|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-465 |
4.45e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 146 ERTLELADYKTKCENQSGFILHLKQLLscgntkfEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLE 225
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 226 KARNDLQTAYEGFVQKLNQQHQtDQTELENRLKEfYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEash 305
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEE-RLEEAEEELAE-AEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAA--- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 306 seKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSE--------NDALNERLKSEEQKQLSREKAN 377
Cdd:TIGR02168 821 --NLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 378 SKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNttlvdkltrFQQENEELKARMDRHMAISRQLSTEQA 457
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEE 968
|
....*...
gi 564389283 458 ALQESLEK 465
Cdd:TIGR02168 969 EARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-480 |
1.29e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 192 EREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEgfvqKLNQQHQTDQTELENRLKEFY--TAECEKLQ 269
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYelLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 270 SIYIEEAEKyKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLLENLLNEKQESLEKQI 349
Cdd:COG1196 302 QDIARLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 350 NDLKSENDALNERLksEEQKQLSREKANSKNPQvmylEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLT 429
Cdd:COG1196 376 EAEEELEELAEELL--EALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564389283 430 RFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-468 |
3.63e-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: 62.77 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 182 LTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGfVQKLNQQHQTDQTELENRLKEF- 260
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILr 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 261 ------------YTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHE 328
Cdd:TIGR02168 309 erlanlerqleeLEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 329 MEKKLL------ENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNE 402
Cdd:TIGR02168 383 TLRSKVaqlelqIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389283 403 KLHQQDLKLMKMEKlvdnnttlvdKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESK 468
Cdd:TIGR02168 462 ALEELREELEEAEQ----------ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-450 |
1.91e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 176 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKarndlqtayegFVQKLNQQHQTDQTELEN 255
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-----------QKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 256 rlkefYTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLL- 334
Cdd:TIGR02168 321 -----LEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ESRLEELEEQLETLRSKVa 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 335 -----ENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDL 409
Cdd:TIGR02168 390 qlelqIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564389283 410 KLMKMEKLVDnntTLVDKLTRFQQENEELKARMDRHMAISR 450
Cdd:TIGR02168 469 ELEEAEQALD---AAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-411 |
4.49e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 176 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQ----------TAYEGFVQKLNQQ 245
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrreleerlEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 246 HQTDQTELENRLKEFYTAECEklqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYE--TSLSEI 323
Cdd:COG1196 332 LEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElaAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 324 KKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEK 403
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
....*...
gi 564389283 404 LHQQDLKL 411
Cdd:COG1196 486 LAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-480 |
7.17e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 222 EKLEKARNDLQtayegfvqklnqqhqtdqtELENRLKEFYTAECEKLQsiyieeaekyktQLQeqfdnlnaahettKLEI 301
Cdd:TIGR02169 170 RKKEKALEELE-------------------EVEENIERLDLIIDEKRQ------------QLE-------------RLRR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 302 EASHSEKV-ELLKKTYETSLSEI---KKSHEMEKKLLENLLNEKQESLEK---QINDLKSENDALNERLK--SEEQKQLS 372
Cdd:TIGR02169 206 EREKAERYqALLKEKREYEGYELlkeKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEelNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 373 REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQE--------NEELKARMDR 444
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEE 365
|
250 260 270
....*....|....*....|....*....|....*.
gi 564389283 445 HMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-480 |
7.79e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 244 QQHQTDQTELENRLK----EFYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEA------SHSEKVELLK 313
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEEleleleEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 314 KTYETSLSEIKKSHEMEKKLLENL--LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELE 391
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE------AEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 392 SLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRhmAISRQLSTEQAALQESLEKESKVNK 471
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE--ELEELEEALAELEEEEEEEEEALEE 446
|
....*....
gi 564389283 472 RLSMENEEL 480
Cdd:COG1196 447 AAEEEAELE 455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-480 |
1.12e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 189 LLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKEFyTAECEKL 268
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEL-EAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 269 QSIY------IEEAEKYKTQLQEQFDNLNAAHETTKLEIE------ASHSEKVELLKKTYETSLSEIKkshEMEKKLLEn 336
Cdd:TIGR02169 307 ERSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EVDKEFAE- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 337 lLNEKQESLEKQINDLKSENDAL--NERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDLKLMkm 414
Cdd:TIGR02169 383 -TRDELKDYREKLEKLKREINELkrELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLE-- 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389283 415 eklvdnntTLVDKLTRFQQENEELKarmdrhmaisrqlsteqaalqeslEKESKVNKRLSMENEEL 480
Cdd:TIGR02169 459 --------QLAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-374 |
5.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 180 EALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKE 259
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 260 FYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLEnlLN 339
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE--LL 469
|
170 180 190
....*....|....*....|....*....|....*
gi 564389283 340 EKQESLEKQINDLKSENDALNERLKSEEQKQLSRE 374
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
282-464 |
1.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 282 QLQEQFDNLNAAHETtkLEIEAshsEKVELLK------KTYETSLSEIKKSHEMEKKL-------LENLLNEKQESLEKQ 348
Cdd:COG4913 229 ALVEHFDDLERAHEA--LEDAR---EQIELLEpirelaERYAAARERLAELEYLRAALrlwfaqrRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 349 INDLKSENDALNERLKSEEQK--QLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKM--------EKLV 418
Cdd:COG4913 304 LARLEAELERLEARLDALREEldELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564389283 419 DNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLE 464
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-481 |
1.41e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 273 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSlseiKKSHEMEKKLLEnlLNEKQESLEKQINDL 352
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLAR--LEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 353 KSEndalneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEK----LVDNNTTLVDKL 428
Cdd:TIGR02168 753 SKE------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltlLNEEAANLRERL 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564389283 429 TRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 481
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-413 |
1.59e-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: 47.07 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 178 KFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENRL 257
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 258 KEFYtaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLE-IEASHSEKVELLKKTYETsLSEIKKSHEMEKKLLEN 336
Cdd:COG4942 104 EELA----ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAE-LAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564389283 337 LLNEKQESLeKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQvmYLEQELESLKAVLEIKNEKLHQQDLKLMK 413
Cdd:COG4942 179 LLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
307-466 |
2.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 307 EKVELLKKTYETSLSEIKKsheMEKKLLEnlLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYL 386
Cdd:COG3883 23 KELSELQAELEAAQAELDA---LQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 387 EQELES-LKAVLEIKNeklhQQDL--KLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESL 463
Cdd:COG3883 98 SGGSVSyLDVLLGSES----FSDFldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
...
gi 564389283 464 EKE 466
Cdd:COG3883 174 EAQ 176
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-481 |
3.10e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 146 ERTLELADYKTKCENQSGFIL----HLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaaSSTC 221
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL---SSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 222 EKLEKARNDLQTayegfVQKLNQQHQTDQTELENRLKEFYTAEC-EKLQSI--YIEEAEKYKTQLQEQFDNLNAAHETTK 298
Cdd:TIGR02169 751 QEIENVKSELKE-----LEARIEELEEDLHKLEEALNDLEARLShSRIPEIqaELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 299 LEIEASHSEKVELLKKTYETSL--SEIKKSHEMEKKLLENLLNEKQE------SLEKQINDLKSENDALNERLKSEEQKQ 370
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEqiKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 371 lsrekaNSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISR 450
Cdd:TIGR02169 906 ------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|.
gi 564389283 451 QLSTEQAALQESLEKESKvnkrLSMENEELL 481
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAK----LEEERKAIL 1006
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
269-480 |
3.32e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 269 QSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKshemekklLENLLNEKQESLEKQ 348
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALAR--------RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 349 INDLKSENDALNERLKSEEQ---KQLSREKANSKNPQVMYL---------EQELESLKAVLEIKNEKLHQQDLKLMKMEK 416
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEelaELLRALYRLGRQPPLALLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389283 417 LVDNNTTLVDKLTRFQQENEE----LKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:COG4942 165 LRAELEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
192-474 |
6.10e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 192 EREEALKQHKTLSQELVSLRGELVAASSTCEKLEkARNDLQTAYEGFVQKLNQQHQTDQTELENRL--KEFYTAECEKLQ 269
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL-ARLEEETAQKNNALKKIRELEAQISELQEDLesERAARNKAEKQR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 270 SIYIEEAEKYKTQLQEQFDNLNAAHE-TTKLEIEASHSEK-VELLKKTYETSLSEIKKSHEME-KKLLENLLNEK--QES 344
Cdd:pfam01576 295 RDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKrnKAN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 345 LEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTL 424
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKK------LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSL 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389283 425 VD----KLTRFQQE-----------NEELKARMDRHMAIS---RQLSTEQAALQESLEKESKVNKRLS 474
Cdd:pfam01576 449 LNeaegKNIKLSKDvsslesqlqdtQELLQEETRQKLNLStrlRQLEDERNSLQEQLEEEEEAKRNVE 516
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
252-369 |
7.80e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 252 ELENRLKEfYTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEM-- 329
Cdd:PRK00409 527 ELERELEQ-KAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGgy 601
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564389283 330 ----EKKLLENL--LNEKQESLEKQINDLKSENDALNE----RLKSEEQK 369
Cdd:PRK00409 602 asvkAHELIEARkrLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
135-472 |
7.94e-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: 45.73 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 135 QTQTAPDVLSTERTLELADYKTKCENQSGFILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTL----SQELVSL 210
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAqdkiNEELKLL 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 211 RGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQ-HQTDQTELENRLKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDN 289
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQ 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 290 LNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQK 369
Cdd:pfam02463 822 LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 370 QLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAIS 449
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
330 340
....*....|....*....|...
gi 564389283 450 RQLSTEQAALQESLEKESKVNKR 472
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEK 1004
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
187-467 |
1.29e-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: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 187 QHLLSEREEALKQHKTLSQeLVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTD----------QTELENR 256
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikdklakIREARDR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 257 LKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyETSLSEIKKSHEMEKKLlen 336
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDERIERAREEQEAA--- 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 337 llNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVM---------YLEQEL----ESLKAVleIKNEK 403
Cdd:pfam12128 484 --NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqagtllhFLRKEApdweQSIGKV--ISPEL 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 404 LHQQDLKLMKMEKLVDNNTTLVDKLTRFQQ--------ENEELKARMD-----------RHMAISRQLSTEQAALQESLE 464
Cdd:pfam12128 560 LHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpewaaSEEELRERLDkaeealqsareKQAAAEEQLVQANGELEKASR 639
|
...
gi 564389283 465 KES 467
Cdd:pfam12128 640 EET 642
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
273-485 |
1.32e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 273 IEEAEKYKTQLQEQFDNLNAAHetTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKqindL 352
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----L 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 353 KSENDALNERLKSEEQKQlsrekansknpQVMYLEQELESLKAVLEIKNEKLHQQDLK---LMKMEKLVDNNTTLVDKLT 429
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLK-----------QLRARIEELRAQEAVLEETQERINRARKAaplAAHIKAVTQIEQQAQRIHT 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564389283 430 RFQ-QENEELKARMDRHMAISRQLS-TEQAALQESLEKESKVNKRLSmeNEELLWKLH 485
Cdd:TIGR00618 315 ELQsKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDAH--EVATSIREI 370
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
194-411 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 194 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLK--------------- 258
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSaadaavakdrselea 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 259 -------------EFYTAECEKLQSIY--IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEI 323
Cdd:pfam12128 327 ledqhgafldadiETAAADQEQLPSWQseLENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 324 KKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERL------------KSEEQKQL---------SREKANSKNPQ 382
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLgelklrlnqataTPELLLQLenfderierAREEQEAANAE 486
|
250 260
....*....|....*....|....*....
gi 564389283 383 VMYLEQELESLKAVLEIKNEKLHQQDLKL 411
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
111-369 |
3.67e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 111 RKSLFTAFNSVEKGRQKNPRSLCIQTQTAPdvlSTERTLELADYKTK---CENQSGFILHLKQLLSCgNTKFEALTVVIQ 187
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLEN---FENKFLKISDIKKKindCLKETESIEKKISSFSI-DSQDTELKENGD 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 188 HLLSERE--EALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYE-GFVQKLNQQHQTDQTELENrLKEFYTAE 264
Cdd:TIGR01612 1651 NLNSLQEflESLKDQK---KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIES-IKELIEPT 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 265 CEKLQSIYI----------EEAEKYKTQLQEQFDNLNAAHE--TTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKK 332
Cdd:TIGR01612 1727 IENLISSFNtndlegidpnEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKK 1806
|
250 260 270
....*....|....*....|....*....|....*..
gi 564389283 333 LLENLLNEKQESLEKQINDLKSENDALNERLKSEEQK 369
Cdd:TIGR01612 1807 SKSYLDDIEAKEFDRIINHFKKKLDHVNDKFTKEYSK 1843
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
247-433 |
3.79e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 247 QTDQTELENRLKEFyTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKleieaSHSEKVELLKKTYETSLSEIKKS 326
Cdd:cd22656 106 ATDDEELEEAKKTI-KALLDDL----LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLTDEGGA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 327 HEMEKklLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA---------------NSKNPQVMYLEQ--- 388
Cdd:cd22656 176 IARKE--IKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLiadltaadtdldnllALIGPAIPALEKlqg 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564389283 389 -------ELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQ 433
Cdd:cd22656 254 awqaiatDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-479 |
4.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 251 TELENRLKEFytaeceKLQSiyiEEAEKYKtQLQEQFD----NLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKks 326
Cdd:COG1196 196 GELERQLEPL------ERQA---EKAERYR-ELKEELKeleaELLLLKLRELEAELEELEAELEELEAELEELEAELA-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 327 hEMEKKLLEnlLNEKQESLEKQINDLKSENDALNERLkSEEQKQLSREKANSKNpqvmyLEQELESLKAVLEIKNEKL-- 404
Cdd:COG1196 264 -ELEAELEE--LRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRE-----LEERLEELEEELAELEEELee 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564389283 405 HQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEE 479
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-460 |
5.20e-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: 42.80 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 198 KQHKTLSQELVSLRGELVAASstcEKLEKARNDLQTAYEgfvqKLNQQHQTDQTELENRLKEFYTAECEKLQSIYiEEAE 277
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVE---DQLEALKSESQNKIE----LLLQQHQDRIEQLISEHEVEITGLTEKASSAR-SQAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 278 KYKTQL---QEQFDNLNAAHETTKLEIEASHSE-KVEL--LKKTYETSLSEIKKS------------------------- 326
Cdd:pfam15921 296 SIQSQLeiiQEQARNQNSMYMRQLSDLESTVSQlRSELreAKRMYEDKIEELEKQlvlanseltearterdqfsqesgnl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 327 HEMEKKLLENL-LNEKQESLEKQ---------------INDLKSEND----------ALNERLKSEEQKQLSREKA---- 376
Cdd:pfam15921 376 DDQLQKLLADLhKREKELSLEKEqnkrlwdrdtgnsitIDHLRRELDdrnmevqrleALLKAMKSECQGQMERQMAaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 377 -NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLV-DNNTTLVDKLTRFQQENEE---LKARMDRHMAISRQ 451
Cdd:pfam15921 456 kNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEitkLRSRVDLKLQELQH 535
|
....*....
gi 564389283 452 LSTEQAALQ 460
Cdd:pfam15921 536 LKNEGDHLR 544
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
273-407 |
5.79e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 273 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEaSHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDL 352
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEA 582
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564389283 353 KSENDALNERLKSEEQKQLSREKANSknpqvmyLEQELESLKAVLEIKNEKLHQQ 407
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKAHE-------LIEARKRLNKANEKKEKKKKKQ 630
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-354 |
6.03e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 194 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLN------QQHQTDQTELENRLKEFYTA--EC 265
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAllrselEELSEELRELESKRSELRREleEL 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 266 EKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYEtSLSEIKKShemekklLENL-------- 337
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR-RLKRLENK-------IKELgpvnlaai 992
|
170 180
....*....|....*....|..
gi 564389283 338 -----LNEKQESLEKQINDLKS 354
Cdd:TIGR02168 993 eeyeeLKERYDFLTAQKEDLTE 1014
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
317-481 |
7.71e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 317 ETSLSEIK--KSHEMEKKLLENLLNEKQESLEkQINDLKSENDALNERLKS--EEQKQLSREKANSKNPQVMYLEQELES 392
Cdd:PRK11281 42 QAQLDALNkqKLLEAEDKLVQQDLEQTLALLD-KIDRQKEETEQLKQQLAQapAKLRQAQAELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 393 LK-AVLEIKNEKL--HQQDLKlmkmEKLVDNNTTLV--------------DKLTRFQQENEELKARMDRHMAISR----Q 451
Cdd:PRK11281 121 LSlRQLESRLAQTldQLQNAQ----NDLAEYNSQLVslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPsqrvL 196
|
170 180 190
....*....|....*....|....*....|
gi 564389283 452 LSTEQAALQESLEkeskvNKRLSMENEELL 481
Cdd:PRK11281 197 LQAEQALLNAQND-----LQRKSLEGNTQL 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
186-351 |
1.17e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 186 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAY---EGFVQKLNQQHQTDQTELEN--RLKEF 260
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNvrNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 261 --YTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEAsHSEKVELLKKTYETSLSEIKKshEMEKkllenlL 338
Cdd:COG1579 92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
|
170
....*....|...
gi 564389283 339 NEKQESLEKQIND 351
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
177-382 |
1.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 177 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENR 256
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 257 LKEFYTAeceKLQSIYIE---EAEKYkTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkKTYETSLSEIKKSHEMEKKL 333
Cdd:COG3883 92 ARALYRS---GGSVSYLDvllGSESF-SDFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564389283 334 LENL---LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQ 382
Cdd:COG3883 166 LEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
185-479 |
1.33e-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: 41.65 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 185 VIQH--LLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQ--------KLNQQHQTDQTELE 254
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 255 NRLKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDN------LNAAHETTKLEIEasHSEKVELLKKTYETSLSEIKKSHE 328
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQMERQQKNervrqeLEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 329 MEKKLLEN-----LLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLK-AVLEIKNE 402
Cdd:pfam17380 435 REVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564389283 403 KlhqqdlKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQL--STEQAALQESLEKESKVNKRLsMENEE 479
Cdd:pfam17380 515 R------KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
177-481 |
1.34e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 177 TKFEALTVVIQHLLSEREEALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYEGF----------------VQ 240
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQRLEKNE---DQLKIITMELQKKSSELEEMTKFKNNKEVELEELkkilaedeklldekkqFE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 241 KLNQQHQTDQTEL----ENRLKEFYTAECE-----KLQSIYIEEAEKYKTQLQEQ---------------FDNLNAAHET 296
Cdd:pfam05483 429 KIAEELKGKEQELifllQAREKEIHDLEIQltaikTSEEHYLKEVEDLKTELEKEklknieltahcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 297 TKLEIE-ASHSEKVELLKKTYETSLSEIKKSHEMEKKLlENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREK 375
Cdd:pfam05483 509 SDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 376 A---------------NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKA 440
Cdd:pfam05483 588 QmkilenkcnnlkkqiENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564389283 441 RMDRHMAisRQLSTEQAALQESLEKESKVNKRLSMENEELL 481
Cdd:pfam05483 668 ISEEKLL--EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
261-480 |
1.71e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 261 YTAECEKLQsiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtYETSLSEIKKSHEMEKKLLE----- 335
Cdd:COG5022 815 YLACIIKLQ--KTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKK-ETIYLQSAQRVELAERQLQElkidv 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 336 ---NLLNEKQESLEKQI--------------NDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLE 398
Cdd:COG5022 892 ksiSSLKLVNLELESEIielkkslssdlienLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSE 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 399 IKNEKLHQQDL-------KLMKMEKLVDNNTTLVDKLTRFQQENEELKAR---MDRHMAISRQLSTEQAALQeSLEKESK 468
Cdd:COG5022 972 EYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELpveVAELQSASKIISSESTELS-ILKPLQK 1050
|
250
....*....|..
gi 564389283 469 VNKRLSMENEEL 480
Cdd:COG5022 1051 LKGLLLLENNQL 1062
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-363 |
1.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 201 KTLSQELVSLRGELVAASSTCEKLEKARNDLQT---AYEG-----FVQKLNQQHQTDQTELENRLKEfYTAECEKLQSIY 272
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQErreALQRlaeysWDEIDVASAEREIAELEAELER-LDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 273 --IEEAEKYKTQLQEQFDNLNAAHETTKLEIEAsHSEKVELLKKTYETSLSEIKKSH--EMEKKL----LENLLNEKQES 344
Cdd:COG4913 692 eqLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLEAAEDLARLELraLLEERFaaalGDAVERELREN 770
|
170
....*....|....*....
gi 564389283 345 LEKQINDLKSENDALNERL 363
Cdd:COG4913 771 LEERIDALRARLNRAEEEL 789
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
295-458 |
1.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 295 ETTKLEIEASHSEKVELLKKTYEtslseiKKSHEMEKKL--LENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLS 372
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRNEFE------KELRERRNELqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 373 REKansknpqvmyLEQELESLKAVLEIKNEK---LHQQDLKLMKMEKLVDNNTTlvDKLTRFQQENEELKARMDRH---- 445
Cdd:PRK12704 126 LEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEADKKakei 193
|
170
....*....|....*
gi 564389283 446 --MAISRqLSTEQAA 458
Cdd:PRK12704 194 laQAIQR-CAADHVA 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-480 |
2.10e-03 |
|
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: 40.81 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 273 IEEA---EKYKTQLQEQFDNLNAAHET-TKLE-IEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKqESLEK 347
Cdd:TIGR02168 161 FEEAagiSKYKERRKETERKLERTRENlDRLEdILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRL-EELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 348 QINDLKSENDALNERLKS-EEQKQLSREKANSKNPQVMYLEQELESL-KAVLEIKNEklhQQDLKLMKMEkLVDNNTTLV 425
Cdd:TIGR02168 240 ELEELQEELKEAEEELEElTAELQELEEKLEELRLEVSELEEEIEELqKELYALANE---ISRLEQQKQI-LRERLANLE 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564389283 426 DKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
178-476 |
2.14e-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: 40.65 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 178 KFEALTVVIQHLLSEREEALKQHKtlsqELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELEnRL 257
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYK----ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-RM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 258 KEfytaeceklqsiyieEAEKYKTQLQEQfdnlNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKklLENL 337
Cdd:pfam07888 156 KE---------------RAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ--LQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 338 LNEKQESLEkQINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKME-K 416
Cdd:pfam07888 215 ITTLTQKLT-TAHRKEAENEALLEELRS------LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQ 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 417 LVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSME 476
Cdd:pfam07888 288 LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
224-434 |
2.17e-03 |
|
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: 40.88 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 224 LEKARNDLQTAYEGFVQKlNQQHQTDQTELENRLKEFYTA-----ECEKLQSIYIEEAEKyktQLQEQFDNLNAAHETT- 297
Cdd:pfam05557 32 LEKKASALKRQLDRESDR-NQELQKRIRLLEKREAEAEEAlreqaELNRLKKKYLEALNK---KLNEKESQLADAREVIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 298 --KLEIEASH--SEKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSENDALNE---RLKSEEQKQ 370
Cdd:pfam05557 108 clKNELSELRrqIQRAELELQSTNSELEELQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAEQRIKElefEIQSQEQDS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389283 371 LSREKANSKNPQVMYLEQELE----------SLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQE 434
Cdd:pfam05557 187 EIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQE 260
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-484 |
2.58e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 264 ECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKlEIEAshseKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQE 343
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEK----EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 344 --SLEKQINDLKSENDALNERLKSEEQKqLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLM----KMEKL 417
Cdd:TIGR02169 760 lkELEARIEELEEDLHKLEEALNDLEAR-LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQEL 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389283 418 VDNNTTLVDKLTRFQQENEELKAR-------MDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKL 484
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-480 |
2.98e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 267 KLQSIYIEEAEKYKTQLQEQFDNL------NAAHETTKLE------IEASHSEKVELLKKTYETSLSEIKKSHEMEKKLL 334
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPGLnviygpNEAGKSTLLAfiramlLERLEKEADELFKPQGRKPELNLKELKELEEELK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 335 E--------NLLNEKQESLEKQINDLKSENDALNERLKSEEQKQlsrekansknpQVMYLEQELESLKAVLEIKNEKLHQ 406
Cdd:COG4717 82 EaeekeeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-----------QLLPLYQELEALEAELAELPERLEE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389283 407 QDLKLMKMEklvdnntTLVDKLTRFQQENEELKARMDRHMAISRQlsTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:COG4717 151 LEERLEELR-------ELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRLAELEEEL 215
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
192-474 |
2.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 192 EREEALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQ-TELENRLKEFYTAECEKlqs 270
Cdd:PRK03918 449 HRKELLEEYT---AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlKELEEKLKKYNLEELEK--- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 271 iyieEAEKYKTqLQEQFDNLNAAHETTKLEIEashseKVELLKKTYETSLSEIKKSHEMEKKL---LENLLNEKQESLEK 347
Cdd:PRK03918 523 ----KAEEYEK-LKEKLIKLKGEIKSLKKELE-----KLEELKKKLAELEKKLDELEEELAELlkeLEELGFESVEELEE 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 348 QINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLM--KMEKLVDNNTTLV 425
Cdd:PRK03918 593 RLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEELREEYLELS 672
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564389283 426 DKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLS 474
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-381 |
3.56e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 165 ILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQ 244
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 245 QHQTDQTELENRLKEFYTAEcekLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYE--TSLSE 322
Cdd:COG4942 116 LGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEerAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564389283 323 IKKshemEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNP 381
Cdd:COG4942 193 LKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
252-445 |
4.42e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 252 ELENRLKEFYtaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETtklEIEASHseKVELLKKTYETSLSEIKKSHEMEK 331
Cdd:pfam06160 241 QLEEQLEENL----ALLENLELDEAEEALEEIEERIDQLYDLLEK---EVDAKK--YVEKNLPEIEDYLEHAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 332 KLLENL-----LNE----KQESLEKQINDLKSENDALNERLKSEEQkqlsrekansknPQVMYLEQELESLKAVLEIKNE 402
Cdd:pfam06160 312 EELERVqqsytLNEneleRVRGLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE 379
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564389283 403 klhQQDLKlMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRH 445
Cdd:pfam06160 380 ---QEEFK-ESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
186-464 |
4.62e-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: 39.95 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 186 IQHLLSEREEALKQHKTLSQ---ELVSLRGELVAASSTCEKLEKARNDL-----QTAYEGFVQKLNQQHQTDQTELENRL 257
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQlraRIEELRAQEAVLEETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 258 KEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkkTYETSLSEIKKSHEMEKKLLENL 337
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT---QHIHTLQQQKTTLTQKLQSLCKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 338 LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKL 417
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 564389283 418 VDNNT---TLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLE 464
Cdd:TIGR00618 482 HLQETrkkAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
320-473 |
4.67e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 320 LSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSENDALNERLKSEEQKQlsreKANSKNPQVMYLEQELESLKAVLEI 399
Cdd:COG1579 33 LAELEDELAALEARLEAA-KTELEDLEKEIKRLELEIEEVEARIKKYEEQL----GNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389283 400 KNEKLhqqdLKLM-KMEKLVDNNTTLVDKLTRFQQENEELKARMDrhmAISRQLSTEQAALQESLEK-ESKVNKRL 473
Cdd:COG1579 108 LEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREElAAKIPPEL 176
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
331-468 |
4.67e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 331 KKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA------NSKNPQVMYLEQELESLKAVLEIKNEKL 404
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNefekelRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389283 405 HQQDLKLMKMEKLVDNNTTLVDKLtrfQQENEELKARMDRHMAISRQLSTEQA--ALQESLEKESK 468
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
185-480 |
5.00e-03 |
|
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: 39.72 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 185 VIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKEFY-TA 263
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEeLQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 264 ECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTK---LEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLlenllnE 340
Cdd:pfam05557 139 ERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKeleFEIQSQEQDSEIV-----KNSKSELARIPELEKEL------E 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 341 KQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyleqeleslKAVLEIKNEKLHQqdlKLMKMEKLVDN 420
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE--------------AATLELEKEKLEQ---ELQSWVKLAQD 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389283 421 NT-------TLVDKLTRFQQENEELKARMD------RHMAISR-QLSTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:pfam05557 271 TGlnlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKARrELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
141-438 |
5.08e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.65 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 141 DVLSTERTLELADYKTKCENQSGFILHLK------QLLSCGNTKFEALTVVIQ---HLLSEREEALkqHKTLsQELVSLR 211
Cdd:TIGR01612 688 AIDNTEDKAKLDDLKSKIDKEYDKIQNMEtatvelHLSNIENKKNELLDIIVEikkHIHGEINKDL--NKIL-EDFKNKE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 212 GELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTElENRLKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLN 291
Cdd:TIGR01612 765 KELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIK-DEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 292 AAHETTK-LEIEASHSEKVEllkktyetslSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQ 370
Cdd:TIGR01612 844 FLNKVDKfINFENNCKEKID----------SEHEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNI 913
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389283 371 LSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHqQDLKLMKMEKLVDN------NTTLVDKLTRFQQENEEL 438
Cdd:TIGR01612 914 NTLKKVDEYIKICENTKESIEKFHNKQNILKEILN-KNIDTIKESNLIEKsykdkfDNTLIDKINELDKAFKDA 986
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-485 |
5.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 186 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYegfvQKLNQQHqtdqtelENRLKEFYTAEC 265
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG----RELTEEH-------RKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 266 EKLQSiYIEEAEKYKTQLQEqfdnlnaahETTKLEIEASHSEKVELLKKTYEtSLSEIKKshEMEKKLLENL--LNEKQE 343
Cdd:PRK03918 462 KRIEK-ELKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAE-QLKELEE--KLKKYNLEELekKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 344 SLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqVMYLEQELESLKAVLEIKN-EKLHQQDLKLMKMEKLVDNNT 422
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYL 605
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389283 423 TLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKLH 485
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
275-468 |
6.19e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 39.35 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 275 EAEKYKTQLQEQFDNLNAAHETTkLEIEASHSEKVELLKKTYETSLS-EIKKSHEMEKK--LLENLLNEKQESLEKQIND 351
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAgEAKQLAEAQKEaeLLRKQLSKTQEELEAQVTL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 352 LKSENDALNERLKSE--------EQKQLS------REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQqdlKLMKMEKL 417
Cdd:pfam07111 220 VESLRKYVGEQVPPEvhsqtwelERQELLdtmqhlQEDRADLQATVELLQVRVQSLTHMLALQEEELTR---KIQPSDSL 296
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564389283 418 VDNNTTLVDKLTRFQQENE-----ELKARMDRHMAISRQLSTEQAALQESLEKESK 468
Cdd:pfam07111 297 EPEFPKKCRSLLNRWREKVfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQ 352
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
307-480 |
6.71e-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: 39.18 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 307 EKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYL 386
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 387 EQELESLKAVLEIKNEKLhQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISrqLSTEQAALQESLEKE 466
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKL-AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD--DEEKLKESEKEKKKA 326
|
170
....*....|....
gi 564389283 467 SKVNKRLSMENEEL 480
Cdd:pfam02463 327 EKELKKEKEEIEEL 340
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
249-445 |
7.39e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.05 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 249 DQTELENRLKEFYTA--ECEK-LQSIYIEEAEKYKTQLQEQFDNLNAAHETtklEIEASHseKVELLKKTYETSLSEIKk 325
Cdd:PRK04778 250 DHLDIEKEIQDLKEQidENLAlLEELDLDEAEEKNEEIQERIDQLYDILER---EVKARK--YVEKNSDTLPDFLEHAK- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 326 shEMEKKLLENL--------LN----EKQESLEKQINDLKSENDALNERLksEEQKQLSREkansknpqvmyLEQELESL 393
Cdd:PRK04778 324 --EQNKELKEEIdrvkqsytLNeselESVRQLEKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEI 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564389283 394 KAVL-EIKNEklhQQDLKLMkMEKLVDNNTTLVDKLTRFQQENEELKARMDRH 445
Cdd:PRK04778 389 LKQLeEIEKE---QEKLSEM-LQGLRKDELEAREKLERYRNKLHEIKRYLEKS 437
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
312-453 |
8.05e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.26 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 312 LKKTYETSLSEIKKSHEMEKKLLENllNEKQESLEKQINDLksendaLNERLKSEEQkqlsrekanskNPQVMYLEQELE 391
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE-----------IIYINKLKLELK 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389283 392 SLKAVLEIKNEKLHqqdlKLMKMEKLVDNNTTLVDKLTRFQ--QENEELKARMDRHMAISRQLS 453
Cdd:TIGR01612 607 EKIKNISDKNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKSELS 666
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
194-480 |
8.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 194 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQT-----ELENRLKEFYTAECEKL 268
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaeEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 269 QSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYEtslsEIKKSHEMEKKLLEnllNEKQESLEKQ 348
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE----EAKKADEAKKKAEE---AKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 349 INDLKSENDALneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDlKLMKMEKlvdnnttlVDKL 428
Cdd:PTZ00121 1492 AEEAKKKADEA--KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--------LKKA 1560
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564389283 429 TRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 480
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
190-437 |
8.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 190 LSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEkarndlqtayegfvqklnqqhqtdqtELENRLKEFYtaecEKLQ 269
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE--------------------------ELKKKLAELE----KKLD 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 270 SIYIEEAEKYKTQLQEQFDNLNAAHETTKlEIEASHSEKVELL--KKTYETSLSEIKKSHEMEKKLLENL--LNEKQESL 345
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLELKdaEKELEREEKELKKLEEELDKAFEELaeTEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 346 EKQINDLKSENDALNERLKSEEQKQLSREKAnSKNPQVMYLEQELESLKAVLE-IKNEK--LHQQDLKLMKMEKLVDNNT 422
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEkLKEELeeREKAKKELEKLEKALERVE 724
|
250
....*....|....*
gi 564389283 423 TLVDKLTRFQQENEE 437
Cdd:PRK03918 725 ELREKVKKYKALLKE 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-412 |
9.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 222 EKLEKARNDLQTAYEGFVQKLNQQHQTDQ--TELENRLKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKL 299
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEelEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 300 EIEAShsekvellkKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKS--EEQKQLSREKAN 377
Cdd:COG4717 154 RLEEL---------RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEleEELEEAQEELEE 224
|
170 180 190
....*....|....*....|....*....|....*
gi 564389283 378 sknpqvmyLEQELESLKAVLEIKNEKLHQQDLKLM 412
Cdd:COG4717 225 --------LEEELEQLENELEAAALEERLKEARLL 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
168-443 |
9.70e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 38.67 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 168 LKQLLSCGNTKFEALTVVIQHLLSEREEALK-QHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQH 246
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 247 QTDQTELENrlkefytaeCEKLQSiyieEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSE-KVELLKKTYETSLSeiKK 325
Cdd:pfam12128 778 RTLERKIER---------IAVRRQ----EVLRYFDWYQETWLQRRPRLATQLSNIERAISElQQQLARLIADTKLR--RA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 326 SHEMEKKLLENLLNEKQESLEKqindLKSENDALNeRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLH 405
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRG----LRCEMSKLA-TLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564389283 406 QQDLKLMKM------EKLVDNNTTLVDKLTRFQQENEELKARMD 443
Cdd:pfam12128 918 NVIADHSGSglaetwESLREEDHYQNDKGIRLLDYRKLVPYLEQ 961
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
328-444 |
9.78e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 37.43 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389283 328 EMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSknpqvmyLEQELESLKAVLEIKNEKLHQQ 407
Cdd:PRK14160 4 ECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEEIIEDSEESNEV-------KIEELKDENNKLKEENKKLENE 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 564389283 408 dlklmkMEklvdnntTLVDKLTRFQQENEELKARMDR 444
Cdd:PRK14160 77 ------LE-------ALKDRLLRTVAEYDNYRKRTAK 100
|
|
| |
