|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
140-452 |
5.58e-127 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 373.10 E-value: 5.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 140 EKQTMQNLNDRLANYLDKVRALEEANTDLENKIKEWYDKygpgsGDGGSGRDYSKYYSIIEDLRNQIIAATVENAGIILH 219
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-----KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 220 IDNARLAADDFRLKYENELCLRQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNHEEEMKNMQGS-SGGEV 298
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 299 TVEMNAAPGTDLTKLLNDMRAQYEELAEQNRREAEERFNKQSASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQ 378
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121941436 379 LAMKSSLEGTLADTEAGYVAQLSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRLLDGE 452
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-450 |
1.49e-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: 54.29 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 241 RQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNHEEemknmqgssgGEVTVEMNAAPGTDLTKLLNDMRAQ 320
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----------LEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 321 YEELAEQ--NRREAEERFNKQSASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQLAMKSSLEGTLADT------ 392
Cdd:TIGR02168 346 LEELKEEleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeiee 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 393 --EAGYVAQLSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRLLD 450
Cdd:TIGR02168 426 llKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-490 |
2.72e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 242 QSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNHEEEMKNMQ--GSSGGEVTVEMNAapgTDLTKLLNDMRA 319
Cdd:COG3883 47 EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsGGSVSYLDVLLGS---ESFSDFLDRLSA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 320 qYEELAEQNRREAEERfnkqsASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQLAMKSSLEGTLADTEAGYVAQ 399
Cdd:COG3883 124 -LSKIADADADLLEEL-----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 400 LSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRLLDGEGGGSSFAEFGGRNSGSVNMGSRDLVSG 479
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAA 277
|
250
....*....|.
gi 121941436 480 DSRSGSCSGQG 490
Cdd:COG3883 278 AASAAGGGAGG 288
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
219-414 |
1.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 219 HIDNARLAA----DDFRLKYENELCLRQSVEADINGLRK--------------VLDDLTMTRSDLEMQIESFTEELAYLR 280
Cdd:PHA02562 203 NIEEQRKKNgeniARKQNKYDELVEEAKTIKAEIEELTDellnlvmdiedpsaALNKLNTAAAKIKSKIEQFQKVIKMYE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 281 KNHEEEmKNMQGSSGGEVTVEMNAAPGTDLTKLLNDMRAQYEELAEQnrreaEERFNKQSAS---LQAQISTDAGAATSA 357
Cdd:PHA02562 283 KGGVCP-TCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI-----MDEFNEQSKKlleLKNKISTNKQSLITL 356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 121941436 358 KNEITELKRTLQaleiELQSQLAMKsslegtlADTEAGYVAQLSEIQTQISALEEEI 414
Cdd:PHA02562 357 VDKAKKVKAAIE----ELQAEFVDN-------AEELAKLQDELDKIVKTKSELVKEK 402
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
140-452 |
5.58e-127 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 373.10 E-value: 5.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 140 EKQTMQNLNDRLANYLDKVRALEEANTDLENKIKEWYDKygpgsGDGGSGRDYSKYYSIIEDLRNQIIAATVENAGIILH 219
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-----KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 220 IDNARLAADDFRLKYENELCLRQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNHEEEMKNMQGS-SGGEV 298
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 299 TVEMNAAPGTDLTKLLNDMRAQYEELAEQNRREAEERFNKQSASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQ 378
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121941436 379 LAMKSSLEGTLADTEAGYVAQLSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRLLDGE 452
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-450 |
1.49e-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: 54.29 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 241 RQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNHEEemknmqgssgGEVTVEMNAAPGTDLTKLLNDMRAQ 320
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----------LEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 321 YEELAEQ--NRREAEERFNKQSASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQLAMKSSLEGTLADT------ 392
Cdd:TIGR02168 346 LEELKEEleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeiee 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 393 --EAGYVAQLSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRLLD 450
Cdd:TIGR02168 426 llKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-490 |
2.72e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 242 QSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNHEEEMKNMQ--GSSGGEVTVEMNAapgTDLTKLLNDMRA 319
Cdd:COG3883 47 EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsGGSVSYLDVLLGS---ESFSDFLDRLSA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 320 qYEELAEQNRREAEERfnkqsASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQLAMKSSLEGTLADTEAGYVAQ 399
Cdd:COG3883 124 -LSKIADADADLLEEL-----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 400 LSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRLLDGEGGGSSFAEFGGRNSGSVNMGSRDLVSG 479
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAA 277
|
250
....*....|.
gi 121941436 480 DSRSGSCSGQG 490
Cdd:COG3883 278 AASAAGGGAGG 288
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
312-452 |
8.08e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 43.99 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 312 KLLNDMRAQYEELaEQNRREAEERFNKQSASLQAQIstdagaaTSAKNEITELKRTLQALEielqsqlamksslegtlad 391
Cdd:pfam14988 22 KLWNQYVQECEEI-ERRRQELASRYTQQTAELQTQL-------LQKEKEQASLKKELQALR------------------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121941436 392 teagYVAQLSEIQTQ-ISALEEEICQIWGETKCQNAEYK-QLLDIKTRLEVEIETYRRLLDGE 452
Cdd:pfam14988 75 ----PFAKLKESQEReIQDLEEEKEKVRAETAEKDREAHlQFLKEKALLEKQLQELRILELGE 133
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
219-414 |
1.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 219 HIDNARLAA----DDFRLKYENELCLRQSVEADINGLRK--------------VLDDLTMTRSDLEMQIESFTEELAYLR 280
Cdd:PHA02562 203 NIEEQRKKNgeniARKQNKYDELVEEAKTIKAEIEELTDellnlvmdiedpsaALNKLNTAAAKIKSKIEQFQKVIKMYE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 281 KNHEEEmKNMQGSSGGEVTVEMNAAPGTDLTKLLNDMRAQYEELAEQnrreaEERFNKQSAS---LQAQISTDAGAATSA 357
Cdd:PHA02562 283 KGGVCP-TCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI-----MDEFNEQSKKlleLKNKISTNKQSLITL 356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 121941436 358 KNEITELKRTLQaleiELQSQLAMKsslegtlADTEAGYVAQLSEIQTQISALEEEI 414
Cdd:PHA02562 357 VDKAKKVKAAIE----ELQAEFVDN-------AEELAKLQDELDKIVKTKSELVKEK 402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-452 |
7.44e-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: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 137 SGGEKQTMQNLNDRLANYLDKVRALEEANTDLENKIKEWYDKYGPGSGDGGSGRDyskyysIIEDLRNQIIAATVENAGI 216
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK------ELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 217 ILHIDNARLAADDFRLKYENELCLRQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKNH---EEEMKNMQGS 293
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 294 SG-GEVTVEMNAAPGTDLTKLLNDMRAQYEELAEQnrreaEERFNKQSASLQAQISTDAGAATSAKNEITELKRTLQALE 372
Cdd:TIGR02168 819 AAnLRERLESLERRIAATERRLEDLEEQIEELSED-----IESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 373 IELQSQLAMKSSLEGTLADTEAGYVA---QLSEIQTQISALEEEICQIWGETkcqNAEYKQLLDIKTRLEVEIETYRRLL 449
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEElreKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEA 970
|
...
gi 121941436 450 DGE 452
Cdd:TIGR02168 971 RRR 973
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
242-414 |
1.05e-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: 40.68 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 242 QSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAylrkNHEEEMKNMQgssggevtvemnaapgTDLTKLLNDMRAQY 321
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLE----AAKTELEDLE----------------KEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 322 EELAEQNRREAEERFNKQSASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQLAMKSSLEGTLADTEAGYVAQLS 401
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170
....*....|...
gi 121941436 402 EIQTQISALEEEI 414
Cdd:COG1579 153 ELEAELEELEAER 165
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
225-464 |
1.17e-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: 41.29 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 225 LAADDFRLKYENELclrQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRK---NHEEEMKNMQGssggevtvE 301
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEA--------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 302 MNAApGTDLTKLLNDMRAQYEELAEQ--------NRREAEERFNKQSASLQAQISTDAGAATSA-KNEITELKRT---LQ 369
Cdd:COG4942 85 LAEL-EKEIAELRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPArREQAEELRADlaeLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 370 ALEIELQSQLAMKSSLEGTLADTEAGYVAQLSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIETYRRll 449
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-- 241
|
250
....*....|....*
gi 121941436 450 dgEGGGSSFAEFGGR 464
Cdd:COG4942 242 --RTPAAGFAALKGK 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-444 |
1.46e-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: 41.59 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 309 DLTKLLNDMRAQYEELAEQnrreaEERFNKQSASLQAQIStdagaatSAKNEITELKRTLQALEIELQSQLAMKSSLEGT 388
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQE-----EEKLKERLEELEEDLS-------SLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 121941436 389 LADTEAGYV-AQLSEIQTQISALEEEICQIWGETKCQNAEYKQLLDIKTRLEVEIET 444
Cdd:TIGR02169 781 LNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-414 |
1.73e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 199 IEDLRNQIIAATVENAGIILHIDNARLAADDFRLKYENElclrqsvEADINGLRKVLDDLTMTRSDLEMQIESFTEELAY 278
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEEL-------ELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 279 LRKNHEEEMKNMQgssggevtvemnaapgtDLTKLLNDMRAQYEELAEQNRREAEERfnKQSASLQAQISTDAGAATSAK 358
Cdd:COG1196 314 LEERLEELEEELA-----------------ELEEELEELEEELEELEEELEEAEEEL--EEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 121941436 359 NEITELKRTLQALEIELQSQLAMKSSLEGTLADTEAGYVAQLSEIQTQISALEEEI 414
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
265-450 |
1.83e-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: 41.26 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 265 LEMQIESFTEE----LAYLRKNHEEEMKnmQGSSGGEVTVEMNAAPGTDLTKLLNDMRAQYEELAEQNRreaeerfnKQS 340
Cdd:pfam15921 243 VEDQLEALKSEsqnkIELLLQQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR--------NQN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 341 ASLQAQISTDAGAATSAKNEITELKRTLQALEIELQSQLAMKSSlEGTLADTEAGYVAQLS-EIQTQISALEEEICQIWG 419
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS-ELTEARTERDQFSQESgNLDDQLQKLLADLHKREK 391
|
170 180 190
....*....|....*....|....*....|.
gi 121941436 420 ETKCQNAEYKQLLDIKTRLEVEIETYRRLLD 450
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTGNSITIDHLRRELD 422
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
190-450 |
2.18e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 190 RDYSKYYSIIEDLRNQIIAATVENAGIIlHI----DNARLAAddfrlKYENELC---LRQSVEADINGLRKVLDDLTMTR 262
Cdd:COG3206 111 GEEASREAAIERLRKNLTVEPVKGSNVI-EIsytsPDPELAA-----AVANALAeayLEQNLELRREEARKALEFLEEQL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 263 SDLEMQIESFTEELAYLRKNHeeemknmqgssgGEVTVEMNAapgTDLTKLLNDMRAQYEElAEQNRREAEERFNkqsaS 342
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKN------------GLVDLSEEA---KLLLQQLSELESQLAE-ARAELAEAEARLA----A 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 343 LQAQISTDAGAATSAKNEitelkRTLQALEIELQSQLAMKSSLEGTLADTEAGYVAQLSEIQTQISALEEEICQIWGETK 422
Cdd:COG3206 245 LRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
250 260
....*....|....*....|....*...
gi 121941436 423 cqnAEYKQLLDIKTRLEVEIETYRRLLD 450
Cdd:COG3206 320 ---AELEALQAREASLQAQLAQLEARLA 344
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
199-443 |
3.45e-03 |
|
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: 40.00 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 199 IEDLRNQIIAATVENAGIILHIDNARLAaddfRLKYENELCLRQSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAY 278
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKIKNK----LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 279 LR---KNHEEEMKNMQGSSGGEVT--------VEMNAAPGTDLTKLLNDMRAQYEELAEQNRREAEERFNKQSAS----- 342
Cdd:TIGR04523 244 KTteiSNTQTQLNQLKDEQNKIKKqlsekqkeLEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNqekkl 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 343 --LQAQISTDAGAATSAKNEITELKRTLQALE---IELQSQLAMKSSLEGTLADTEAGYVAQLSEIQTQISALEEEICQI 417
Cdd:TIGR04523 324 eeIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
250 260
....*....|....*....|....*.
gi 121941436 418 WGETKCQNAEYKQLLDIKTRLEVEIE 443
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIE 429
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
141-414 |
9.83e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 141 KQTMQNLNDRLANYLDKVRALEEAntdlenkikewydkygpgsgdggsgrdyskyysiIEDLRNQiiaatvenAGIIlhi 220
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAA----------------------------------LEEFRQK--------NGLV--- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 221 dnarlaaddfrlkyenelclrqSVEADINGLRKVLDDLTMTRSDLEMQIESFTEELAYLRKnheeemknmQGSSGGEVTV 300
Cdd:COG3206 209 ----------------------DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA---------QLGSGPDALP 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121941436 301 EMNAAPgtdltkLLNDMRAQYEELaEQNRREAEERFNKQS---ASLQAQIStdagaatSAKNEI-TELKRTLQALEIELQ 376
Cdd:COG3206 258 ELLQSP------VIQQLRAQLAEL-EAELAELSARYTPNHpdvIALRAQIA-------ALRAQLqQEAQRILASLEAELE 323
|
250 260 270
....*....|....*....|....*....|....*...
gi 121941436 377 SQLAMKSSLEGTLADTEAgYVAQLSEIQTQISALEEEI 414
Cdd:COG3206 324 ALQAREASLQAQLAQLEA-RLAELPELEAELRRLEREV 360
|
|
|