|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
82-368 |
6.31e-17 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 81.12 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038 4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 151 IRLVKQKlfkvtkecvaYQYQLECRQQDVAQFADFREV----------LTTRATQLSEELAQLRDAYQKQKEQLRQQL-- 218
Cdd:pfam00038 84 AEDFRQK----------YEDELNLRTSAENDLVGLRKDldeatlarvdLEAKIESLKEELAFLKKNHEEEVRELQAQVsd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 219 -------EAPPSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQ 291
Cdd:pfam00038 154 tqvnvemDAARKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLE 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370454671 292 AEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:pfam00038 231 IELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-359 |
2.53e-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: 66.23 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 96 QAVAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYklhAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 175
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEK-ALAELRKELEELEEEL---EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 176 QQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 255
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 256 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 335
Cdd:TIGR02168 827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260
....*....|....*....|....
gi 1370454671 336 LRNGVQLQQQKNKEMEQLRLSLAE 359
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQ 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-368 |
4.64e-09 |
|
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: 57.85 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 131 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFREVLTTRATQLSEELAQL 203
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 204 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 283
Cdd:COG4942 96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 284 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1370454671 364 YKAML 368
Cdd:COG4942 251 LKGKL 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-368 |
4.89e-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: 58.91 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 83 DLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREpalqEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVT 162
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 163 KECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFEN 242
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAE-----LEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 243 LMAESRQDLEEEYEPQFLRLLErkeagtkaLQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKR-DEEVQQ 321
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEE 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370454671 322 YREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-328 |
9.86e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 76 EENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHelvllrepaLQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVK 155
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEL---------LEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 156 QKLfkvtkecvaYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQ----KQKEQLRQQLEAPPSQRDghflq 231
Cdd:COG4913 290 LEL---------LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE----- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 232 ESRRLSAQFENLMAesRQDLEEEYEPQflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALV 311
Cdd:COG4913 356 ERERRRARLEALLA--ALGLPLPASAE--EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
250 260
....*....|....*....|
gi 1370454671 312 RQKR---DEEVQQYREQLEE 328
Cdd:COG4913 432 ERRKsniPARLLALRDALAE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-363 |
2.17e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 135 KLHAQAE--LERDGLREEIRLVKQKLfkvtkecvaYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLrdayQKQKE 212
Cdd:COG1196 204 PLERQAEkaERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAEL----EAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 213 QLRQQLEAppsqrdghFLQESRRLSAQFENLMAEsrqdlEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA 292
Cdd:COG1196 271 ELRLELEE--------LELELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370454671 293 EARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-364 |
5.61e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 141 ELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDA-------------- 206
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienvkselkelear 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 207 ---YQKQKEQLRQQLEAPPSQRDGHFLQES-----------RRLSAQFENLMAE-SRQDLEEEYEPQFLRLLERKEAGTK 271
Cdd:TIGR02169 767 ieeLEEDLHKLEEALNDLEARLSHSRIPEIqaelskleeevSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 272 ALQRT-QAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYReqleEMEERQRQLRNGVQLQQQKNKEM 350
Cdd:TIGR02169 847 EQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR----ELERKIEELEAQIEKKRKRLSEL 922
|
250
....*....|....
gi 1370454671 351 EQLRLSLAEELSTY 364
Cdd:TIGR02169 923 KAKLEALEEELSEI 936
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
138-358 |
3.82e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 138 AQAELERDGLREEIRLVKQKLFKVTKECVAYQyqlecRQQDVAQFADFREVLTTRATQLSEELAQLRDAY---QKQKEQL 214
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 215 RQQL----EAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYePQFLRLLERKEAGTKALQrtqaeiQEMKEALRPL 290
Cdd:COG3206 246 RAQLgsgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNH-PDVIALRAQIAALRAQLQ------QEAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370454671 291 QAEARQLRLQNRNLEDQIALVRQKrdeeVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 358
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-354 |
1.15e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 190 TTRATQLSEELAQL-RDAYQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFENLMAESRQDLEEeYEPQFLRLLERKEA 268
Cdd:TIGR02168 212 AERYKELKAELRELeLALLVLRLEELREELEELQEE-----LKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 269 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEevqqYREQLEEMEERQRQLRNGVQLQQQKNK 348
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE----LAEELAELEEKLEELKEELESLEAELE 361
|
....*.
gi 1370454671 349 EMEQLR 354
Cdd:TIGR02168 362 ELEAEL 367
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
73-368 |
1.45e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 73 PSMEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 152
Cdd:PRK10929 96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 153 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFREVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 227
Cdd:PRK10929 160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 228 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 297
Cdd:PRK10929 234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 298 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRngvQLQQQKNKEM--EQLRLsLAEELSTY 364
Cdd:PRK10929 313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLR---QIRQADGQPLtaEQNRI-LDAQLRTQ 388
|
....
gi 1370454671 365 KAML 368
Cdd:PRK10929 389 RELL 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-332 |
2.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 98 VAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQ 177
Cdd:COG4913 663 VASAEREIAELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 178 DVAQF------ADFREVLTTRAT-QLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLSA------QFENLM 244
Cdd:COG4913 742 LARLElralleERFAAALGDAVErELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdleslpEYLALL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 245 AESRQDLEEEYEPQFLRLLERKEAGTKA--LQRTQAEIQEMKEALRPLQAEARQLRLqnrNLEDQIAL-VRQKRDEEVQQ 321
Cdd:COG4913 822 DRLEEDGLPEYEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDPLNDSLKRIPF---GPGRYLRLeARPRPDPEVRE 898
|
250
....*....|.
gi 1370454671 322 YREQLEEMEER 332
Cdd:COG4913 899 FRQELRAVTSG 909
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-382 |
2.67e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 101 LEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTK--------ECVAYQYQL 172
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 173 ECRQQDVAQFADFREVLTTRATQLSEELAQL---RDAYQKQKEQLRQQLEAPPSQRDghflqesrRLSAQFENL---MAE 246
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRRD--------KLTEEYAELkeeLED 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 247 SRQDLEEEyEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVqqyreql 326
Cdd:TIGR02169 369 LRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE------- 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 327 EEMEERQRQLR----NGVQLQQQKNKEMEQLRlSLAEELSTYKAMLLPKSLEQADAPTSQ 382
Cdd:TIGR02169 441 EEKEDKALEIKkqewKLEQLAADLSKYEQELY-DLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
28-366 |
2.98e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 28 DRIQFVEGPVEPGKPTSPEHVV-YEGETVTRAEKSNPEESLRAEQSpSMEENLSIEDLELLEGRfqqcvqavaQLEEERD 106
Cdd:pfam17380 237 ERRKESFNLAEDVTTMTPEYTVrYNGQTMTENEFLNQLLHIVQHQK-AVSERQQQEKFEKMEQE---------RLRQEKE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 107 QLIHELVllREPALQEVQQVHQDIL----AAYKLHAQAELERDGLREEIRLVKQKlfkvtkecvayQYQLECRQQDVAQf 182
Cdd:pfam17380 307 EKAREVE--RRRKLEEAEKARQAEMdrqaAIYAEQERMAMERERELERIRQEERK-----------RELERIRQEEIAM- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 183 adfrEVLTTRatqlseELAQLRDAYQKQKEQLRQQLEAPPSQRdghFLQESR-RLSAQFENLMAESRQDLEEEYEPQFLR 261
Cdd:pfam17380 373 ----EISRMR------ELERLQMERQQKNERVRQELEAARKVK---ILEEERqRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 262 LLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQyreqleEMEERQRQLRNGVQ 341
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEER 513
|
330 340
....*....|....*....|....*
gi 1370454671 342 LQQQKNKEMEQLRLSLAEELSTYKA 366
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREA 538
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-378 |
4.51e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 169 QYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQqLEAppsqrdghflqESRRLSAQFENLMAESR 248
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEA-----------ELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 249 QDLEEEYEpqflrLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQ 325
Cdd:COG1196 285 EAQAEEYE-----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAE 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370454671 326 LEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADA 378
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-368 |
4.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 186 REVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLmAESRQDLeeeyePQFLRLLER 265
Cdd:COG4913 612 LAALEAELAELEEELAEA----EERLEALEAELDA---------LQERREALQRLAEY-SWDEIDV-----ASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 266 KEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRD---EEVQQYREQLEEMEERQRQLRNGV-- 340
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeEELDELQDRLEAAEDLARLELRALle 752
|
170 180 190
....*....|....*....|....*....|
gi 1370454671 341 -QLQQQKNKEME-QLRLSLAEELSTYKAML 368
Cdd:COG4913 753 eRFAAALGDAVErELRENLEERIDALRARL 782
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-359 |
5.74e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 169 QYQLECRQQDVAQFADFrevLTTRATQLSEELAQLRDAYQKQKEQlrQQLEAPPSQRDGhFLQESRRLSAQFENLMAEsR 248
Cdd:COG3206 163 EQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKL-LLQQLSELESQLAEARAE-L 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 249 QDLEEEYepQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN-------RNLEDQIALVRQKRDEEVQQ 321
Cdd:COG3206 236 AEAEARL--AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR 313
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370454671 322 YRE----QLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAE 359
Cdd:COG3206 314 ILAsleaELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-336 |
1.44e-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: 44.34 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 125 QVHQDILAayKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQleCRQQDVAQFADFREVLTTrATQLSEELAQLR 204
Cdd:pfam15921 263 QQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ--ARNQNSMYMRQLSDLEST-VSQLRSELREAK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 205 DAYQKQKEQLRQQLEAPPS-------QRDgHFLQESRRLSAQFENLMA-----ESRQDLEEEyepQFLRLLERKEAGTKA 272
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANSelteartERD-QFSQESGNLDDQLQKLLAdlhkrEKELSLEKE---QNKRLWDRDTGNSIT 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370454671 273 LQRTQAEIQEMKEALRPLQAEARQLRLQNR-NLEDQIALVRQKRD--EEVQQYREQLEEMEERQRQL 336
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKV 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-340 |
1.79e-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: 44.29 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQ-QVH---------QDILAAYKLHAQ-AELERDGLREE 150
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGeleaeiaslERSIAEKERELEdAEERLAKLEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRD---AYQKQKEQLRQQLEapPSQRDG 227
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelkDYREKLEKLKREIN--ELKREL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 228 HFLQE-SRRLSAQFENLMAESrqdleEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLED 306
Cdd:TIGR02169 409 DRLQEeLQRLSEELADLNAAI-----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
250 260 270
....*....|....*....|....*....|....
gi 1370454671 307 qialvrqkrdeEVQQYREQLEEMEERQRQLRNGV 340
Cdd:TIGR02169 484 -----------ELSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-367 |
2.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 191 TRATQLSEELAQLRDAYQkQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLMAESR--QDLEEEYEPQFLRllERKEA 268
Cdd:COG4913 225 EAADALVEHFDDLERAHE-ALEDAREQIEL---------LEPIRELAERYAAARERLAelEYLRAALRLWFAQ--RRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 269 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIalvRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKnk 348
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEAL-- 367
|
170
....*....|....*....
gi 1370454671 349 eMEQLRLSLAEELSTYKAM 367
Cdd:COG4913 368 -LAALGLPLPASAEEFAAL 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
264-376 |
2.46e-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: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 264 ERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQLEEMEERQRQLRNgv 340
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRA-- 97
|
90 100 110
....*....|....*....|....*....|....*..
gi 1370454671 341 QLQQQKNKEMEQLR-LSLAEELSTYKAMLLPKSLEQA 376
Cdd:COG4942 98 ELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDA 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-385 |
3.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 138 AQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQ 217
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 218 LEAppSQRDGH------FLQESRRLSAQFENL-----MAESRQDLEEEYEpqflRLLERKEAGTKALQRTQAEIQEMKEA 286
Cdd:COG3883 92 ARA--LYRSGGsvsyldVLLGSESFSDFLDRLsalskIADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 287 LRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKA 366
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250
....*....|....*....
gi 1370454671 367 MLLPKSLEQADAPTSQAGG 385
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGA 264
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
98-357 |
5.36e-04 |
|
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: 42.63 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 98 VAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGlREEIRLVKQKLFKVTKEcvayqyqlecrqq 177
Cdd:COG3096 787 LEELRAERDELAEQYAKASF-DVQKLQRLHQAFSQFVGGHLAVAFAPDP-EAELAALRQRRSELERE------------- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 178 dVAQFADFREVLTTRATQLSEELAQLR-----------DAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQFENLMAE 246
Cdd:COG3096 852 -LAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlladETLADRLEELREELDA--AQEAQAFIQQHGKALAQLEPLVAV 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 247 SRQDLEeeyepQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA----EARQLRLQNRNLEDQIalvrqkrdeevqqy 322
Cdd:COG3096 929 LQSDPE-----QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyeDAVGLLGENSDLNEKL-------------- 989
|
250 260 270
....*....|....*....|....*....|....*
gi 1370454671 323 REQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSL 357
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASL 1024
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-362 |
6.83e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 171 QLECRQQDVAQFADFREVLTTRATQlsEELAQLRDAYQKQKEQ--LRQQLEAPPSQRDGHfLQESRRLSAQFENLmAESR 248
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLelLEAELEELRAELARL-EAELERLEARLDAL-REEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 249 QDLEEEYEPQFLRLLERKEagtKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEE 328
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLE---REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1370454671 329 MEERQRQLRNGVQ---------------LQQQKN---KEMEQLRLSLAEELS 362
Cdd:COG4913 403 LEEALAEAEAALRdlrrelreleaeiasLERRKSnipARLLALRDALAEALG 454
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
82-401 |
1.19e-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: 41.48 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREP-------------ALQEVQ----QVHQDILA---AYKLHAQAE 141
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslksqladyqqALDVQQtraiQYQQAVQAlekARALCGLPD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 142 LERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEElaqlrDAYQKQKEQLRQQleap 221
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERS-----QAWQTARELLRRY---- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 222 PSQRdgHFLQESRRLSAQFENL--MAESRQDLE---EEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQ 296
Cdd:COG3096 505 RSQQ--ALAQRLQQLRAQLAELeqRLRQQQNAErllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 297 LRLQNRNLEDQIALVRQKR------DEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEElstykamllP 370
Cdd:COG3096 583 LRQQLEQLRARIKELAARApawlaaQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAAR---------K 653
|
330 340 350
....*....|....*....|....*....|.
gi 1370454671 371 KSLEQADAPTSQAGGMETQSQGDLCEEKSGV 401
Cdd:COG3096 654 QALESQIERLSQPGGAEDPRLLALAERLGGV 684
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
198-350 |
1.49e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.13 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 198 EELA----QLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLS--------AQFENLMAESRQDLEEEYEPQFLRLLER 265
Cdd:pfam13779 509 EEIAklmqELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTqqdlqrmlDRIEELARSGRRAEAQQMLSQLQQMLEN 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 266 KEAGTKALQRTQAeIQEMKEALRPLQAEAR---QLRLQN-RNLEDQIALVRQKRDEEVQQYR------------------ 323
Cdd:pfam13779 589 LQAGQPQQQQQQG-QSEMQQAMDELGDLLReqqQLLDETfRQLQQQGGQQQGQPGQQGQQGQgqqpgqggqqpgaqmppq 667
|
170 180 190
....*....|....*....|....*....|
gi 1370454671 324 ---EQLEEMEERQRQLRNGVQLQQQKNKEM 350
Cdd:pfam13779 668 ggaEALGDLAERQQALRRRLEELQDELKEL 697
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-383 |
2.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 202 QLRDAYQKQKEQLRQQLEappsQRDGHFLQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQ-RTQAEI 280
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAE----EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEE 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 281 QEMKEALRPLQAEARQLRLQNRNLEDQIALVRQ---KRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSL 357
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
170 180
....*....|....*....|....*.
gi 1370454671 358 AEELStyKAMLLPKSLEQADAPTSQA 383
Cdd:PTZ00121 1712 AEEKK--KAEELKKAEEENKIKAEEA 1735
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
96-368 |
2.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 96 QAVAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGlREEIRLVKQKlfkvtkecvayqyqlecR 175
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSF-DVQKLQRLHQAFSRFIGSHLAVAFEADP-EAELRQLNRR-----------------R 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 176 QQDVAQFADFREV---LTTRATQLSEELAQLR-----------DAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQFE 241
Cdd:PRK04863 847 VELERALADHESQeqqQRSQLEQAKEGLSALNrllprlnlladETLADRVEEIREQLDE--AEEAKRFVQQHGNALAQLE 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 242 NLMAESRQDlEEEYEpqflrllerkeagtkalqRTQAEIQEMKEALRPLQAEARQLR--LQNRN---LEDQIALVrQKRD 316
Cdd:PRK04863 925 PIVSVLQSD-PEQFE------------------QLKQDYQQAQQTQRDAKQQAFALTevVQRRAhfsYEDAAEML-AKNS 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370454671 317 EEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:PRK04863 985 DLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQML 1036
|
|
| M3A_DCP |
cd06456 |
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ... |
240-369 |
3.38e-03 |
|
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.
Pssm-ID: 341051 [Multi-domain] Cd Length: 653 Bit Score: 39.75 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 240 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 303
Cdd:cd06456 7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370454671 304 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:cd06456 87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
62-352 |
3.82e-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: 39.94 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 62 NPEESLRAEQSPSMEENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQE-VQQVHQDILAAykLHAQA 140
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADrLEELREELDAA--QEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 141 ELERDGlrEEIRLVKQKLFKVTK-----ECVAYQY-QLECRQQDVAQFADFREVLTTRATQLS-EELAQLRDAYQKQKEQ 213
Cdd:COG3096 911 FIQQHG--KALAQLEPLVAVLQSdpeqfEQLQADYlQAKEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 214 LRQQLEAPPSQRDghflqESRrlsaqfenLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALrPLQAE 293
Cdd:COG3096 989 LRARLEQAEEARR-----EAR--------EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQA-DAEAE 1054
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370454671 294 ARQlRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQ 352
Cdd:COG3096 1055 ERA-RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
241-360 |
4.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 241 ENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQ------- 313
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeerreir 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370454671 314 ------KRDEEVQQYREQLEEMEERQRQLRngvqlqqQKNKEMEQLRLSLAEE 360
Cdd:COG2433 463 kdreisRLDREIERLERELEEERERIEELK-------RKLERLKELWKLEHSG 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-366 |
4.31e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 198 EELAQLRDAYQKQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLMAESRQDLEE-EYEPQFLRLLERKEAGTKALQRT 276
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEE---------LEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 277 QAEIQEMKEALRP---LQAEARQLRLQNRNLEDQIALVRQKRD----EEVQQYREQLEEMEERQRQLRNGVQLQQQKNKE 349
Cdd:COG4717 145 PERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1370454671 350 MEQLRLSLAEELSTYKA 366
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
198-336 |
4.64e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.35 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 198 EELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQ 277
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQ 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370454671 278 AEIQEmkEALRPLQAEARQLrLQNRNLEDQIALVRQKRDeevqQYREQLEEMEERQRQL 336
Cdd:pfam09731 374 AEAHE--EHLKDVLVEQEIE-LQREFLQDIKEKVEEERA----GRLLKLNELLANLKGL 425
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
63-240 |
7.91e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 63 PEESLRAEQSPSMEENLSIedlelLEGRFQQCVQAVAQLEEERDQliHELVLLREPALQEVQQVHQDILAAYKLHAQAEL 142
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSE-----LEQRLRQQQRAERLLAEFCKR--LGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454671 143 E-RDGLREEIRLVKQKLFKVTK---ECVAYQYQLE-CRQQDVAQFADFREVLTTRATQLSEE--LAQLRDAYQKQKEQLR 215
Cdd:PRK04863 579 ErRMALRQQLEQLQARIQRLAArapAWLAAQDALArLREQSGEEFEDSQDVTEYMQQLLEREreLTVERDELAARKQALD 658
|
170 180
....*....|....*....|....*
gi 1370454671 216 QQLEApPSQRDGHFLQESRRLSAQF 240
Cdd:PRK04863 659 EEIER-LSQPGGSEDPRLNALAERF 682
|
|
| |
