|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
88-399 |
7.11e-120 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 351.53 E-value: 7.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 88 NEKETMQFLNDRLASYLERVRSLEENNAELECRIREQCEPDATPVCPDYQRYFDTIEELQQKILCTKAENSRLAVQVDNC 167
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 168 KLAADDFRSKYESELSLRQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLLCLKKDHEEEVNLLREQLGD-RLNVEL 246
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 247 DTAPTVDLNKVLDEMRCQYERVLANNRRDAEEWFAAQTEELNQQQMSSAEQLQGCQTEMLELKRTANTLEIELQAQQTLT 326
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57012428 327 ESLECTVAETEAQYSTQLAQMQCLIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEINTYRGLLEKEDSR 399
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-386 |
1.65e-07 |
|
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: 52.84 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 169 LAADDFRSKYESELslrQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLLCLKK---DHEEEVNLLREQLgDRLNVE 245
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAEL-AELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 246 LDTaptvdLNKVLDEMRCQYERVLA----NNRRDAEEWFAAQT------------EELNQQQMSSAEQLQGCQTEMLELK 309
Cdd:COG4942 92 IAE-----LRAELEAQKEELAELLRalyrLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57012428 310 RtantleiELQAQQTLTESLECTVAETEAQYSTQLAQMQCLIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEI 386
Cdd:COG4942 167 A-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-388 |
4.25e-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: 52.37 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 97 NDRLASYLERVRSLEENNAELEcrireQCEPDATPVCPDYQRYFDTIEELQQKILCTKAENSRLAVQVDNCKLAADDFRS 176
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIE-----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 177 KYESELSLRQL-------VENDISGLRGILGELTLCKSDLEAHVESLKDDLlclkKDHEEEVNLLREQLgDRLNVELDTa 249
Cdd:TIGR02168 741 EVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREAL-DELRAELTL- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 250 ptvdlnkvLDEMRCQYERVLANNRRDAEEWfAAQTEELNQQQMSSAEQLQGCQTEMLELKRTANTLEIELQAQQTLTESL 329
Cdd:TIGR02168 815 --------LNEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 57012428 330 ECTVAETEAQYSTQLAQmqclIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEINT 388
Cdd:TIGR02168 886 EEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
88-399 |
7.11e-120 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 351.53 E-value: 7.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 88 NEKETMQFLNDRLASYLERVRSLEENNAELECRIREQCEPDATPVCPDYQRYFDTIEELQQKILCTKAENSRLAVQVDNC 167
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 168 KLAADDFRSKYESELSLRQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLLCLKKDHEEEVNLLREQLGD-RLNVEL 246
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 247 DTAPTVDLNKVLDEMRCQYERVLANNRRDAEEWFAAQTEELNQQQMSSAEQLQGCQTEMLELKRTANTLEIELQAQQTLT 326
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57012428 327 ESLECTVAETEAQYSTQLAQMQCLIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEINTYRGLLEKEDSR 399
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-386 |
1.65e-07 |
|
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: 52.84 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 169 LAADDFRSKYESELslrQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLLCLKK---DHEEEVNLLREQLgDRLNVE 245
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAEL-AELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 246 LDTaptvdLNKVLDEMRCQYERVLA----NNRRDAEEWFAAQT------------EELNQQQMSSAEQLQGCQTEMLELK 309
Cdd:COG4942 92 IAE-----LRAELEAQKEELAELLRalyrLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57012428 310 RtantleiELQAQQTLTESLECTVAETEAQYSTQLAQMQCLIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEI 386
Cdd:COG4942 167 A-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-388 |
4.25e-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: 52.37 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 97 NDRLASYLERVRSLEENNAELEcrireQCEPDATPVCPDYQRYFDTIEELQQKILCTKAENSRLAVQVDNCKLAADDFRS 176
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIE-----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 177 KYESELSLRQL-------VENDISGLRGILGELTLCKSDLEAHVESLKDDLlclkKDHEEEVNLLREQLgDRLNVELDTa 249
Cdd:TIGR02168 741 EVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREAL-DELRAELTL- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 250 ptvdlnkvLDEMRCQYERVLANNRRDAEEWfAAQTEELNQQQMSSAEQLQGCQTEMLELKRTANTLEIELQAQQTLTESL 329
Cdd:TIGR02168 815 --------LNEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 57012428 330 ECTVAETEAQYSTQLAQmqclIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEINT 388
Cdd:TIGR02168 886 EEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
143-368 |
5.72e-07 |
|
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: 51.30 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 143 IEELQQKIlctKAENSRLAVQvdncklaaddfRSKYESELSLRQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLLC 222
Cdd:COG4942 29 LEQLQQEI---AELEKELAAL-----------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 223 LKKDHEEEVNLLREQLG--------DRLNVELDTAPTVDLNKVLdemrcQYERVLANNRRDAEEWFAAQTEELNQQQMSS 294
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlgrqPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57012428 295 AEQLQGCQTEMLELKRTANTLEIELQAQQTLTESLEctvaETEAQYSTQLAQMQCLIDSVEHQLAEIRCDLERQ 368
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
171-348 |
6.23e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 171 ADDFRSKYESELS----LRQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLLCLKKD---HEEEVNLLREQLGDRLN 243
Cdd:COG3883 14 ADPQIQAKQKELSelqaELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 244 VELDTAPTV----------DLNKVLDemRCQYERVLANNRRDAEEWFAAQTEELNQQQMSSAEQLQGCQTEMLELKRTAN 313
Cdd:COG3883 94 ALYRSGGSVsyldvllgseSFSDFLD--RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 57012428 314 TLEIELQAQQTLTESLECTVAETEAQYSTQLAQMQ 348
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
284-362 |
3.41e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.53 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 284 TEELNQQQMSSAEQ--------LQGCQTEMLELKRTANTL--EIELQAQQTLTESLECTVAETEAQYST----------Q 343
Cdd:COG3524 171 SERAREDAVRFAEEeveraeerLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAELEAELAAlrsylspnspQ 250
|
90
....*....|....*....
gi 57012428 344 LAQMQCLIDSVEHQLAEIR 362
Cdd:COG3524 251 VRQLRRRIAALEKQIAAER 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-330 |
3.50e-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: 43.12 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 80 CEEGTFNSNEKET--------MQFLNDRLASYLERVRSLEENNAELECRIREQCEPDATpVCPDYQRYFDTIEELQQKIL 151
Cdd:TIGR02168 255 LEELTAELQELEEkleelrleVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN-LERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 152 CTKAENSR-------LAVQVDNCKLAADDFRSKYESELSLRQLVENDISGLRGILGELTLCKSDLEAHVESLKDDLlclk 224
Cdd:TIGR02168 334 ELAEELAEleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL---- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 225 kdheeevnllrEQLGDRLNVELDTAPTVDLNKVLDEMRCQYERVlaNNRRDAEEWFAAQTEELNQQQMSSAEQLQGCQTE 304
Cdd:TIGR02168 410 -----------ERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260
....*....|....*....|....*.
gi 57012428 305 MLELKRTANTLEIELQAQQTLTESLE 330
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-391 |
9.03e-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: 41.58 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 176 SKY-----ESELSLRQLVENdISGLRGILGELTLCKSDLEAHVESLKDdllcLKKDHEEEVNLLREQLGDRLNV---ELD 247
Cdd:TIGR02168 168 SKYkerrkETERKLERTREN-LDRLEDILNELERQLKSLERQAEKAER----YKELKAELRELELALLVLRLEElreELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 248 TaptvdLNKVLDEMRCQYERvLANNRRDAEEwfaaQTEELNQQQMSSAEQLQGCQTEMLELKRTANTLEIELQAQQTLTE 327
Cdd:TIGR02168 243 E-----LQEELKEAEEELEE-LTAELQELEE----KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57012428 328 SLECTVAETEAQ----------YSTQLAQMQCLIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEINTYRG 391
Cdd:TIGR02168 313 NLERQLEELEAQleeleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-400 |
1.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 272 NRRDAEEWF-----AAQTEELNQQQMSSAEQLQGCQTEMLELKRTANTLEIELQAQQTLTE---------SLECTVAETE 337
Cdd:COG4913 595 RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELE 674
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57012428 338 AQYStQLAQMQCLIDSVEHQLAEIRCDLERQNQEYKVLLDTKARLECEINTYRGLLEKEDSRL 400
Cdd:COG4913 675 AELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-406 |
1.71e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 82 EGTFNSNEKETMqfLNDRLASYLERVRSLEEN--NAELECRIREQCEPDATPVCPDYQRYFDTIEELQQKILCTKAENS- 158
Cdd:COG5185 201 SGTVNSIKESET--GNLGSESTLLEKAKEIINieEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSk 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 159 RLAVQVDNcklAADDFRSKYE--SELSLRQLVENDISGLRGILGELTLCKS--DLEAHVES----LKDDLLCLKKDHEEE 230
Cdd:COG5185 279 RLNENANN---LIKQFENTKEkiAEYTKSIDIKKATESLEEQLAAAEAEQEleESKRETETgiqnLTAEIEQGQESLTEN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 231 VNLLR---EQLGDRLNVELDTAPTVDLNKVLDEMRCQYERVLANNRRDAEEWFAAQTEELNQQQMSSAE---QLQGCQTE 304
Cdd:COG5185 356 LEAIKeeiENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEElqrQIEQATSS 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 305 MLELKRTANTLEIELQAQQTLTES------------LECTVAETEAQYSTQLAQMQCLIDSVEHQLAEIRCDLERQNQEY 372
Cdd:COG5185 436 NEEVSKLLNELISELNKVMREADEesqsrleeaydeINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
330 340 350
....*....|....*....|....*....|....
gi 57012428 373 KVLLDTKARLECEINTYRGLLEKEDSRlPCNPGS 406
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALE-NLIPAS 548
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-284 |
3.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 135 DYQRYFDTIEELQQKILCTKAENSRLA----VQVDNcklaADDFRSK---YESELSLRQLVENDISGLRGILGEL----- 202
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAAllaeAGVED----EEELRAAleqAEEYQELKEELEELEEQLEELLGELeelle 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 203 TLCKSDLEAHVESLKDDLlclkKDHEEEVNLLREQLGdRLNVELDTAPTVDLnkvLDEMRCQYERVLANNRRDAEEWFAA 282
Cdd:COG4717 424 ALDEEELEEELEELEEEL----EELEEELEELREELA-ELEAELEQLEEDGE---LAELLQELEELKAELRELAEEWAAL 495
|
..
gi 57012428 283 QT 284
Cdd:COG4717 496 KL 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
177-390 |
3.60e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 177 KYESELSLrQLVENDISGLRGILGELTLCKSDLEAHVESLKD-----------DLLCLKKDHEEEVNLLREQLGDRLNVE 245
Cdd:COG3206 52 VYEASATL-LVEPQSSDVLLSGLSSLSASDSPLETQIEILKSrpvlervvdklNLDEDPLGEEASREAAIERLRKNLTVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 246 LDTAPTV--------D-------LNKVLDEMRCQYERVLANNRRDAEEWFAAQTEELnQQQMSSAEQlqgcqtEMLELKR 310
Cdd:COG3206 131 PVKGSNVieisytspDpelaaavANALAEAYLEQNLELRREEARKALEFLEEQLPEL-RKELEEAEA------ALEEFRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 311 TANTLEIELQAQQTLTEslectVAETEAQYST---QLAQMQCLIDSVEHQLAEIRCDLER--QNQEYKVLLDTKARLECE 385
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQ-----LSELESQLAEaraELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAE 278
|
....*
gi 57012428 386 INTYR 390
Cdd:COG3206 279 LAELS 283
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-399 |
4.52e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 208 DLEAHVESLKDDLLC----------LKKDHEEEVNLLREQLGDrlnveldtapTVDLNKVLDEMRCQYERVLANNRRDAE 277
Cdd:pfam01576 268 ELEAQISELQEDLESeraarnkaekQRRDLGEELEALKTELED----------TLDTTAAQQELRSKREQEVTELKKALE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 278 E---WFAAQTEELNQQQMSSAEQLQgcqtEMLE--------LKRTANTLEIELQAQQTLTESLECTVAETEAQYSTQLAQ 346
Cdd:pfam01576 338 EetrSHEAQLQEMRQKHTQALEELT----EQLEqakrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57012428 347 MQCLidSVEHQlaeircDLERQNQEykvLLDTKARLECEINTYRGLLEKEDSR 399
Cdd:pfam01576 414 LQEL--QARLS------ESERQRAE---LAEKLSKLQSELESVSSLLNEAEGK 455
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
183-395 |
4.62e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.44 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 183 SLRQLVENDISGLRGILGELT----LCKSDLEAHV--ESLKDDL------LCLKK-------DHEEEVNLLREQLGDRLN 243
Cdd:pfam12128 535 TLLHFLRKEAPDWEQSIGKVIspelLHRTDLDPEVwdGSVGGELnlygvkLDLKRidvpewaASEEELRERLDKAEEALQ 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 244 VELDTAPTVD-----LNKVLDEMRCQYERVLA---NNRRDAEEWFAAQTEELNQQQMSSAEQLQGCQTEMLELKRTANTL 315
Cdd:pfam12128 615 SAREKQAAAEeqlvqANGELEKASREETFARTalkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 316 EIELQA--QQTLTESLECTVA------ETEAQYSTQLAQMQCLIDSVEHQL-AEIR-CDLERQNQEYKVLLD--TKARLE 383
Cdd:pfam12128 695 DKKHQAwlEEQKEQKREARTEkqaywqVVEGALDAQLALLKAAIAARRSGAkAELKaLETWYKRDLASLGVDpdVIAKLK 774
|
250
....*....|..
gi 57012428 384 CEINTYRGLLEK 395
Cdd:pfam12128 775 REIRTLERKIER 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-401 |
6.10e-03 |
|
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: 39.27 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 136 YQRYFDTIEELQQKILCTKAEnsRLAVQVDNCKLAADDFRSKYESELSLRQLVENDISGLRGILGELtlckSDLEAHVES 215
Cdd:TIGR02168 215 YKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 216 LKDDLLCLKKDHEEEVNLLREQLgDRLNVELdtaptvdlnKVLDEMRCQYERVLANNRRDAEEWfAAQTEELNQQQMSSA 295
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERL-ANLERQL---------EELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 296 EQLQGCQTEMLELKRTANTLEIELQAQQTLTESLECTVAETEAQYSTQLAQMQCLIDSVEHQLAEIRcDLERQNQEYKvl 375
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAE-- 434
|
250 260
....*....|....*....|....*.
gi 57012428 376 ldtKARLECEINTYRGLLEKEDSRLP 401
Cdd:TIGR02168 435 ---LKELQAELEELEEELEELQEELE 457
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
228-381 |
9.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012428 228 EEEVNLLREQLgDRLNVELDtaptvDLNKVLDEMRCQYERvLANNRRDAEEwfaaQTEELNQQQMSSAEQLQGCQTEMLE 307
Cdd:COG4372 44 QEELEQLREEL-EQAREELE-----QLEEELEQARSELEQ-LEEELEELNE----QLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57012428 308 LKRTANTLEIELQAQQTLTESLECTVAETEAQYSTQLAQmqclIDSVEHQLAEIRCDLERQNQEYKVLLDTKAR 381
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE----LKELEEQLESLQEELAALEQELQALSEAEAE 182
|
|
| |
