|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
76-385 |
1.49e-121 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 355.77 E-value: 1.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 76 NEKLAMQNLNDRLASYLEKVRSLEQSNSKLEAQIKQWYETNAPSTIRDYSSYYAQIKELQDQIKDAQIENARCVLQIDNA 155
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 156 KLAAEDFRLKFETERGMRITVEADLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRRQLG-NNVNVEV 234
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 235 DAAPGLNLGEIMNEMRQKYEILAQKNLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMK 314
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997589331 315 ESLERTLEETKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLEQEIATYRRLLEGED 385
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-413 |
5.67e-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: 64.69 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 173 RITVEADLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRRQLGNNVNVEvdaapglnlgEIMNEMRQK 252
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE----------AEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 253 YEILaqknlQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLERTLEETKARY---A 329
Cdd:TIGR02168 770 LEEA-----EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedlE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 330 SQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLEQEIATYRRLLE--GEDIKTTEYQLNTLEAKDIKKTRKI 407
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelSEELRELESKRSELRRELEELREKL 924
|
....*.
gi 1997589331 408 KTVVEE 413
Cdd:TIGR02168 925 AQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
129-420 |
5.35e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 129 AQIKELQDQIKDAQIENARCVLQIDNAKLAAEDFRLKFETERGMRITVEADLQGLSKVYDDLTLQKTDLEIQIEELNKDL 208
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 209 ALLKKEHQEEVEVLRRQLGNNVNVEVDAApGLNLGEIMNEMRQKYEILAQKNLQEAKEQFERQTQTLEKQVTVNIEELRG 288
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELE-EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 289 TEVQVTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKT 368
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1997589331 369 RLEQEIATYRRLLEGEDIKTTEYQLNTLEAKDIKKTRKIKTVVEEVVDGKVV 420
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
82-384 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 82 QNLNDRLASYLEKVRSLEQSNSKLEAQIkqwyetnaPSTIRDYSSYYAQIKELQDQIKDAQIENARCVLQIDNAKLAAED 161
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKEL--------EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 162 FRLKFETERGMRITVEADLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRRQLGNNVNVEVdaapglN 241
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER------R 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 242 LGEIMNEMRQKYEILAQknLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLERTL 321
Cdd:TIGR02168 840 LEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1997589331 322 EETKAryasQLAAIQEMLSSLEAQLMQIRsdtERQNQEYNILLDIKTRLEQEIATYRRLLEGE 384
Cdd:TIGR02168 918 EELRE----KLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-413 |
5.11e-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: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 176 VEADLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLKKEHQEEvEVLRRQLGNNVNVEVDAAPGLNLGEIMNEMRQKYEI 255
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 256 LAQKNLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASQLAAI 335
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1997589331 336 QEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLEQEIATYRRLLEGEDIKTTEYQLNTLEAKDIKKTRKIKTVVEE 413
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-414 |
7.50e-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: 54.68 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 158 AAEDFRLKFETERGMRITVEA-DLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLkkehQEEVEVLRRQLgNNVNVEVDA 236
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQEL----EEKLEELRLEV-SELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 237 APG--LNLGEIMNEMRQKYEILAQK--NLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLS 312
Cdd:TIGR02168 286 LQKelYALANEISRLEQQKQILRERlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 313 MKESLERTLEETKA---RYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLEQEIATYRRLLEGEDIKTT 389
Cdd:TIGR02168 366 ELEELESRLEELEEqleTLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260
....*....|....*....|....*
gi 1997589331 390 EYQLNTLEAKDIKKTRKIKTVVEEV 414
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREEL 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-351 |
7.82e-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: 54.69 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 82 QNLNDRLAsylEKVRSLEQSNSKLEAQIKQWY---ETNAPSTIRDYSSYYAQIKELQDQIKDAQIENARCVLQIDNAKLA 158
Cdd:TIGR02169 261 SELEKRLE---EIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 159 AEDFRLKFETERGMRITVEADLQGLSKVYDdltlqktDLEIQIEELNKDLALLKKEHQEEVEVLRRqlgnnvnvevdaap 238
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELE-------DLRAELEEVDKEFAETRDELKDYREKLEK-------------- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 239 glnLGEIMNEMRQKyeilaQKNLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLE 318
Cdd:TIGR02169 397 ---LKREINELKRE-----LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 1997589331 319 RTLEETKARYA---SQLAAIQEMLSSLEAQLMQIRS 351
Cdd:TIGR02169 469 QELYDLKEEYDrveKELSKLQRELAEAEAQARASEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-382 |
9.65e-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: 54.68 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 123 DYSSYYAQIKELQDQIKDAQIENARCVLQIDNAKLAAEDFRLKFETergmritVEADLQGLSKVYDDLTLQKTDLEIQIE 202
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 203 ELNKDLALLKKEHQEEVEVLRRQLGNNVNVEVDAApglNLGEIMNEMRQKYEILAQK--NLQEAKEQFERQTQTLEKQVT 280
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAEleELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 281 VNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESL-ERTLEETKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQE 359
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260
....*....|....*....|...
gi 1997589331 360 YNILLDIKTRLEQEIATYRRLLE 382
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELA 485
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-372 |
1.38e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 189 DLTLQKTDLEIQIEELNKDLALLKKEhQEEVEVLRRQLGNNVNVEVDAAPGLNLGEIMNEMRQKYEILAQKnLQEAKEQF 268
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAE-LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE-LAELSARY 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 269 ER---QTQTLEKQVTVNIEELRgtevqvTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASqlaaiqemLSSLEAQ 345
Cdd:COG3206 287 TPnhpDVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAE 352
|
170 180
....*....|....*....|....*..
gi 1997589331 346 LMQIRSDTERQNQEYNILLdikTRLEQ 372
Cdd:COG3206 353 LRRLEREVEVARELYESLL---QRLEE 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-349 |
7.85e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 78 KLAMQNLNDRLASYLEKVRSLEQSNSKLEAQIKQwYETNAPSTIRDYSSYYAQIKELQDQIKDAQIENARCVLQIDNAKL 157
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 158 AAEDFRLKFETERgmritveadlqglsKVYDDLTLQKTDLEIQIEELNKDLALLKKE---HQEEVEVLRRQLgNNVNVEV 234
Cdd:TIGR02168 352 ELESLEAELEELE--------------AELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARL-ERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 235 DaapglNLGEIMNEMRQKYEILAQKNLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMK 314
Cdd:TIGR02168 417 E-----RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
250 260 270
....*....|....*....|....*....|....*..
gi 1997589331 315 ESLERTLE--ETKARYASQLAAIQEMLSSLEAQLMQI 349
Cdd:TIGR02168 492 DSLERLQEnlEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-350 |
1.52e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 114 ETNAPSTIRDYSSYYAQIKELQDQIKDAQienaRCVLQIDNAKLAAEDFRLKFETERGMRITVEA-DLQGLSKVYDDLTL 192
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAR----EQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 193 QKTDLEIQIEELNKDLALLKKEH---QEEVEVLRRQLgnnvnvevDAAPGLNLGEIMNEMRQKYEILAQKnlQEAKEQFE 269
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLdalREELDELEAQI--------RGNGGDRLEQLEREIERLERELEER--ERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 270 RQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASQLAAIQEMLSSLEAQLMQI 349
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
.
gi 1997589331 350 R 350
Cdd:COG4913 446 R 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-388 |
1.71e-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: 46.68 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 135 QDQIKDAQIENARCVLQIDNAKLAAEDFRLKFETERGMRITVEADLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLKKE 214
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 215 HQEEVEVLRRQLgnNVNVEVDAAPGLNLgeimnemrqkyeILAQKNLQEAKEQFERqTQTLEKQVTVNIEELRGTEVQVT 294
Cdd:COG4942 99 LEAQKEELAELL--RALYRLGRQPPLAL------------LLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 295 ELRRsyqtleiELQSQLSMKESLERTLEETKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLEQEI 374
Cdd:COG4942 164 ALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....
gi 1997589331 375 ATYRRLLEGEDIKT 388
Cdd:COG4942 237 AAAAERTPAAGFAA 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
197-382 |
3.45e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 197 LEIQIEELNKDLAllkkEHQEEVEVLRRQlgnNVNVEVDAAPGLNLGEImNEMRQKYEiLAQKNLQEAKEQFERQTQTLE 276
Cdd:COG3206 180 LEEQLPELRKELE----EAEAALEEFRQK---NGLVDLSEEAKLLLQQL-SELESQLA-EARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 277 KQVTVNIEELRGTEVQvtELRRSYQTLEIELQSQLS-----------MKESLERTLEETKARYASQLAAIQEMLSSLEAQ 345
Cdd:COG3206 251 SGPDALPELLQSPVIQ--QLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1997589331 346 LMQIRSDTERQNQEYNILLDIK---TRLEQEIATYRRLLE 382
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
129-375 |
6.01e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 129 AQIKELQDQIKDAQIENARCVLQID--NAKLAAEDFRLKFETERGMRITVEADLQGLSKVyDDLTLQKTDLEIQIEELNK 206
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISelEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 207 DLALLKKEHQ----------EEVEVLRRQLGNnVNVEVDAapglnLGEIMNEMRQKYEILAQKnLQE----AKEQFERQT 272
Cdd:TIGR02169 316 ELEDAEERLAkleaeidkllAEIEELEREIEE-ERKRRDK-----LTEEYAELKEELEDLRAE-LEEvdkeFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 273 QTLEK--QVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASQLAAIQEMLSSLEAQLMQIR 350
Cdd:TIGR02169 389 DYREKleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260
....*....|....*....|....*
gi 1997589331 351 SDTERQNQEYNILLDIKTRLEQEIA 375
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-319 |
6.28e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 75 GNEKLAMQNLNDRLASylEKVRSLEQSNSKLEAQIKQW----YETNAPSTIRDYSSYYAQ--IKELQDQIKDAQIENARC 148
Cdd:TIGR02169 775 HKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIearlREIEQKLNRLTLEKEYLEkeIQELQEQRIDLKEQIKSI 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 149 VLQIDNAKLAAEDFRLKFETERGMRITVEADLQGLSKVYDDLTLQKTDLEIQIEELNKDLAlLKKEHQEEVEVlRRQLGN 228
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRLSELKA-KLEALE 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 229 NVNVEVDAAPGLNLGEIMNEMrqkyeilAQKNLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQ 308
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIPEEEL-------SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
250
....*....|.
gi 1997589331 309 SQLSMKESLER 319
Cdd:TIGR02169 1004 AILERIEEYEK 1014
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
80-336 |
1.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 80 AMQNLNDRLASYLEKVRSLEQsnsKLEaQIKQwyETNAPSTIRDYSSYYAQIKELQDQIKDAQIENArcvlqidnaklAA 159
Cdd:COG3206 176 ALEFLEEQLPELRKELEEAEA---ALE-EFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAELA-----------EA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 160 EDFRLKFETERGMRITVEADLQGlSKVYDDLTLQKTDLEIQIEELnkdLALLKKEH------QEEVEVLRRQLGNNVNve 233
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAEL---SARYTPNHpdvialRAQIAALRAQLQQEAQ-- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 234 vdaapglnlgEIMNEMRQKYEILaQKNLQEAKEQFERQTQtlekqvtvNIEELRGTEVQVTELRRSYQTLEielqsqlSM 313
Cdd:COG3206 313 ----------RILASLEAELEAL-QAREASLQAQLAQLEA--------RLAELPELEAELRRLEREVEVAR-------EL 366
|
250 260
....*....|....*....|...
gi 1997589331 314 KESLERTLEETKARYASQLAAIQ 336
Cdd:COG3206 367 YESLLQRLEEARLAEALTVGNVR 389
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
292-422 |
2.46e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 292 QVTELRRSYQTLEIElqsqlsmKESLERtleETKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLE 371
Cdd:COG0542 412 ELDELERRLEQLEIE-------KEALKK---EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1997589331 372 QeiatyrrllEGEDIKTTEYQLNTLEAKDIKKTRKIKTVVEEVVDGKVVSS 422
Cdd:COG0542 482 Q---------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSR 523
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
135-374 |
2.76e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 135 QDQIKDAQIENARCVLQIDNAKLAAEDFRLKFETERGMRITVEADLQGLS-KVYDDLTLQKTDLEIQIEELNKDLALLKK 213
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 214 EHQEEVEVLRRQLGNNvNVEVDAAPGLNLGEIMNEMRQ-KYEILA-QKNLQEAKEQFERQTQTLEKQVTVNIEELRGTEV 291
Cdd:pfam12128 697 KHQAWLEEQKEQKREA-RTEKQAYWQVVEGALDAQLALlKAAIAArRSGAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 292 QVTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEYNILLDIKTRLE 371
Cdd:pfam12128 776 EIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
...
gi 1997589331 372 QEI 374
Cdd:pfam12128 856 VRL 858
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
193-431 |
3.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 193 QKTDLEIQIEELNKDLALLKK---EHQEEVEVLRRQLGNNVNVEVDAAPGLNLGEIMNEMRQKYEILAQ--------KNL 261
Cdd:COG4913 611 KLAALEAELAELEEELAEAEErleALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldassddlAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 262 QEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKESLERTLEETKARYASQLAAIQEMLSS 341
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 342 LEAQLMQIRSDTERQNQE-YNILLDIKTRLEQEIATYRRLLEGEDikttEYQ--LNTLEAKDI-KKTRKIKTVVEEVVDG 417
Cdd:COG4913 771 LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLP----EYLalLDRLEEDGLpEYEERFKELLNENSIE 846
|
250 260
....*....|....*....|
gi 1997589331 418 KV------VSSEVKEIEENI 431
Cdd:COG4913 847 FVadllskLRRAIREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-359 |
3.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 155 AKLAAEDFRLKFETERGMRITVEADLQGLSKVYDDLTLqKTDLEIQIEELNKdlallKKEHQEEVEVLRRQlgnnvnvev 234
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLRE-----KREALAELNDERRE--------- 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 235 daapglNLGEIMNEMRQKYEILAQKNLQEAKEQFERQTQTLEkQVTVNIEELRGtevQVTELRRSYQTLEIELQSQLSMK 314
Cdd:PRK02224 628 ------RLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE-QVEEKLDELRE---ERDDLQAEIGAVENELEELEELR 697
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1997589331 315 ESLERtLEETKARyasqLAAIQEMLSSLEAQLMQIRSDTERQNQE 359
Cdd:PRK02224 698 ERREA-LENRVEA----LEALYDEAEELESMYGDLRAELRQRNVE 737
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
256-386 |
5.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 256 LAQKNLQEA------KEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELQSQLSMKEsLERTLEETKarya 329
Cdd:PRK11281 60 LVQQDLEQTlalldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ-LESRLAQTL---- 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1997589331 330 SQLAAIQEMLSSLEAQLMQIRSDTER-QNQEYNILldikTRLeQEIatyRRLLEGEDI 386
Cdd:PRK11281 135 DQLQNAQNDLAEYNSQLVSLQTQPERaQAALYANS----QRL-QQI---RNLLKGGKV 184
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-413 |
7.37e-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: 38.21 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 242 LGEIMNEMRQKYEILAQknLQEAKEQFERQTQTLEKQVTVNIEELRGTEVQVTELRRSYQTLEIELqsqlsmkESLERTL 321
Cdd:COG4942 29 LEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-------AELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 322 EETKARYASQLAAIQEM------------------------------------------LSSLEAQLMQIRSDTERQNQE 359
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllspedfldavrrlqylkylaparreqaeelradLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997589331 360 YNILLDIKTRLEQEIATYRRLLEG--EDIKTTEYQLNTLEAKDIKKTRKIKTVVEE 413
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
86-381 |
7.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 86 DRLASYLEKVRSLEQSNSKLEAQIKQWyeTNAPSTIRDYSSYYAQIKELQDQIKD-AQIENARCVLQIDNAKLAAEDfrl 164
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEAL--EAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASS--- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 165 kfetergmritveADLQGLSKVYDDLTLQKTDLEIQIEELNKDLALLKKEH---QEEVEVLRRQLGNNVNvEVDAAPGLN 241
Cdd:COG4913 685 -------------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELeqaEEELDELQDRLEAAED-LARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 242 LGEimnemrQKYEILAQKNLQEAKEQFERQTQTLEkqvtvniEELRGTEVQVTELRRSY--------QTLEIELQSQ--- 310
Cdd:COG4913 751 LEE------RFAAALGDAVERELRENLEERIDALR-------ARLNRAEEELERAMRAFnrewpaetADLDADLESLpey 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589331 311 LSMKESLERT-LEETKARYASQL--AAIQEM---LSSLEAQLMQIRSDTERQNQ-----EYN----ILLDIKTRLEQEIA 375
Cdd:COG4913 818 LALLDRLEEDgLPEYEERFKELLneNSIEFVadlLSKLRRAIREIKERIDPLNDslkriPFGpgryLRLEARPRPDPEVR 897
|
....*.
gi 1997589331 376 TYRRLL 381
Cdd:COG4913 898 EFRQEL 903
|
|
| |
