|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-360 |
3.04e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKKLL---WEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsfcRLQTEKETLfNDSRNKIEELQQRkEA 118
Cdd:COG1196 217 ELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEA---ELEELRLEL-EELELELEEAQAE-EY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 119 DLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVssqsADAQEQVEGLLAENSALRTSLAALEQIQ 198
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 199 TAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 278
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 279 KVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVE 358
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
..
gi 569008872 359 EL 360
Cdd:COG1196 528 VL 529
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-486 |
1.94e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 142 AELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQH 221
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 222 RQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEELG 301
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 302 AVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEA 381
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 382 EESLQQQQQEQEETLKLcrEEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQevkdtVDGQRILEKKGSAVLK 461
Cdd:COG1196 459 EALLELLAELLEEAALL--EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL-----LAGLRGLAGAVAVLIG 531
|
330 340
....*....|....*....|....*
gi 569008872 462 DLKRqlhLERKRADKLQERLQEILT 486
Cdd:COG1196 532 VEAA---YEAALEAALAAALQNIVV 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-570 |
3.25e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 43 LKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLsEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK------ 116
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEAQAEEYELLAELARLEQDIarleer 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 117 ----EADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLA 192
Cdd:COG1196 311 rrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 193 ALEQIQTAKTQELNmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEAR 272
Cdd:COG1196 391 ALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 273 KSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRH-------EKELLGVRARYERELRELHEDKKRQEEEL--RGQIREE 343
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 344 KARTRELENLQHTVEELQAQvhsmDGAKGWFERRLKEAEESLQQQQQEQEETLKLcREEHAAELKGKDEELQNVREQL-- 421
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAA----KAGRATFLPLDKIRARAALAAALARGAIGAA-VDLVASDLREADARYYVLGDTLlg 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 422 -QQAQEERDGHVKTISNLKQEVKD-TVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVL 499
Cdd:COG1196 625 rTLVAARLEAALRRAVTLAGRLREvTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008872 500 SEMNSPSRTQTGDSSSVSSFSYREILKEKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQE 570
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-372 |
1.57e-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: 71.24 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 43 LKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNdsrnkIEELQQRKEADLKA 122
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA-----LANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 123 QLARTQKLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKT 202
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLD--------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 203 QELNMLReqtselaselqhrqAEYEELMGQKDDLNSQLQeslransRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmL 282
Cdd:TIGR02168 379 EQLETLR--------------SKVAQLELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKKLEEAE--L 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 283 DELAMEtLQEKSQHKEELGAVRLRHEKELLGVRARYErELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQA 362
Cdd:TIGR02168 436 KELQAE-LEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
330
....*....|
gi 569008872 363 QVHSMDGAKG 372
Cdd:TIGR02168 514 NQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
41-364 |
1.90e-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: 70.86 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 41 VELKWEMEREEKKLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQesfcRLQTEKETLFNDSRNKIEELQQRKEAdl 120
Cdd:TIGR02168 673 LERRREIEELEEKI--EELEEKIAELEKALAELRKELEELEEELEQLR----KELEELSRQISALRKDLARLEAEVEQ-- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 121 kaQLARTQKLQQELEAANQSLAELRDQRQGERlEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTA 200
Cdd:TIGR02168 745 --LEERIAQLSKELTELEAEIEELEERLEEAE-EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 201 KTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKV 280
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 281 MLDEL---AMETLQEKSQHKEELGAVRLRHEKeLLGVRARYERELRELHEDkkrqeeELRGQIREEKARTRELENLQHTV 357
Cdd:TIGR02168 902 ELRELeskRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSL------TLEEAEALENKIEDDEEEARRRL 974
|
....*..
gi 569008872 358 EELQAQV 364
Cdd:TIGR02168 975 KRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-486 |
1.91e-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: 70.86 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 64 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL--FNDSRNKIEElqQRKEADLKAQLA-RTQKLQQELEAANQS 140
Cdd:TIGR02168 151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLdrLEDILNELER--QLKSLERQAEKAeRYKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 141 LAELRDQRQGERLEhaaALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQ 220
Cdd:TIGR02168 229 LLVLRLEELREELE---ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 221 HRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmldelamETLQEKSQHKEEL 300
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------AELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 301 gavrlrhEKELLGVRARYerelrelhEDKKRQEEELRGQIREEKARtreLENLQHTVEELQAQVhsmdgakgwfERRLKE 380
Cdd:TIGR02168 378 -------EEQLETLRSKV--------AQLELQIASLNNEIERLEAR---LERLEDRRERLQQEI----------EELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 381 AEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVl 460
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV- 508
|
410 420
....*....|....*....|....*.
gi 569008872 461 kdlkRQLHLERKRADKLQERLQEILT 486
Cdd:TIGR02168 509 ----KALLKNQSGLSGILGVLSELIS 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-475 |
3.48e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 48 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLAR- 126
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEAKk 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 127 ---TQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQ 203
Cdd:PTZ00121 1446 adeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 204 ELNMLREQTSelASELqhRQAEYEElmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR----- 278
Cdd:PTZ00121 1526 EAKKAEEAKK--ADEA--KKAEEKK---KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevm 1598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 279 KVMLDELAMETLQEKSQHKEELGAVRLRHEKEllgVRARYErELRELHEDKKRQEEELRGQIREEKARTRELENlqhtvE 358
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE---EKKKVE-QLKKKEAEEKKKAEELKKAEEENKIKAAEEAK-----K 1669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 359 ELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEH---AAELKGKDEELQNVREQLQQAQEE-------- 427
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkAEELKKAEEENKIKAEEAKKEAEEdkkkaeea 1749
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 569008872 428 --RDGHVKTISNLKQEVKDTVDGQRileKKGSAVL------KDLKRQLHLERKRAD 475
Cdd:PTZ00121 1750 kkDEEEKKKIAHLKKEEEKKAEEIR---KEKEAVIeeeldeEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-601 |
9.05e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 49 REEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEELQQRKEADLK---AQLA 125
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKA 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 126 RTQKLQQELEAANQSlAELRDQRQGERLEHAAALRALQDQVsSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTqel 205
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEK-KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK--- 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 206 nmlREQTSELASELQHRQAEYEelmgQKDDLNSQLQESLRANSrlLEQLQEIGQEKEQLTQDLQEARKSAE-KRKVMLDE 284
Cdd:PTZ00121 1426 ---KAEEKKKADEAKKKAEEAK----KADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 285 LAMETLQEKSQHKEELGAVRLRHEKellgvraRYERELRELHEdkKRQEEELRGQIREEKA-RTRELENLQHTVEELQA- 362
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEE--AKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAe 1567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 363 QVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKgKDEELQNVREQLQQAQEERDGHVKTISNLKQEV 442
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 443 KDTvDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEiltnskSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYR 522
Cdd:PTZ00121 1647 KKA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 523 EILKEKESSAIPARSLSSSPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 601
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-292 |
9.31e-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: 65.46 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 38 LAEVELKWE---MEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ 114
Cdd:TIGR02168 262 LQELEEKLEelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 115 RKEadlkaqlaRTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAAL 194
Cdd:TIGR02168 342 LEE--------KLEELKEELESLEAELEELEAELE-ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 195 EqiqtaktQELNMLREQTSELASELQhrQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKS 274
Cdd:TIGR02168 413 E-------DRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250
....*....|....*...
gi 569008872 275 AEKRKVMLDelAMETLQE 292
Cdd:TIGR02168 484 LAQLQARLD--SLERLQE 499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-464 |
1.14e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 50 EEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESfCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQK 129
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 130 LQQELEAANQS--------LAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQvegllAENSALRTSlAALEQIQTAK 201
Cdd:PTZ00121 1520 EAKKADEAKKAeeakkadeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE-----DKNMALRKA-EEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 202 TQELNMLREQTSELASElQHRQAEYEELMGQK-------DDLNSQLQESLRANSRLLEQLQEigQEKEQLTQDLQEARKS 274
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEElkkaeeeKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKA 1670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 275 AEKRKvmldelAMETLQEKSQHKEELGAVRLRHEKEllgvrARYERELRELHEDKKRQEEELRgqiREEKARTRELENLQ 354
Cdd:PTZ00121 1671 EEDKK------KAEEAKKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKAEELK---KAEEENKIKAEEAK 1736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 355 HTVEElqaqvhsmdgakgwfERRlKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELqnVREQLQQAQEERDGHV-K 433
Cdd:PTZ00121 1737 KEAEE---------------DKK-KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVdK 1798
|
410 420 430
....*....|....*....|....*....|.
gi 569008872 434 TISNLKQEVKDTVDGQrileKKGSAVLKDLK 464
Cdd:PTZ00121 1799 KIKDIFDNFANIIEGG----KEGNLVINDSK 1825
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-484 |
1.97e-10 |
|
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: 64.31 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 48 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ--RKEADLKAQLA 125
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAaeRELAQLQARLD 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 126 RTQKLQQELEAANQSLAELRDQRQG---------------ERLEHA--AALRALQDQVSSQSADAQEQVEGLLAENSALR 188
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdEGYEAAieAALGGRLQAVVVENLNAAKKAIAFLKQNELGR 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 189 TSLAALEQIQTAKTQELNMLREQTS--------------------------------------ELASELQH--------- 221
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIegflgvakdlvkfdpklrkalsyllggvlvvddldnalELAKKLRPgyrivtldg 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 222 ----------------------RQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARksaekRK 279
Cdd:TIGR02168 653 dlvrpggvitggsaktnssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-----RQ 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 280 VMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEE 359
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 360 LQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEET------LKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVK 433
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 569008872 434 TISNLKQEVKDTVDGQRILEKKgsavLKDLKRQLHLERKRADKLQERLQEI 484
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESK----RSELRRELEELREKLAQLELRLEGL 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
65-278 |
2.13e-10 |
|
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: 63.24 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 65 SKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAEL 144
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 145 RDQRQGERLEHAAALRALQDQ---------VSSQSA-DAQEQVEGLLAENSALRTSLAALEQIQT---AKTQELNMLREQ 211
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplallLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008872 212 TSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 278
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-483 |
2.69e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDS-RNKIEELQQRKEADL 120
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAaKKKAEEKKKADEAKK 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 121 KAQLAR-----TQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALE 195
Cdd:PTZ00121 1399 KAEEDKkkadeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 196 QIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRA--NSRLLEQLQEIGQ-EKEQLTQDLQEAR 272
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAEEkKKADELKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 273 KSAEKRKVmldelametlqEKSQHKEELGAVRLRHEKELLGV-RARYERELRELHEDKKRQEEELRGQiREEKARTRELE 351
Cdd:PTZ00121 1559 KAEEKKKA-----------EEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELK 1626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 352 NlqhtVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREE--HAAELKGKDEELQNVREQLQQAQEERD 429
Cdd:PTZ00121 1627 K----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 569008872 430 gHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQE 483
Cdd:PTZ00121 1703 -KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-460 |
1.78e-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: 61.24 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 68 AETSRLQEELAKLSEKLKKKQESFCRLQTEKETL--FNDSRNKIEELQQ----RKEADLKAQLARTQKLQQELEAANQSL 141
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAerYQALLKEKREYEGyellKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 142 AELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAEnsaLRTSLAALEQIQTAKTQELNmlreqtsELASELQH 221
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE---LEAEIASLERSIAEKERELE-------DAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 222 RQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEarksaekrkvmLDELAMETLQEKSQHKEELG 301
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-----------VDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 302 AVRLRHEkELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELqaqvhsmdgakgwfERRLKea 381
Cdd:TIGR02169 396 KLKREIN-ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--------------EWKLE-- 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569008872 382 eeslqqqqqeqeeTLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVL 460
Cdd:TIGR02169 459 -------------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
46-357 |
4.21e-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: 60.08 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 46 EMEREEKKLLwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEAD---LKA 122
Cdd:TIGR02169 685 GLKRELSSLQ-SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL-EELEEDLSSLEQEIENVkseLKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 123 QLARTQKLQQELEAANQSLAELRDQRQGERLEH-AAALRALQDQVSSQSADAQE---QVEGLLAENSALRTSLAALEQIQ 198
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 199 TAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 278
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 279 KVM-------LDELAMETLQEKSQHKEELGAVRLRHEKELLGVRAR------------YERELRELHEDKKRQE--EELR 337
Cdd:TIGR02169 923 KAKlealeeeLSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiqeYEEVLKRLDELKEKRAklEEER 1002
|
330 340
....*....|....*....|
gi 569008872 338 GQIREekaRTRELENLQHTV 357
Cdd:TIGR02169 1003 KAILE---RIEEYEKKKREV 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-486 |
4.87e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMER-EEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQRKE 117
Cdd:PRK02224 217 ELDEEIERyEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELaeeVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 118 ----------ADLKAQLARTQKLQQELEAANQSLAELRdQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSAL 187
Cdd:PRK02224 297 dllaeaglddADAEAVEARREELEDRDEELRDRLEECR-VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 188 RTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEsLRANSRLLEQLQEIGQEkeqltqd 267
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE-LEATLRTARERVEEAEA------- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 268 LQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYER--ELRELH------EDKKRQEEELRGQ 339
Cdd:PRK02224 448 LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERaeDLVEAEdrierlEERREDLEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 340 IREEKARTRE-LENLQHTVEELQAQvhsmdgAKGWFERRLKEAEESLQQQQQ-----EQEETLKLCRE---------EHA 404
Cdd:PRK02224 528 RRETIEEKRErAEELRERAAELEAE------AEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIEslerirtllAAI 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 405 AELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGsavlkdlkrqlhlERKRADKLQERLQEI 484
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARE-------------DKERAEEYLEQVEEK 668
|
..
gi 569008872 485 LT 486
Cdd:PRK02224 669 LD 670
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-596 |
3.71e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 46 EMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSE----KLKKKQESFCRLQTEKETlfnDSRNKIEELQQRKEADlK 121
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDakrvEIARKAEDARKAEEARKA---EDAKKAEAARKAEEVR-K 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 122 AQLARTQKLQQELEAANQSLAELR--DQRQGERLEHAAALRALQD-QVSSQSADAQEQVEGLLAENSALRTSLAALEQIQ 198
Cdd:PTZ00121 1190 AEELRKAEDARKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEaKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 199 TAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANsRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 278
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 279 KVMLDELAMETlqEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRG--QIREEKARTRELENLQHT 356
Cdd:PTZ00121 1349 KAEAEAAADEA--EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKK 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 357 VEELQA---------QVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREE--HAAELKGKDEELQNVREQLQQAQ 425
Cdd:PTZ00121 1427 AEEKKKadeakkkaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAA 1506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 426 EERDghvKTISNLKQEVKDTVDGQRILEKKGSAvlKDLKRQlhLERKRADKLQeRLQEILTNSKSRTGLEELVLSEMNSP 505
Cdd:PTZ00121 1507 EAKK---KADEAKKAEEAKKADEAKKAEEAKKA--DEAKKA--EEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 506 SRTQTGDSSSVSSFSYREILK-EKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVS 584
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
570
....*....|..
gi 569008872 585 SASMAEDLCRKS 596
Cdd:PTZ00121 1659 NKIKAAEEAKKA 1670
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-368 |
3.81e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 117 EADLKAQLARTQKLQQELEAANQSLAELRDQRqgERLEHAAALralqdqvssqsADAQEQVEGLLAENSALRTSLAALEQ 196
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQI--ELLEPIREL-----------AERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 197 iqtakTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslransrLLEQLQEI-GQEKEQLTQDLQEARKSA 275
Cdd:COG4913 287 -----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDE-------LEAQIRGNgGDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 276 EKRKVMLDELAmetlqeksQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQH 355
Cdd:COG4913 355 EERERRRARLE--------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250
....*....|...
gi 569008872 356 TVEELQAQVHSMD 368
Cdd:COG4913 427 EIASLERRKSNIP 439
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-359 |
1.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 114 QRKEADLKAQLARtqkLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQ--SADAQEQVEGLLAENSALRTSL 191
Cdd:COG4913 609 RAKLAALEAELAE---LEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 192 AALEQiqtaktqelnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEA 271
Cdd:COG4913 685 DDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 272 RKSAEKRKVMLDELAMETLQEKSQHKEELGavrlRHEKELLGVRAR---------------------YERELRELHEDK- 329
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLN----RAEEELERAMRAfnrewpaetadldadleslpeYLALLDRLEEDGl 829
|
250 260 270
....*....|....*....|....*....|
gi 569008872 330 KRQEEELRGQIREEKarTRELENLQHTVEE 359
Cdd:COG4913 830 PEYEERFKELLNENS--IEFVADLLSKLRR 857
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-350 |
2.44e-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: 54.29 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKKLLWEQLQGLESSKQAETsrLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLK 121
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLESLERRIA 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 122 AQLARTQKLQQELEAANQSLAELRDQRqgerlehaAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAK 201
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEI--------EELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 202 TQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANsrlleqLQEIGQEKEQLTQDLQEARKSAEKrkvm 281
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT------LEEAEALENKIEDDEEEARRRLKR---- 976
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569008872 282 ldelametLQEKsqhKEELGAVRLRHEKELLGVRARYErELRELHEDKKRQEEELRGQIREEKARTREL 350
Cdd:TIGR02168 977 --------LENK---IKELGPVNLAAIEEYEELKERYD-FLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
42-246 |
2.84e-07 |
|
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: 53.23 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKKLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLK 121
Cdd:COG4942 31 QLQQEIAELEKEL--AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-EKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 122 AQLARTQKL-----------QQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTS 190
Cdd:COG4942 108 ELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAP-ARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569008872 191 LAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRA 246
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
50-478 |
4.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 50 EEKKLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfnDSRNKIEELQQRKEAdLKAQLARTQK 129
Cdd:COG4717 71 KELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKL--EKLLQLLPLYQELEA-LEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 130 LQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLR 209
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 210 EQTSELASELQhRQAEYEELMGQKDDLNSQ-LQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAME 288
Cdd:COG4717 227 EELEQLENELE-AAALEERLKEARLLLLIAaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 289 TLQEKSqHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARtRELENLQHTVEEL--QAQVHS 366
Cdd:COG4717 306 ELQALP-ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQLEELEQEIAALlaEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 367 MDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKD---EELQNVREQLQQAQEERDGHVKTISNLKQEVK 443
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430
....*....|....*....|....*....|....*
gi 569008872 444 DTVDGQRILEKKgsAVLKDLKRQLHLERKRADKLQ 478
Cdd:COG4717 464 QLEEDGELAELL--QELEELKAELRELAEEWAALK 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
113-489 |
4.42e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 113 QQRKEADLK-----AQLARTQKLQQELEAANQSLaelrdQRQGER----LEHAAALRALQDQVSSQSAD-AQEQVEGLLA 182
Cdd:TIGR02168 172 ERRKETERKlertrENLDRLEDILNELERQLKSL-----ERQAEKaeryKELKAELRELELALLVLRLEeLREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 183 ENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKE 262
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 263 QLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEelgavrlrhekellgvraryereLRELHEDKKRQEEELRGQIRE 342
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEE-----------------------LEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 343 EKARTRELENlqhTVEELQAQVHSMDgakgwferrlkeaeES----LQQQQQEQEETLKLCREEHAAELKGKDEELQNVR 418
Cdd:TIGR02168 384 LRSKVAQLEL---QIASLNNEIERLE--------------ARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008872 419 EQLQQAQEERDGHVKTISNLKQEVkdtvdgqrileKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 489
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREEL-----------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-280 |
4.63e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 72 RLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEAD-----LKAQLARTQKLQQELEAANQSLAELRD 146
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEidvasAEREIAELEAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 147 QRQGERLEHaAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQEL-------NMLREQTSELASEL 219
Cdd:COG4913 693 QLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaaALGDAVERELRENL 771
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008872 220 QHRQAEYEELMGQK---------------DDLNSQLQESLRANSRLLEQLQEIGQEK-EQLTQDLQEARKSAEKRKV 280
Cdd:COG4913 772 EERIDALRARLNRAeeeleramrafnrewPAETADLDADLESLPEYLALLDRLEEDGlPEYEERFKELLNENSIEFV 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-490 |
1.17e-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: 52.38 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 150 GERLEHAAALRALQDQVSSQSAdaQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEEL 229
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRL--RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 230 MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmlDELAMETLQEKsqhkeelgavrlrhek 309
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEI---------------- 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 310 ellgvraryERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEaeeslqqqq 389
Cdd:TIGR02169 797 ---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN--------- 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 390 qeqeetLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTvdgqrilekkgSAVLKDLKRQLHL 469
Cdd:TIGR02169 859 ------LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-----------EAQIEKKRKRLSE 921
|
330 340
....*....|....*....|.
gi 569008872 470 ERKRADKLQERLQEILTNSKS 490
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGE 942
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
40-483 |
1.25e-06 |
|
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: 51.89 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 40 EVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieELQQRKEAD 119
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ---------EEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 120 LKAQLARTQKLQQELEAANQSLAELRDQRQGERL-EHAAALRALQDQVSSQSADAQEQvEGLLAENSALRTSLAALEQIQ 198
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLaAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 199 TAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNS--QLQESLRAnsrLLEQLQEIGQEKEQLTQDL-QEARKSA 275
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQKTT---LTQKLQSLCKELDILQREQaTIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 276 EKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRgQIREEKARTRELEnlQH 355
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-QIHLQETRKKAVV--LA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 356 TVEELQAQVHSmdgakgwFERRLKEAEESLQQQQQEQEETLKLCREE-----HAAELKGKDEELQNVREQLQQAQEERDG 430
Cdd:TIGR00618 495 RLLELQEEPCP-------LCGSCIHPNPARQDIDNPGPLTRRMQRGEqtyaqLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 569008872 431 HVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQE 483
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
38-367 |
1.32e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 38 LAEVELKWEMEREEKKLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQT----EKETLFNDSRNKIEELQ 113
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEE-RLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 114 QRK---EADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTS 190
Cdd:COG4717 206 QRLaelEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 191 LAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQE 270
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 271 ARkSAEKRKVMLDELAMETLQEKSQHkeelgAVRLRHEKELLGVRARYERELREL---------HEDKKRQEEELRGQIR 341
Cdd:COG4717 366 EE-LEQEIAALLAEAGVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEE 439
|
330 340
....*....|....*....|....*.
gi 569008872 342 EEKARTRELENLQHTVEELQAQVHSM 367
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQL 465
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
94-444 |
1.90e-06 |
|
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: 51.66 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 94 LQTEKETLFNDSRNKIEELQQRKEAdlkaqlaRTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADA 173
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQD-------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 174 QEQVEGLLAENSALRTSLAALEQIQTAKTQElnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLranSRLLEQ 253
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 254 LQEIGQEKEQ----LTQDLQEARKSAEKRKvMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYE--RELRELHE 327
Cdd:pfam15921 390 EKELSLEKEQnkrlWDRDTGNSITIDHLRR-ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 328 DKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHsmdgakgwfERRLKEAEESLQQQQQEQEETLKLCREEHaaeL 407
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---------EKERAIEATNAEITKLRSRVDLKLQELQH---L 536
|
330 340 350
....*....|....*....|....*....|....*..
gi 569008872 408 KGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKD 444
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
93-354 |
1.96e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 93 RLQTEKETLFNDSRNKIEElqqRKEADLKAQLARtqkLQQELEAANQSLAELRDQRqgerlEHAAALRALQDQVSSQSAD 172
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEE---KEEKDLHERLNG---LESELAELDEEIERYEEQR-----EQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 173 AQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAE--------------YEELMGQKDDLNS 238
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeavearREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 239 QLQ-------------ESLRANSRLLE-QLQEIGQEKEQLTQDLQEARKSAEKRKVMLDEL--AMETLQEksqhkeelga 302
Cdd:PRK02224 329 RLEecrvaaqahneeaESLREDADDLEeRAEELREEAAELESELEEAREAVEDRREEIEELeeEIEELRE---------- 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 569008872 303 vRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 354
Cdd:PRK02224 399 -RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
73-271 |
2.92e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 73 LQEELAKLseklkKKQESfcrLQTEKETLFNDSRNKIEELQQRKEadlkaQLARTQKLQQELEAANQSLAElrDQRQGER 152
Cdd:PRK11281 41 VQAQLDAL-----NKQKL---LEAEDKLVQQDLEQTLALLDKIDR-----QKEETEQLKQQLAQAPAKLRQ--AQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 153 LEHAAA-----------LRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTA------KTQELNML-----RE 210
Cdd:PRK11281 106 LKDDNDeetretlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlyansqRLQQIRNLlkggkVG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569008872 211 QTSELASELQHRQAEYEELMGQkddlNSQLQESLRANSrlleQLQEIGQEK-----------EQLTQDLQEA 271
Cdd:PRK11281 186 GKALRPSQRVLLQAEQALLNAQ----NDLQRKSLEGNT----QLQDLLQKQrdyltariqrlEHQLQLLQEA 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-352 |
6.61e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 172 DAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEY--EELMGQKDDLNSQLQEsLRANSR 249
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 250 LLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDElAMETLQEksQHKEELGAVRLRHEKELLGVRARYERELRELHEDK 329
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEE--ELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*
gi 569008872 330 KRQE--EELRGQIREEKARTRELEN 352
Cdd:COG4913 763 VERElrENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
75-247 |
6.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 75 EELAKLSEKLKKKQESFCRLQTEKETL--FNDSR--NKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQ- 149
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALrlWFAQRrlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 150 --GERLEHAAA-LRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEY 226
Cdd:COG4913 335 ngGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|.
gi 569008872 227 EELMGQKDDLNSQLqESLRAN 247
Cdd:COG4913 415 RDLRRELRELEAEI-ASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-509 |
7.09e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 256 EIGQEKEQLTQDLQEARKSAEKRKVMLDELA--METLQEKSQHKEELGAVRLRHEkellgvraryERELRELHEDKKRQE 333
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKR----------EYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 334 EELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEE 413
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 414 LQNVREQLQQAQEERDGHVKTISNLKQEVKDtvdgQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTG 493
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250
....*....|....*.
gi 569008872 494 LEELVLSEMNSPSRTQ 509
Cdd:TIGR02169 393 KLEKLKREINELKREL 408
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
42-366 |
7.30e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLK 121
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 122 AQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAK 201
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 202 TQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVM 281
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 282 LDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQ 361
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
....*
gi 569008872 362 AQVHS 366
Cdd:pfam02463 494 KLEER 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-367 |
8.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 167 SSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEY-------EELMGQKDDLNSQ 239
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleaelAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 240 LQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELA------METLQEKSQHKEELGAVRLRHEKELLG 313
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569008872 314 VRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSM 367
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
57-267 |
9.21e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 57 EQLQGLESSKQaETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNK--IEELQQRKEADLKAQlartQKLQQEL 134
Cdd:PRK11281 70 ALLDKIDRQKE-ETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLRQLESRLAQTLDQL----QNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 135 EAANQSLAELrdQRQGERlehaaalraLQDQVSSQSADAQE---QVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQ 211
Cdd:PRK11281 145 AEYNSQLVSL--QTQPER---------AQAALYANSQRLQQirnLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRK 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 212 TSELASELQH-RQAEYEELMGQKDDLNSQ---LQESLraNSRLLEQLQEigQEKEQLTQD 267
Cdd:PRK11281 214 SLEGNTQLQDlLQKQRDYLTARIQRLEHQlqlLQEAI--NSKRLTLSEK--TVQEAQSQD 269
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-310 |
9.64e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 109 IEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQrqgerLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALR 188
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 189 TSLAALEQIQtaKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQDL 268
Cdd:COG4717 123 KLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569008872 269 QEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 310
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-362 |
1.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 34 APMPLAEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSE-----------------KLKKKQESFCRLQT 96
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRERVEELEA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 97 EKETLfndsRNKIEELQQRKEA--DLKAQLARTQKLQQELEAANQSLAELRDqRQGERLEHAAALRALQDQVSSQSADAQ 174
Cdd:PRK02224 483 ELEDL----EEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERRE-TIEEKRERAEELRERAAELEAEAEEKR 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 175 EQVEGLLAENSALRTSLAALEQIQTAKTQELNMLrEQTSELASELQHRQAEYEELMGQKDDLNSQlqeslraNSRLLEQL 254
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAEL-------NDERRERL 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 255 QEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEElgavrlrHEKELLGVRARYERELRELhedkkrqeE 334
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE-------ERDDLQAEIGAVENELEEL--------E 694
|
330 340
....*....|....*....|....*...
gi 569008872 335 ELRGQIREEKARTRELENLQHTVEELQA 362
Cdd:PRK02224 695 ELRERREALENRVEALEALYDEAEELES 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-458 |
1.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 48 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKEtlfndsrnKIEELQQRKEaDLKAQLART 127
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE--------RLEELKKKLK-ELEKRLEEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 128 QKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLA----ALEQIQTAKT- 202
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKelkkAIEELKKAKGk 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 203 -----------QELNMLREQTSELA---SELQHRQAEYEELMGQKDDLNSQL--QESLRANSRLLEQLQEIGQEKEQLT- 265
Cdd:PRK03918 438 cpvcgrelteeHRKELLEEYTAELKrieKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKELEEKLKKYNl 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 266 QDLQEARKSAEKRKVMLDELAME--TLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIRE- 342
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEl 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 343 -------------EKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKG 409
Cdd:PRK03918 598 epfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAG 677
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 569008872 410 KDEELQNVREQLQQAQeerdghvKTISNLKQEVKDTVDGQRILEKKGSA 458
Cdd:PRK03918 678 LRAELEELEKRREEIK-------KTLEKLKEELEEREKAKKELEKLEKA 719
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
137-364 |
1.09e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 137 ANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSlaaleqiqtaktQELNMLREQTSELA 216
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 217 SELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLE--QLQEIGQEKEQLTQDLQEARksaekrkvmldelamETLQEKS 294
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELS---------------ARYTPNH 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569008872 295 ----QHKEELGAVRLRHEKELLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 364
Cdd:COG3206 291 pdviALRAQIAALRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
72-364 |
1.40e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 72 RLQEELAKLSEKLKKKQESFCRLQTEKEtlfnDSRNKIEELQQRKEaDLKAQLArtqKLQQELEAA-------NQSLAEL 144
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQE----ENEARAEAAEEEVD-ELKSQLA---DYQQALDVQqtraiqyQQAVQAL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 145 RDQRQgerLEHAAALRA--LQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAktqeLNMLREQTSELASELQHR 222
Cdd:PRK04863 424 ERAKQ---LCGLPDLTAdnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQA----YQLVRKIAGEVSRSEAWD 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 223 QAEyeELMGQkddlnsqlQESLRAnsrLLEQLQEIGQEKEQLTQDLQEARkSAEKrkvMLDELAMEtLQEKSQHKEELGA 302
Cdd:PRK04863 497 VAR--ELLRR--------LREQRH---LAEQLQQLRMRLSELEQRLRQQQ-RAER---LLAEFCKR-LGKNLDDEDELEQ 558
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569008872 303 VRLRHEKELLGVRArYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 364
Cdd:PRK04863 559 LQEELEARLESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQS 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-353 |
1.86e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 48 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLART 127
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 128 QKLQQELEAANQSLA---------ELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgLLAENSALRTSLAALEQIQ 198
Cdd:COG1196 505 GFLEGVKAALLLAGLrglagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE-YLKAAKAGRATFLPLDKIR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 199 TAKTQELNMLREQTSELASELQHRQAEYEELM-----------------------------------GQKDDLNSQLQES 243
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgrtlvaarleaalrravtlagrlrevtLEGEGGSAGGSLT 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 244 LRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELR 323
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
330 340 350
....*....|....*....|....*....|....*.
gi 569008872 324 ELHEDKKRQEEELRGQIREEKAR------TRELENL 353
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELErelerlEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-457 |
1.92e-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: 47.45 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 190 SLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQ 269
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 270 EARKSAEKRKVMLDELaMETLQEKSQHKEELGAVRLRHEKELLgVRARYereLRELHEDKKRQEEELRGQIREEKARTRE 349
Cdd:COG4942 94 ELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 350 LENLQHTVEELQAQVhsmdgakgwferrlkeaeeslqQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQEERD 429
Cdd:COG4942 169 LEAERAELEALLAEL----------------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250 260
....*....|....*....|....*...
gi 569008872 430 GHVKTISNLKQEVKDTVDGQRILEKKGS 457
Cdd:COG4942 227 ALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
112-346 |
2.25e-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: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 112 LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEH-AAALRALQDQVSSQSADAQEQVEGLLAENSALRTS 190
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 191 LAALEQIQTAKTQELNMLRE--QTSELASELQHRQAEYEELMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQDL 268
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIA---LRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569008872 269 QEARKSAEKRKVMLDElAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELrelhedKKRQEEELRGQIREEKAR 346
Cdd:COG3206 319 EAELEALQAREASLQA-QLAQLEARLAELPELEAELRRLEREVEVARELYESLL------QRLEEARLAEALTVGNVR 389
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
108-326 |
2.36e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 108 KIEEL-QQRKEADLKA-----QLARTQKLQQELEAAN-QSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGL 180
Cdd:PHA02562 175 KIRELnQQIQTLDMKIdhiqqQIKTYNKNIEEQRKKNgENIARKQNKYD-ELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 181 LAENSALRTSLAALE-QIQTAK---------------TQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESL 244
Cdd:PHA02562 254 SAALNKLNTAAAKIKsKIEQFQkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 245 RANSRLLEQLQEIGQEKeqltQDLQEARKSAEKRKVMLDELAMETLqeksQHKEELGAVRlRHEKELLGVRARYERELRE 324
Cdd:PHA02562 334 EQSKKLLELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFV----DNAEELAKLQ-DELDKIVKTKSELVKEKYH 404
|
..
gi 569008872 325 LH 326
Cdd:PHA02562 405 RG 406
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
67-358 |
2.95e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 67 QAETSRLQEELAKLSEKLKKKQ---ESFCRLQTEKETLF--NDSRNKIEELQQRK---EADLKAQLARTQKLQQELEAAN 138
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHLAVAfeADPEAELRQLNRRRvelERALADHESQEQQQRSQLEQAK 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 139 QSLAELR----------DQRQGERLEHAAA--LRALQDQVS-SQSADAQEQVEGLLaenSALRTSLAALEQIQTAKTQEL 205
Cdd:PRK04863 872 EGLSALNrllprlnllaDETLADRVEEIREqlDEAEEAKRFvQQHGNALAQLEPIV---SVLQSDPEQFEQLKQDYQQAQ 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 206 NMLRE--QTSELASELQHRQAE--YEE---LMGQKDDLNSQLQESLR----ANSRLLEQLQEIGQEKEQLTQDLQEARKS 274
Cdd:PRK04863 949 QTQRDakQQAFALTEVVQRRAHfsYEDaaeMLAKNSDLNEKLRQRLEqaeqERTRAREQLRQAQAQLAQYNQVLASLKSS 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 275 AEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRARYERELR-ELHEDKKRQEEELRGQIREEKARTRELENL 353
Cdd:PRK04863 1029 YDAKRQMLQELKQE-LQDLGVPADSGAEERARARRDELHARLSANRSRRnQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
....*
gi 569008872 354 QHTVE 358
Cdd:PRK04863 1108 REQVV 1112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-267 |
3.52e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 38 LAEVELKWEMEREEKKLLWEQLQGLESSKQAETSR---LQEELAKLSEKLKKKQESFCRLQTE---KETLFNDSRNKIEE 111
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldeLRAELTLLNEEAANLRERLESLERRiaaTERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 112 LQQRkEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSL 191
Cdd:TIGR02168 850 LSED-IESLAAEIEELEELIEELESELEALLNERASLE----EALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 192 AALEQIQTAKTQELNMLREQTSELAS------------------ELQHRQA------------------EYEELMGQKDD 235
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSltleeaealenkieddeeEARRRLKrlenkikelgpvnlaaieEYEELKERYDF 1004
|
250 260 270
....*....|....*....|....*....|..
gi 569008872 236 LNSQLQESLRANSRLLEQLQEIGQEKEQLTQD 267
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
80-484 |
4.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 80 LSEKLKKKQESFCRLQTEKETLFNDSRNKIEE---LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQG-ERLEH 155
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 156 AAALRALQDQVSSQSADAQEQVEGL---LAENSALRTSLAALEQIQTAKTQELNMLREQTS-ELASELQHRQAEYEELMG 231
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 232 QKddlnSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEL 311
Cdd:COG4717 207 RL----AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 312 LGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQH--------TVEELQAQVHSMDGAKGWFERRLKEAEE 383
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalglppdlSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 384 SLQQQQQEQEETL-KLCREEHAAELKGKDEELQNvREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKkgsavLKD 462
Cdd:COG4717 363 LQLEELEQEIAALlAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELEEE-----LEE 436
|
410 420
....*....|....*....|..
gi 569008872 463 LKRQLHLERKRADKLQERLQEI 484
Cdd:COG4717 437 LEEELEELEEELEELREELAEL 458
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-484 |
5.39e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 67 QAETSRLQEELAKLSEKLKKKQESFcrlqTEKETLFNDSRNKIEELQQRKEaDLKAQLartQKLQQELEAANQSLAELRD 146
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEI----NEKTTEISNTQTQLNQLKDEQN-KIKKQL---SEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 147 QRQgerlEHAAALRALQDQ--------VSSQSADAQEQVEGL---LAEN----SALRTSLAALEQIQTAKTQELNMLREQ 211
Cdd:TIGR04523 289 QLN----QLKSEISDLNNQkeqdwnkeLKSELKNQEKKLEEIqnqISQNnkiiSQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 212 TSELASELQHRQAEYEE-------LMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDE 284
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 285 LAMETLQEKSQHKeELGAVRLRHEKELlgvrARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 364
Cdd:TIGR04523 445 LTNQDSVKELIIK-NLDNTRESLETQL----KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 365 HSMdgakgwferrlkeaeeslqqqqQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQ--EERDGHVKTISNLKQEV 442
Cdd:TIGR04523 520 SSL----------------------KEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQ 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 569008872 443 KDTVDGQRILE---KKGSAVLKDLKRQLHLERKRADKLQERLQEI 484
Cdd:TIGR04523 578 KSLKKKQEEKQeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
39-297 |
5.83e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 39 AEVELKWEMEREEKKLLWEQLQGLESSK-QAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE 117
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 118 ADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQ-DQVSSQSADAQEQVEGLL--AENSALRTSLAAL 194
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEAKkeAEEDKKKAEEAKK 1751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 195 EQIQTAKTQELNMLREQTSELASELQHRQAEyEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKS 274
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
250 260
....*....|....*....|...
gi 569008872 275 AEKRKVMLDELAMETLQEKSQHK 297
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHK 1853
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
43-489 |
6.12e-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: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 43 LKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKkqesfcRLQTEKETLFNDSRNKIEELQQRKEADLKA 122
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINR------ARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 123 QLA-RTQKLQQELEAANQSlAELRDQRQGERLEHAaalralQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAK 201
Cdd:TIGR00618 319 KMRsRAKLLMKRAAHVKQQ-SSIEEQRRLLQTLHS------QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 202 TQELNMLREQTSELASE---LQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 278
Cdd:TIGR00618 392 TQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 279 KVMLDELAMETLQEKSQHKEElGAVRLRHEKEllgvraRYERELRELHEDKKRQeeelrgQIREEKARTRELENLQHTVE 358
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVV-LARLLELQEE------PCPLCGSCIHPNPARQ------DIDNPGPLTRRMQRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 359 ELQAQVHSMDGaKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNL 438
Cdd:TIGR00618 539 QLETSEEDVYH-QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 569008872 439 KQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 489
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
106-363 |
6.47e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 106 RNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQ-----------RQGERLEHAAALRALQDQVSSQSADAQ 174
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSfsgssttdtglTKGSRFTHTEKLQFTNEAPAATSSPPT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 175 EQVEgllaensalrtslaaLEQIQTAKTQELNMLREQTSELASELQhrqaEYEELMGQKDDLNSQLQESLRANSRLLEQL 254
Cdd:pfam05667 322 KVET---------------EEELQQQREEELEELQEQLEDLESSIQ----ELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 255 QEIGQEKEQLTQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEElgavrlrHEKELLgvrARYeRELRELHEDKKRQEE 334
Cdd:pfam05667 383 EKQYKVKKKTLDLLPDAEENIAKLQALVDASA-QRLVELAGQWEK-------HRVPLI---EEY-RALKEAKSNKEDESQ 450
|
250 260
....*....|....*....|....*....
gi 569008872 335 ELRGQIREEKARTRELENLQHTVEELQAQ 363
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKEELYKQ 479
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
65-269 |
6.91e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 65 SKQAETSR----LQEELAKLSEKLKKKQESFCRLQTEKETL-----FNDSRNKIEELQQRK---EADLKAQLARTQKLQQ 132
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVdlseeAKLLLQQLSELESQLaeaRAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 133 ELEAANQSLAEL-RDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAA-LEQIQTAKTQELNMLRE 210
Cdd:COG3206 248 QLGSGPDALPELlQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008872 211 QTSELASELQHRQAEYEELMGQKDDLNsQLQESLRANSR----LLEQLQEIGQEKEQLTQDLQ 269
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELR-RLEREVEVARElyesLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
42-352 |
7.20e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKKLLWEQLQGLESSKQAETSRL--QEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK--- 116
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLlkQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkv 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 117 EADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQ 196
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 197 IQTAKTQELNMLREqtsELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAE 276
Cdd:pfam02463 869 LQELLLKEEELEEQ---KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569008872 277 KRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELEN 352
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
74-491 |
7.87e-05 |
|
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: 46.37 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 74 QEELAKLSEKLKKKQESFCRLQTEkETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELrdqrqgerl 153
Cdd:pfam12128 470 DERIERAREEQEAANAEVERLQSE-LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF--------- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 154 ehaaalralqdqVSSQSADAQEQVEGLLAENSALRTSLAAlEQIQTAKTQELNM----LREQTSELASELQHRQAEYEEL 229
Cdd:pfam12128 540 ------------LRKEAPDWEQSIGKVISPELLHRTDLDP-EVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERL 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 230 mgqkDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEK 309
Cdd:pfam12128 607 ----DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 310 ELLGVraryERELRELHEDKKRQEEELRGQIREekARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAeeslqqqq 389
Cdd:pfam12128 683 RLNSL----EAQLKQLDKKHQAWLEEQKEQKRE--ARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAE-------- 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 390 qeqeetLKLCREEHAAELKGKDEELQNV------REQLQQ--AQEERDGHVKTI-------------SNLKQEVKDTVDG 448
Cdd:pfam12128 749 ------LKALETWYKRDLASLGVDPDVIaklkreIRTLERkiERIAVRRQEVLRyfdwyqetwlqrrPRLATQLSNIERA 822
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 569008872 449 QRILEKKGSAVLKDLKR---QLHLERKRADKLQERLQEILTNSKSR 491
Cdd:pfam12128 823 ISELQQQLARLIADTKLrraKLEMERKASEKQQVRLSENLRGLRCE 868
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
57-295 |
1.13e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 57 EQLQG----LESSKQAETSRLQ-----EELAKLSEKLKKKqesfcrLQTEKETLFNDSRN-KIEELQQRKEADLKAQLAR 126
Cdd:PRK10929 48 EALQSalnwLEERKGSLERAKQyqqviDNFPKLSAELRQQ------LNNERDEPRSVPPNmSTDALEQEILQVSSQLLEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 127 TQKLQQELEAANQ---SLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALE--QIQTAK 201
Cdd:PRK10929 122 SRQAQQEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELElaQLSANN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 202 TQELNMLR-----EQTSELASELQ--------HRQAEYEE-------LMGQKDDLNSQLQESLRAN---SRLLEQ----L 254
Cdd:PRK10929 202 RQELARLRselakKRSQQLDAYLQalrnqlnsQRQREAERalestelLAEQSGDLPKSIVAQFKINrelSQALNQqaqrM 281
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 569008872 255 QEIGQEKEQLTQDLQEARKsaekrkvmldelAMETLQEKSQ 295
Cdd:PRK10929 282 DLIASQQRQAASQTLQVRQ------------ALNTLREQSQ 310
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
39-367 |
1.33e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 39 AEVELKWEMEREEKKLLWEQLQG---------LESSKQAETSRLQ---------EELAKLSEKLKK------KQESFCRL 94
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNniekmilafEELRVQAENARLEmhfklkedhEKIQHLEEEYKKeindkeKQVSLLLI 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 95 Q-TEKET-------LFNDSRNKIEELQQR---KEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQ 163
Cdd:pfam05483 248 QiTEKENkmkdltfLLEESRDKANQLEEKtklQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 164 DQVSSQSADAQEQVEGLLAEN---SALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQL 240
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 241 QE---SLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMET----------LQEKSQHKEELGAVRLR- 306
Cdd:pfam05483 408 EElkkILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseehyLKEVEDLKTELEKEKLKn 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569008872 307 -----HEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSM 367
Cdd:pfam05483 488 ieltaHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV 553
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
109-372 |
1.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 109 IEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRdqrqgERLEHAAALRalqdqvsSQSADAQEQVEGLLAENSALR 188
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLE-----KEVKELEELK-------EEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 189 TSLAALEQIQTAKTQELNMLREQTSELaSELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDL 268
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 269 QEARKSAEKRKVMLDELamETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR 348
Cdd:PRK03918 338 ERLEELKKKLKELEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260
....*....|....*....|....
gi 569008872 349 ELENlqhTVEELQAQVHSMDGAKG 372
Cdd:PRK03918 416 ELKK---EIKELKKAIEELKKAKG 436
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
75-299 |
1.42e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.10 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 75 EELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLE 154
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 155 HAAALRALQDQVSSQSADAQEQVegllaensalrTSLAALEQiQTAKTQELNMLREQTSELASELQHRQAEYEElmgqKD 234
Cdd:pfam03528 84 ATVSENTKQEAIDEVKSQWQEEV-----------ASLQAIMK-ETVREYEVQFHRRLEQERAQWNQYRESAERE----IA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008872 235 DLNSQLQEslransrlleqlqeiGQEKEQLTQDLQEARKSAEKRK--VMLDELAMETLQEKSQHKEE 299
Cdd:pfam03528 148 DLRRRLSE---------------GQEEENLEDEMKKAQEDAEKLRsvVMPMEKEIAALKAKLTEAED 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
50-253 |
1.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 50 EEKKLLWEQLQGLESSKQAetsrLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRnkIEELQQRkEADLKAQLARtqk 129
Cdd:COG3206 212 EEAKLLLQQLSELESQLAE----ARAELAEAEARLAALRAQLGSGPDALPELLQSPV--IQQLRAQ-LAELEAELAE--- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 130 LQQELEAANQSLAELRDQRqgerlehAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQiqtaKTQELNMLR 209
Cdd:COG3206 282 LSARYTPNHPDVIALRAQI-------AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA----RLAELPELE 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569008872 210 EQTSELASELQHRQAEYEELMGQKDDLNSQLQESLrANSRLLEQ 253
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEARLAEALTV-GNVRVIDP 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
64-280 |
1.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 64 SSKQAETSRLQEELAKLSEKLKKKQESFcrlqteketlfndsrNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAE 143
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---------------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 144 LRDQRqGERLEHAAALRALQDQVSS--QSADAQEQVEGLLAENSALRTSLAALEQIQTAKtQELNMLREQTSELASELQH 221
Cdd:COG3883 84 RREEL-GERARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569008872 222 RQAEYEElmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKV 280
Cdd:COG3883 162 LKAELEA---AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
99-295 |
1.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 99 ETLFNDSRNKIEELQQrKEADLKAQLArtqKLQQELEAANQSLAELRDQRQGERlEHAAALRALQDQVSSQSADAQEQVE 178
Cdd:COG3883 15 DPQIQAKQKELSELQA-ELEAAQAELD---ALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 179 GLLAENSALRTSLAALEQIQTAKTQE--------LNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRL 250
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569008872 251 LEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQ 295
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-285 |
2.09e-04 |
|
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: 44.83 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 38 LAEVELKWEMEREEKKLLWEQLQGLesSKQAETSRLQEELAKlsEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE 117
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQLVQA--NGELEKASREETFAR--TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 118 A---DLKAQL-ARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgllAENSALRT---- 189
Cdd:pfam12128 682 ErlnSLEAQLkQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALETwykr 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 190 SLAAL---EQIQTAKTQELNMLrEQTSELASELQHRQAEYEELMG-----QKDDLNSQLQESLRANSRLLEQLQEIGQEK 261
Cdd:pfam12128 759 DLASLgvdPDVIAKLKREIRTL-ERKIERIAVRRQEVLRYFDWYQetwlqRRPRLATQLSNIERAISELQQQLARLIADT 837
|
250 260
....*....|....*....|....
gi 569008872 262 EQLTQDLQEARKSAEKRKVMLDEL 285
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSEN 861
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
70-310 |
2.09e-04 |
|
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: 44.83 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 70 TSRLQEELAKLSEKLKKKQESFCRLQTEKetlfndsrnKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQ 149
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKE---------RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 150 GERLEHAAalRALQDQVSS-----QSADAQEQVEGLLAENSALRTSLAALEQIQTaktqelnmlreqtsELASELQHRQA 224
Cdd:NF012221 1608 RDAILEES--RAVTKELTTlaqglDALDSQATYAGESGDQWRNPFAGGLLDRVQE--------------QLDDAKKISGK 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 225 EYEELMGQKDDLNSQLQESLRANSRLLEQLQeigQEKEQLTQDLQEARKSAEKRKvmLDELAMETLQEKSQHKEELGA-- 302
Cdd:NF012221 1672 QLADAKQRHVDNQQKVKDAVAKSEAGVAQGE---QNQANAEQDIDDAKADAEKRK--DDALAKQNEAQQAESDANAAAnd 1746
|
....*...
gi 569008872 303 VRLRHEKE 310
Cdd:NF012221 1747 AQSRGEQD 1754
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-501 |
2.37e-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: 44.72 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 39 AEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQE-------ELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEE 111
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREakrmyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 112 LQQ------RKEADLKAQLARTQKLQQELEAANQSLAELR---DQRQGERLEHAAALRAL----QDQVSSQSADAQ---- 174
Cdd:pfam15921 379 LQKlladlhKREKELSLEKEQNKRLWDRDTGNSITIDHLRrelDDRNMEVQRLEALLKAMksecQGQMERQMAAIQgkne 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 175 --EQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLL- 251
Cdd:pfam15921 459 slEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKn 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 252 --EQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDEL----------AMETLQEKSQHKEELGAVRLRHeKELLGVRARYE 319
Cdd:pfam15921 539 egDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtAGAMQVEKAQLEKEINDRRLEL-QEFKILKDKKD 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 320 RELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGwferRLKEAEESLQQQQQEQEETLKLC 399
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN----SLSEDYEVLKRNFRNKSEEMETT 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 400 REEHAAELKGKDEELQNVREQLqQAQEERDGH-VKTISNLKQEV---KDTVDGQRILEKKGSAVLKDLKRQLHLERKRAD 475
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQTRNTL-KSMEGSDGHaMKVAMGMQKQItakRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKN 772
|
490 500
....*....|....*....|....*.
gi 569008872 476 KLQERLQEILTNSKSRTGLEELVLSE 501
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQ 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-235 |
2.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 45 WEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLseklkkkqesfcrlqteketlfndsRNKIEELQQRKEADLKAQL 124
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDEL-------------------------EAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 125 ARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQE 204
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
170 180 190
....*....|....*....|....*....|.
gi 569008872 205 LNMLREQTSELASELQHRQAEYEELMGQKDD 235
Cdd:COG4913 428 IASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
72-379 |
2.54e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 72 RLQEELAKLSEKLKKKQESFCRLQTEKEtlfndsRNKIEELQQRKEAD-LKAQLArtqKLQQELEA----------ANQS 140
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLA------EAEARLEAAEEEVDsLKSQLA---DYQQALDVqqtraiqyqqAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 141 LAELRDQRQGERL------EHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAktqelnMLREQTSE 214
Cdd:COG3096 422 LEKARALCGLPDLtpenaeDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGE------VERSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 215 LASELQHRQAEYEELMGQKDDLNSQLQESlranSRLLEQLQEIGQEKEQLTQDLQEARKSAEkrkvMLDELAME---TLQ 291
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAE----ELEELLAEleaQLE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 292 EKSQHKEELGAVRLRHEKELLGVRARYER------ELRELHEDKKRQEEE--------------LRGQIREEKARTRELE 351
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKElaarapAWLAAQDALERLREQsgealadsqevtaaMQQLLEREREATVERD 647
|
330 340
....*....|....*....|....*...
gi 569008872 352 NLQHTVEELQAQVHSMDGAKGWFERRLK 379
Cdd:COG3096 648 ELAARKQALESQIERLSQPGGAEDPRLL 675
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
39-267 |
3.43e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 39 AEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESF-----CRLQTEKETLFNDSRNKIEELQ 113
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 114 QRKEADL-KAQLARTQKLQQELEAANQSLAELRDQRQGERL---EHAAALRALQDQVSSQSADAQEQVEGLLAENSALRT 189
Cdd:PTZ00121 1640 KKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569008872 190 SLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQD 267
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
48-250 |
3.46e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 48 EREEKKLlwEQLQGLESSKQAETSRLQEELAKLSEKLKK-KQESFCRL-QTEKETLFNDSRNKIEELQQ----------- 114
Cdd:PRK11281 76 DRQKEET--EQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLSTLsLRQLESRLAQTLDQLQNAQNdlaeynsqlvs 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 115 ------RKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRA--------------LQDQVSSQSADAQ 174
Cdd:PRK11281 154 lqtqpeRAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAqndlqrkslegntqLQDLLQKQRDYLT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 175 EQVEGLLAENSALRTSL------AALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANS 248
Cdd:PRK11281 234 ARIQRLEHQLQLLQEAInskrltLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKN 313
|
..
gi 569008872 249 RL 250
Cdd:PRK11281 314 WL 315
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-484 |
3.80e-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: 43.90 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 242 ESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYErE 321
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE-K 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 322 LRELHEDKKRQEEELRGQIREEKARTRELEN-----LQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETL 396
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 397 klcreEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADK 476
Cdd:TIGR02169 336 -----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
....*...
gi 569008872 477 LQERLQEI 484
Cdd:TIGR02169 411 LQEELQRL 418
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
64-196 |
3.93e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 64 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQtekETLfndsrnkieelqqrkeADLKAQLARTQKLQQELEAANQSLAE 143
Cdd:PRK09039 49 SGKDSALDRLNSQIAELADLLSLERQGNQDLQ---DSV----------------ANLRASLSAAEAERSRLQALLAELAG 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 569008872 144 LRDQRQGERLEHAAALRALQDQvssqSADAQEQVEGLLAENSALRTSLAALEQ 196
Cdd:PRK09039 110 AGAAAEGRAGELAQELDSEKQV----SARALAQVELLNQQIAALRRQLAALEA 158
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
46-276 |
4.32e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 46 EMEREEKKLLWEQLqGLESSKQAETSRLQEELAKLSEKLKKKQESFCR---LQTEKETLFNDSRNKIEELQQRKEADLKA 122
Cdd:pfam17380 357 ERKRELERIRQEEI-AMEISRMRELERLQMERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAEQEEARQR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 123 QLARTQKlQQELEAANQSLAELRDQRQGERLEHAAALRALQ----DQVSSQSADAQEQVEGLLAENSALRTSlAALEQIQ 198
Cdd:pfam17380 436 EVRRLEE-ERAREMERVRLEEQERQQQVERLRQQEEERKRKklelEKEKRDRKRAEEQRRKILEKELEERKQ-AMIEEER 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569008872 199 TAKTQELNMLREQTSeLASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAE 276
Cdd:pfam17380 514 KRKLLEKEMEERQKA-IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
36-258 |
5.51e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 36 MPLAEVELKWEMEREEKKLLWEQLQGLESSKQAETSRL---QEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEEL 112
Cdd:TIGR00618 655 LTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 113 QQRKEADLKAQ-----LARTQKLQQELEAANQSLAELRDQRQGERLEHAAAlralqdQVSSQSADAQEQVEGLLAENSAL 187
Cdd:TIGR00618 735 AAREDALNQSLkelmhQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA------EIQFFNRLREEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008872 188 RTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIG 258
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
47-367 |
6.16e-04 |
|
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: 43.29 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 47 MEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLAR 126
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 127 TQKLQQELEAANqslaelrdqrqgerlehAAALRALQDQVSSQSADaQEQVEGLLAENSALRTSLAALEQIQTAKTQELN 206
Cdd:pfam12128 317 VAKDRSELEALE-----------------DQHGAFLDADIETAAAD-QEQLPSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 207 MLREQTSE-----LASELQHRQAEYEELMGQKDDLNSQLQESLRA-NSRLLEQLQEIGQEKEQLTQDLQEArksaekrKV 280
Cdd:pfam12128 379 RRRSKIKEqnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL-------KL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 281 MLDELAM--ETLQEKSQHKEELGAVRLRHEKEllgvRARYERELRELHEDKKRQEEELRgQIREEKARTRELEN-LQHTV 357
Cdd:pfam12128 452 RLNQATAtpELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQASE-ALRQASRRLEERQSaLDELE 526
|
330
....*....|
gi 569008872 358 EELQAQVHSM 367
Cdd:pfam12128 527 LQLFPQAGTL 536
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
133-584 |
7.45e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 133 ELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgllaENSALRTSLAALEQIQTAKTQELNMLREQT 212
Cdd:pfam05557 31 ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE----LNRLKKKYLEALNKKLNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 213 SELASELQHRQaeyEELMGQKDDLNSQLQESLRANSRLlEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMEtLQE 292
Cdd:pfam05557 107 SCLKNELSELR---RQIQRAELELQSTNSELEELQERL-DLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFE-IQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 293 KSQHKEELGAVRLRhekelLGVRARYERELRELHEDKKRqeeelrgqireekartreLENLQHTVEELQAQVHSMdgakg 372
Cdd:pfam05557 182 QEQDSEIVKNSKSE-----LARIPELEKELERLREHNKH------------------LNENIENKLLLKEEVEDL----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 373 wfERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEEL-----QNVREQLQQAQEERDGHVKTISNLKQEVKDTVD 447
Cdd:pfam05557 234 --KRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 448 GQRILEKKGSAVLKDLKrQLHLERKRADKLQERLQ-EILTNSKSRTGLEELVLS---EMN----SPSRTQTGDSSSVSSF 519
Cdd:pfam05557 312 ARRELEQELAQYLKKIE-DLNKKLKRHKALVRRLQrRVLLLTKERDGYRAILESydkELTmsnySPQLLERIEEAEDMTQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 520 SY---------------REILKEKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVS 584
Cdd:pfam05557 391 KMqahneemeaqlsvaeEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-496 |
7.98e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 206 NMLRE-QTSELASELQhrqAEYEELMGQKDDLnsqlqESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDE 284
Cdd:COG4913 216 YMLEEpDTFEAADALV---EHFDDLERAHEAL-----EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 285 LAMETLQEKSQhkeelgavRLRHEKELLGVRaryERELRELHEDKKRQEEELRGQIREEKarTRELENLQHTVEELQAQV 364
Cdd:COG4913 288 RRLELLEAELE--------ELRAELARLEAE---LERLEARLDALREELDELEAQIRGNG--GDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 365 hsmdgakgwfERRLKEaeeslqqqqqeqeetlklcREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKD 444
Cdd:COG4913 355 ----------EERERR-------------------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 569008872 445 TVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEE 496
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
38-194 |
1.30e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 38 LAEVELKWEMEREEKKLLWE--QLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQR 115
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569008872 116 KEADLKAQlARTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAAL 194
Cdd:COG3096 601 APAWLAAQ-DALERLREQSGEALADSQEVTAAMQ-QLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
75-377 |
1.30e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 75 EELAKLSEKLKKKQESFCRLQTEKETLFNDSRNkIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRdQRQGERLE 154
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAG-LTRRLSAAEGELEELVARLAKLEAALREAEAAKEELR-IELRDKTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 155 HAAALRAlqdqvssQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKD 234
Cdd:pfam19220 119 QAEALER-------QLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 235 DLNSQLQEslraNSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmldELAMETLQ-EKSQHKEELGAVRLRH---EKE 310
Cdd:pfam19220 192 ELTRRLAE----LETQLDATRARLRALEGQLAAEQAERERAEAQL----EEAVEAHRaERASLRMKLEALTARAaatEQL 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008872 311 LLGVRARyereLRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERR 377
Cdd:pfam19220 264 LAEARNQ----LRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEER 326
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
98-466 |
1.41e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 98 KETLFNDSRNKIEELQQR------------------KEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAAL 159
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMmlshegvlqeirsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 160 RALQDQVSSQSADAQEQVEGLLAENSalrtslAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQ 239
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 240 LQESLRANSRLLEQLQEIGQEKEQLTQDLQEarkSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARyE 319
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIE---ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR-E 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 320 RELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG-AKGWFERRLKEAEESLQQQQQEQEETlkl 398
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSeCQGQMERQMAAIQGKNESLEKVSSLT--- 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008872 399 creehaAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTvdgQRILEKKGSAVLK-----DLKRQ 466
Cdd:pfam15921 468 ------AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK---ERAIEATNAEITKlrsrvDLKLQ 531
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-325 |
1.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 48 EREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLart 127
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL-AELLKELEELGFESVEELEERL--- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 128 qklqQELEAANQSLAELRDQRQgeRLEhaaALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQElnM 207
Cdd:PRK03918 595 ----KELEPFYNEYLELKDAEK--ELE---REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--E 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 208 LREQTSELASELQHRQAEYEELMGQKDDLNSQLqESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAM 287
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAL 742
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 569008872 288 ETLQE-KSQHKEEL-----GAVRLRHEKELLGVRARYERELREL 325
Cdd:PRK03918 743 SKVGEiASEIFEELtegkySGVRVKAEENKVKLFVVYQGKERPL 786
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
37-379 |
1.81e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 37 PLAEVELKWEMEREEKKLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQT---EKETLFNDSRNKIEELQ 113
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdieEQETLLGTIMPEEESAK 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 114 qrkeaDLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAAlralqdQVSSQSADAQEQVEGLLAENSALRT-SLA 192
Cdd:TIGR00606 786 -----VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKlIQD 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 193 ALEQIQT--AKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQE 270
Cdd:TIGR00606 855 QQEQIQHlkSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 271 ARKSAE------KRKVMLDELAMETLQEKSQHKEElgAVRLRHEKELLGV----------RARYERELRELHED---KKR 331
Cdd:TIGR00606 935 SNKKAQdkvndiKEKVKNIHGYMKDIENKIQDGKD--DYLKQKETELNTVnaqleecekhQEKINEDMRLMRQDidtQKI 1012
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 569008872 332 QEEELRGQ----IREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLK 379
Cdd:TIGR00606 1013 QERWLQDNltlrKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID 1064
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
74-274 |
1.98e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.51 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 74 QEELAKLSEKLKKKQESFCRlQTEKETLFNDSRNKIEELQQRKE---ADLKAQLARTQKLQQE--LEAANQSLAELrdQR 148
Cdd:pfam13779 508 DEEIAKLMQELREALDDYMQ-ALAEQAQQNPQDLQQPDDPNAQEmtqQDLQRMLDRIEELARSgrRAEAQQMLSQL--QQ 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 149 QGERLEhAAALRALQDQVSSQSADAQEQVEGLLAENSAL-----RTSLAALEQIQTAKTQELNMLREQTSELASELQHRQ 223
Cdd:pfam13779 585 MLENLQ-AGQPQQQQQQGQSEMQQAMDELGDLLREQQQLldetfRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQ 663
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569008872 224 AEYEELMGQKDDLNSQlQESLRanSRLLEQLQEIGQEK-EQLTQDLQEARKS 274
Cdd:pfam13779 664 MPPQGGAEALGDLAER-QQALR--RRLEELQDELKELGgKEPGQALGDAGRA 712
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-263 |
2.03e-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: 41.64 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 73 LQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQqrkeadlkaqlARTQKLQQELEAANQSLAELRDQRQGER 152
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME-----------TTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 153 LEHAAALRAlqdqvssqSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQ 232
Cdd:pfam15921 720 GSDGHAMKV--------AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569008872 233 KDDLNSQ----------LQESLRANSRLLEQLQEIGQEKEQ 263
Cdd:pfam15921 792 LEVLRSQerrlkekvanMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
38-500 |
2.09e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 38 LAEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE 117
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 118 ADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADA-----QEQVEGLLAENSALRTSLA 192
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVllaliKDGVGGRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 193 -ALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEA 271
Cdd:pfam02463 536 vAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 272 RkSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREE-------- 343
Cdd:pfam02463 616 D-EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAEselakeei 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 344 KARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQ 423
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008872 424 AQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLS 500
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
97-379 |
2.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 97 EKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSSQSADAQEQ 176
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE--------QLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 177 VEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQE 256
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 257 IGQEKEQLTQDLQ-----EARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKR 331
Cdd:COG4372 162 LQEELAALEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569008872 332 QEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLK 379
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
50-352 |
2.55e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 50 EEKKLLWEQLQGLESSKQAET--SRLQEELAKLS-EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLAR 126
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDklEKLVEQNTDLRlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 127 TQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENsALRTSLAALEQIQtaktQELN 206
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFK----DTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 207 MLREqtselASELQHRQAEyeelmGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELA 286
Cdd:COG5185 388 STKE-----SLDEIPQNQR-----GYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREA 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008872 287 METLQEKSQHKEELGAVRLRHEKELLGVRA-RYERELRELhedkKRQEEELRGQIREEKARTRELEN 352
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSKKEDLNEELtQIESRVSTL----KATLEKLRAKLERQLEGVRSKLD 520
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
131-268 |
2.55e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 131 QQELEAANQSLAELRDQRQGERlehaaalralqdqvsSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLRE 210
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLER---------------QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008872 211 QTSELASELQHRQAEYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEIGQEKEQLTQDL 268
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
163-354 |
2.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 163 QDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQE 242
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 243 SLRANSRL---------------LEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDelamETLQEKSQHKEELGAVRlrh 307
Cdd:COG3883 98 SGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELE----AKLAELEALKAELEAAK--- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569008872 308 eKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 354
Cdd:COG3883 171 -AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
80-174 |
2.97e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 40.86 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 80 LSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQ---- 149
Cdd:PRK06975 344 LNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQasvhqlDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRDDWMiaev 423
|
90 100 110
....*....|....*....|....*....|
gi 569008872 150 GERLEHAAALRALQDQVSS-----QSADAQ 174
Cdd:PRK06975 424 EQMLSSASQQLQLTGNVQLalialQNADAR 453
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
105-284 |
3.03e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 105 SRNKIEELQQRKEADLKAQLARTQKLQQEL------------EAANQSLAELRDQRQGERLEHAAA---LRALQDQVSSQ 169
Cdd:PRK11448 51 ALLGIYEPPCENQHDLLRRLGKEGFLPDEIldvfhklrkignKAVHEFHGDHREALMGLKLAFRLAvwfHRTYGKDWDFK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 170 SADAQEQVEgllaensalrtSLAALEQIQtaktQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSR 249
Cdd:PRK11448 131 PGPFVPPED-----------PENLLHALQ----QEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 569008872 250 LLEQLQEIGQEKEQLTQDLQEARKSAEKR---KVMLDE 284
Cdd:PRK11448 196 LEAQLEQLQEKAAETSQERKQKRKEITDQaakRLELSE 233
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
52-178 |
3.35e-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: 40.39 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 52 KKLLWEQLQGLESSKQaetsRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRKEADLKAQLARTQKLQ 131
Cdd:smart00787 146 KEGLDENLEGLKEDYK----LLMKELELLNSIKPKLRDRKDALEEELRQL----KQLEDELEDCDPTELDRAKEKLKKLL 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 569008872 132 QELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVE 178
Cdd:smart00787 218 QEIMIKVKKLEELEEELQ-ELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
51-143 |
4.48e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 51 EKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADL-KAQLARTQK 129
Cdd:pfam03938 16 EGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELqKKQQELLQP 95
|
90
....*....|....
gi 569008872 130 LQQELEAANQSLAE 143
Cdd:pfam03938 96 IQDKINKAIKEVAK 109
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-372 |
4.79e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 58 QLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFND--SRNKIEELQQRKEADLKAQLAR------TQK 129
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESEraARNKAEKQRRDLGEELEALKTEledtldTTA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 130 LQQELEAA-NQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNML 208
Cdd:pfam01576 317 AQQELRSKrEQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 209 reQTSELASELQHRQAEyeelmGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDEL--- 285
Cdd:pfam01576 397 --QQAKQDSEHKRKKLE-----GQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesq 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 286 ---AMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELR--------------ELHEDKKRQEEELRGQIREEKAR-- 346
Cdd:pfam01576 470 lqdTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEakrnverqlstlqaQLSDMKKKLEEDAGTLEALEEGKkr 549
|
330 340
....*....|....*....|....*..
gi 569008872 347 -TRELENLQHTVEELQAQVHSMDGAKG 372
Cdd:pfam01576 550 lQRELEALTQQLEEKAAAYDKLEKTKN 576
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-300 |
4.95e-03 |
|
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: 40.34 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 32 PLAPMPLAEVELKWEMEREEKKLLWEQLQGLEssKQAETSRLQEELAKlsEKLKKKQESFCRLQTEKETLFNDSRNKIEE 111
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQD--VRLHLQQCSQELAL--KLTALHALQLTLTQERVREHALSIRVLPKE 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 112 LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQrqgerLEHAAALRALQDQVSSQSADAQEQVEGllaENSALRTSL 191
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL-----ETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 192 AALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQ--------LQEIGQEKEQ 263
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigqeipsdEDILNLQCET 825
|
250 260 270
....*....|....*....|....*....|....*....
gi 569008872 264 LTQDLQEARKSAEKRKVMLDELAMETLQ--EKSQHKEEL 300
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKyeECSKQLAQL 864
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
57-275 |
5.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 57 EQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQRkEADLKAQLARTQKLQQELEA 136
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAE-IEERREELGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 137 ANQSLAELRDQRQ-GERLEHAAALRALQDQVSS---QSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQT 212
Cdd:COG3883 101 SVSYLDVLLGSESfSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008872 213 SELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSA 275
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
67-483 |
5.26e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 67 QAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL----------------FNDSRNKIEELQQRKEADLKAQLART--- 127
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTeakikkleedillledQNSKLSKERKLLEERISEFTSNLAEEeek 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 128 ----QKLQQELEAANQSLAELRDQRQGERLEHAAALRALQdqvsSQSADAQEQVEGLLAENSALRTSLAaleqiqtAKTQ 203
Cdd:pfam01576 175 akslSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----GESTDLQEQIAELQAQIAELRAQLA-------KKEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 204 ELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmld 283
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQ---- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 284 ELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEdkkRQEEELRGQIREEKARtrelENLQHTVEELQAQ 363
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTE---QLEQAKRNKANLEKAK----QALESENAELQAE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 364 VHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLcREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVK 443
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ-RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 569008872 444 DTvdgQRILEKKGSAVLKDLKRQLHLERKRADkLQERLQE 483
Cdd:pfam01576 472 DT---QELLQEETRQKLNLSTRLRQLEDERNS-LQEQLEE 507
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
46-335 |
6.25e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 46 EMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKlkkkqesfcrlQTEKETLFNDSRNKIEELQQRKEADLKAQLA 125
Cdd:pfam07888 58 EKEKERYKRDREQWERQRRELESRVAELKEELRQSREK-----------HEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 126 RTQKLQqELEAANQSLA------ELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQT 199
Cdd:pfam07888 127 HEARIR-ELEEDIKTLTqrvlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 200 AKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRK 279
Cdd:pfam07888 206 TQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLT 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 569008872 280 VMLDELAMETLQEKSQHKEELGAVRLRHEKEllgvRARYERELRELHEDKKRQEEE 335
Cdd:pfam07888 286 LQLADASLALREGRARWAQERETLQQSAEAD----KDRIEKLSAELQRLEERLQEE 337
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
42-351 |
8.74e-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: 39.34 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 42 ELKWEMEREEKkllweqLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEketlfnDSRNKIEELQQRKEADLK 121
Cdd:pfam17380 307 EKAREVERRRK------LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE------ERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 122 AQLARTQKLQQELEAANqslaelrdQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSlaALEQIQTAK 201
Cdd:pfam17380 375 SRMRELERLQMERQQKN--------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 202 TQELNMLREqtselasELQHRQAEYEELMGQKDDLNSQLQESLRANsrllEQLQEIGQEKEQLTQDLQEARKSA---EKR 278
Cdd:pfam17380 445 AREMERVRL-------EEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELEERKQAmieEER 513
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569008872 279 KVMLDELAMETLQEK-SQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKR-----QEEELRGQIREEKARTRELE 351
Cdd:pfam17380 514 KRKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRleameREREMMRQIVESEKARAEYE 592
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
160-428 |
8.89e-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: 39.34 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 160 RALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASElQHRQAEYEELMGQKDDLNSQ 239
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 240 LQESLR---ANSRLLEQLQ-EIGQEKEQLTQDLQEARK-----SAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 310
Cdd:pfam17380 366 RQEEIAmeiSRMRELERLQmERQQKNERVRQELEAARKvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 311 LLGVRARYERELRELHEDKKRQEEELR----GQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQ 386
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 569008872 387 QQQQEQEETLKLCREEHAAELKGkdEELQNVREQLQQAQEER 428
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM--EERRRIQEQMRKATEER 565
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
67-360 |
9.45e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 67 QAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNkIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRD 146
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 147 QRQG------------ERLEHAAA-----LRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLR 209
Cdd:pfam10174 423 RVKSlqtdssntdtalTTLEEALSekeriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 210 EQTSELASELQHRQAEYEEL---MGQKDDLNSQLQESLRANSRLLEQLQ---EIGQEKEQLTQDLQEARKSAEKRKVMLD 283
Cdd:pfam10174 503 EHASSLASSGLKKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRtnpEINDRIRLLEQEVARYKEESGKAQAEVE 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 284 ELaMETLQE-------KSQHKEELGAVRLRHEKEllgvRARYERELREL-HEDKKRQEEELRGQIREEKARTRELENLQh 355
Cdd:pfam10174 583 RL-LGILREvenekndKDKKIAELESLTLRQMKE----QNKKVANIKHGqQEMKKKGAQLLEEARRREDNLADNSQQLQ- 656
|
....*
gi 569008872 356 tVEEL 360
Cdd:pfam10174 657 -LEEL 660
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
102-257 |
9.63e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 102 FNDSRNKIEELQQRKEADLKAQLARTQKLQ-QELEAAnqsLAELRDQRQGERLEHAAALRALQDQVSSQS----ADAQEQ 176
Cdd:COG2433 345 YDAYKNKFERVEKKVPPDVDRDEVKARVIRgLSIEEA---LEELIEKELPEEEPEAEREKEHEERELTEEeeeiRRLEEQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008872 177 VEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELA---SELQHRQAEYEELmgqKDDLNsQLQESLRANSRLLEQ 253
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrkdREISRLDREIERL---ERELE-EERERIEELKRKLER 497
|
....
gi 569008872 254 LQEI 257
Cdd:COG2433 498 LKEL 501
|
|
| |
