|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-586 |
1.22e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 244 QQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQ 323
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELR-LELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 324 ADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEELGAV 403
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-AELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 404 RLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEE 483
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 484 SLLQQEQEQEETLKQCRE-----QHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQevkdtVDGQRILEKKGSA 558
Cdd:COG1196 454 LEEEEEALLELLAELLEEaalleAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL-----LAGLRGLAGAVAV 528
|
330 340
....*....|....*....|....*...
gi 1958806473 559 VLKDLKRqlhLERKRADKLQERLQEILT 586
Cdd:COG1196 529 LIGVEAA---YEAALEAALAAALQNIVV 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-481 |
4.56e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 190 LKWEMEREEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRKEAdLKAQLARTQKLQQELEAAN 269
Cdd:COG1196 232 LKLRELEAELEELEAELE--ELEAELEELEAELAELEAELEEL----RLELEELELELEE-AQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 270 QSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNmLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSR 349
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 350 LLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL--AMETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHE 427
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLeeELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806473 428 DKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG-AKGWFERRLKEA 481
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGfLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-601 |
2.49e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 57 KALSKSKKAQEVEVLLSEKEMLQAKLHSQEEDFRLQNstlmAEFSKLCSQLEQLELENRQLKEgvpgaagphvdgELLRL 136
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRL------------ELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 137 QAENTALQKNMAALQERYGKEavrpsavsEGQGDPpgdvlpislspmplaEVELKWEMEREEKKLLWEQLQGLELSEKLK 216
Cdd:COG1196 280 ELELEEAQAEEYELLAELARL--------EQDIAR---------------LEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 217 KKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgeRLEHAAALRALQDQ 296
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA--QLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 297 IQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAE 376
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 377 KRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYEREL------------RELHEDKKRQEEELRGQ----- 439
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqnivVEDDEVAAAAIEYLKAAkagra 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 440 --IREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKqcREQHAAELKGKEEELQNV 517
Cdd:COG1196 575 tfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA--ALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 518 RDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEEL 597
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
....
gi 1958806473 598 VLSE 601
Cdd:COG1196 733 EREE 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-586 |
1.39e-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: 62.00 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 259 QKLQQELEAANQsLAELRDQ-RQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLN 337
Cdd:TIGR02168 203 KSLERQAEKAER-YKELKAElRELELALLVLRLEELREELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 338 SQLQEslrANSRLLEQLQEMgQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHE---KEMLGV 414
Cdd:TIGR02168 281 EEIEE---LQKELYALANEI-SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 415 RARYErELRELHEDKKRQEEELRGQIREEKARTRELEN----LQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQ 490
Cdd:TIGR02168 357 EAELE-ELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 491 EQEETLKQCREQHAAELKGK----EEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVlkdlkRQ 566
Cdd:TIGR02168 436 KELQAELEELEEELEELQEElerlEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-----KA 510
|
330 340
....*....|....*....|
gi 1958806473 567 LHLERKRADKLQERLQEILT 586
Cdd:TIGR02168 511 LLKNQSGLSGILGVLSELIS 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-542 |
1.40e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 251 LKAQLartQKLQQELEAAN--QSLAELRDQRQGERLehAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEE 328
Cdd:COG1196 198 LERQL---EPLERQAEKAEryRELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 329 LMGQKDDLNSQLQESLRANSRLLEQLQEMGQEK---EQLIQDLQEARKSAEKRKVMLDElAMETLQEKSQHKEELGAVRL 405
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAELEE-ELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 406 RHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESL 485
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806473 486 LQQEQEQEETLKQcREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEV 542
Cdd:COG1196 431 AELEEEEEEEEEA-LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-472 |
8.92e-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: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 185 LAEVELKWEMEREEKKLLWEQLQGLELS-EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE------ADLKAQLAR 257
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 258 TQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLN 337
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 338 SQLQEslraNSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLgvrar 417
Cdd:TIGR02168 400 NEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL----- 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806473 418 yeRELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKG 472
Cdd:TIGR02168 471 --EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-467 |
2.43e-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: 56.70 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 253 AQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQiqtakTQELNMLREQNTELAAELKHRQADYEELMGQ 332
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 333 KDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELA------METLQEKSQHKEELGAVRLR 406
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806473 407 HEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSM 467
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-575 |
2.97e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 28 SDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQL 107
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 108 EQLELENRQLKEGVPGAAGPHVDGELLRLQAEntalQKNMAALQERYGKEAVRpsavsegqgdppgdvlpislspmplAE 187
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK-------------------------AD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 188 VELKWEMEREEKKLLWEQLQGLELSEKLKKKQESfCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEA 267
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 268 AnqslaelrdqRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESlRAN 347
Cdd:PTZ00121 1527 A----------KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 348 SRLLEQLQEMGQEKEQLIQDlQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRAryeRELRELHE 427
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA---AEEAKKAE 1671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 428 DKKRQEEELRgqiREEKARTRELENLQHTVEElqaqvhsmdgAKGWFERRLKEAEESLLQQEQEQEETLkqcREQHAAEL 507
Cdd:PTZ00121 1672 EDKKKAEEAK---KAEEDEKKAAEALKKEAEE----------AKKAEELKKKEAEEKKKAEELKKAEEE---NKIKAEEA 1735
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806473 508 KGKEEELQNVRDQLQQAQEERdghvKTISNLKQEVKDTVDGQRileKKGSAVL------KDLKRQLHLERKRAD 575
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKKAEEIR---KEKEAVIeeeldeEDEKRRMEVDKKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-584 |
3.82e-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: 57.37 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 278 QRQGERLEHAAALRALQDQIqTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEM 357
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 358 GQEKEQLIQDLQEARKSAEKrkvmldelAMETLQEKSQHKEELGAVRLRHEKEMLGVRARY---ERELRELHEDKKRQEE 434
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEE--------AEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 435 ELRGQIREEKARTRELENLQHTVEELQAQVhsmdgakgwferrlkeaeesllqqeqeqeetlkqcrEQHAAELKGKEEEL 514
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDI------------------------------------ESLAAEIEELEELI 868
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 515 QNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKgsavLKDLKRQLHLERKRADKLQERLQEI 584
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESK----RSELRRELEELREKLAQLELRLEGL 934
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-422 |
4.66e-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: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 210 ELSEKLKKKQESFCRLQTEKETlFNDSRNKIEELQQRKEA-DLKAQLARTQKLQQELEAANQSLAELRDQR---QGERLE 285
Cdd:COG4913 242 EALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELerlEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 286 HAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLI 365
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806473 366 QDLQEARKSAEKRKvmldELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYEREL 422
Cdd:COG4913 401 EALEEALAEAEAAL----RDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-584 |
4.69e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKkaQEVEVLLSEKEMLQAKLHSQE 86
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL--AELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 87 EdfrlQNSTLMAEFSKLCSQLEQLELENRQLKEgvpgaagphvdgELLRLQAENTALQKNMAALQERYGKEAVRPSAVSE 166
Cdd:COG1196 316 E----RLEELEEELAELEEELEELEEELEELEE------------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 167 gqgdppgdvlpislspmplAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQR 246
Cdd:COG1196 380 -------------------ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL-EEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 247 KEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADY 326
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 327 EELMGQKDDLNSQLQESLRA-NSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRL 405
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAAlEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 406 RhekemlgvRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG--AKGWFERRLKEAEE 483
Cdd:COG1196 600 A--------VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGgsAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 484 SLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDL 563
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|.
gi 1958806473 564 KRQLHLERKRADKLQERLQEI 584
Cdd:COG1196 752 ALEELPEPPDLEELERELERL 772
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
235-580 |
1.49e-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: 55.46 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 235 DSRNKIEELQQR-KEADLKAQLARTQ--KLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQT------AKTQEL 305
Cdd:TIGR02169 174 KALEELEEVEENiERLDLIIDEKRQQleRLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAierqlaSLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 306 NMLREQNTELAAELKHRQADYEELMGQKDDLNS----QLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEkrkvm 381
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE----- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 382 ldELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARyERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQ 461
Cdd:TIGR02169 329 --AEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 462 AQvhsmdgakgwfERRLKEAEESLLQQEQEQEETLKQCREQHA---AELKGKEEELQNVRDQLQQAQEERDGHVKTISNL 538
Cdd:TIGR02169 406 RE-----------LDRLQEELQRLSEELADLNAAIAGIEAKINeleEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958806473 539 KQEvkdtvdgQRILEKKgsavLKDLKRQLHLERKRADKLQER 580
Cdd:TIGR02169 475 KEE-------YDRVEKE----LSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-450 |
4.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 37 ELSSLRQKVAYLdkefskAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQ 116
Cdd:TIGR02168 678 EIEELEEKIEEL------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 117 lkegvpgaagphvdgellrLQAENTALQKNMAALQERYGKEAVRPSAVSEGqgdppgdvlpislspmpLAEVELKWEMER 196
Cdd:TIGR02168 752 -------------------LSKELTELEAEIEELEERLEEAEEELAEAEAE-----------------IEELEAQIEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 197 EEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLFNDSRNK---IEELQQRKE------ADLKAQLARTQKLQQELEA 267
Cdd:TIGR02168 796 EELKALREALD--ELRAELTLLNEEAANLRERLESLERRIAATerrLEDLEEQIEelsediESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 268 ANQSLAELRDQRQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRAN 347
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 348 srlleqLQEMGQEKEQLIQDLQEARKSAEKrkvmldelametLQEKsqhKEELGAVRLRHEKEMLGVRARYErELRELHE 427
Cdd:TIGR02168 953 ------LEEAEALENKIEDDEEEARRRLKR------------LENK---IKELGPVNLAAIEEYEELKERYD-FLTAQKE 1010
|
410 420
....*....|....*....|...
gi 1958806473 428 DKKRQEEELRGQIREEKARTREL 450
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEIDREARER 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-468 |
8.42e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 248 EADLKAQLARTQKLQQELEAANQSLAELRDQR--------QGERLEHAAALRALQDQIQTA-----KTQELNMLREQNTE 314
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIellepireLAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 315 LAAELKHRQADYEELMGQKDDLNSQLQEslransrLLEQLQEM-GQEKEQLIQDLQEARKSAEKRKVMLDELAmetlqek 393
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDE-------LEAQIRGNgGDRLEQLEREIERLERELEERERRRARLE------- 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806473 394 sQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMD 468
Cdd:COG4913 366 -ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
211-410 |
9.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 211 LSEKLKKKQESFCRLQTEKETLFNDsrnKIEELQQRKEAdLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAAL 290
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLK---ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 291 RALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQEslrANSRLLEQLQEMGQEKEQLIQDLQE 370
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958806473 371 ARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 410
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
239-410 |
2.56e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 239 KIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAalRALQDQIqTAKTQELNMLREQNT---EL 315
Cdd:NF012221 1566 RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEES--RAVTKEL-TTLAQGLDALDSQATyagES 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 316 AAELKHRQAD------YEELMGQKDDLNSQLQESLRANSRLLEQLQ------EMGQEK-EQLI----QDLQEARKSAEKR 378
Cdd:NF012221 1643 GDQWRNPFAGglldrvQEQLDDAKKISGKQLADAKQRHVDNQQKVKdavaksEAGVAQgEQNQanaeQDIDDAKADAEKR 1722
|
170 180 190
....*....|....*....|....*....|....
gi 1958806473 379 KvmLDELAMETLQEKSQHKEELGA--VRLRHEKE 410
Cdd:NF012221 1723 K--DDALAKQNEAQQAESDANAAAndAQSRGEQD 1754
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
213-399 |
4.05e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 50.10 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 213 EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRA 292
Cdd:pfam03528 11 AELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVATVSENT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 293 LQDQIQTAKTQelnmLREQNTELAAELKHRQADYE----ELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDL 368
Cdd:pfam03528 91 KQEAIDEVKSQ----WQEEVASLQAIMKETVREYEvqfhRRLEQERAQWNQYRESAEREIADLRRRLSEGQEEENLEDEM 166
|
170 180 190
....*....|....*....|....*....|...
gi 1958806473 369 QEARKSAEKRK--VMLDELAMETLQEKSQHKEE 399
Cdd:pfam03528 167 KKAQEDAEKLRsvVMPMEKEIAALKAKLTEAED 199
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-449 |
8.46e-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: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 196 REEKKLLWEQLQ--GLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQELEA 267
Cdd:TIGR02169 250 EEELEKLTEEISelEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslERSIAEKERELEDAEERLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 268 ANQSLAELRDQRQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRAN 347
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELK-EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 348 SRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHE 427
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
250 260
....*....|....*....|..
gi 1958806473 428 dKKRQEEELRGQIREEKARTRE 449
Cdd:TIGR02169 488 -LQRELAEAEAQARASEERVRG 508
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
256-443 |
1.32e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 256 ARTQKLQQELEAANQSLAELrdQRQGERLEH----AAALR-------ALQDQIQTAKtQELNMLREQN---TELAAELKH 321
Cdd:COG3096 893 DRLEELREELDAAQEAQAFI--QQHGKALAQleplVAVLQsdpeqfeQLQADYLQAK-EQQRRLKQQIfalSEVVQRRPH 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 322 -RQADYEELMGQKDDLNSQLQESLR----ANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQ----- 391
Cdd:COG3096 970 fSYEDAVGLLGENSDLNEKLRARLEqaeeARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqa 1049
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806473 392 ----------EKSQHKEELGAVRLRhEKEMLGVRARYERELRELHEDKKRQEEELRgQIREE 443
Cdd:COG3096 1050 daeaeerariRRDELHEELSQNRSR-RSQLEKQLTRCEAEMDSLQKRLRKAERDYK-QEREQ 1109
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-457 |
1.36e-05 |
|
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: 48.91 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 210 ELSEKLKKKQESFCRLQTEKETLFND-SRNKIEELQQRKEaDLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAA 288
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELS-KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 289 ALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEMGQEKEQLI 365
Cdd:TIGR02169 841 QRIDLKEQIKSIE-KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKErdeLEAQLRELERKIEELEAQIEKKRKRL 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 366 QDLQEARKSAEKRkvmLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRAR------------YERELRELHEDKKRQE 433
Cdd:TIGR02169 920 SELKAKLEALEEE---LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiqeYEEVLKRLDELKEKRA 996
|
250 260
....*....|....*....|....*.
gi 1958806473 434 --EELRGQIREekaRTRELENLQHTV 457
Cdd:TIGR02169 997 klEEERKAILE---RIEEYEKKKREV 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-378 |
1.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 185 LAEVELKWEMEREEKKLLWEQLQGLE-----LSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQ 259
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALErriaaLARRIRALEQELAALEAELAEL-EKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 260 KL-----------QQELEAANQSLAELRDQRQgERLEHAAALRALQDQIQtAKTQELNMLREQNTELAAELKHRQADYEE 328
Cdd:COG4942 115 RLgrqpplalllsPEDFLDAVRRLQYLKYLAP-ARREQAEELRADLAELA-ALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958806473 329 LMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKR 378
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
243-464 |
2.32e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 243 LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHR 322
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 323 QADYEELMGQKDDLNSQLQESlRANSRLLEQLQEMGQEKEQLIQDLQEarksaekrkvmlDELAMETLQeksqhkEELGA 402
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTP------------NHPDVIALR------AQIAA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806473 403 VRLRHEKEMLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 464
Cdd:COG3206 303 LRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-609 |
3.50e-05 |
|
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: 47.37 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 356 EMGQEKEQLIQDLQEARKSAEKRKVMLDELA--METLQEKSQHKEELGAVRLRHEkemlgvraryERELRELHEDKKRQE 433
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKR----------EYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 434 EELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEE 513
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 514 LQNVRDQLQQAQEERDGHVKTISNLKQEVKDtvdgQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTG 593
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250
....*....|....*.
gi 1958806473 594 LEELVLSEMNSPSRTQ 609
Cdd:TIGR02169 393 KLEKLKREINELKREL 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-459 |
3.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 196 REEKKLLWEQLQGLElsEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEAD-----LKAQLARTQKLQQELEAANQ 270
Cdd:COG4913 609 RAKLAALEAELAELE--EELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEidvasAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 271 SLAELRDQrqgerlehaaaLRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRAnsRL 350
Cdd:COG4913 686 DLAALEEQ-----------LEELEAELEELE-EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 351 LEQLQEMGQEK--EQLIQDLQEARKSAEKRkvmLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRArYERELRELHED 428
Cdd:COG4913 752 EERFAAALGDAveRELRENLEERIDALRAR---LNRAEEELERAMRAFNREWPAETADLDADLESLPE-YLALLDRLEED 827
|
250 260 270
....*....|....*....|....*....|..
gi 1958806473 429 K-KRQEEELRGQIREEKarTRELENLQHTVEE 459
Cdd:COG4913 828 GlPEYEERFKELLNENS--IEFVADLLSKLRR 857
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-557 |
4.76e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 287 AAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQ 366
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 367 DLQEARKSAEKRKVMLDELaMETLQEKSQHKEELGAVRLRHEKEMLgVRARYereLRELHEDKKRQEEELRGQIREEKAR 446
Cdd:COG4942 91 EIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 447 TRELENLQHTVEELQAQVhsmdgakgwfERRLKEAEESLLQqeqeqeetlkqcREQHAAELKGKEEELQNVRDQLQQAQE 526
Cdd:COG4942 166 RAELEAERAELEALLAEL----------EEERAALEALKAE------------RQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|.
gi 1958806473 527 ERDGHVKTISNLKQEVKDTVDGQRILEKKGS 557
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
308-584 |
8.11e-05 |
|
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: 46.21 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 308 LREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAM 387
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 388 ETLQEKSQHKE--------ELGAVRLRHEKEMLGVRARYER------ELRELHEDKKRQEEELRGQIREEKARTRELENL 453
Cdd:TIGR02169 752 EIENVKSELKElearieelEEDLHKLEEALNDLEARLSHSRipeiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 454 QHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREqHAAELKGKEEELQNVRDQLQQAQEERDGHVK 533
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD-LESRLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958806473 534 TISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHL--ERKRADKLQERLQEI 584
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeEELSLEDVQAELQRV 963
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-370 |
8.25e-05 |
|
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: 46.21 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 7 EEEFQRMQTQLLELRTnnyqlsdelrkngvELSSLRQKVAYLDKEFSKAQKALSKSKKaqEVEVLLSEKEMLQAKLHSQE 86
Cdd:TIGR02169 673 PAELQRLRERLEGLKR--------------ELSSLQSELRRIENRLDELSQELSDASR--KIGEIEKEIEQLEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 87 EdfrlqnstlmaefsklcsQLEQLELENRQLKEGVpgaagPHVDGELLRLQAENTALQKNMAALQERYGKeavrpsavse 166
Cdd:TIGR02169 737 E------------------RLEELEEDLSSLEQEI-----ENVKSELKELEARIEELEEDLHKLEEALND---------- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 167 gqgdppgdvLPISLSPMPLAEVELKWEMEREEKKLLWEQLQGLELS-EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ 245
Cdd:TIGR02169 784 ---------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 246 RKEaDLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQelnmlREQNTELAAELKHRQAD 325
Cdd:TIGR02169 855 EIE-NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ-----IEKKRKRLSELKAKLEA 928
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958806473 326 YEELMGQKDDLNSQLQESlRANSRLLEQLQEMGQEKEQLIQDLQE 370
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
187-322 |
1.28e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 187 EVELKWEMEREEKKLLWEQlqglELSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQrKEADLKAQLARTQKLQQELE 266
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEK----ELRERRNELQKLEKRLLQKEENL----DRKLELLEK-REEELEKKEKELEQKQQELE 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806473 267 AANQSLAELRDQRQgERLEHAAALRALQdqiqtAKTQELNMLREQNTELAAELKHR 322
Cdd:PRK12704 128 KKEEELEELIEEQL-QELERISGLTAEE-----AKEILLEKVEEEARHEAAVLIKE 177
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-462 |
1.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 185 LAEVELKWEmEREEKKLLWEQLQGLELS-EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK---EADLKAQLARTQK 260
Cdd:PRK02224 484 LEDLEEEVE-EVEERLERAEDLVEAEDRiERLEERREDLEELIAERRETIEEKRERAEELRERAaelEAEAEEKREAAAE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 261 LQQELEAANQSLAELRDQRQ--GERLEHAAALRALQDQIqTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNS 338
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAelKERIESLERIRTLLAAI-ADAEDEIERLREKREALAELNDERRERLAEKRERKRELEA 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 339 QLQESLransrlleqlqemgqekeqlIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVrlrhekemlgvrary 418
Cdd:PRK02224 642 EFDEAR--------------------IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV--------------- 686
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958806473 419 ERELRELhedkkrqeEELRGQIREEKARTRELENLQHTVEELQA 462
Cdd:PRK02224 687 ENELEEL--------EELRERREALENRVEALEALYDEAEELES 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-442 |
2.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 2 AQALSEEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQ-EVEVLLSEKEMLQA 80
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeELEEALAELEEEEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 81 KLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEgvpgaagphvdgELLRLQAENTALQKNMAALQERYGKEAVR 160
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA------------ALAELLEELAEAAARLLLLLEAEADYEGF 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 161 PSAVSEGQGDPPGDVLPISLSPMPLAEVELKWEMEREEkkLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKI 240
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL--AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 241 EELQQRKEADLKAQLARtqklqqELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREqnTELAAELK 320
Cdd:COG1196 585 RAALAAALARGAIGAAV------DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE--VTLEGEGG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 321 HRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEEL 400
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958806473 401 GAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIRE 442
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-584 |
3.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 197 EEKKLLWEQLQglELSEKLKKKQESFCRLQtEKETLFNDSRNKIEELQQR-----KEADLKAQLARTQKLQQELEAANQS 271
Cdd:COG4717 71 KELKELEEELK--EAEEKEEEYAELQEELE-ELEEELEELEAELEELREElekleKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 272 LAELRDQRQgERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKddlnSQLQESLRANSRLL 351
Cdd:COG4717 148 LEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL----AELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 352 EQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKR 431
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 432 QEEELRGQIREEKARTRELENLqhtVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGK- 510
Cdd:COG4717 303 EAEELQALPALEELEEEELEEL---LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEa 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806473 511 ----EEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKG-SAVLKDLKRQLHLERKRADKLQERLQEI 584
Cdd:COG4717 380 gvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-395 |
4.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 210 ELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRD---------QRQ 280
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDAL-QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgeraralYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 281 GERLEHAAAL---RALQDQIQTAKTqeLNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEM 357
Cdd:COG3883 99 GGSVSYLDVLlgsESFSDFLDRLSA--LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958806473 358 GQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQ 395
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
216-589 |
4.65e-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: 43.80 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 216 KKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQD 295
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 296 QIQTAKTQE--LNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARK 373
Cdd:TIGR00618 387 QKTTLTQKLqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 374 SAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMlgvraryERELRELHEDKKRQeeelrgQIREEKARTRELENL 453
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC-------PLCGSCIHPNPARQ------DIDNPGPLTRRMQRG 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 454 QHTVEELQAQVHSMDGaKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVK 533
Cdd:TIGR00618 534 EQTYAQLETSEEDVYH-QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806473 534 TISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 589
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
197-529 |
5.00e-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: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 197 EEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKI------EELQQRKEADLKAQLARTQKLQQELEAANQ 270
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 271 SLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHR---QADYEELMGQKDDLNSQLQESLRAN 347
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRdelESVREEFIQKGDEVKCKLDKSEENA 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 348 SRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEK---SQHKEELGAVRLRHEK---EMLGVRARYERE 421
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgSAENKQLNAYEIKVNKlelELASAKQKFEEI 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 422 LRELH---EDKKRQEEELRGQIREEKARTRELENLQHTVE-----ELQAQVHSMDGAKGWFERRLKEaEESLLQQEQEQE 493
Cdd:pfam05483 656 IDNYQkeiEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEE-RDSELGLYKNKE 734
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958806473 494 ETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERD 529
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKE 770
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
193-578 |
5.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 193 EMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRKEAdlKAQLARTQKLQQELEAANQSL 272
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL----REELEKLEKLLQL--LPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 273 AELRDQRQgERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLE 352
Cdd:COG4717 149 EELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 353 QLQ--EMGQEKEQLIQDLQEAR----------------KSAEKRKVMLDELAM-----------ETLQEKSQHKEELGAV 403
Cdd:COG4717 228 ELEqlENELEAAALEERLKEARlllliaaallallglgGSLLSLILTIAGVLFlvlgllallflLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 404 RLRHEKEMLgVRARYERELRELHEDKKRQEEELRGQIR------------EEKARTRELENLQHTVEELQAQVHSMDGAK 471
Cdd:COG4717 308 QALPALEEL-EEEELEELLAALGLPPDLSPEELLELLDrieelqellreaEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 472 -----GWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTV 546
Cdd:COG4717 387 lraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420 430
....*....|....*....|....*....|..
gi 1958806473 547 DGQRILEKKgsAVLKDLKRQLHLERKRADKLQ 578
Cdd:COG4717 467 EDGELAELL--QELEELKAELRELAEEWAALK 496
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
235-527 |
6.19e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 235 DSRNKIEELQQRKEA---DLKAQLARTQKLQQELEAANQSLA----ELRDQRQGERLEhaAALRALqdqiqTAKTQELNM 307
Cdd:PRK04863 297 TSRRQLAAEQYRLVEmarELAELNEAESDLEQDYQAASDHLNlvqtALRQQEKIERYQ--ADLEEL-----EERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 308 LREQNTELAAELKHRQADYEElmgQKDDLNSQLQESLRAnsrlLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELam 387
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEE---EVDELKSQLADYQQA----LDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNA-- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 388 ETLQEKSQHKEELGAVRLRHEKEMLGV----RARYERELRELH--------EDKKRQEEELRGQIREEKARTRELENLQH 455
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVaqaaHSQFEQAYQLVRkiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806473 456 TVEELQAQVHSMDGAkgwfERRLKEAEESLLQQEQEQEETLKqCREQHAAELKGKEEELQNVRDQ---LQQAQEE 527
Cdd:PRK04863 521 RLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQ-LQEELEARLESLSESVSEARERrmaLRQQLEQ 590
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
189-580 |
8.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 189 ELKWEMEREEKKLLWEQLQGLElsEKLKKKQESFCRLQTEKETLfndsrnkieelQQRKEaDLKAQLARTQKLQQELEAA 268
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLE--SELAELDEEIERYEEQREQA-----------RETRD-EADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 269 NQSLAELRDQRQGERLEHAAALRALQDQIQTAKTqelnmLREQNTELAAELKHRQADYEELMGQKDDLNSQLQ------- 341
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEE-----LEEERDDLLAEAGLDDADAEAVEARREELEDRDEelrdrle 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 342 -------------ESLRANSRLLE-QLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL-------------AMETLQEKS 394
Cdd:PRK02224 332 ecrvaaqahneeaESLREDADDLEeRAEELREEAAELESELEEAREAVEDRREEIEELeeeieelrerfgdAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 395 QHKEELGAVRLRHEKEMLGVRARYE------RELRELHEDKKRQE--------------EELRGQIREEKARTRELENLQ 454
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRtarervEEAEALLEAGKCPEcgqpvegsphvetiEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 455 HTVE----------ELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQcREQHAAELKGKEEELQNVRDQLQQA 524
Cdd:PRK02224 492 EEVEerleraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806473 525 QEErdghVKTISNLKQEVKDTVDGQRILEKKGSAvLKDLKRQLHLERKRADKLQER 580
Cdd:PRK02224 571 REE----VAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAEL 621
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
213-586 |
9.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 213 EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQrKEADLKAQLARTQKLQQELEAANQSLAELRDQ---RQGERLEHAAA 289
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISS-ELPELREELEKLEKEVKELEELKEEIEELEKElesLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 290 LRALQDQIQTAKtQELNMLREQNTELAaELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQ 369
Cdd:PRK03918 261 IRELEERIEELK-KEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 370 EARKSAEKRKVMLDELamETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRE 449
Cdd:PRK03918 339 RLEELKKKLKELEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 450 LENlqhTVEELQAQVHSMDGAKGW-----------FERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVR 518
Cdd:PRK03918 417 LKK---EIKELKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 519 ---------DQLQQAQEERDGH-VKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRA------DKLQERLQ 582
Cdd:PRK03918 494 eliklkelaEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAelekklDELEEELA 573
|
....
gi 1958806473 583 EILT 586
Cdd:PRK03918 574 ELLK 577
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
238-368 |
9.71e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 238 NKIEELQQ--RKEADLKAQLARTQKLQQELEAanqSLAELRDqrqgeRLEHAAALRALQDQIQTAKTQELNMLREQNTEL 315
Cdd:PRK09039 50 GKDSALDRlnSQIAELADLLSLERQGNQDLQD---SVANLRA-----SLSAAEAERSRLQALLAELAGAGAAAEGRAGEL 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806473 316 AAELKHRQADYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEMGQEKEQLIQDL 368
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
208-316 |
1.52e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 42.01 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 208 GLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQELEAANQSLAELRDqrqg 281
Cdd:PRK06975 341 GYALNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQasvhqlDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRD---- 416
|
90 100 110
....*....|....*....|....*....|....*
gi 1958806473 282 erlehaAALRALQDQIQTAKTQELNMlrEQNTELA 316
Cdd:PRK06975 417 ------DWMIAEVEQMLSSASQQLQL--TGNVQLA 443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-472 |
1.56e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 73 SEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEgvpgaagphvdgellRLQAENTALQKNMAALQE 152
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR---------------MYEDKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 153 RYGKEAVRPSAVSEGQGDPpGDVLPISLSPMPLAEVELkwEMEREEKKLLWEQLQGLELS------------------EK 214
Cdd:pfam15921 357 ELTEARTERDQFSQESGNL-DDQLQKLLADLHKREKEL--SLEKEQNKRLWDRDTGNSITidhlrrelddrnmevqrlEA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 215 LKKKQESFCRLQTEKETLFNDSRNKIEElqqrKEADLKAQLARTQKL-----------QQELEAANQSLAELRDQRQger 283
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAIQGKNESLE----KVSSLTAQLESTKEMlrkvveeltakKMTLESSERTVSDLTASLQ--- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 284 lEHAAALRALQDQIQT------AKTQELNMLREQNTelaaELKHRQADYEEL---MGQKDDLNSQLQESLRANSRLLEQ- 353
Cdd:pfam15921 507 -EKERAIEATNAEITKlrsrvdLKLQELQHLKNEGD----HLRNVQTECEALklqMAEKDKVIEILRQQIENMTQLVGQh 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 354 ---LQEMGQEKEQLIQDLQEARKSAEKRKVMLD--------------ELAMETLQEKSQHKEELGAVR-LRHEKEMLGVR 415
Cdd:pfam15921 582 grtAGAMQVEKAQLEKEINDRRLELQEFKILKDkkdakirelearvsDLELEKVKLVNAGSERLRAVKdIKQERDQLLNE 661
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806473 416 ARYER-ELRELHEDKKRQEEELRGQIREEKARTR----ELENLQHTVEELQAQVHSMDGAKG 472
Cdd:pfam15921 662 VKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQSELEQTRNTLKSMEGSDG 723
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
224-377 |
1.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 224 RLQTEKETLfNDSRNKIEELQQRK-----EADLKAQLARTQKLQQELEAANQSLAELRDQ----RQGERLEHAAALRALQ 294
Cdd:COG3206 183 QLPELRKEL-EEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARlaalRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 295 DQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLE-QLQEMGQEKEQLIQDLQEARK 373
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQLEA 341
|
....
gi 1958806473 374 SAEK 377
Cdd:COG3206 342 RLAE 345
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
237-463 |
3.23e-03 |
|
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: 40.78 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 237 RNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQ-----------RQGERLEHAAALRALQDQIQTAKTQEL 305
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSfsgssttdtglTKGSRFTHTEKLQFTNEAPAATSSPPT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 306 NMLREQNTElaaelKHRQADYEELMGQKDDLNS---QLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVML 382
Cdd:pfam05667 322 KVETEEELQ-----QQREEELEELQEQLEDLESsiqELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 383 --DELAMETLQEK----SQHKEELGAVRLRHEKEMLgvrARYeRELRELHEDKKRQEEELRGQIREEKARTRELENLQHT 456
Cdd:pfam05667 397 pdAEENIAKLQALvdasAQRLVELAGQWEKHRVPLI---EEY-RALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQ 472
|
....*..
gi 1958806473 457 VEELQAQ 463
Cdd:pfam05667 473 KEELYKQ 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
341-574 |
5.05e-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: 40.13 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 341 QESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHekemlgvrARYER 420
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--------AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 421 ELRELHEDKKRQEEELRGQIRE-EKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQc 499
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806473 500 rEQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRA 574
Cdd:COG4942 170 -EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
226-544 |
6.06e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 226 QTEKETLFNDSRNKIEELQQRKEADL-----KAQLARTQ--KLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQ 298
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLISEHEVEItglteKASSARSQanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 299 TAKTQELNMLREQNTELA---AELKHRQADYEELMGQKDDLNSQLQESLranSRLLEQLQEMGQEKEQ---LIQDLQEAR 372
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVlanSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKREKELSLEKEQnkrLWDRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 373 KSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYE--RELRELHEDKKRQEEELRGQIREEKARTREL 450
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 451 ENLQHTVEELQAQVHSmdgakgwferrlKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDG 530
Cdd:pfam15921 492 ESSERTVSDLTASLQE------------KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
330
....*....|....
gi 1958806473 531 HVKTISNLKQEVKD 544
Cdd:pfam15921 560 KDKVIEILRQQIEN 573
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
238-574 |
6.27e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 238 NKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAA 317
Cdd:pfam15921 95 NESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 318 -------------ELKHRQADYEELMGQK----DDLNSQLQESL-RANSRLLEQLQ-EMGQEKEQL--IQDLQEARKSAE 376
Cdd:pfam15921 175 lrkmmlshegvlqEIRSILVDFEEASGKKiyehDSMSTMHFRSLgSAISKILRELDtEISYLKGRIfpVEDQLEALKSES 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 377 KRKVmldELAMEtlqeksQHKEELGAVRLRHEKEMLGVRARyERELRELHEDKKRQEEELRGQIREEKAR-TRELENLQH 455
Cdd:pfam15921 255 QNKI---ELLLQ------QHQDRIEQLISEHEVEITGLTEK-ASSARSQANSIQSQLEIIQEQARNQNSMyMRQLSDLES 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 456 TVEELQAQVHSmdgAKGWFERRLKEAEESLLQQEQEQEETLKQcREQHA--------------AELKGKEEELQNVRDQL 521
Cdd:pfam15921 325 TVSQLRSELRE---AKRMYEDKIEELEKQLVLANSELTEARTE-RDQFSqesgnlddqlqkllADLHKREKELSLEKEQN 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806473 522 QQAQEERDGHVKTISNLKQEVKD-TVDGQRIlekkgSAVLKDLKR--QLHLERKRA 574
Cdd:pfam15921 401 KRLWDRDTGNSITIDHLRRELDDrNMEVQRL-----EALLKAMKSecQGQMERQMA 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-584 |
6.61e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 349 RLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELametLQEKSQHKEELGavRLRHEKEMLGvraRYERELRELHED 428
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL----SQELSDASRKIG--EIEKEIEQLE---QEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 429 KKRQEEELRGQIREEKArtrELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELK 508
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 509 GK-----------EEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTvdgQRILEKKGSAVLKDLKRQLHLERKRaDKL 577
Cdd:TIGR02169 819 QKlnrltlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEELEELEAALRDLESRLGDLKKER-DEL 894
|
....*..
gi 1958806473 578 QERLQEI 584
Cdd:TIGR02169 895 EAQLREL 901
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
190-467 |
7.00e-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: 40.21 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 190 LKWEMEREEKKLLWEQLQGL-----ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQE 264
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLhfgykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 265 LEAANQSL--------------AELRDQRQGERLEHAAALRALQDQIQ--TAKTQELNMLREQ--NTELAAELKHRQADY 326
Cdd:pfam12128 324 LEALEDQHgafldadietaaadQEQLPSWQSELENLEERLKALTGKHQdvTAKYNRRRSKIKEqnNRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 327 EELMGQKDDLNSQLQESLRA-NSRLLEQLQEMGQEKEQLIQDLQEArksaekrKVMLDELAM--ETLQEKSQHKEELGAV 403
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL-------KLRLNQATAtpELLLQLENFDERIERA 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806473 404 RLRHEKEmlgvRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSM 467
Cdd:pfam12128 477 REEQEAA----NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8-466 |
7.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 8 EEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQEE 87
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 88 DFRlQNSTLMAEFSKLCSQLEQLELENRQLKEGVPgaagPHVDGELLRLQAENTALQKNMAALQERYGKEAVRPSAVSEg 167
Cdd:COG4717 154 RLE-ELRELEEELEELEAELAELQEELEELLEQLS----LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 168 qgdppgdvlpislspmPLAEVELKWEMEREEKKLLWEQLQGLELS-----EKLKKKQESFCRLQTEKETLFNDSRNKIEE 242
Cdd:COG4717 228 ----------------ELEQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 243 LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHR 322
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806473 323 QADYEELMGQKDDlnsqlqESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMET-LQEKSQHKEELG 401
Cdd:COG4717 372 IAALLAEAGVEDE------EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEeLEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806473 402 AVRLRHEKEMLGVRARYER-ELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHS 466
Cdd:COG4717 446 EELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| |
