|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
145-454 |
9.81e-126 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 373.49 E-value: 9.81e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 145 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 224
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 225 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 303
Cdd:pfam00038 78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 304 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQL 383
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827193856 384 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-448 |
1.12e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 203 IDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAY 282
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 283 L---KKNHEEEMKDLRnvstGDVNVEMNAApgVDLTQLLNNMRSQYEQL----------AEQNRKDAEAWfNEKSKELTT 349
Cdd:TIGR02168 773 AeeeLAEAEAEIEELE----AQIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT-ERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 350 EIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYcvqlSQIQAQISALEEQLQQIRAETECQN 429
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELEELR 921
|
250
....*....|....*....
gi 1827193856 430 TEYQQLLDIKIRLENEIQT 448
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDN 940
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
236-454 |
1.70e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 236 LKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPgvdLT 315
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 316 QLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAE 395
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827193856 396 TEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-454 |
2.17e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 256 RRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNV-------STGDVNVEMNAAP---------------GVD 313
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleelSRQISALRKDLARleaeveqleeriaqlSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 314 LTQLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASL 393
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827193856 394 AETEGRYCV---QLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:TIGR02168 834 AATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-454 |
8.11e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 242 VALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRnvstgdvnvemnaapgvDLTQLLNNM 321
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-----------------EAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 322 RSQYEQLAEQNRKDAEawfneKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYC 401
Cdd:COG1196 294 LAELARLEQDIARLEE-----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827193856 402 VQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-454 |
2.85e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 201 KTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYE----NEVALRQSVEADINGLRRV----------LDELTLTK 266
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAELARLEQDIARLeerrreleerLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 267 ADLEMQIESLTEELAYLKKNHEEEMKDLRnvstgdvnvemnaapgvDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKE 346
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELE-----------------EAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 347 LT---------TEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRycvqLSQIQAQISALEEQ 417
Cdd:COG1196 389 LEalraaaelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE----EAELEEEEEALLEL 464
|
250 260 270
....*....|....*....|....*....|....*..
gi 1827193856 418 LQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
255-454 |
1.03e-04 |
|
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: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 255 LRRVLDELTLTKADLEMQIESLTEELAylkkNHEEEMKDLRNvSTGDVNVEMNAApgvDLTQLLNNMRSQYEQlAEQNRK 334
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQ-KNGLVDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 335 DAEAWFNEKSKELTTEID-----NNIEQISSYKSEITELRRNVQALE----------IELQSQLAlkqSLEASLAETEGR 399
Cdd:COG3206 237 EAEARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIA---ALRAQLQQEAQR 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827193856 400 YCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
208-451 |
1.17e-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: 44.75 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 208 NQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNH 287
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 288 EEEMKDLRNV-----STGDVNVEMNAAPGVDLTQLLNNMRSqYEQLAEQNRkdaeawfnekskeltteidnniEQISSYK 362
Cdd:COG4942 100 EAQKEELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARR----------------------EQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 363 SEITELRRNVQALEIELQSQLALKQSLEASLAETEgrycVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRL 442
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*....
gi 1827193856 443 ENEIQTYRS 451
Cdd:COG4942 233 EAEAAAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-452 |
2.47e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 195 DYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAaddfRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIE 274
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK----LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 275 SLTEELAYLK---KNHEEEMKDLRNVSTGDVN--------VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNE- 342
Cdd:TIGR04523 236 KKQQEINEKTteiSNTQTQLNQLKDEQNKIKKqlsekqkeLEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSe 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 343 ------KSKELTTEIDNNIEQISSYKSEITELRRNVQALE---IELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISA 413
Cdd:TIGR04523 316 lknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
250 260 270
....*....|....*....|....*....|....*....
gi 1827193856 414 LEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSL 452
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
313-448 |
3.70e-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: 43.90 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 313 DLTQLLNNMRSQYEQLAEQNRKdaeawFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEAS 392
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827193856 393 LAETegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQT 448
Cdd:TIGR02169 788 LSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
246-424 |
3.79e-04 |
|
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: 42.60 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 246 QSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAApgvdltqllnnmRSQY 325
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK------------KYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 326 EQLAEQNRKDAEAwfnekskeLTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYCVQLS 405
Cdd:COG1579 81 QLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170
....*....|....*....
gi 1827193856 406 QIQAQISALEEQLQQIRAE 424
Cdd:COG1579 153 ELEAELEELEAEREELAAK 171
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
357-452 |
4.15e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 357 QISSYKSEITELRRNVQALEIELQsqlALKQSLEASLAEtegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQLL 436
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKE---ALKKEQDEASFE-------RLAELRDELAELEEELEALKARWEAEKELIEEIQ 474
|
90
....*....|....*.
gi 1827193856 437 DIKIRLENEIQTYRSL 452
Cdd:COG0542 475 ELKEELEQRYGKIPEL 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-454 |
9.55e-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: 42.35 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 250 ADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTgdvnvEMNAAPGV--DLTQLLNNMRSQYEQ 327
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-----EIEELQKElyALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 328 LAEQnrkdaEAWFNEKSKELTTEIDNNieqissyKSEITELRRNVQALEIELQSQLALKQSLEASLAETEgrycvqlsqi 407
Cdd:TIGR02168 307 LRER-----LANLERQLEELEAQLEEL-------ESKLDELAEELAELEEKLEELKEELESLEAELEELE---------- 364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1827193856 408 qAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:TIGR02168 365 -AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
206-449 |
1.29e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 206 LKNQILNLTTDNANILLQIDNARLAADDFRlKYENEvaLRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKK 285
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYN-KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 286 NHEEEMKDLRNVSTGDVNVEMNaapgVDLTQLLNNMRSQY-------EQLAEQNRKDAEAwfNEKSKELTT---EIDNNI 355
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSK----IEQFQKVIKMYEKGgvcptctQQISEGPDRITKI--KDKLKELQHsleKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 356 EQISSYKSEITELRRNVQaleiELQSQLA-LKQSLEASLAetegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 434
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|....*
gi 1827193856 435 LLDIKIRLENEIQTY 449
Cdd:PHA02562 391 IVKTKSELVKEKYHR 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
223-426 |
1.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 223 QIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNV----- 297
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 298 ----STGDVNVEMNAApgvDLTQLLNNMrSQYEQLAEQNRKDAEAWfneksKELTTEIDNNIEQISSYKSEITELRRNVQ 373
Cdd:COG3883 97 rsggSVSYLDVLLGSE---SFSDFLDRL-SALSKIADADADLLEEL-----KADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827193856 374 ALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETE 426
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
341-436 |
1.77e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 341 NEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGrycvQLSQIQAQISALEEQLQQ 420
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAE 94
|
90
....*....|....*.
gi 1827193856 421 IRAETECQNTEYQQLL 436
Cdd:COG4942 95 LRAELEAQKEELAELL 110
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
146-451 |
4.16e-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: 40.49 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 146 EKVTMQN----LNDRLASYLDKVRALEESNYEL-------EGKIKEWY-----EKHGNSHQGEPR----DYSKYYKTIDD 205
Cdd:pfam15921 487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQhlkneGDHLRNVQTECEalklQMAEKDKVIEI 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 206 LKNQILNLTT-----DNANILLQIDNARLAAD--DFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLemqIESLTE 278
Cdd:pfam15921 567 LRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEinDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 279 ELAYLKKNHEEEMKDLRNVSTGDVNvemnaapgvdltqlLNNMRSQYEQLAEQnrkdaeawFNEKSKELTTEIDNNIEQI 358
Cdd:pfam15921 644 RLRAVKDIKQERDQLLNEVKTSRNE--------------LNSLSEDYEVLKRN--------FRNKSEEMETTTNKLKMQL 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 359 SSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGrycvQLSQIQAQISALEEQLQQIRAE----TECQNTEYQQ 434
Cdd:pfam15921 702 KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQE 777
|
330 340
....*....|....*....|
gi 1827193856 435 LLDI---KIRLENEIQTYRS 451
Cdd:pfam15921 778 LSTVateKNKMAGELEVLRS 797
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-434 |
7.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 246 QSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEmKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQY 325
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827193856 326 EQLAEQNRKDAEAWfnEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQS-----QLALKQSLEASLAE--TEG 398
Cdd:COG4913 685 DDLAALEEQLEELE--AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELRALLEERFAAalGDA 762
|
170 180 190
....*....|....*....|....*....|....*.
gi 1827193856 399 RYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 434
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| |
