVLENSETMLSDLDEQINAARTKLEATKKKAEQvAKDTEAFKKNHETQFASLTAQNATLLAQH- 606
Cdd:pfam02463 340 LEKELKELEIKRE----AEEEEEEELEKLQEKLEQLEEELLAKKKLESE-RLSSAAKLKEEELELKSEEEKEAQLLLELa 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 238031448 607 QKLEAERDQLIKKHDDTVAELQDAKLKGLQEDKAVNSILPEHLQEDIKDTVSVETPFD 664
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
377-514 |
3.82e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 377 QRQQDEQNAQKKLEQKQRKLQY---EEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQfdlialKQRELDGKQNEL 453
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEkleAALLEAKELLLRERNQQRQEARREREELQREEERLVQ------KEEQLDARAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238031448 454 DEsvQEDQKIREALVLEKTNLE--------EKISTEAAQ--RKQARDEELTSLQAERDEEVAPLVAGLERE 514
Cdd:PRK12705 101 DN--LENQLEEREKALSARELEleelekqlDNELYRVAGltPEQARKLLLKLLDAELEEEKAQRVKKIEEE 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-689 |
3.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 373 KAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQ---KLEEKQNKEIDKQVRREKLDAD--KEGEKSKQFDLIALKQRELD 447
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEearKAEDAKKAEAVKKAEEAKKDAEeaKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 448 GKQNELDESVQEDQKiREALVLEKTNlEEKISTEAAQRKQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREE 527
Cdd:PTZ00121 1263 AHFARRQAAIKAEEA-RKADELKKAE-EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 528 LEASYNEHHTRAEGHNNVLENSETMLSDLDEQINAARTKLEATKKKAEQVAKDTEAFKKNHETQfasltaQNATLLAQHQ 607
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK------KKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 608 KLEAERDQLIKKHDDtVAELQDAKLKGLQEDKAvnsilpEHLQEDIKDTVSVETPFDHSKFKFEPEPFVEESVEQKKPES 687
Cdd:PTZ00121 1415 AAKKKADEAKKKAEE-KKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
..
gi 238031448 688 PK 689
Cdd:PTZ00121 1488 AK 1489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
402-638 |
4.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 402 LRKQKLEEKQNKEIDKQVRREKLdadkegEKSKQFDLIALKQRELDGKQNELDESVQEDQKIREALVlEKTNLEEKISTE 481
Cdd:COG4717 294 AREKASLGKEAEELQALPALEEL------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR-EAEELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 482 AAQrkQARDEELTSLQAERDEEVAPLVAGLERETGILNELIAEREELEASYNEHHTRAEGHNNV-----LENSETMLSDL 556
Cdd:COG4717 367 ELE--QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeeLEELEEELEEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 557 DEQINAARTKLEATKKKAEQVAKDTEAFKKNHEtqFASLTAQNATLLAQHQKLEAERDQLikkhDDTVAELQDAKLKGLQ 636
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGELAELLQE--LEELKAELRELAEEWAALKLALELL----EEAREEYREERLPPVL 518
|
..
gi 238031448 637 ED 638
Cdd:COG4717 519 ER 520
|
|
| Selenoprotein_S |
pfam06936 |
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ... |
366-409 |
4.65e-03 |
|
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.
Pssm-ID: 462043 [Multi-domain] Cd Length: 192 Bit Score: 39.05 E-value: 4.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 238031448 366 VVQQIDSKAALQRQQDEQNAQ-KKLEQKQRKLqyEEELRKQKLEE 409
Cdd:pfam06936 79 VKRQEALEASRLRMQEELDAQaEKFKEKQKQL--EEEKRRQKIEM 121
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
372-651 |
5.05e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 372 SKAALQRQQDEQNAQKKLEQKQRKLQYEEELRKQKLEEKQ-NKEID-------------KQVRREKLDADKEGEKSKQfd 437
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhNEEAEslredaddleeraEELREEAAELESELEEARE-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 438 liALKQREldGKQNELDESVQEDQK--------------IREALVLEKTNLEEKISTEAAQRKQARD--EELTSLQAE-- 499
Cdd:PRK02224 378 --AVEDRR--EEIEELEEEIEELRErfgdapvdlgnaedFLEELREERDELREREAELEATLRTARErvEEAEALLEAgk 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 500 -----RDEEVAPLVAGLERETGILNELIAEREELE---ASYNEHHTRAEGHNNV---LENSETMLSDLDEQINAARTKLE 568
Cdd:PRK02224 454 cpecgQPVEGSPHVETIEEDRERVEELEAELEDLEeevEEVEERLERAEDLVEAedrIERLEERREDLEELIAERRETIE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 569 ATKKKAEQVAK-----DTEAFKKNHETQFASLTAQN-----ATLLAQHQKLEAERDQL--IKKHDDTVAELQDA------ 630
Cdd:PRK02224 534 EKRERAEELREraaelEAEAEEKREAAAEAEEEAEEareevAELNSKLAELKERIESLerIRTLLAAIADAEDEierlre 613
|
330 340
....*....|....*....|.
gi 238031448 631 KLKGLQEdkaVNSILPEHLQE 651
Cdd:PRK02224 614 KREALAE---LNDERRERLAE 631
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
365-579 |
9.31e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.55 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 365 PVVQQIDSKAALQRQQDEQNAQKKL-EQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKEGEKSKQFDLIAL-K 442
Cdd:pfam15709 314 ERSEEDPSKALLEKREQEKASRDRLrAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLrK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 443 QReldgkqneldesvQEDQKIREALVLEKTNLEEKISTEAAQRKQAR-DEELTSLQAERDEEVAPLVAGLERETGILNEL 521
Cdd:pfam15709 394 QR-------------LEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238031448 522 IAEREELEASYNEHHtRAEGHNNVLENSETMLSDLDE----QINAARTKLEATKKKAEQVAK 579
Cdd:pfam15709 461 LAEEQKRLMEMAEEE-RLEYQRQKQEAEEKARLEAEErrqkEEEAARLALEEAMKQAQEQAR 521
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
367-507 |
9.56e-03 |
|
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: 38.75 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 367 VQQIDSK-AALQRQQDE-----QNAQKKLEQKQRKLQYEEELRKQKLEEKQNKEIDKQVRREKLDADKE----GEKSKQF 436
Cdd:COG1579 12 LQELDSElDRLEHRLKElpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238031448 437 -------DLIALKQRELDGKQNELDESVQEDQKIREALVLEKTNLEEKISTEAAQRKQAR---DEELTSLQAERDEEVAP 506
Cdd:COG1579 92 ealqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELaelEAELEELEAEREELAAK 171
|
.
gi 238031448 507 L 507
Cdd:COG1579 172 I 172
|
|
| |
