|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
104-423 |
5.83e-140 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 402.76 E-value: 5.83e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 104 NEKITMQNLNDRLASYLDKVRALEEANADLEVKIHDWYQKQTPtSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDN 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 184 ARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwvppilqEMKEFSSQLA 263
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEE-------EVRELQAQVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 264 -GQVNVEMDAAPGVDLTRVLAEMREQYEAMAEKNRRDVEAWFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIE 342
Cdd:pfam00038 153 dTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 343 LQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDA 422
Cdd:pfam00038 233 LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEEC 312
|
.
gi 1034599643 423 K 423
Cdd:pfam00038 313 R 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-427 |
6.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 122 KVRALEEANADLEVKIHDWYQKQTptSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDNARLAADDFRLKYENELAL 201
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELE--ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 202 RQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHeewvppilqemKEFSSQLagqvnvemdaapgvDLTRV 281
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-----------DELRAEL--------------TLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 282 LAEMREQYEAMAEKNRRDVEAWFfsktEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETE 361
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRL----EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 362 CRYATQLQQIQGL---IGGLEAQLSELRCEMEA-QNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGI 427
Cdd:TIGR02168 894 SELEELSEELRELeskRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-432 |
5.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 148 SPECDYSQYFKTIEELRDKIMATTIDNSRVIlEI----DNARLAAddfrlKYENELA---LRQGVEADINGLRRVLDELT 220
Cdd:COG3206 108 DPLGEEASREAAIERLRKNLTVEPVKGSNVI-EIsytsPDPELAA-----AVANALAeayLEQNLELRREEARKALEFLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 221 LARTDLEMQIEGLNEELAYLKKNH-----EEWVPPILQEMKEFSSQLAgqvnvemdaapgvDLTRVLAEMREQYEAMAEK 295
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLA-------------EARAELAEAEARLAALRAQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 296 NRRDVEAwffskteelnKEVASNTEMIQTSKTEITDLRRTMQELE----------IELQSQL-SMKAGLENSLAETECRY 364
Cdd:COG3206 249 LGSGPDA----------LPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIaALRAQLQQEAQRILASL 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034599643 365 ATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLdiktRLEQEIATYRSLLEGQDAKMAGIAIREA 432
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
306-422 |
3.46e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 306 SKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAgLENSLAETEcryaTQLQQIQGLIGGLEAQLSEL 385
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ-LESRLAQTL----DQLQNAQNDLAEYNSQLVSL 154
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034599643 386 RCEME-AQNQEYKMLldikTRLeQEIatyRSLLEGQDA 422
Cdd:PRK11281 155 QTQPErAQAALYANS----QRL-QQI---RNLLKGGKV 184
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
104-423 |
5.83e-140 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 402.76 E-value: 5.83e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 104 NEKITMQNLNDRLASYLDKVRALEEANADLEVKIHDWYQKQTPtSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDN 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 184 ARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwvppilqEMKEFSSQLA 263
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEE-------EVRELQAQVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 264 -GQVNVEMDAAPGVDLTRVLAEMREQYEAMAEKNRRDVEAWFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIE 342
Cdd:pfam00038 153 dTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 343 LQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDA 422
Cdd:pfam00038 233 LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEEC 312
|
.
gi 1034599643 423 K 423
Cdd:pfam00038 313 R 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-427 |
6.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 122 KVRALEEANADLEVKIHDWYQKQTptSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDNARLAADDFRLKYENELAL 201
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELE--ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 202 RQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHeewvppilqemKEFSSQLagqvnvemdaapgvDLTRV 281
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-----------DELRAEL--------------TLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 282 LAEMREQYEAMAEKNRRDVEAWFfsktEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETE 361
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRL----EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 362 CRYATQLQQIQGL---IGGLEAQLSELRCEMEA-QNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGI 427
Cdd:TIGR02168 894 SELEELSEELRELeskRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-432 |
4.75e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 194 KYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEEL----AYLKKNHEEWVPPILQEMKEFSSQLAGQVNVE 269
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 270 MDAApgvDLTRVLAEMREQYEAMAEKNRRDVEAwFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIE------- 342
Cdd:TIGR02169 311 AEKE---RELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrde 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 343 ---LQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLS--------------ELRCEMEAQNQEYKMLLDIKTR 405
Cdd:TIGR02169 387 lkdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgieakineleeekeDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270
....*....|....*....|....*....|.
gi 1034599643 406 LEQEI----ATYRSLLEGQDAKMAGIAIREA 432
Cdd:TIGR02169 467 YEQELydlkEEYDRVEKELSKLQRELAEAEA 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-432 |
5.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 148 SPECDYSQYFKTIEELRDKIMATTIDNSRVIlEI----DNARLAAddfrlKYENELA---LRQGVEADINGLRRVLDELT 220
Cdd:COG3206 108 DPLGEEASREAAIERLRKNLTVEPVKGSNVI-EIsytsPDPELAA-----AVANALAeayLEQNLELRREEARKALEFLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 221 LARTDLEMQIEGLNEELAYLKKNH-----EEWVPPILQEMKEFSSQLAgqvnvemdaapgvDLTRVLAEMREQYEAMAEK 295
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLA-------------EARAELAEAEARLAALRAQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 296 NRRDVEAwffskteelnKEVASNTEMIQTSKTEITDLRRTMQELE----------IELQSQL-SMKAGLENSLAETECRY 364
Cdd:COG3206 249 LGSGPDA----------LPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIaALRAQLQQEAQRILASL 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034599643 365 ATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLdiktRLEQEIATYRSLLEGQDAKMAGIAIREA 432
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-392 |
8.16e-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: 44.75 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 180 EIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEWVPPILQEMKE-F 258
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 259 SSQLAGQVNVEMDAAPGVDLTRVLAEMREQYEAMAEKnrrdveawffskTEELN---KEVASNTEMIQTSKTEITDLRRT 335
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------------AEELRadlAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034599643 336 MQELEIELQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQ 392
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-433 |
1.31e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 180 EIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEWVPPILQEMKEFS 259
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 260 SQLAGQVNVEMDAAPGVDLTRVLAEMREQYEAMAEKNRRDVEAW------FFSKTEELNKEVASNTEMIQTSKTEITDLR 333
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealdeLRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 334 RTMQELE---IELQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEI 410
Cdd:TIGR02168 838 RRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260
....*....|....*....|...
gi 1034599643 411 ATYRSLLEGQDAKMAGIAIREAY 433
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
186-432 |
2.37e-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: 43.21 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 186 LAADDFRLKYENELalrQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwvppILQEMKEFSSQLAgQ 265
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELA-E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 266 VNVEMDAapgvdLTRVLAEMREQYEAM---AEKNRRDVEAWFFSKTEELNKEVASNT---EMIQTSKTEITDLRRTMQEL 339
Cdd:COG4942 88 LEKEIAE-----LRAELEAQKEELAELlraLYRLGRQPPLALLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 340 EIELQSQLSMKAGLENSLAETEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKmlldiktRLEQEIATYRSLLEG 419
Cdd:COG4942 163 AALRAELEAERAELEALLAELE----EERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIAR 231
|
250
....*....|...
gi 1034599643 420 QDAKMAGIAIREA 432
Cdd:COG4942 232 LEAEAAAAAERTP 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-426 |
1.02e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 105 EKITMQN----LNDRLASYLDKVRALEEANADL-------EVKIHDWYQKQTP------TSPECD-----YSQYFKTIEE 162
Cdd:pfam15921 487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQHLKNEgdhlrnVQTECEalklqMAEKDKVIEI 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 163 LRDKIM--------------ATTIDNSRVILEIDNARLAADDFRLkyenelaLRQGVEADINGLRRVLDELTLARTDLem 228
Cdd:pfam15921 567 LRQQIEnmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKI-------LKDKKDAKIRELEARVSDLELEKVKL-- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 229 qIEGLNEELAYLKknheewvppilqEMKEFSSQLAGQVNVEMDAapgvdltrvLAEMREQYEAMAEKnrrdveawFFSKT 308
Cdd:pfam15921 638 -VNAGSERLRAVK------------DIKQERDQLLNEVKTSRNE---------LNSLSEDYEVLKRN--------FRNKS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 309 EELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENslaetecryatQLQQIQGLIGGLEAQLSELRCE 388
Cdd:pfam15921 688 EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK-----------QITAKRGQIDALQSKIQFLEEA 756
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034599643 389 MEAQNQEYKMLLDIKTRLEQEIATYRSllegQDAKMAG 426
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVAT----EKNKMAG 790
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
206-434 |
2.66e-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: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 206 EADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwvppILQEMKEfssqlagqVNVEMDAApGVDLTRVLAEM 285
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEA--------LQAEIDKL-QAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 286 REQYEAMAE------KNRRDVEAW-----------FFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLS 348
Cdd:COG3883 82 EERREELGEraralyRSGGSVSYLdvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 349 MKAGLENSLAETEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGIA 428
Cdd:COG3883 162 LKAELEAAKAELE----AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*.
gi 1034599643 429 IREAYS 434
Cdd:COG3883 238 AAAAAA 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-432 |
2.88e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 193 LKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwvppiLQEmkEFSSQLAGQVNVEMDA 272
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-----AQA--EEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 273 APGVDLTRVLAEMREQYEAMAEKNRRDVEAwFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAG 352
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 353 LENSLAETEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGIAIREA 432
Cdd:COG1196 384 LAEELLEAL----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
306-422 |
3.46e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 306 SKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAgLENSLAETEcryaTQLQQIQGLIGGLEAQLSEL 385
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ-LESRLAQTL----DQLQNAQNDLAEYNSQLVSL 154
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034599643 386 RCEME-AQNQEYKMLldikTRLeQEIatyRSLLEGQDA 422
Cdd:PRK11281 155 QTQPErAQAALYANS----QRL-QQI---RNLLKGGKV 184
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
158-431 |
5.27e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 158 KTIEELRDKIMATTidnsrviLEIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEEL 237
Cdd:COG1196 267 AELEELRLELEELE-------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 238 AYLKKNHEEWVPPILQEMKEFSSQLAGQVNVEMDAAPGVD--LTRVLAEMREQYEAMAEKNRRDVEAwffSKTEELNKEV 315
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEelEELAEELLEALRAAAELAAQLEELE---EAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 316 ASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETECRYATQLQQIQgligGLEAQLSELRCEMEAQNQE 395
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA----LLEAALAELLEELAEAAAR 492
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034599643 396 YKMLLDIKTRLEQEIATYRSLLEGQDAKMAGIAIRE 431
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-392 |
8.92e-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: 37.60 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 203 QGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwvppILQEMKEFSSQLAgqvnvemdaapgvDLTRVL 282
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIE-------------EVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 283 AEMREQyeAMAEKNRRDVEAwffskteeLNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETEC 362
Cdd:COG1579 76 KKYEEQ--LGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190
....*....|....*....|....*....|
gi 1034599643 363 RYATQLQQIQGLIGGLEAQLSELRCEMEAQ 392
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
200-421 |
9.99e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 200 ALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEwVPPILQEMKEFSSQLagQVNVEMDAAPGVDLT 279
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK-LKERLEELEEDLSSL--EQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599643 280 RVLAEMREQY----EAMAEKNRRDVEawffSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLEN 355
Cdd:TIGR02169 765 ARIEELEEDLhkleEALNDLEARLSH----SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034599643 356 SLAETECRYATQLQQIQGLIGGLEAQLSELRcEMEAQNQEY-KMLLDIKTRLEQEIATYRSLLEGQD 421
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELE-ELEAALRDLeSRLGDLKKERDELEAQLRELERKIE 906
|
|
|