|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
79-390 |
5.99e-145 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 413.93 E-value: 5.99e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 79 NEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNA 158
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 159 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVG-GQVSVEV 237
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 238 DSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189055338 318 AALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-395 |
1.27e-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: 60.07 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 130 YYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKE 209
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 210 ELAYL----------------KKNHEEEISTLRGQVGGQVSVEVDSapgtdLAKILSDMRSQYEVMAEQNRKDAEAWfts 273
Cdd:TIGR02168 310 RLANLerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEELEEQL--- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 274 rtEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETE-ARFGAQLAHIQALISGIEAQLGDV 352
Cdd:TIGR02168 382 --ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 189055338 353 RADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLS 395
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-385 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 186 LRRVLDELTLARTDLEMQIEGLKEELAylkkNHEEEISTLRGQVGGqVSVEVDsapGTDLAKILSDMRSQYeVMAEQNRK 265
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEE---AKLLLQQLSELESQL-AEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 266 DAEAWFTSRTEELNREVAGHTEQLQMSrsEVTDLRRTLQGLEIELQSQLS-----------MKAALEDTLAETEARFGAQ 334
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 189055338 335 LAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIK---SRLEQEIATYRSLLE 385
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
276-389 |
4.55e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 276 EELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAE------------------------TEARF 331
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAElagagaaaegragelaqeldsekqVSARA 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189055338 332 GAQLAHIQALISGIEAQLGDVRA---DSERQNQEYQ-RLMDIKSRLE-------QEIATYRS--------LLEGQED 389
Cdd:PRK09039 136 LAQVELLNQQIAALRRQLAALEAaldASEKRDRESQaKIADLGRRLNvalaqrvQELNRYRSeffgrlreILGDREG 212
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
79-390 |
5.99e-145 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 413.93 E-value: 5.99e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 79 NEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNA 158
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 159 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVG-GQVSVEV 237
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 238 DSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189055338 318 AALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-395 |
1.27e-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: 60.07 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 130 YYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKE 209
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 210 ELAYL----------------KKNHEEEISTLRGQVGGQVSVEVDSapgtdLAKILSDMRSQYEVMAEQNRKDAEAWfts 273
Cdd:TIGR02168 310 RLANLerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEELEEQL--- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 274 rtEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETE-ARFGAQLAHIQALISGIEAQLGDV 352
Cdd:TIGR02168 382 --ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 189055338 353 RADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLS 395
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-387 |
3.88e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 132 TTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEEL 211
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 212 AYLKKNH---EEEISTLRGQVGGQVS-VEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRT--EELNREVAGH 285
Cdd:TIGR02168 799 KALREALdelRAELTLLNEEAANLRErLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEliEELESELEAL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 286 TEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEarfgAQLAHIQALISGIEAQLGDVRadsERQNQEYQR 365
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQ---ERLSEEYSL 951
|
250 260
....*....|....*....|..
gi 189055338 366 LMDIKSRLEQEIATYRSLLEGQ 387
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-378 |
2.69e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 137 LRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKK 216
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 217 NHEEEISTLRgqvggqvsvevdsapgtdlakilsdmRSQYEVMAEQNRKDAeawFTSRTEELNREVAGHTEQLQMSRSEV 296
Cdd:TIGR02169 372 ELEEVDKEFA--------------------------ETRDELKDYREKLEK---LKREINELKRELDRLQEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 297 TDLRRTLQGLEielQSQLSMKAALEDTLAETEArfgaqlahIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQE 376
Cdd:TIGR02169 423 ADLNAAIAGIE---AKINELEEEKEDKALEIKK--------QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
..
gi 189055338 377 IA 378
Cdd:TIGR02169 492 LA 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-385 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 186 LRRVLDELTLARTDLEMQIEGLKEELAylkkNHEEEISTLRGQVGGqVSVEVDsapGTDLAKILSDMRSQYeVMAEQNRK 265
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEE---AKLLLQQLSELESQL-AEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 266 DAEAWFTSRTEELNREVAGHTEQLQMSrsEVTDLRRTLQGLEIELQSQLS-----------MKAALEDTLAETEARFGAQ 334
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 189055338 335 LAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIK---SRLEQEIATYRSLLE 385
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-388 |
4.01e-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: 42.75 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 178 SVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEE---EISTLRGQVGgQVSVEVDSapgtdLAKILSDMRS 254
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRD-KLTEEYAE-----LKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 255 QyevmAEQNRKDAEAWFtsrteelnREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEAR---F 331
Cdd:TIGR02169 372 E----LEEVDKEFAETR--------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 189055338 332 GAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQE 388
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
80-379 |
4.34e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 80 EKLTMQN----LNDRLASYLDKVRALEAANGEL-------EVKIRDWYQKQGPGpsRDYSHYYTTIQDLRDKILGATIEN 148
Cdd:pfam15921 487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQHLKNEG--DHLRNVQTECEALKLQMAEKDKVI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 149 SRIVLQIDN-ARLAADDFRTKfETEQALRMSVEADINGLRRVLDELTLART-------DLEMQIEGLKEELAYLKKNHEE 220
Cdd:pfam15921 565 EILRQQIENmTQLVGQHGRTA-GAMQVEKAQLEKEINDRRLELQEFKILKDkkdakirELEARVSDLELEKVKLVNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 221 EISTLRG--QVGGQVSVEVDSAPGTdlakiLSDMRSQYEVMAEQnrkdaeawFTSRTEELNREVAGHTEQLQMSRSEVTD 298
Cdd:pfam15921 644 RLRAVKDikQERDQLLNEVKTSRNE-----LNSLSEDYEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 299 LRRTLQGLeiELQSQLSMKAALEDTLAETEARfgAQLAHIQALISGIEAQLGDVradserqNQEYQRLMDIKSRLEQEIA 378
Cdd:pfam15921 711 TRNTLKSM--EGSDGHAMKVAMGMQKQITAKR--GQIDALQSKIQFLEEAMTNA-------NKEKHFLKEEKNKLSQELS 779
|
.
gi 189055338 379 T 379
Cdd:pfam15921 780 T 780
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
276-389 |
4.55e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 276 EELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAE------------------------TEARF 331
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAElagagaaaegragelaqeldsekqVSARA 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189055338 332 GAQLAHIQALISGIEAQLGDVRA---DSERQNQEYQ-RLMDIKSRLE-------QEIATYRS--------LLEGQED 389
Cdd:PRK09039 136 LAQVELLNQQIAALRRQLAALEAaldASEKRDRESQaKIADLGRRLNvalaqrvQELNRYRSeffgrlreILGDREG 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-390 |
5.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 179 VEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEvdsapgTDLAKILSDMRSQYEV 258
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL------AELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 259 MAEQNRKDAEAwfTSRTEELNREVAGHTEQLQMSRSEVTDL---RRTLQGLEIELQSQLSMKAALEDTLAETEARFGAQL 335
Cdd:COG1196 311 RRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 189055338 336 AHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-382 |
6.48e-04 |
|
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: 41.67 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 154 QIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLkknhEEEISTLRGQVGGQV 233
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL----RAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 234 SVevdsapgtdlakiLSDMRSQYEVMAEQNRKDAEAWFTSRT--EELNREVAGHTEQLQMSRSEVTDLRRtlqgleiELQ 311
Cdd:COG4942 111 RA-------------LYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRA-------ELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189055338 312 SQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRS 382
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
154-364 |
2.51e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 154 QIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLkknhEEEISTLRGQVGGQV 233
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 234 -SVEVDSAPGTDLAKIL-----SDMRSQYEVMAEQNRKDAEAwfTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLE 307
Cdd:COG3883 93 rALYRSGGSVSYLDVLLgsesfSDFLDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 189055338 308 IELQSQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQ 364
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
137-380 |
7.82e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.46 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 137 LRDKILGATIENSRIVLQIDNA--RLAAddfRTKFETEQalRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYL 214
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEEQ--RKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 215 KKNHEEEISTLrgqvggqvsvevdSAPGTDLAKILSDMRS--QYEVMAE---------QNRKDAEAWFTSRTEELN---- 279
Cdd:PHA02562 247 VMDIEDPSAAL-------------NKLNTAAAKIKSKIEQfqKVIKMYEkggvcptctQQISEGPDRITKIKDKLKelqh 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055338 280 --REVAGHTEQLQMSRSEVTDLRRTLQgleiELQSQLSmkaaledTLAETEARFGAQLAHIQALISGIEAQLGDVRADSE 357
Cdd:PHA02562 314 slEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKIS-------TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250 260
....*....|....*....|...
gi 189055338 358 RQNQEYQRLMDIKSRLEQEIATY 380
Cdd:PHA02562 383 KLQDELDKIVKTKSELVKEKYHR 405
|
|
|