|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
100-411 |
1.53e-132 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 399.68 E-value: 1.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 100 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 178
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 179 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 258
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 259 KDYLKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 338
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281185500 339 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 411
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-367 |
2.64e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 104 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 183
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 184 RLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLK 263
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 264 TDISTALKEIRSQLESHSDQNMHQAEewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 343
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLE-----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|....
gi 281185500 344 QLSDIEERHNHDLSSYQDTIQQLE 367
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELA 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
128-411 |
6.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 128 EIEAEIQALRqKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSdhLEEDIHRLKERFEEEARLRDDTEAAIRALR 207
Cdd:COG1196 197 ELERQLEPLE-RQAEKAERYRELKEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 208 KDIEeaslvkvELDKKVQSLQDEVAflrsNHEEEVADLLAQIQAshiTVERKDYLKTDISTALKEIRSQLESHSDqnmHQ 287
Cdd:COG1196 274 LELE-------ELELELEEAQAEEY----ELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEE---LE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 288 AEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLE 367
Cdd:COG1196 337 EEL------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 281185500 368 NELRgtkwEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 411
Cdd:COG1196 411 ALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-353 |
1.14e-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: 68.93 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 103 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 181
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 182 IHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVERKDY 261
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 262 LKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESL 341
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250
....*....|..
gi 281185500 342 ERQLSDIEERHN 353
Cdd:TIGR02168 495 ERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
121-419 |
2.63e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 121 YLEQQNKEIEAEIQ-ALRQKQASHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDT 199
Cdd:COG1196 215 YRELKEELKELEAElLLLKLRELEAEL-EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 200 EAAIRALRKDIEEASLVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLES 279
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 280 HSDQNMHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSY 359
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281185500 360 QDTIQQLENELRGTKWEMARHLRE---YQDLLNVKMALDIEIAAYRKLLEGEETRFSTFAGSI 419
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
128-486 |
2.97e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 128 EIEAEIQALRQKQAsHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLrddtEAAIRALR 207
Cdd:PRK02224 191 QLKAQIEEKEEKDL-HERL-NGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 208 KDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDIST---ALKEIRSQLESHSDQ- 283
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEElrdRLEECRVAAQAHNEEa 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 284 -----NMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNhDLSS 358
Cdd:PRK02224 345 eslreDADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE-ELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 359 YQDTIQQLENELRGTKWEMARHLREYQDLLN----------VKMALDIE-IAAYRKLLEGEETRFSTFAGSITgplyTHR 427
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpVEGSPHVEtIEEDRERVEELEAELEDLEEEVE----EVE 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 428 PPITISSKIQKPKVEAPKLKVQHKFVEEIIEETKVE-DEKSEMEEALTAITEELAVSMKE 486
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEERREDLEELIAERRETiEEKRERAEELRERAAELEAEAEE 555
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-347 |
5.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 101 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEE 180
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 181 DIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshitverkd 260
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE--------- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 261 ylKTDISTALKEIRSQLESHSDQNMHQAEEwfkcrYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKES 340
Cdd:COG1196 423 --LEELEEALAELEEEEEEEEEALEEAAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*..
gi 281185500 341 LERQLSD 347
Cdd:COG1196 496 LLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-345 |
5.89e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQASHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDS-----DHLEEDIHRLKERFEEEARLR 196
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 197 DDTEAAIRALRKDIEEASLVKVE-LDKKVQSLQDEVAfLRSNHEEEVADLLAQIQASHITVERkdylktdistALKEIRS 275
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEqLEREIERLERELE-ERERRRARLEALLAALGLPLPASAE----------EFAALRA 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 276 QLESHSDQnmhqaeewfkcryakLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQL 345
Cdd:COG4913 388 EAAALLEA---------------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-399 |
9.18e-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: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 130 EAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKD 209
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 210 IEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDIsTALKEIRSQLESHSDQNMHQAE 289
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 290 EWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLsdieERHNHDLSSYQDTIQQLENE 369
Cdd:TIGR02168 835 ATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL----ALLRSELEELSEELRELESK 909
|
250 260 270
....*....|....*....|....*....|
gi 281185500 370 LRgtkwEMARHLREYQDLLNvKMALDIEIA 399
Cdd:TIGR02168 910 RS----ELRRELEELREKLA-QLELRLEGL 934
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
10-74 |
9.77e-10 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 55.86 E-value: 9.77e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281185500 10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRSM-LAPRLAYSSAMLSSAESS 74
Cdd:pfam04732 2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSSrSSSRSSYPSLAADSLDFS 69
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-379 |
2.20e-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: 61.62 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 101 EKEQLQGLNDRFAGYIEKVHY-LEQQNKEIEAEIQALRQkqaSHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 179
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEE---LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 180 EDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERK 259
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 260 DYLKTDISTALKEIRSQLEshsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKE 339
Cdd:TIGR02169 395 EKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 281185500 340 SLERQLSDIEERHNHDlssyQDTIQQLENELRGTKWEMAR 379
Cdd:TIGR02169 459 QLAADLSKYEQELYDL----KEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-371 |
3.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 98 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 177
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 178 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVE 257
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 258 RKDYLKTDISTALKEIRSQLESHS------DQNMHQAEEWFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQLQS- 326
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKEl 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 281185500 327 -----KSI-ELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELR 371
Cdd:TIGR02168 985 gpvnlAAIeEYEELKERYDFLTAQKEDLTEA----KETLEEAIEEIDREAR 1031
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-389 |
3.16e-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: 60.85 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEE-EARLRD--- 197
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHsri 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 198 ---------------DTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHITVERK 259
Cdd:TIGR02169 794 peiqaelskleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEEL 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 260 DYLKTDISTALKEIRSQLESHSDQ--NMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE------L 331
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsL 953
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 281185500 332 ESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLeNELRGTKWEMARHLREYQDLLN 389
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-393 |
1.13e-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: 59.30 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRatLEMVNHEKAQVQLDS---------DHLEEDIHRLKERFEEE 192
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKelyalaneiSRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 193 ARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKE 272
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 273 ---IRSQLESHSDQnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE 349
Cdd:TIGR02168 395 iasLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 281185500 350 ER---HNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 393
Cdd:TIGR02168 468 EEleeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-369 |
1.49e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 116 IEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMvnhekAQVQLDSDHLEEDIHRLKERFEeeaRL 195
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----SWDEIDVASAEREIAELEAELE---RL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 196 RDDTeAAIRALRKDIEEASLVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRS 275
Cdd:COG4913 681 DASS-DDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 276 QlESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE-IAEYRRQLQSKSIELESVrgtkESLERQLSDIEerhNH 354
Cdd:COG4913 756 A-AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLE---ED 827
|
250
....*....|....*
gi 281185500 355 DLSSYQDTIQQLENE 369
Cdd:COG4913 828 GLPEYEERFKELLNE 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-408 |
4.93e-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: 56.99 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 85 NGGSGPGGDYKLSRSNEKEQLQGlndRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMV 164
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 165 NHEKAQVQLDSDHLEEDIHRL------------------KERFEEEARLRDDTEAAIRALRKDIEEASlvkvELDKKVQS 226
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELeaeieeleerleeaeeelAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 227 LQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEShsdqnmhqaeewfkcrYAKLTEAAEQN 306
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL----------------IEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 307 KEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLsdieERHNHDLSSYQDTIQQLENELRGTKwemARHLREYQD 386
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSL 951
|
330 340
....*....|....*....|..
gi 281185500 387 LLNVKMALDIEIAAYRKLLEGE 408
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-405 |
5.95e-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: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 102 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEI--RELRATLEMVNHEKAQVQLDSDHLE 179
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 180 EdihrLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERK 259
Cdd:COG4913 689 A----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 260 DYLKTDISTALKEIRSQLESHSDQ---NMHQAEEWFKCRYAKLTEAAEQNKE--AIRS--AKEEIAEY----RRQLQSKS 328
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEElerAMRAFNREWPAETADLDADLESLPEylALLDrlEEDGLPEYeerfKELLNENS 844
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281185500 329 IelESVRGTKESLERQLSDIEERhnhdlssyqdtIQQLENELRGTKWEMARHLReyqdlLNVKMALDIEIAAYRKLL 405
Cdd:COG4913 845 I--EFVADLLSKLRRAIREIKER-----------IDPLNDSLKRIPFGPGRYLR-----LEARPRPDPEVREFRQEL 903
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-388 |
6.95e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 98 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 172
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 173 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEeaslvkvELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQAS 252
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 253 HITVERK-DYLKTDISTALKEIRSQLESHSDqnmhqAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 331
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLREDADD-----LEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 281185500 332 ESVRGTKESLERQLSDIEERHNhDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 388
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-403 |
1.01e-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: 55.16 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 178 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE 257
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 258 -RKDYLKTDISTALKEIRSQLESH--SDQNMHQAEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESV 334
Cdd:COG4942 101 aQKEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281185500 335 RGTKESLERQLSDIEERHnhdlssyQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRK 403
Cdd:COG4942 180 LAELEEERAALEALKAER-------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-248 |
4.85e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 101 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYD--QEIRELRATLEMVNH----------EK 168
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPErleeleerleEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 169 AQVQLDSDHLEEDIHRLKERFEEEARLRD-DTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLA 247
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
.
gi 281185500 248 Q 248
Cdd:COG4717 239 A 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-303 |
6.05e-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: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 101 EKEQLQGLNDRFAGYI--EKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLemvnhekAQVQLDS-DH 177
Cdd:COG4913 270 RLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI-------RGNGGDRlEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 178 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshitve 257
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD------ 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 281185500 258 rkdyLKTDISTALKEIRSQLESHS--DQNMHQAEEWFkCRYAKLTEAA 303
Cdd:COG4913 417 ----LRRELRELEAEIASLERRKSniPARLLALRDAL-AEALGLDEAE 459
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
102-245 |
6.23e-07 |
|
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: 51.46 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 102 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQA-SHAQLGDAYDQeiRELRAtlemVNHEKAQVQLDSDHLEE 180
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNN--KEYEA----LQKEIESLKRRISDLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281185500 181 DIHRLKERFEEEARLRDDTEAAIRALRKDIEEAslvKVELDKKVQSLQDEVAFLRSNHEEEVADL 245
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
94-353 |
1.30e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 94 YKLSRSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQL 173
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 174 DSDHLEEDIHRLKERfeeearlRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHE---EEVADLLAQIQ 250
Cdd:PRK02224 301 EAGLDDADAEAVEAR-------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelrEEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 251 ASHITVERKDYLKTDISTALKEIRSQLESHSDQnMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS- 326
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAg 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 281185500 327 ------KSIE-------LESVRGTKESLERQLSDIEERHN 353
Cdd:PRK02224 453 kcpecgQPVEgsphvetIEEDRERVEELEAELEDLEEEVE 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-850 |
3.60e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 274 RSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQ-SKSIELESVRGTKESLERQLSDIEERH 352
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEdARKAEEARKAEDAKKAEAARKAEEVRK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 353 NHDLSSYQDtIQQLENELRGTKWEMARHLREYQDllnVKMALDIEIAAYRKLLEGEETRFSTFAGSITGPLYTHRPPITI 432
Cdd:PTZ00121 1190 AEELRKAED-ARKAEAARKAEEERKAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 433 SSKIQKPKVEAPKLKVQHKFVEEI--IEETKVEDEKSEMEEALTAITEELAVSMKEEKKEAAEEKEEEPEAEEEEVAAKK 510
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKkkADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 511 SPVKATAPEVKEEEGEKEEEEGQEEEEEEDEGAKSDQAEEGGSEKEGSSEKEEGEQEEGETEAEAEGEEAEAKEEKKVEE 590
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 591 KSEEVATKEElvadAKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVS 670
Cdd:PTZ00121 1426 KAEEKKKADE----AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 671 KSPVEEKAKSPVPKSPVEEAKSKAEVGKGEQKEEEEKEVKEAPKEEKVE-KKEEKPKDVPEKKKAESPVKEEAVAEVVTI 749
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 750 TKSVKVHLEKETKEEGKPLQQEKEKEKAGGEGGSEEEGSdKGAKGSRKEDIAVNGEVEGKEEVEQETKEKGSGREEEKGV 829
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
570 580
....*....|....*....|.
gi 281185500 830 VTNGLDLSPADEKKggDKSEE 850
Cdd:PTZ00121 1661 IKAAEEAKKAEEDK--KKAEE 1679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-379 |
3.93e-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: 50.15 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 124 QQNKEIEAEIQALRqkqashaqlgdaydQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLkerfeeeARLRDDTEAAI 203
Cdd:COG4942 20 DAAAEAEAELEQLQ--------------QEIAELEKELAALKKEEKALLKQLAALERRIAAL-------ARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 204 RALRKDIEeaslvkvELDKKVQSLQDEVAFLRsnheEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQ 283
Cdd:COG4942 79 AALEAELA-------ELEKEIAELRAELEAQK----EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 284 NMHQAEEwfkcrYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTI 363
Cdd:COG4942 148 RREQAEE-----LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250
....*....|....*.
gi 281185500 364 QQLENELRGTKWEMAR 379
Cdd:COG4942 223 EELEALIARLEAEAAA 238
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
98-388 |
5.26e-06 |
|
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: 49.89 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 98 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 177
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 178 LEEDIHRL-KERFEEEARLRD------DTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLR------SNHEEEVAD 244
Cdd:pfam07888 155 MKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 245 LLAQIQAS----HITVERKDYLKTDI-STALKEIRSQLESH-------------SDQNMHQAEEwfKCRYAKLTEAAEQN 306
Cdd:pfam07888 235 LLEELRSLqerlNASERKVEGLGEELsSMAAQRDRTQAELHqarlqaaqltlqlADASLALREG--RARWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 307 KEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQD 386
Cdd:pfam07888 313 AEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
..
gi 281185500 387 LL 388
Cdd:pfam07888 390 LL 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-333 |
6.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 127 KEIEAEIQALRQKQASHAQLgdaYDQEIRELRATLEMVNHEKAQVQLdsdhLEEDIHRLKERFEEEARLRDDTEAAIRAL 206
Cdd:COG4717 49 ERLEKEADELFKPQGRKPEL---NLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 207 RKDIEeaslvKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQNMH 286
Cdd:COG4717 122 EKLLQ-----LLPLYQELEALEAELAEL----PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 281185500 287 QAEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 333
Cdd:COG4717 193 ELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
595-910 |
9.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 595 VATKEELVADAKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEE-KGKSPVPKSPVEEKGKSPVSKSP 673
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdKKKADELKKAAAAKKKADEAKKK 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 674 VEEKAKSPVPKSPVEEA------KSKAEVGKGEQKEEEEKEVKEAPKEEKVEKKEEKPKDVPEKKKAESPVKEEAVAevv 747
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAkkadeaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK--- 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 748 titksvKVHLEKETKEEGKPLQQEKEKEKAGGEGGSEEEGSDKGAKGSRKEDIAVNGEVEGKEEVEQETKEKGSGREEEK 827
Cdd:PTZ00121 1504 ------KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 828 GVVTNGLDLSPADEKKGGD--KSEEKVVVTKTVEKITSEGGDGATKYITKSVTVTQKVEEHEETFEEKLVSTKKVEKVTS 905
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEvmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
....*
gi 281185500 906 HAIVK 910
Cdd:PTZ00121 1658 ENKIK 1662
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-278 |
1.04e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 97 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQAS-HAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 175
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELLRALYRLGRQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 176 DHLEEDIHRL-------KERFEEEARLRDDTEaAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQ 248
Cdd:COG4942 129 EDFLDAVRRLqylkylaPARREQAEELRADLA-ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190
....*....|....*....|....*....|
gi 281185500 249 IQASHITVERKDYLKTDISTALKEIRSQLE 278
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
122-351 |
1.63e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEE-EARLRDDTE 200
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 201 AAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRsNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESH 280
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281185500 281 SDQNmhqaeewfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 351
Cdd:COG4942 184 EEER------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-406 |
1.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 198 DTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVaflrsnheeevaDLLAQIQASHITVERKDYLKTDISTALKEI---- 273
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL------------DALQERREALQRLAEYSWDEIDVASAEREIaele 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 274 --RSQLESHSDQnmhqaeewfkcrYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 351
Cdd:COG4913 675 aeLERLDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 352 H----------------------------NHDLSSYQDTIQQLENELRGTkweMARHLREYQDLLNvkmALDIEIAA--- 400
Cdd:COG4913 743 ArlelralleerfaaalgdaverelrenlEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLESlpe 816
|
....*.
gi 281185500 401 YRKLLE 406
Cdd:COG4913 817 YLALLD 822
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-864 |
3.84e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 271 KEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEE 350
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEA 1204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 351 rhnhdlssyqdtIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRklleGEETRFSTFAGSITGPLYTHRPPI 430
Cdd:PTZ00121 1205 ------------ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK----AEEERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 431 TISSKIQKPKVEAPKLKVQHKfveEIIEETKVEDEKSEMEEALTAITEELAVSMKEEKKEAAEEKEEEPEAEEEEVAAKK 510
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEK---KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 511 SPVKATAPEVKEEEGEKEEEEGQEEEEEEDEGAKSDQAEEGGSEKEGSSEKEEGEQEEGETEaeaegeeaeakeekkvee 590
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA------------------ 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 591 kseevatkEELvadaKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVS 670
Cdd:PTZ00121 1408 --------DEL----KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 671 KSPVEEKAKSPVPKSPVEEAKSKAEvgkGEQKEEEEKEVKEAPKEEKVEKKEEKPKDVPEKKKAESPVKEEAVAEVVTIT 750
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 751 KSVKVHLEKETKEEGKPLQQEKEKEKAGGEGGSEEEGSDKGAKGSRKEDIAVNGEVEGKEEVEQETKEKGS--GREEEKG 828
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEK 1632
|
570 580 590
....*....|....*....|....*....|....*....
gi 281185500 829 VVTNGLDLSPADEKKGGD---KSEEKVVVTKTVEKITSE 864
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAE 1671
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
122-264 |
5.55e-05 |
|
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: 45.69 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQAshaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKER------------- 188
Cdd:COG1579 22 LEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeal 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281185500 189 ---FEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshITVERKDYLKT 264
Cdd:COG1579 95 qkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE--LEAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
134-375 |
2.03e-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: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 134 QALRQKQASHAQLGDAYDQEIRELRATLE---------MVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIR 204
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 205 ALRKDIEEASLVKVEL--DKKVQSLQDEVAFLRSnheeEVADLLAQIQASHITVERkdyLKTDISTALKEIRSQLEshsd 282
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIA---LRAQIAALRAQLQQEAQ---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 283 qnmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDT 362
Cdd:COG3206 313 ---------------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
250
....*....|...
gi 281185500 363 iqQLENELRGTKW 375
Cdd:COG3206 378 --RLAEALTVGNV 388
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
102-406 |
3.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 102 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGD----AYDQEIRELRATLEMVNHEKAQVQLDSDH 177
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 178 LEEDIHRLKERFE--EEARLRDDTEAAIRALRKDIEEASLV--------------------------------------K 217
Cdd:COG4717 218 AQEELEELEEELEqlENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgllallflllareK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 218 VELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQASHI-----------TVERKDYLKTDISTALKEIR-SQLESHSDQNM 285
Cdd:COG4717 298 ASLGKEAEELQALPA-LEELEEEELEELLAALGLPPDlspeellelldRIEELQELLREAEELEEELQlEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 286 HQA-----EEWFKCryAKLTEAAEQNKEAIRSAKEEIAEYR--RQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSS 358
Cdd:COG4717 377 AEAgvedeEELRAA--LEQAEEYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 281185500 359 YQDTIQQLENELRGTKWEMARHlrEYQDLLNVKMALDIEIAAYRKLLE 406
Cdd:COG4717 455 LAELEAELEQLEEDGELAELLQ--ELEELKAELRELAEEWAALKLALE 500
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
601-694 |
4.81e-04 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 42.75 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 601 LVADAKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGK-SPVPKSPVEEKGKSPVskSPVEEKAK 679
Cdd:PRK10819 52 MVAPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIPKPEPKPKPKPKpKPKPVKKVEEQPKREV--KPVEPRPA 129
|
90
....*....|....*
gi 281185500 680 SPVPKSPVEEAKSKA 694
Cdd:PRK10819 130 SPFENTAPARPTSST 144
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
100-351 |
6.07e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 100 NEKEQLQGLnDRFAG---YIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELratlemvnhEKAQVQLDSD 176
Cdd:COG0497 139 DPDAQRELL-DAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------EAAALQPGEE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 177 -HLEEDIHRLkERFEEearLRDDTEAAIRALrkDIEEASLVKVeLDKKVQSLQDevaflRSNHEEEVADLLAQIQASHIT 255
Cdd:COG0497 209 eELEEERRRL-SNAEK---LREALQEALEAL--SGGEGGALDL-LGQALRALER-----LAEYDPSLAELAERLESALIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 256 VErkdylktDISTALKEIRSQLEShSDQNMHQAEEwfkcRYAklteaaeqnkeAIRSAK-------EEIAEYRRQLQSKS 328
Cdd:COG0497 277 LE-------EAASELRRYLDSLEF-DPERLEEVEE----RLA-----------LLRRLArkygvtvEELLAYAEELRAEL 333
|
250 260
....*....|....*....|...
gi 281185500 329 IELESVRGTKESLERQLSDIEER 351
Cdd:COG0497 334 AELENSDERLEELEAELAEAEAE 356
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
216-407 |
6.53e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 216 VKVELDK-KVQSLQDEVAFLRSNHEEEVADLLAQIQASHitvERKDYLKTDISTA---LKEIRSQLESHSDQNMHQAEEw 291
Cdd:PRK11281 41 VQAQLDAlNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK---EETEQLKQQLAQApakLRQAQAELEALKDDNDEETRE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 292 fkcRYAKLTEAAEQNK-----EAIRSAKEEIAEYRRQLQSksielesvrgtkeslerqLSDIEERHNHDLSSYQDTIQQL 366
Cdd:PRK11281 117 ---TLSTLSLRQLESRlaqtlDQLQNAQNDLAEYNSQLVS------------------LQTQPERAQAALYANSQRLQQI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 281185500 367 ENELRGTKWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 407
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
100-406 |
7.25e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 100 NEKEQLQGLNDRFAGYIEKVhylEQQNKEIEAEiqalRQKQAshaQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 179
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSI---ESLKKKIEEY----SKNIE---RMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 180 EDIHRLKERfeeearlrddteaaIRALRKDIEEASLVKVEL--------------DKKVQSLQDEVAFLRSNHEEEVADL 245
Cdd:PRK01156 423 SKVSSLNQR--------------IRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREI 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 246 laQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQNMHQAE-EWFKCRYAKLTEA---AEQNKEAIRSAKEEIAEYR 321
Cdd:PRK01156 489 --EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADlEDIKIKINELKDKhdkYEEIKNRYKSLKLEDLDSK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 322 RQ------LQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRgtkwEMARHLREYQDLLNVKMALD 395
Cdd:PRK01156 567 RTswlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR----EIENEANNLNNKYNEIQENK 642
|
330
....*....|.
gi 281185500 396 IEIAAYRKLLE 406
Cdd:PRK01156 643 ILIEKLRGKID 653
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
173-411 |
8.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 173 LDSDHLEEDIHRLKERFEEEARLRD---DTEAAIRALRkDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQi 249
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLERAHEaleDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 250 qashitverkdylktdistALKEIRSQLESHsDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAK-EEIAEYRRQLQSKS 328
Cdd:COG4913 296 -------------------ELEELRAELARL-EAELERLEA----RLDALREELDELEAQIRGNGgDRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 329 IELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGE 408
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
...
gi 281185500 409 ETR 411
Cdd:COG4913 432 ERR 434
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
605-684 |
1.39e-03 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 42.05 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 605 AKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPvSKSPVEEKAKSPVPK 684
Cdd:PLN02226 163 AIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEP-QLPPKERERRVPMTR 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
174-882 |
1.68e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 174 DSDHLEEDIHRLKERFEEEARLrddTEAAIRALRKDIEEASLVKvELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASH 253
Cdd:PTZ00121 1078 DFDFDAKEDNRADEATEEAFGK---AEEAKKTETGKAEEARKAE-EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 254 ITVERK--DYLKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAA-----EQNKEAIRSAKEE--IAEYRRQL 324
Cdd:PTZ00121 1154 VEIARKaeDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAArkaeeERKAEEARKAEDAkkAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 325 QSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLE----NELRgtKWEMARHLREYQDLLNVKMALDIEIAA 400
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarkaDELK--KAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 401 YRKLLEGEETRFSTFAGSITGPLYTHRPPITISSKIQKPKVEAPKLKVQHKFVEEIIEETKVEDEKSEMEEALTAITEEL 480
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 481 AVSMKEEKKEAAEEKEEEPEAEEEEVAAKKSPVKATAPEVKEEEGEKEEEEGQEEEEEEDEGAKSDQAEEGGSEKEGSSE 560
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 561 KEEGEQEEGETEAEAEGEEAEAKEEKKVEEKSEEVATK---EELVADAKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEE 637
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 638 KGKSPVPKSpvEEKGKSPVPKSPVEEKG----KSPVSKSpVEEKAKSPVPKSPVEEAKSKAEVGKGEQKEEEEKEVKEAP 713
Cdd:PTZ00121 1552 KKAEELKKA--EEKKKAEEAKKAEEDKNmalrKAEEAKK-AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 714 KEEKVEKKEEKPKDVPEKKKAESPVKEEavaEVVTITKSVKVHLEKETKEEGKPLQQEKEKEKAGGEGGSEEEGSDKGAK 793
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAE---EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 794 GSRKEDiavngevegkeEVEQETKEKGSGREEEKGVVTNGLDLSPADEKKGGDKSEEKVVVTKTVEKITSEGGDGATKYI 873
Cdd:PTZ00121 1706 ELKKKE-----------AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
....*....
gi 281185500 874 TKSVTVTQK 882
Cdd:PTZ00121 1775 KEKEAVIEE 1783
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
217-369 |
1.75e-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: 41.54 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 217 KVELDKKVQSLQDEVAFLRSnHEEEVADLLAQIQASHITVERKdylktdiSTALKEIRSQLESHSDQNMHQAEEwfkcry 296
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMK-ELELLNSIKPKLRDRKDALEEE-------LRQLKQLEDELEDCDPTELDRAKE------ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 297 aKLTEAAEQNKEAirsaKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHN-------HDLSSYQDTIQQLENE 369
Cdd:smart00787 212 -KLKKLLQEIMIK----VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEqcrgftfKEIEKLKEQLKLLQSL 286
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
122-387 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQASHAqlgdaydQEIRELRATLEMVNHEKAQVQ-LDSDHLEedihrlkERFEEEARLRDDTE 200
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLR-------QQLDQLKEQLQLLNKLLPQANlLADETLA-------DRLEELREELDAAQ 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 201 AAIRALRKDIEEASlvkvELDKKVQSLQ------DEVAFLRSNHEEEVADLLAQIQASHITVERKDYL-----------K 263
Cdd:COG3096 907 EAQAFIQQHGKALA----QLEPLVAVLQsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFsyedavgllgeN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 264 TDISTALKEIRSQLE---SHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL-----ESVR 335
Cdd:COG3096 983 SDLNEKLRARLEQAEearREAREQLRQAQA----QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281185500 336 GTKESLERQLSDIEERhnhdLSSYQDTIQQLENELRGTKWEMARHLREYQDL 387
Cdd:COG3096 1059 IRRDELHEELSQNRSR----RSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
103-389 |
1.92e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 103 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDA--------------YDQEIRELRATLEMVNHEK 168
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAEL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 169 AQVQLDSDHLEEDIHRLKERFEEEARL------RDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRS------ 236
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIerleerREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaeae 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 237 ----NHEEEVADLLAQIQASHITVERKDYLKTDIST---------ALKEIRSQLESHSDQNMHQAEEwFKCRYAKL---- 299
Cdd:PRK02224 565 eeaeEAREEVAELNSKLAELKERIESLERIRTLLAAiadaedeieRLREKREALAELNDERRERLAE-KRERKRELeaef 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 300 ----TEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNH------DLSSYQDTIQQLENE 369
Cdd:PRK02224 644 dearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREAlenrveALEALYDEAEELESM 723
|
330 340
....*....|....*....|.
gi 281185500 370 LRGTKWEM-ARHLREYQDLLN 389
Cdd:PRK02224 724 YGDLRAELrQRNVETLERMLN 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
151-371 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 151 DQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEAslvKVELDKKVQSLQDE 230
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 231 VAFLRSNheEEVADLLAQIQAShitverkdylkTDISTALKEIrSQLESHSDQNMHQAEEwfkcrYAKLTEAAEQNKEAI 310
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLGS-----------ESFSDFLDRL-SALSKIADADADLLEE-----LKADKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281185500 311 RSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELR 371
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
607-692 |
2.91e-03 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 40.44 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 607 VEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGK-SPVPKSPVEEKGKSPVPksPVEEKGKSPVSKSPVEEKAKSPVPKS 685
Cdd:PRK10819 71 VVEPEPEPEPIPEPPKEAPVVIPKPEPKPKPKPKpKPKPVKKVEEQPKREVK--PVEPRPASPFENTAPARPTSSTATAA 148
|
....*..
gi 281185500 686 PVEEAKS 692
Cdd:PRK10819 149 ASKPVTS 155
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-292 |
3.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 98 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 177
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 178 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVE 257
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190
....*....|....*....|....*....|....*.
gi 281185500 258 RKDYLKTDISTAL-KEIRSQLESHSDQNMHQAEEWF 292
Cdd:COG1196 471 EAALLEAALAELLeELAEAAARLLLLLEAEADYEGF 506
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
122-249 |
3.17e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQAshaqlgDAYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEarlrDDTEA 201
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQD------EASFERLAELRDELAE--------------LEEELEALKARWEAE----KELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 281185500 202 AIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEV-ADLLAQI 249
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVtEEDIAEV 520
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
100-366 |
4.40e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 100 NEKEQLQGLNDRFAGYieKVHYLEQQnKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEM-VNHEKAQVQLDSDHL 178
Cdd:pfam12128 248 QEFNTLESAELRLSHL--HFGYKSDE-TLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGeLSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 179 EedihrlkeRFEEEARLRDDTEAAIRAL--------RKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQ 250
Cdd:pfam12128 325 E--------ALEDQHGAFLDADIETAAAdqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 251 ASHITV-ERKDYLKTDISTALKEIRSQLESHSDQNMHQAEE----------WFKCRYAKLT------EAAEQNKEAIRSA 313
Cdd:pfam12128 397 DKLAKIrEARDRQLAVAEDDLQALESELREQLEAGKLEFNEeeyrlksrlgELKLRLNQATatpellLQLENFDERIERA 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 281185500 314 KEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQL 366
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
103-387 |
4.77e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 40.45 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 103 EQLQGLNDR----FAGYIEKVHYLEQQNKEIEaeiQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDhl 178
Cdd:pfam04108 24 EELVVLLAKiaflRRGLSVQLANLEKVREGLE---KVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 179 EEDIHRLKERFEEearlrDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSnheeevaDLLAQIQASHITVER 258
Cdd:pfam04108 99 EEKQKTLLDFIDE-----DSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQK-------ELESLSSPSESISLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 259 KDYLK--TDISTALKEIRSQLESHSDQnMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL----E 332
Cdd:pfam04108 167 PTLLKelESLEEEMASLLESLTNHYDQ-CVTAVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLqkllE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 281185500 333 SVRGTKESLERQLSDIEERHNHdLSSYQDTIQQLENELRGTKWEMARHLREYQDL 387
Cdd:pfam04108 246 QKNSLIDELLSALQLIAEIQSR-LPEYLAALKEFEERWEEEKETIEDYLSELEDL 299
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
122-354 |
7.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 122 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNhekaqvQLDSDHLEEDIHRLKERFE--EEAR----- 194
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLN------LLADETLADRVEEIREQLDeaEEAKrfvqq 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 195 --------------LRDDTEAaIRALRKDIEEASLVKVELDKKVQSLQDEVAflRSNH--EEEVADLLAQiqashiTVER 258
Cdd:PRK04863 916 hgnalaqlepivsvLQSDPEQ-FEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAHfsYEDAAEMLAK------NSDL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 259 KDYLKTDISTA---LKEIRSQLESHSDQnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEI----------AEYRRQLQ 325
Cdd:PRK04863 987 NEKLRQRLEQAeqeRTRAREQLRQAQAQ-LAQYNQ----VLASLKSSYDAKRQMLQELKQELqdlgvpadsgAEERARAR 1061
|
250 260 270
....*....|....*....|....*....|.
gi 281185500 326 SKSI--ELESVRGTKESLERQLSDIEERHNH 354
Cdd:PRK04863 1062 RDELhaRLSANRSRRNQLEKQLTFCEAEMDN 1092
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-279 |
8.59e-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: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281185500 149 AYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIE--EASLVKVELDKKVQS 226
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 281185500 227 LQDEVAFL---RSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLES 279
Cdd:COG1579 94 LQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
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