|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-497 |
5.76e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 189 ELKWEMEREEKKLLWEQLQGLesskQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRKEAdLK 268
Cdd:COG1196 217 ELKEELKELEAELLLLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEEL----RLELEELELELEE-AQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 269 AQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNmLREQNTELAAELKHRQADYEELMGQ 348
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 349 KDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL--AMETLQEKSQHKEELGAVRLRHEKE 426
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLeeELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 427 MLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG-AKGWFERRLKEA 497
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGfLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-602 |
1.80e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 260 QQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQ 339
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELR-LELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 340 ADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEELGAV 419
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-AELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 420 RLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEE 499
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 500 SLLQQEQEQEETLKQCRE-----QHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQevkdtVDGQRILEKKGSA 574
Cdd:COG1196 454 LEEEEEALLELLAELLEEaalleAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL-----LAGLRGLAGAVAV 528
|
330 340
....*....|....*....|....*...
gi 1958806467 575 VLKDLKRqlhLERKRADKLQERLQEILT 602
Cdd:COG1196 529 LIGVEAA---YEAALEAALAAALQNIVV 553
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-717 |
4.24e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 196 REEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEELQQRKEADLK---AQLA 272
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKA 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 273 RTQKLQQELEAANQSlAELRDQRQGERLEHAAALRALQDQIQtaKTQELNMLREQNTELAAELKHRQADYE--------- 343
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKK--KADEAKKKAEEDKKKADELKKAAAAKKkadeakkka 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 344 ELMGQKDDLNSQLQESLRANSrlLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQH-KEELGAVRLR 422
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEaKKKADEAKKA 1505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 423 HEKEMLGVRARYERELRELHEDKKRQEEELRGQIR--EEKARTREL---ENLQHTVEELQA-QVHSMDGAKGWFERRLKE 496
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELkkaEELKKAEEKKKAeEAKKAEEDKNMALRKAEE 1585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 497 AEESLLQQEQEQEETLKQCREQHAAELKgKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTvDGQRILEKKGSAVL 576
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-EELKKAEEENKIKA 1663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 577 KDLKRQLHLERKRADKLQERLQEiltnskSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYREILKEKESSAIPARSLSS 656
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 657 SPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 717
Cdd:PTZ00121 1738 EAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-602 |
9.20e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 260 QQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlEHAAALRALQDQIQTaktqelnmLREQNTELAAELKHRQ 339
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLEE--------LRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 340 ADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAV 419
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 420 RLRHEKeMLGVRARYERELRELHEdKKRQEEELRGQIREEKARtreLENLQHTVEELQAQVhsmdgakgwfERRLKEAEE 499
Cdd:TIGR02168 368 EELESR-LEELEEQLETLRSKVAQ-LELQIASLNNEIERLEAR---LERLEDRRERLQQEI----------EELLKKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 500 SLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVlkdl 579
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV---- 508
|
330 340
....*....|....*....|...
gi 1958806467 580 kRQLHLERKRADKLQERLQEILT 602
Cdd:TIGR02168 509 -KALLKNQSGLSGILGVLSELIS 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-488 |
9.02e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 190 LKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEkLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE----- 264
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQilrer 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 265 -ADLKAQLARTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYE 343
Cdd:TIGR02168 311 lANLERQLEELEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 344 ELMGQKDDLNSQLQEslraNSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRH 423
Cdd:TIGR02168 390 QLELQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806467 424 EKEMLgvraryeRELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKG 488
Cdd:TIGR02168 466 LREEL-------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-591 |
6.67e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 28 SDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQL 107
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 108 EQLELENRQLKEGVPGAAGPHVDGELLRLQAEntalqknmaalqERYGKEAVRPSAVSEGQGDppgdvlpislspmplae 187
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAE------------EKKKADEAKKKAEEAKKAD----------------- 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 188 vELKweMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsfcrlqteketlfnDSRNKIEELQQRKEADL 267
Cdd:PTZ00121 1448 -EAK--KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE--------------EAKKKADEAKKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 268 KAQLARTQKLQQELEAAnqslaelrdqRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMG 347
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEA----------KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 348 QKDDLNSQLQESlRANSRLLEQLQEMGQEKEQLIQDlQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEM 427
Cdd:PTZ00121 1581 RKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 428 LGVRAryeRELRELHEDKKRQEEELRgqiREEKARTRELENLQHTVEElqaqvhsmdgAKGWFERRLKEAEESLLQQEQE 507
Cdd:PTZ00121 1659 NKIKA---AEEAKKAEEDKKKAEEAK---KAEEDEKKAAEALKKEAEE----------AKKAEELKKKEAEEKKKAEELK 1722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 508 QEETLkqcREQHAAELKGKEEELQNVRDQLQQAQEERdghvKTISNLKQEVKDTVDGQRileKKGSAVL------KDLKR 581
Cdd:PTZ00121 1723 KAEEE---NKIKAEEAKKEAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKKAEEIR---KEKEAVIeeeldeEDEKR 1792
|
570
....*....|
gi 1958806467 582 QLHLERKRAD 591
Cdd:PTZ00121 1793 RMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-599 |
1.00e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 195 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLAR- 273
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEAKk 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 274 ---TQKLQQELEAANQSLAELRDQRQGERLEHAAAlralqdqiQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKD 350
Cdd:PTZ00121 1446 adeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE--------EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 351 DLNSQLQESLRA--NSRLLEQLQEMGQ-EKEQLIQDLQEARKSAEKRKVmldelametlQEKSQHKEELGAVRLRHEKEM 427
Cdd:PTZ00121 1518 AEEAKKADEAKKaeEAKKADEAKKAEEkKKADELKKAEELKKAEEKKKA----------EEAKKAEEDKNMALRKAEEAK 1587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 428 LGVRARYERELRELHEDKKRQEEELRGQiREEKARTRELENlqhtVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQE 507
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKK----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 508 QEETLKQCRE--QHAAELKGKEEELQNVRDQLQQAQEERDgHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHL 585
Cdd:PTZ00121 1663 AAEEAKKAEEdkKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
410
....*....|....
gi 1958806467 586 ERKRADKLQERLQE 599
Cdd:PTZ00121 1742 DKKKAEEAKKDEEE 1755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-600 |
1.74e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKkaQEVEVLLSEKEMLQAKLHSQE 86
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL--AELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 87 EdfrlqnstlmaefsklcsQLEQLELENRQLKEGVPGAAgphvdGELLRLQAENTALQKNMAALQERYGKEAVRpsavse 166
Cdd:COG1196 316 E------------------RLEELEEELAELEEELEELE-----EELEELEEELEEAEEELEEAEAELAEAEEA------ 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 167 gqgdppgdvlpislspmpLAEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQesfcRLQTEKE 246
Cdd:COG1196 367 ------------------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE----RLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 247 TLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLRE 326
Cdd:COG1196 425 EL-EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 327 QNTELAAELKHRQADYEELMGQKDDLNSQLQESLRA-NSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMET 405
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAlEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 406 LQEKSQHKEELGAVRLRhekemlgvRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG 485
Cdd:COG1196 584 ARAALAAALARGAIGAA--------VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 486 --AKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVD 563
Cdd:COG1196 656 gsAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590
....*....|....*....|....*....|....*..
gi 1958806467 564 GQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEI 600
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-465 |
8.27e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 191 KWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKE 264
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 265 ADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEE 344
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK-EELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 345 LMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHE 424
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYE 468
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958806467 425 KEMLGVRARYERELRELHEdKKRQEEELRGQIREEKARTRE 465
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSK-LQRELAEAEAQARASEERVRG 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
269-483 |
2.97e-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: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 269 AQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQiqtakTQELNMLREQNTELAAELKHRQADYEELMGQ 348
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 349 KDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELA------METLQEKSQHKEELGAVRLR 422
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806467 423 HEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSM 483
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
185-473 |
3.25e-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: 57.39 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 185 LAEVELKWEMEREEKKLLWEQLQGLE---SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFND-SRNKIEELQ 260
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQ 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 261 QRKEaDLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQA 340
Cdd:TIGR02169 798 AELS-KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE-KEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 341 DYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRkvmLDELAMETLQEKSQHKEELG 417
Cdd:TIGR02169 876 ALRDLESRLGDLKKErdeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE---LSEIEDPKGEDEEIPEEELS 952
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 418 AVRLRHEKEMLGVRAR------------YERELRELHEDKKRQE--EELRGQIREekaRTRELENLQHTV 473
Cdd:TIGR02169 953 LEDVQAELQRVEEEIRalepvnmlaiqeYEEVLKRLDELKEKRAklEEERKAILE---RIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-466 |
3.64e-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: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 37 ELSSLRQKVAYLdkefskAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQ 116
Cdd:TIGR02168 678 EIEELEEKIEEL------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 117 lkegvpgaagphvdgellrLQAENTALQKNMAALQERYGKEAVRPSAVSEGqgdppgdvlpislspmpLAEVELKWEMER 196
Cdd:TIGR02168 752 -------------------LSKELTELEAEIEELEERLEEAEEELAEAEAE-----------------IEELEAQIEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 197 EEKKLLWEQLqgleSSKQAETSRLQEELAKLSEKLKKKQesfcRLQTEKETLFNDSRNKIEELQQRkEADLKAQLARTQK 276
Cdd:TIGR02168 796 EELKALREAL----DELRAELTLLNEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSED-IESLAAEIEELEE 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 277 LQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQL 356
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 357 QESLRANsrlleqLQEMGQEKEQLIQDLQEARKSAEKrkvmldelametLQEKsqhKEELGAVRLRHEKEMLGVRARYEr 436
Cdd:TIGR02168 946 SEEYSLT------LEEAEALENKIEDDEEEARRRLKR------------LENK---IKELGPVNLAAIEEYEELKERYD- 1003
|
410 420 430
....*....|....*....|....*....|
gi 1958806467 437 ELRELHEDKKRQEEELRGQIREEKARTREL 466
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-438 |
4.18e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 219 RLQEELAKLS------EKLKKKQESFCRLQTEKETlFNDSRNKIEELQQRKEA-DLKAQLARTQKLQQELEAANQSLAEL 291
Cdd:COG4913 229 ALVEHFDDLErahealEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 292 RDQR---QGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLE 368
Cdd:COG4913 308 EAELerlEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 369 QLQEMGQEKEQLIQDLQEARKSAEKRKvmldELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYEREL 438
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAAL----RDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-394 |
6.80e-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: 55.54 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 189 ELKWEMEREEKKLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLK 268
Cdd:COG4942 31 QLQQEIAELEKEL--AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-EKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 269 AQLARTQKL-----------QQELEAANQSLAELRDQRQgERLEHAAALRALQDQIQtAKTQELNMLREQNTELAAELKH 337
Cdd:COG4942 108 ELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAP-ARREQAEELRADLAELA-ALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806467 338 RQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKR 394
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-596 |
2.28e-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: 54.69 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 251 DSRNKIEELQQR-KEADLKAQLARTQ--KLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQT------AKTQEL 321
Cdd:TIGR02169 174 KALEELEEVEENiERLDLIIDEKRQQleRLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAierqlaSLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 322 NMLREQNTELAAELKHRQADYEELMGQKDDLNS----QLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEkrkvm 397
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE----- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 398 ldELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARyERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQ 477
Cdd:TIGR02169 329 --AEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 478 AQvhsmdgakgwfERRLKEAEESLLQQEQEQEETLKQCREQHA---AELKGKEEELQNVRDQLQQAQEERDGHVKTISNL 554
Cdd:TIGR02169 406 RE-----------LDRLQEELQRLSEELADLNAAIAGIEAKINeleEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958806467 555 KQEvkdtvdgQRILEKKgsavLKDLKRQLHLERKRADKLQER 596
Cdd:TIGR02169 475 KEE-------YDRVEKE----LSKLQRELAEAEAQARASEER 505
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
217-426 |
4.28e-07 |
|
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: 54.07 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 217 TSRLQEELAKLSEKLKKKQESFCRLQTEKetlfndsrnKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQ 296
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKE---------RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 297 GERLEHAAalRALQDQIqTAKTQELNMLREQNT---ELAAELKHRQAD------YEELMGQKDDLNSQLQESLRANSRLL 367
Cdd:NF012221 1608 RDAILEES--RAVTKEL-TTLAQGLDALDSQATyagESGDQWRNPFAGglldrvQEQLDDAKKISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 368 EQLQ------EMGQEK-EQLI----QDLQEARKSAEKRKvmLDELAMETLQEKSQHKEELGA--VRLRHEKE 426
Cdd:NF012221 1685 QKVKdavaksEAGVAQgEQNQanaeQDIDDAKADAEKRK--DDALAKQNEAQQAESDANAAAndAQSRGEQD 1754
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-475 |
4.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 219 RLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEAD-----LKAQLARTQKLQQELEAANQSLAELRD 293
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEidvasAEREIAELEAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 294 QrqgerlehaaaLRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRAnsRLLEQLQEM 373
Cdd:COG4913 693 Q-----------LEELEAELEELE-EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 374 GQEK--EQLIQDLQEARKSAEKRkvmLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRArYERELRELHEDK-KRQEE 450
Cdd:COG4913 759 LGDAveRELRENLEERIDALRAR---LNRAEEELERAMRAFNREWPAETADLDADLESLPE-YLALLDRLEEDGlPEYEE 834
|
250 260
....*....|....*....|....*
gi 1958806467 451 ELRGQIREEKarTRELENLQHTVEE 475
Cdd:COG4913 835 RFKELLNENS--IEFVADLLSKLRR 857
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-600 |
9.54e-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: 52.75 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKaQEVEVLLSEKEMLQAKLHSQE 86
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEELQEEL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 87 EDFRLQNSTLMAEFSKLCSQLEQLElenrqlkegvpgaagphvdGELLRLQAENTALQknmaALQERYGKEAVRPSAVSE 166
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAE-------------------RELAQLQARLDSLE----RLQENLEGFSEGVKALLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 167 GQGDPPGDVLPISlspmPLAEVELKWEMEREekKLLWEQLQ-----GLESSKQAETSRLQEELAK-----LSEKLKKKQE 236
Cdd:TIGR02168 514 NQSGLSGILGVLS----ELISVDEGYEAAIE--AALGGRLQavvveNLNAAKKAIAFLKQNELGRvtflpLDSIKGTEIQ 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 237 SFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLAR---TQKLQQELEAANQSLAELRD-QRQGERLEHAAAL---RAL 309
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvVDDLDNALELAKKLRPGYRIvTLDGDLVRPGGVItggSAK 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 310 QDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQlqeslransrlLEQLQEMGQEKEQLIQDLQEARK 389
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE-----------LEQLRKELEELSRQISALRKDLA 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 390 SAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEmlgvraryERELRELHEDKKRQEEELRGQIREEKARTRELENL 469
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--------EEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 470 QHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQcREQHAAELKGKEEELQNVRDQLQQAQEERDGHVK 549
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLNERASLEE 887
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1958806467 550 TISNLKQEVKDTVDGQRILEKKgsavLKDLKRQLHLERKRADKLQERLQEI 600
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESK----RSELRRELEELREKLAQLELRLEGL 934
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-484 |
1.02e-06 |
|
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: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 264 EADLKAQLARTQKLQQELEAANQSLAELRDQR--------QGERLEHAAALRALQDQIQTA-----KTQELNMLREQNTE 330
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIellepireLAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 331 LAAELKHRQADYEELMGQKDDLNSQLQEslransrLLEQLQEM-GQEKEQLIQDLQEARKSAEKRKVMLDELAmetlqek 409
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDE-------LEAQIRGNgGDRLEQLEREIERLERELEERERRRARLE------- 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806467 410 sQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMD 484
Cdd:COG4913 366 -ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
227-426 |
1.22e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 227 LSEKLKKKQESFCRLQTEKETLFNDsrnKIEELQQRKEAdLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAAL 306
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLK---ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 307 RALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQEslrANSRLLEQLQEMGQEKEQLIQDLQE 386
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958806467 387 ARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 426
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-708 |
1.51e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 186 AEVELKWEMERE-EKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsFCRLQTEKETLFNDSRNKIEELQQRKE 264
Cdd:PTZ00121 1202 AEAARKAEEERKaEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE-IRKFEEARMAHFARRQAAIKAEEARKA 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 265 ADLKAqlARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTaKTQELNMLREQNTElAAELKHRQadyEE 344
Cdd:PTZ00121 1281 DELKK--AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKK-AAEAAKAE---AE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 345 LMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL--AMETLQEKSQHKEELGAVRLR 422
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKA 1433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 423 HEKEMLGVRARYERELRELHEDKKRQEEELRGQirEEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLL 502
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA--EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 503 QQEQEQEETLKQCREQHAAELKGKEEELQNVR-----DQLQQAQEERDG-HVKTISNLKQEVKDTVDGQRILEKKGSAvl 576
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkkaDELKKAEELKKAeEKKKAEEAKKAEEDKNMALRKAEEAKKA-- 1589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 577 kDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYREILKEKESSAIPARSLSS 656
Cdd:PTZ00121 1590 -EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806467 657 SPQAQPPRPAELSDEEVAElfqRLAETQQEKWMLE----EKVKHLEVSSASMAEDL 708
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDE---KKAAEALKKEAEEakkaEELKKKEAEEKKKAEEL 1721
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-372 |
2.91e-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: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 38 LSSLRQKVAYLDKEFSKAQK--ALSKSKKAQEVEVLLSEKEMLQAKLH---SQEEDFRLQNSTLMAEFSKLCSQLEQLEL 112
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERykELKAELRELELALLVLRLEELREELEelqEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 113 ENRQLKEGVPGAagphvDGELLRLQAENTALQKNMAALQERYgKEAVRPSAVSEGQGDppgdvlpislspmplaevelKW 192
Cdd:TIGR02168 275 EVSELEEEIEEL-----QKELYALANEISRLEQQKQILRERL-ANLERQLEELEAQLE--------------------EL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 193 EMEREEKKLLWEQLQGLESSKQAETSRLQEELAklseKLKKKQESFCRLQTEKETLFNDSRNKIEELQQrKEADLKAQLA 272
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQLEL-QIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 273 RtqkLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDL 352
Cdd:TIGR02168 404 R---LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340
....*....|....*....|
gi 1958806467 353 NSQLQEsLRANSRLLEQLQE 372
Cdd:TIGR02168 481 ERELAQ-LQARLDSLERLQE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
215-576 |
3.35e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 215 AETSRLQEELAKLSEKLKKKQESFCRLQTEKETL--FNDSRNKIEELQQ----RKEADLKAQLARTQKLQQELEAANQSL 288
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAerYQALLKEKREYEGyellKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 289 AELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLE 368
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 369 Q-------LQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL---AMETLQEKSQHKEELGAVRLRHEkEMLGVRARYEREL 438
Cdd:TIGR02169 337 EieelereIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkeFAETRDELKDYREKLEKLKREIN-ELKRELDRLQEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 439 RELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELqaqvhsmdgakgwfERRLKEAEESllqqeqeqeetlkqcREQ 518
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--------------EWKLEQLAAD---------------LSK 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806467 519 HAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVL 576
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
222-415 |
3.88e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 50.10 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 222 EELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLE 301
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 302 HAAALRALQDQIQTAKTQelnmLREQNTELAAELKHRQADYE----ELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEK 377
Cdd:pfam03528 84 ATVSENTKQEAIDEVKSQ----WQEEVASLQAIMKETVREYEvqfhRRLEQERAQWNQYRESAEREIADLRRRLSEGQEE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958806467 378 EQLIQDLQEARKSAEKRK--VMLDELAMETLQEKSQHKEE 415
Cdd:pfam03528 160 ENLEDEMKKAQEDAEKLRsvVMPMEKEIAALKAKLTEAED 199
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
272-459 |
1.76e-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: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 272 ARTQKLQQELEAANQSLAELrdQRQGERLEH----AAALR-------ALQDQIQTAKtQELNMLREQN---TELAAELKH 337
Cdd:COG3096 893 DRLEELREELDAAQEAQAFI--QQHGKALAQleplVAVLQsdpeqfeQLQADYLQAK-EQQRRLKQQIfalSEVVQRRPH 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 338 -RQADYEELMGQKDDLNSQLQESLR----ANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQ----- 407
Cdd:COG3096 970 fSYEDAVGLLGENSDLNEKLRARLEqaeeARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqa 1049
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 408 ----------EKSQHKEELGAVRLRhEKEMLGVRARYERELRELHEDKKRQEEELRgQIREE 459
Cdd:COG3096 1050 daeaeerariRRDELHEELSQNRSR-RSQLEKQLTRCEAEMDSLQKRLRKAERDYK-QEREQ 1109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
259-480 |
2.92e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 259 LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHR 338
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 339 QADYEELMGQKDDLNSQLQESlRANSRLLEQLQEMGQEKEQLIQDLQEarksaekrkvmlDELAMETLQeksqhkEELGA 418
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTP------------NHPDVIALR------AQIAA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 419 VRLRHEKEMLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 480
Cdd:COG3206 303 LRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
196-478 |
2.98e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 196 REEKKLLWEQLQGLESSKQAETSRLQE-----ELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK---EADL 267
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERaedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAaelEAEA 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 268 KAQLARTQKLQQELEAANQSLAELRDQRQ--GERLEHAAALRALQDQIqTAKTQELNMLREQNTELAAELKHRQADYEEL 345
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAelKERIESLERIRTLLAAI-ADAEDEIERLREKREALAELNDERRERLAEK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 346 MGQKDDLNSQLQESLransrlleqlqemgqekeqlIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVrlrhek 425
Cdd:PRK02224 633 RERKRELEAEFDEAR--------------------IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV------ 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958806467 426 emlgvraryERELRELhedkkrqeEELRGQIREEKARTRELENLQHTVEELQA 478
Cdd:PRK02224 687 ---------ENELEEL--------EELRERREALENRVEALEALYDEAEELES 722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-625 |
3.98e-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: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 372 EMGQEKEQLIQDLQEARKSAEKRKVMLDELA--METLQEKSQHKEELGAVRLRHEkemlgvraryERELRELHEDKKRQE 449
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKR----------EYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 450 EELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEE 529
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 530 LQNVRDQLQQAQEERDGHVKTISNLKQEVKDtvdgQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTG 609
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250
....*....|....*.
gi 1958806467 610 LEELVLSEMNSPSRTQ 625
Cdd:TIGR02169 393 KLEKLKREINELKREL 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-600 |
4.04e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 219 RLQEELAKLSEKLKKKQESFCRLQtEKETLFNDSRNKIEELQQR-----KEADLKAQLARTQKLQQELEAANQSLAELRD 293
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREElekleKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 294 QRQgERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKddlnSQLQESLRANSRLLEQLQEM 373
Cdd:COG4717 154 RLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL----AELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 374 GQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELR 453
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 454 GQIREEKARTRELENLqhtVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGK-----EE 528
Cdd:COG4717 309 ALPALEELEEEELEEL---LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvedEE 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958806467 529 ELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKG-SAVLKDLKRQLHLERKRADKLQERLQEI 600
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-386 |
4.18e-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: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 7 EEEFQRMQTQLLELRTnnyqlsdelrkngvELSSLRQKVAYLDKEFSKAQKALSKSKKaqEVEVLLSEKEMLQAKLHSQE 86
Cdd:TIGR02169 673 PAELQRLRERLEGLKR--------------ELSSLQSELRRIENRLDELSQELSDASR--KIGEIEKEIEQLEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 87 EdfrlqnstlmaefsklcsQLEQLELENRQLKEGVpgaagPHVDGELLRLQAENTALQKNMAALQERygkeavrpsavse 166
Cdd:TIGR02169 737 E------------------RLEELEEDLSSLEQEI-----ENVKSELKELEARIEELEEDLHKLEEA------------- 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 167 gqgdppgdvlpislspmpLAEVELKWEMEReekkllWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKE 246
Cdd:TIGR02169 781 ------------------LNDLEARLSHSR------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 247 TLFNDSR---NKIEELQQRKEaDLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQelnm 323
Cdd:TIGR02169 837 ELQEQRIdlkEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ---- 911
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958806467 324 lREQNTELAAELKHRQADYEELMGQKDDLNSQLQESlRANSRLLEQLQEMGQEKEQLIQDLQE 386
Cdd:TIGR02169 912 -IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
303-573 |
5.82e-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: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 303 AAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQ 382
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 383 DLQEARKSAEKRKVMLDELaMETLQEKSQHKEELGAVRLRHEKEMLgVRARYereLRELHEDKKRQEEELRGQIREEKAR 462
Cdd:COG4942 91 EIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 463 TRELENLQHTVEELQAQVhsmdgakgwfERRLKEAEESLLQqeqeqeetlkqcREQHAAELKGKEEELQNVRDQLQQAQE 542
Cdd:COG4942 166 RAELEAERAELEALLAEL----------EEERAALEALKAE------------RQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|.
gi 1958806467 543 ERDGHVKTISNLKQEVKDTVDGQRILEKKGS 573
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
212-393 |
6.09e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 212 SKQAETSR----LQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQrkeADLKAQLArtqKLQQELEAANQS 287
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL---SELESQLA---EARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 288 LAELRDQRQGERlehAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLL 367
Cdd:COG3206 242 LAALRAQLGSGP---DALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
|
170 180
....*....|....*....|....*..
gi 1958806467 368 E-QLQEMGQEKEQLIQDLQEARKSAEK 393
Cdd:COG3206 319 EaELEALQAREASLQAQLAQLEARLAE 345
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
185-605 |
7.53e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 185 LAEVELKWEMEREEKKLLWEQLQGLESSKQAEtsRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE 264
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 265 ADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQE--LNMLREQNTELAAELKHRQADY 342
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLqsLCKELDILQREQATIDTRTSAF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 343 EELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEElgavrlr 422
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV------- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 423 hekemlGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGaKGWFERRLKEAEESLL 502
Cdd:TIGR00618 493 ------LARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH-QLTSERKQRASLKEQM 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 503 QQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQ 582
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL 645
|
410 420
....*....|....*....|...
gi 1958806467 583 LHLERKRADKLQERLQEILTNSK 605
Cdd:TIGR00618 646 TALHALQLTLTQERVREHALSIR 668
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-594 |
9.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 197 EEKKLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieelqqRKEADLKAQLARTQK 276
Cdd:COG4717 71 KELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKL-------------EKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 277 LQQELEAANQSLAELRDQRQgERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQL 356
Cdd:COG4717 137 LEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 357 QESLRANSRLLEQLQ--EMGQEKEQLIQDLQEAR----------------KSAEKRKVMLDELAM-----------ETLQ 407
Cdd:COG4717 216 EEAQEELEELEEELEqlENELEAAALEERLKEARlllliaaallallglgGSLLSLILTIAGVLFlvlgllallflLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 408 EKSQHKEELGAVRLRHEKEMLgVRARYERELRELHEDKKRQEEELRGQIR------------EEKARTRELENLQHTVEE 475
Cdd:COG4717 296 EKASLGKEAEELQALPALEEL-EEEELEELLAALGLPPDLSPEELLELLDrieelqellreaEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 476 LQAQVHSMDGAK-----GWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKT 550
Cdd:COG4717 375 LLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958806467 551 ISNLKQEVKDTVDGQRILEKKgsAVLKDLKRQLHLERKRADKLQ 594
Cdd:COG4717 455 LAELEAELEQLEEDGELAELL--QELEELKAELRELAEEWAALK 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-600 |
9.78e-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: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 324 LREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAM 403
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 404 ETLQEKSQHKE--------ELGAVRLRHEKEMLGVRARYER------ELRELHEDKKRQEEELRGQIREEKARTRELENL 469
Cdd:TIGR02169 752 EIENVKSELKElearieelEEDLHKLEEALNDLEARLSHSRipeiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 470 QHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREqHAAELKGKEEELQNVRDQLQQAQEERDGHVK 549
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD-LESRLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958806467 550 TISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHL--ERKRADKLQERLQEI 600
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeEELSLEDVQAELQRV 963
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
187-619 |
1.49e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 187 EVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieELQQRKEAD 266
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ---------EEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 267 LKAQLARTQKLQQELEAANQSLAELRDQRQGERL-EHAAALRALQDQIQTAKTQelnmLREQNTELAAELKHRQA---DY 342
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLaAHIKAVTQIEQQAQRIHTE----LQSKMRSRAKLLMKRAAhvkQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 343 EELMGQKDDLNSQLQESLRaNSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETlQEKSQHKEELGAVRLR 422
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIH-IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC-KELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 423 H--EKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEES 500
Cdd:TIGR00618 416 TsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 501 LLQQEQEQEETLKQCREQHAAELKGKE--------EELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKG 572
Cdd:TIGR00618 496 LLELQEEPCPLCGSCIHPNPARQDIDNpgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958806467 573 SAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSEMN 619
Cdd:TIGR00618 576 TQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-488 |
1.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 229 EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQrKEADLKAQLARTQKLQQELEAANQSLAELRDQ---RQGERLEHAAA 305
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISS-ELPELREELEKLEKEVKELEELKEEIEELEKElesLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 306 LRALQDQIQTAKtQELNMLREQNTELAaELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQ 385
Cdd:PRK03918 261 IRELEERIEELK-KEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 386 EARKSAEKRKVMLDELamETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRE 465
Cdd:PRK03918 339 RLEELKKKLKELEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260
....*....|....*....|...
gi 1958806467 466 LENlqhTVEELQAQVHSMDGAKG 488
Cdd:PRK03918 417 LKK---EIKELKKAIEELKKAKG 436
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
211-411 |
1.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 211 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKetlfNDSRNKIEELQQRKEAdLKAQLArtqKLQQELEAANQSLAE 290
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDK-LQAEIA---EAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 291 -LRD-QRQGERLEHAAAL---RALQDQIQTAKTqeLNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSR 365
Cdd:COG3883 91 rARAlYRSGGSVSYLDVLlgsESFSDFLDRLSA--LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958806467 366 LLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQ 411
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-620 |
1.90e-04 |
|
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: 45.05 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 9 EFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVevLLSEKEMLQAKLHSQEED 88
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE--LAEELAELEEKLEELKEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 89 FRLQNstlmAEFSKLCSQLEQLELENRQLKEGVPGAAGPHVdgELLRLQAENTALQKNMAALQERYGKEAVRPSAVSEGQ 168
Cdd:TIGR02168 353 LESLE----AELEELEAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 169 GDppgdvlpiSLSPMPLAEVElkweMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL 248
Cdd:TIGR02168 427 LK--------KLEEAELKELQ----AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 249 FNDSRN--------KIEELQQRKEADLKAQLARTQKLQQELEAA-NQSLAELRDQRQGERLEHAAALRALQ--------- 310
Cdd:TIGR02168 495 ERLQENlegfsegvKALLKNQSGLSGILGVLSELISVDEGYEAAiEAALGGRLQAVVVENLNAAKKAIAFLkqnelgrvt 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 311 ----DQIQTAKTQELNMLREQNTE----LAAELKHRQADYEELMGQ-------KDDLNS--QLQESLRANSRLLEQLQEM 373
Cdd:TIGR02168 575 flplDSIKGTEIQGNDREILKNIEgflgVAKDLVKFDPKLRKALSYllggvlvVDDLDNalELAKKLRPGYRIVTLDGDL 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 374 --------GQEKEQLIQDLQEARKSAEKRKVMldELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEdk 445
Cdd:TIGR02168 655 vrpggvitGGSAKTNSSILERRREIEELEEKI--EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-- 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 446 krQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCrEQHAAELKG 525
Cdd:TIGR02168 731 --LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 526 KEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAV------LKDLKRQLHLERKRADKLQERLQE 599
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieeLEELIEELESELEALLNERASLEE 887
|
650 660
....*....|....*....|.
gi 1958806467 600 ILTNSKSRTGLEELVLSEMNS 620
Cdd:TIGR02168 888 ALALLRSELEELSEELRELES 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-335 |
2.12e-04 |
|
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: 45.06 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 38 LSSLRQKVAYLDKEFSKAQK--ALSKSKKAQEVEVLLSEKEMLQAklhsQEEDFRLQNSTLMAEFSKLCSQLEQLELE-- 113
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERyqALLKEKREYEGYELLKEKEALER----QKEAIERQLASLEEELEKLTEEISELEKRle 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 114 -NRQLKEGVPGAAGPHVDGELLRLQAENTALQKNMAALQeryGKEAVRPSAVSEGQGDPPGDVLPISLSPMPLAEVELKW 192
Cdd:TIGR02169 269 eIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE---RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 193 EMEREEKKLLWEQLQGLESSKQAETSRLQE---ELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE--ADL 267
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelADL 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806467 268 KAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQtAKTQELNMLREQNTELAAEL 335
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY-DLKEEYDRVEKELSKLQREL 492
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
135-385 |
3.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 135 RLQAENTALQKNMAALQERYGKEAVRPSAVSegqgDPPGDVLPISLSPMPLAEVELKWEMEREEKKLLWEQLQGLESskQ 214
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALK----DDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNS--Q 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 215 AETSRLQEELAK--LSEKLKKKQESFCRLQTEKEtlfnDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELR 292
Cdd:PRK11281 151 LVSLQTQPERAQaaLYANSQRLQQIRNLLKGGKV----GGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 293 DQR-----QGERLEHAaaLRALQDQI---------QTAK---TQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQ 355
Cdd:PRK11281 227 KQRdyltaRIQRLEHQ--LQLLQEAInskrltlseKTVQeaqSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTL 304
|
250 260 270
....*....|....*....|....*....|
gi 1958806467 356 LQESLRANSRLLEQLQEMGQEKEQlIQDLQ 385
Cdd:PRK11281 305 TQQNLRVKNWLDRLTQSERNIKEQ-ISVLK 333
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-389 |
4.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 214 QAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRKeadLKAQLARTQKLQQELEAANQSLaelrD 293
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDAL----REELDELEAQI---RGNGGDRLEQLEREIERLEREL----E 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 294 QRQGERLEHAAALRALQDQIQTAKtQELNMLREQNTELAAELKHRQADYEElmgQKDDLNSQLQESLRANSRLLEQLQEM 373
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASA-EEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASL 431
|
170
....*....|....*.
gi 1958806467 374 GQEKEQLIQDLQEARK 389
Cdd:COG4913 432 ERRKSNIPARLLALRD 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
189-596 |
4.21e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 189 ELKWEMEREEKKLLWEQLQGLESskqaETSRLQEELAKLSEKLKKKQEsfcRLQTEKETLfNDSRNKIEELQQRKEA--D 266
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLES----ELAELDEEIERYEEQREQARE---TRDEADEVL-EEHEERREELETLEAEieD 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 267 LKAQLARTQKlqqELEAANQSLAELRDQRQ--GERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHRQADYEE 344
Cdd:PRK02224 263 LRETIAETER---EREELAEEVRDLRERLEelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 345 LMGQKddlnsqlqESLRANSRLLE-QLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL-------------AMETLQEKS 410
Cdd:PRK02224 340 HNEEA--------ESLREDADDLEeRAEELREEAAELESELEEAREAVEDRREEIEELeeeieelrerfgdAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 411 QHKEELGAVRLRHEKEMLGVRARYE------RELRELHEDKKRQE--------------EELRGQIREEKARTRELENLQ 470
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRtarervEEAEALLEAGKCPEcgqpvegsphvetiEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 471 HTVE----------ELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQcREQHAAELKGKEEELQNVRDQLQQA 540
Cdd:PRK02224 492 EEVEerleraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806467 541 QEErdghVKTISNLKQEVKDTVDGQRILEKKGSAvLKDLKRQLHLERKRADKLQER 596
Cdd:PRK02224 571 REE----VAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAEL 621
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
251-543 |
7.15e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 251 DSRNKIEELQQRKEA---DLKAQLARTQKLQQELEAANQSLA----ELRDQRQGERLEhaAALRALqdqiqTAKTQELNM 323
Cdd:PRK04863 297 TSRRQLAAEQYRLVEmarELAELNEAESDLEQDYQAASDHLNlvqtALRQQEKIERYQ--ADLEEL-----EERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 324 LREQNTELAAELKHRQADYEElmgQKDDLNSQLQESLRAnsrlLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELam 403
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEE---EVDELKSQLADYQQA----LDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNA-- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 404 ETLQEKSQHKEELGAVRLRHEKEMLGV----RARYERELRELH--------EDKKRQEEELRGQIREEKARTRELENLQH 471
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVaqaaHSQFEQAYQLVRkiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806467 472 TVEELQAQVHSMDGAkgwfERRLKEAEESLLQQEQEQEETLKqCREQHAAELKGKEEELQNVRDQ---LQQAQEE 543
Cdd:PRK04863 521 RLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQ-LQEELEARLESLSESVSEARERrmaLRQQLEQ 590
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-488 |
8.29e-04 |
|
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: 43.18 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 73 SEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEgvpgaagphvdgellRLQAENTALQKNMAALQE 152
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR---------------MYEDKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 153 RYGKEAVRPSAVSEGQGDPpGDVLPISLSPMPLAEVELkwEMEREEKKLLWEQLQGLESSKQAETSRLQE---ELAKLsE 229
Cdd:pfam15921 357 ELTEARTERDQFSQESGNL-DDQLQKLLADLHKREKEL--SLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRL-E 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 230 KLKKKQESFCRLQTEKETLFNDSRNKIEElqqrKEADLKAQLARTQKL-----------QQELEAANQSLAELRDQRQge 298
Cdd:pfam15921 433 ALLKAMKSECQGQMERQMAAIQGKNESLE----KVSSLTAQLESTKEMlrkvveeltakKMTLESSERTVSDLTASLQ-- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 299 rlEHAAALRALQDQIQT------AKTQELNMLREQNTelaaELKHRQADYEEL---MGQKDDLNSQLQESLRANSRLLEQ 369
Cdd:pfam15921 507 --EKERAIEATNAEITKlrsrvdLKLQELQHLKNEGD----HLRNVQTECEALklqMAEKDKVIEILRQQIENMTQLVGQ 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 370 ----LQEMGQEKEQLIQDLQEARKSAEKRKVMLD--------------ELAMETLQEKSQHKEELGAVR-LRHEKEMLGV 430
Cdd:pfam15921 581 hgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDkkdakirelearvsDLELEKVKLVNAGSERLRAVKdIKQERDQLLN 660
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958806467 431 RARYER-ELRELHEDKKRQEEELRGQIREEKARTR----ELENLQHTVEELQAQVHSMDGAKG 488
Cdd:pfam15921 661 EVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQSELEQTRNTLKSMEGSDG 723
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
204-392 |
1.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 204 EQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQK------- 276
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-QAEIAEAEAEIEERREELGERARALYRsggsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 277 LQQELEAanQSLAELRDQ---------RQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAElkhrQADYEELMG 347
Cdd:COG3883 105 LDVLLGS--ESFSDFLDRlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958806467 348 QKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAE 392
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-458 |
1.09e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 7 EEEFQRMQTQLLELRTNNYQLSDEL-RKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQ 85
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 86 EEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAGPHVDGELLRLQAE---NTALQKNMAALQERYGKEAVRPS 162
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEaalAELLEELAEAAARLLLLLEAEAD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 163 AVSEGQGDPPGDVLPISLSPMPLAEVELKWEMEREEkkLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFcrLQ 242
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA--ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF--LP 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 243 TEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRAlqdqiqtaktqeln 322
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-------------- 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 323 mlREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELA 402
Cdd:COG1196 645 --RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806467 403 METLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIRE 458
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
254-384 |
1.12e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 254 NKIEELQQ--RKEADLKAQLARTQKLQQELEAanqSLAELRDqrqgeRLEHAAALRALQDQIQTAKTQELNMLREQNTEL 331
Cdd:PRK09039 50 GKDSALDRlnSQIAELADLLSLERQGNQDLQD---SVANLRA-----SLSAAEAERSRLQALLAELAGAGAAAEGRAGEL 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806467 332 AAELKHRQADYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEMGQEKEQLIQDL 384
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-712 |
1.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 193 EMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSE----KLKKKQESFCRLQ----TEKETLFNDSRNKIE------- 257
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDakrvEIARKAEDARKAEearkAEDAKKAEAARKAEEvrkaeel 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 258 ---------ELQQRKEADLKAQLARTQKLQQELEA---ANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLR 325
Cdd:PTZ00121 1194 rkaedarkaEAARKAEEERKAEEARKAEDAKKAEAvkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 326 EQNTELAAELKH----RQAD---YEELMGQKDDLNSQLQESLRANsRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVML 398
Cdd:PTZ00121 1274 AEEARKADELKKaeekKKADeakKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 399 DELAMETlqEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRG--QIREEKARTRELENLQHTVEEL 476
Cdd:PTZ00121 1353 EAAADEA--EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEK 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 477 QAQVHSMDGAKGwfERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVrDQLQQAQEERDGHVKTISNLKQ 556
Cdd:PTZ00121 1431 KKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 557 EVKDTVDGQRILEKKGSAVLKDLKrqlhlERKRADKLQeRLQEILTNSKSRTGLEELVLSEMNSPSRTQTGDSSSVSSFS 636
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAE-----EAKKADEAK-KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 637 YREILKEKESSAIP-------------ARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVSSAS 703
Cdd:PTZ00121 1582 KAEEAKKAEEARIEevmklyeeekkmkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
....*....
gi 1958806467 704 MAEDLCRKS 712
Cdd:PTZ00121 1662 KAAEEAKKA 1670
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
219-480 |
1.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 219 RLQEELAKLSEKLKKKQESFCRLQTEKEtlfnDSRNKIEELQQRKEaDLKAQLARTQK---LQQ----ELEAANQSLAEL 291
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQE----ENEARAEAAEEEVD-ELKSQLADYQQaldVQQtraiQYQQAVQALERA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 292 RDQRQGERLEHAAA---LRALQDQIQTAkTQELNMLREQ-NTELAAELKHRQAdYEELMGQKDDLN-SQLQESLRANSRL 366
Cdd:PRK04863 427 KQLCGLPDLTADNAedwLEEFQAKEQEA-TEELLSLEQKlSVAQAAHSQFEQA-YQLVRKIAGEVSrSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 367 LEQLQEMGQEKEQLIQDLQEARKSAEKRKV---MLDELAMEtLQEKSQHKEELGAVRLRHEKEMLGVRArYERELRELHE 443
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSELEQRLRQQQRaerLLAEFCKR-LGKNLDDEDELEQLQEELEARLESLSE-SVSEARERRM 582
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958806467 444 DKKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 480
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQS 619
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
182-392 |
1.98e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 182 PMPLAEVELKWEMEREEKKLLWEQlqglessKQAETSRLQEELAKLSEKLKKKQESfCRLQTEKETLFNDSRNKIEE--- 258
Cdd:PRK10246 656 TLPQEDEEASWLATRQQEAQSWQQ-------RQNELTALQNRIQQLTPLLETLPQS-DDLPHSEETVALDNWRQVHEqcl 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 259 -LQ---QRKEADLKAQLARTQKLQQELEAANQS---------LAELRDQRQGERLEhaAALRALQDQIQTAKTqelnMLR 325
Cdd:PRK10246 728 sLHsqlQTLQQQDVLEAQRLQKAQAQFDTALQAsvfddqqafLAALLDEETLTQLE--QLKQNLENQRQQAQT----LVT 801
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806467 326 EQNTELAAELKHR------QADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQ---LIQDLQEARKSAE 392
Cdd:PRK10246 802 QTAQALAQHQQHRpdgldlTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQqqaLMQQIAQATQQVE 877
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
221-386 |
2.47e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.51 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 221 QEELAKLSEKLKKKQESFCRlQTEKETLFNDSRNKIEELQQRKE---ADLKAQLARTQKLQQE--LEAANQSLAELrdQR 295
Cdd:pfam13779 508 DEEIAKLMQELREALDDYMQ-ALAEQAQQNPQDLQQPDDPNAQEmtqQDLQRMLDRIEELARSgrRAEAQQMLSQL--QQ 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 296 QGERLEhAAALRALQDQIQTAKTQELN----MLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQ 371
Cdd:pfam13779 585 MLENLQ-AGQPQQQQQQGQSEMQQAMDelgdLLREQQQLLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQ 663
|
170
....*....|....*
gi 1958806467 372 EMGQEKEQLIQDLQE 386
Cdd:pfam13779 664 MPPQGGAEALGDLAE 678
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
227-332 |
2.54e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.24 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 227 LSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQELEAANQSLAELRDqrqgerl 300
Cdd:PRK06975 344 LNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQasvhqlDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRD------- 416
|
90 100 110
....*....|....*....|....*....|..
gi 1958806467 301 ehaAALRALQDQIQTAKTQELNMlrEQNTELA 332
Cdd:PRK06975 417 ---DWMIAEVEQMLSSASQQLQL--TGNVQLA 443
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-569 |
2.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 185 LAEVELKWEMEREEKKLLWEQLQGLES---SKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL---FNDSRNKIEE 258
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEEraeELREEAAELESELEEAREAVEDRREEIEELEEEIEELrerFGDAPVDLGN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 259 LQQRKEaDLKAQLARTQKLQQELEAANQSLAELRdqRQGERL----------------EHAAALRALQDQIQTAKTqELN 322
Cdd:PRK02224 410 AEDFLE-ELREERDELREREAELEATLRTARERV--EEAEALleagkcpecgqpvegsPHVETIEEDRERVEELEA-ELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 323 MLREQNTEL------AAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKV 396
Cdd:PRK02224 486 DLEEEVEEVeerlerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 397 MLDElAMETLQEKSQHKEELGAVRLRHEK--EMLGVRARYERE---LRELHEDKKRQEEELRGQIREEKARTRELEnlqh 471
Cdd:PRK02224 566 EAEE-AREEVAELNSKLAELKERIESLERirTLLAAIADAEDEierLREKREALAELNDERRERLAEKRERKRELE---- 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 472 tvEELQaqvhsmdgakgwfERRLKEAEESLLQQeqeqeetlkqcrEQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTI 551
Cdd:PRK02224 641 --AEFD-------------EARIEEAREDKERA------------EEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
410
....*....|....*...
gi 1958806467 552 SNLKQEVKDTVDGQRILE 569
Cdd:PRK02224 694 EELRERREALENRVEALE 711
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
204-401 |
3.18e-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: 41.36 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 204 EQLQGLESSKQAETSRLQEELAklsEKLKKKQESFCRLQTEKETLFNDSRnkiEELQQRKEADLKAQLARTQKLQQELEA 283
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALA---ERKDSANERLNSLEAQLKQLDKKHQ---AWLEEQKEQKREARTEKQAYWQVVEGA 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 284 ANQSLAELRDQRQGERLEHAAALRALQ------------DQIQTAKTQELNMLREQNTELAAELKHRQADYEELMG---- 347
Cdd:pfam12128 727 LDAQLALLKAAIAARRSGAKAELKALEtwykrdlaslgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQetwl 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806467 348 -QKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL 401
Cdd:pfam12128 807 qRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
253-479 |
4.13e-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: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 253 RNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQ-----------RQGERLEHAAALRALQDQIQTAKTQEL 321
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSfsgssttdtglTKGSRFTHTEKLQFTNEAPAATSSPPT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 322 NMLREQNTElaaelKHRQADYEELMGQKDDLNS---QLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVML 398
Cdd:pfam05667 322 KVETEEELQ-----QQREEELEELQEQLEDLESsiqELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 399 --DELAMETLQEK----SQHKEELGAVRLRHEKEMLgvrARYeRELRELHEDKKRQEEELRGQIREEKARTRELENLQHT 472
Cdd:pfam05667 397 pdAEENIAKLQALvdasAQRLVELAGQWEKHRVPLI---EEY-RALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQ 472
|
....*..
gi 1958806467 473 VEELQAQ 479
Cdd:pfam05667 473 KEELYKQ 479
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
194-483 |
4.42e-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: 40.59 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 194 MEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLAR 273
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 274 TQKLQQELEAANQSL--------------AELRDQRQGERLEHAAALRALQDQIQ--TAKTQELNMLREQ--NTELAAEL 335
Cdd:pfam12128 317 VAKDRSELEALEDQHgafldadietaaadQEQLPSWQSELENLEERLKALTGKHQdvTAKYNRRRSKIKEqnNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 336 KHRQADYEELMGQKDDLNSQLQESLRA-NSRLLEQLQEMGQEKEQLIQDLQEArksaekrKVMLDELAM--ETLQEKSQH 412
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL-------KLRLNQATAtpELLLQLENF 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806467 413 KEELGAVRLRHEKEmlgvRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSM 483
Cdd:pfam12128 470 DERIERAREEQEAA----NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-590 |
6.38e-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: 39.75 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 357 QESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHekemlgvrARYER 436
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--------AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 437 ELRELHEDKKRQEEELRGQIRE-EKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQc 515
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806467 516 rEQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRA 590
Cdd:COG4942 170 -EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
193-545 |
6.50e-03 |
|
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: 40.09 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 193 EMEREE-KKLLWEQLQGLESSKQAEtsrlqeelaKLSEKLKKKQESFCRLQTEKETLFNDSRNKI------EELQQRKEA 265
Cdd:pfam05483 404 EVELEElKKILAEDEKLLDEKKQFE---------KIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktsEEHYLKEVE 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 266 DLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQNTELAAELKHR---QADY 342
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRdelESVR 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 343 EELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEK---SQHKEELGAV 419
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgSAENKQLNAY 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 420 RLRHEK---EMLGVRARYERELRELH---EDKKRQEEELRGQIREEKARTRELENLQHTVE-----ELQAQVHSMDGAKG 488
Cdd:pfam05483 635 EIKVNKlelELASAKQKFEEIIDNYQkeiEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKH 714
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806467 489 WFERRLKEaEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERD 545
Cdd:pfam05483 715 QYDKIIEE-RDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKE 770
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
199-328 |
6.57e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 199 KKLLWEQLQGLESSKQaetsRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRKEADLKAQLARTQKLQ 278
Cdd:smart00787 146 KEGLDENLEGLKEDYK----LLMKELELLNSIKPKLRDRKDALEEELRQL----KQLEDELEDCDPTELDRAKEKLKKLL 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 279 QELEAANQSLAELRDQRQgerlEHAAALRALQDQIQTAKTQ--ELNMLREQN 328
Cdd:smart00787 218 QEIMIKVKKLEELEEELQ----ELESKIEDLTNKKSELNTEiaEAEKKLEQC 265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
365-600 |
8.10e-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: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 365 RLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELametLQEKSQHKEELGavRLRHEKEMLGvraRYERELRELHED 444
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL----SQELSDASRKIG--EIEKEIEQLE---QEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 445 KKRQEEELRGQIREEKArtrELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELK 524
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 525 GK-----------EEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTvdgQRILEKKGSAVLKDLKRQLHLERKRaDKL 593
Cdd:TIGR02169 819 QKlnrltlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEELEELEAALRDLESRLGDLKKER-DEL 894
|
....*..
gi 1958806467 594 QERLQEI 600
Cdd:TIGR02169 895 EAQLREL 901
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
193-392 |
8.70e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 193 EMEREEKKLLWEQlqglESSKQAETSRLQEELAKLSEKLK----KKQESFCRLQTEKEtlfnDSRNKIEELQQRKEADLK 268
Cdd:pfam17380 417 QQKVEMEQIRAEQ----EEARQREVRRLEEERAREMERVRleeqERQQQVERLRQQEE----ERKRKKLELEKEKRDRKR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 269 AQLARTQKLQQELEAANQSLAELRDQRQGERLEhaaalralqdqiqtaktqelnmLREQNTELAAELKHRQADYEELMGQ 348
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEKE----------------------MEERQKAIYEEERRREAEEERRKQQ 546
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958806467 349 KDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAE 392
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
195-401 |
8.96e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 195 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKetlfndsrnkieelqqrkeADLKAQLART 274
Cdd:PHA02562 214 NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA-------------------AKIKSKIEQF 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 275 QKLQ-------------QELEAANQSLAELRDQRQgerlEHAAALRALQDQIQTAKTQ--ELNMLREQNTELAAELKHRQ 339
Cdd:PHA02562 275 QKVIkmyekggvcptctQQISEGPDRITKIKDKLK----ELQHSLEKLDTAIDELEEImdEFNEQSKKLLELKNKISTNK 350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806467 340 ADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDEL 401
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
242-560 |
9.25e-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: 39.72 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 242 QTEKETLFNDSRNKIEELQQRKEADL-----KAQLARTQ--KLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQ 314
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLISEHEVEItglteKASSARSQanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 315 TAKTQELNMLREQNTELA---AELKHRQADYEELMGQKDDLNSQLQESLranSRLLEQLQEMGQEKEQ---LIQDLQEAR 388
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVlanSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKREKELSLEKEQnkrLWDRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 389 KSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYE--RELRELHEDKKRQEEELRGQIREEKARTREL 466
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806467 467 ENLQHTVEELQAQVHSmdgakgwferrlKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDG 546
Cdd:pfam15921 492 ESSERTVSDLTASLQE------------KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
330
....*....|....
gi 1958806467 547 HVKTISNLKQEVKD 560
Cdd:pfam15921 560 KDKVIEILRQQIEN 573
|
|
| |
