|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
11-318 |
9.49e-25 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 106.93 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 11 EKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAE-EARSLRQQLDELSWATALAEGERDALR 89
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEkEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 90 RELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRAR 169
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 170 AtgpaAPPPRL----REVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLE 245
Cdd:pfam00038 162 A----ARKLDLtsalAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112382237 246 QLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGE 318
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-316 |
6.30e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 55 EGQARCAEEARSLRQQLDELSWATALAEgeRDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALL 134
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 135 GRLQAERRGLDAAHERDVRELRARAASLTmhfRARAtgpaapppRLREvhdsyALLVAESWRETVQLYEDEVRELEEALR 214
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRR---ELEE--------RLEE-----LEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 215 RGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEygiQAEERQRVIDcLEDEKATLTLAMADWLRDY 294
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA---AAELAAQLEE-LEEAEEALLERLERLEEEL 423
|
250 260
....*....|....*....|..
gi 112382237 295 QDLLQVKTGLSLEVATYRALLE 316
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALE 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-317 |
9.40e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 57 QARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGR 136
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 137 LQAERRGLDAAHERDVRELRARAASLTMHFRARAtgpaappPRLREVHDSYALLVAEswRETVQLYEDEVRELEEALRRG 216
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELA-------EAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 217 QESRLQAEEETrlcAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDcLEDEKATLTLAMADWLRDYQD 296
Cdd:COG1196 413 LERLERLEEEL---EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAE 488
|
250 260
....*....|....*....|.
gi 112382237 297 LLQVKTGLSLEVATYRALLEG 317
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEG 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-271 |
3.32e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 11 EKAELQELNARLYdyvcrvrelerenllleeelrGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRR 90
Cdd:COG1196 279 LELELEEAQAEEY---------------------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 91 ELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERrgldAAHERDVRELRARAASLTMHFRARA 170
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL----LEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 171 tgpaapppRLREVHDSYallvAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRAR 250
Cdd:COG1196 414 --------ERLERLEEE----LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|.
gi 112382237 251 LEDALLRMREEYGIQAEERQR 271
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-297 |
9.19e-10 |
|
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: 63.92 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 63 EARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERR 142
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 143 GLDAAHErdvrELRARAASLTMHFRARATGPAAPPPRLREVHDSyallvAESWRETVQLYEDEVRELEEALRRGQESRLQ 222
Cdd:TIGR02168 758 ELEAEIE----ELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-----LKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112382237 223 AEEETRLCAQEAEALRREALGLEQLRARLEDALlrmrEEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDL 297
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
62-261 |
2.43e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSWATALAEgERDALRRELRELQRLDA-----EERAARGRLDAELGAQQRELQEALGARAALEALLGR 136
Cdd:COG4913 242 EALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 137 LQAERRGLDAAHE----RDVRELRARAASLTmhfRARAtgpaapppRLREVHDSYALLV----------AESWRETVQLY 202
Cdd:COG4913 321 LREELDELEAQIRgnggDRLEQLEREIERLE---RELE--------ERERRRARLEALLaalglplpasAEEFAALRAEA 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 112382237 203 EDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREE 261
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-283 |
7.48e-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: 60.84 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 57 QARCAEEARSLRQQLDELSWATAL-------------------AEGERDALRRELRELQRLDAEERAARGRLDAELGAQQ 117
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVlrleelreeleelqeelkeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 118 RELQEALGARAALEALLGRLQAERRGLDAAHER-------------------------------DVRELRARAASLTMHF 166
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEEleaqleeleskldelaeelaeleekleelkeELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 167 RARATGPAAPPPRLREVHDSYALLV--AESWRETVQLYEDEVRELEEalRRGQESRLQAEEETRLCAQEAEALRREALGL 244
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLElqIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 112382237 245 EQLRARLEDALLRMREEYGIQAEER---QRVIDCLEDEKATL 283
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELeeaEQALDAAERELAQL 487
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
49-318 |
1.56e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.65 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 49 REGLWAE--------GQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQREL 120
Cdd:COG3903 563 EGRRWLEralaaageAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAA 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 121 QEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQ 200
Cdd:COG3903 643 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAA 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 201 LYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEK 280
Cdd:COG3903 723 AAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAA 802
|
250 260 270
....*....|....*....|....*....|....*...
gi 112382237 281 ATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGE 318
Cdd:COG3903 803 AAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAA 840
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-319 |
1.20e-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: 55.93 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 54 AEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRldaeeraargrldaELGAQQRELQEALGARAALEAL 133
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--------------RIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 134 LGRLQAERRGLDAAHERDVRELRARAASLTMHFRaratgpaAPPPRLrevhdsyaLLVAESWRETV---QLYEDEVRELE 210
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGR-------QPPLAL--------LLSPEDFLDAVrrlQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 211 EALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALlrmreeygiqaEERQRVIDCLEDEKATLTLAMADW 290
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-----------AERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*....
gi 112382237 291 LRDYQDLLQVKTGLSLEVATYRALLEGES 319
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
54-336 |
4.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 54 AEGQARCAEEARSLRQQLDELSWATALAEGERDALRREL-RELQRLDAEERAA-------RGRLDAELGAQQRELQEALG 125
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELaEAAARLLLLLEAEadyegflEGVKAALLLAGLRGLAGAVA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 126 ARAALEALLGRLQAERRGLDAAH--ERDVRELRARAASLTMHFRARAT---------GPAAPPPRLREVHDSYALLVAES 194
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAAVDLVASD 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 195 WRE----------TVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGI 264
Cdd:COG1196 608 LREadaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112382237 265 QAEERQRVID---CLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESNPEIVIWAEHVENMPSE 336
Cdd:COG1196 688 LAEEELELEEallAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-299 |
1.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 85 RDALRRELRELQRLDAEERAARGRLDAELgAQQRELQEALGAR----------AALEALLGRLQAERRGLDAAHErDVRE 154
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLaeyswdeidvASAEREIAELEAELERLDASSD-DLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 155 LRARAAsltmhfRARAtgpaapppRLREVHDSYALLVAESWR--ETVQLYEDEVRELEEALRRGqESRLQAEEETRLCAQ 232
Cdd:COG4913 690 LEEQLE------ELEA--------ELEELEEELDELKGEIGRleKELEQAEEELDELQDRLEAA-EDLARLELRALLEER 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112382237 233 EAEALRREAlgLEQLRARLEDALLRMREEygiQAEERQRVIDCLEDEKATLTLAMADW------LRDYQDLLQ 299
Cdd:COG4913 755 FAAALGDAV--ERELRENLEERIDALRAR---LNRAEEELERAMRAFNREWPAETADLdadlesLPEYLALLD 822
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
53-331 |
1.40e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 53.10 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 53 WAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAA---------------RGRLDAELGA-Q 116
Cdd:COG3903 497 YYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAalapfwflrgllregRRWLERALAAaG 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 117 QRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWR 196
Cdd:COG3903 577 EAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 197 ETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCL 276
Cdd:COG3903 657 AAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAAL 736
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 112382237 277 EDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESNPEIVIWAEHVE 331
Cdd:COG3903 737 AAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
90-304 |
1.95e-06 |
|
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: 50.69 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 90 RELRELQRLDAEE---RAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLdaahERDVRELRARAAsltmhf 166
Cdd:COG1579 7 RALLDLQELDSELdrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 167 RARAtgpaapppRLREVHDSyallvaeswREtvqlYEDEVRELEEALRRgqesRLQAEEETRLCAQEAEALRREALGLEQ 246
Cdd:COG1579 77 KYEE--------QLGNVRNN---------KE----YEALQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 112382237 247 LRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAM-ADWLRDYQDLLQVKTGL 304
Cdd:COG1579 132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERIRKRKNGL 190
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-283 |
2.01e-06 |
|
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: 52.76 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 58 ARCAEEARSLRQQLDELSWATALAEGErdaLRRELRELQRLDAEERAARGRLdAELGAQQRELQEalgARAALEALLGRL 137
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQEEEKLKERL-EELEEDLSSLEQ---EIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 138 QAERrgldAAHERDVRELRARAASLTMHFRaratgpaapPPRLREVHDSYallvaESWRETVQLYEDEVRELEEALRRGQ 217
Cdd:TIGR02169 764 EARI----EELEEDLHKLEEALNDLEARLS---------HSRIPEIQAEL-----SKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112382237 218 ESRLQAEEETrlcaQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATL 283
Cdd:TIGR02169 826 LEKEYLEKEI----QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-279 |
2.66e-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: 52.37 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 12 KAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRE 91
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 92 LRELQRLDAEERAARGRLDAELGAQQRELQ----EALGARAALEALLGRLQAERRGLDAAHERdVRELRARAASLTmHFR 167
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTllneEAANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLA-AEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 168 ARATgpaAPPPRLREVHDSyALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQL 247
Cdd:TIGR02168 862 EELE---ELIEELESELEA-LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270
....*....|....*....|....*....|..
gi 112382237 248 RARLEDALlrmREEYGIQAEERQRVIDCLEDE 279
Cdd:TIGR02168 938 IDNLQERL---SEEYSLTLEEAEALENKIEDD 966
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-269 |
3.41e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 89 RRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLtmhfra 168
Cdd:COG4913 595 RRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER------ 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 169 ratgpaapppRLREVHDSYALLVAESwrETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREalgLEQLR 248
Cdd:COG4913 669 ----------EIAELEAELERLDASS--DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQ 733
|
170 180
....*....|....*....|.
gi 112382237 249 ARLEDALLRMREEYGIQAEER 269
Cdd:COG4913 734 DRLEAAEDLARLELRALLEER 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-253 |
6.18e-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: 51.21 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 5 RLQTGPEKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGE 84
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 85 RDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTm 164
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 165 hfraratgpaapPPRLREVHDSyallVAESWRETVQLYEdEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGL 244
Cdd:TIGR02168 432 ------------EAELKELQAE----LEELEEELEELQE-ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
....*....
gi 112382237 245 EQLRARLED 253
Cdd:TIGR02168 495 ERLQENLEG 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
58-261 |
8.93e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 58 ARCAEEARSLRQQLDEL----SWATALAEgERDALRRELRELQRLDAEERAARGRLDAELGA---QQRELQEALGARAAL 130
Cdd:COG4913 664 ASAEREIAELEAELERLdassDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQaeeELDELQDRLEAAEDL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 131 EALLGRLQAERR----GLDAAHERDVRELRARAASL-TMHFRARAtgpaapppRLREVHDSYallvAESWRETVQLYEDE 205
Cdd:COG4913 743 ARLELRALLEERfaaaLGDAVERELRENLEERIDALrARLNRAEE--------ELERAMRAF----NREWPAETADLDAD 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 112382237 206 VRELEEALRRGQesRLQAEEETRLCAQEAEALRREALG-LEQLRARLEDALLRMREE 261
Cdd:COG4913 811 LESLPEYLALLD--RLEEDGLPEYEERFKELLNENSIEfVADLLSKLRRAIREIKER 865
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-309 |
1.00e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 11 EKAELQELNARLydyvcrvrELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRR 90
Cdd:COG1196 450 EEAELEEEEEAL--------LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 91 ELRELQRLDAEERAARGRLDAELGA--QQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRA 168
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 169 RATGPAAPPPRLREVHDSYALLVAESW-----------RETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEAL 237
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVaarleaalrraVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112382237 238 RREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDcLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVA 309
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLE-EELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
69-256 |
1.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 69 QQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLdAELGAQQRELQEALGARAA---LEALLGRLQAERRGLD 145
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLLQLLPLyqeLEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 146 AAHERdVRELRARAASLTMHFRARAtgpaapppRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEE 225
Cdd:COG4717 150 ELEER-LEELRELEEELEELEAELA--------ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190
....*....|....*....|....*....|.
gi 112382237 226 ETRLCAQEAEALRREALgLEQLRARLEDALL 256
Cdd:COG4717 221 ELEELEEELEQLENELE-AAALEERLKEARL 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-289 |
1.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 1 MLSWRLQTGPEKAELQELNARLYDYVCRVrelerenllleEELRGRRGREGLWAEGQARCAEEARSLRQQLDELswATAL 80
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERL-----------EELEERLEELRELEEELEELEAELAELQEELEEL--LEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 81 AEGERDALRRELRELQRLDAEERAARgrldAELGAQQRELQEALGARAALEALLGRLQAERRgLDAAherdvrELRARAA 160
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELE----EELEEAQEELEELEEELEQLENELEAAALEER-LKEA------RLLLLIA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 161 SLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRRE 240
Cdd:COG4717 256 AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 112382237 241 ALGLEQLRARLEDALLRMREeygIQAEERQRVIDCLEDEKATLtLAMAD 289
Cdd:COG4717 336 PEELLELLDRIEELQELLRE---AEELEEELQLEELEQEIAAL-LAEAG 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
64-177 |
2.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 64 ARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRG 143
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
90 100 110
....*....|....*....|....*....|....
gi 112382237 144 LDAAHERDVRELRARAASLTMHFRARATGPAAPP 177
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAALKGKLPWP 258
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
53-161 |
3.37e-05 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 48.43 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 53 WAEGQARCAEEARSLRQQLDEL-SWATALAE----GERDALRRELRELQRLDAEERAARGRLDAELGAqqrELQEALGAR 127
Cdd:pfam04632 241 LARLRTEGAGTVPELAALLDELaAWEAALAAealqAALAALRARLRALRPALPLDFDTAAELLARLAD---LLAELAEAL 317
|
90 100 110
....*....|....*....|....*....|....
gi 112382237 128 AALEALLGRLQAERRGLDAAHERDVRELRARAAS 161
Cdd:pfam04632 318 ASCRALRHPIAQGARPARLARHRDHGAALLNGLR 351
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-273 |
3.58e-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: 48.53 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAER 141
Cdd:TIGR02169 287 EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 142 RGLdaahERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQL---------YEDEVRELEEA 212
Cdd:TIGR02169 367 EDL----RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELadlnaaiagIEAKINELEEE 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112382237 213 LRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYgIQAEERQRVI 273
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-AEAEAQARAS 502
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
66-162 |
7.55e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 66 SLRQQLDELSWATALAEGERDALRRELRELQRL--DAEERAarGRLDAELGAQQRELQEALGARAAL----EALLGRLQA 139
Cdd:PRK09039 78 DLQDSVANLRASLSAAEAERSRLQALLAELAGAgaAAEGRA--GELAQELDSEKQVSARALAQVELLnqqiAALRRQLAA 155
|
90 100
....*....|....*....|...
gi 112382237 140 ERRGLDAAHERDvRELRARAASL 162
Cdd:PRK09039 156 LEAALDASEKRD-RESQAKIADL 177
|
|
| CHAD |
smart00880 |
The CHAD domain is an alpha-helical domain functionally associated with some members of the ... |
65-214 |
1.09e-04 |
|
The CHAD domain is an alpha-helical domain functionally associated with some members of the adenylate cyclase family; It has conserved histidines that may chelate metals.
Pssm-ID: 214880 [Multi-domain] Cd Length: 262 Bit Score: 45.85 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 65 RSLRQQLDELswataLAEGERDALRRELRELQRLDAEERAargrLDAELGAQQRELQEALGARAALEALLGRLQAERrgl 144
Cdd:smart00880 36 RSALRLFRPV-----LPREAAAALRAELRWLARELGPLRD----LDVLLERLLELLAALLPELPALDALVAALEARR--- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112382237 145 DAAHERDVRELRARAASLTMH-----FRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALR 214
Cdd:smart00880 104 AAARRALLAALDSARYTALLLdlsrwLATPPWQPAADDKAARPLADFAAKALRRLLRKLRRAFPAARALLDDEAL 178
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
62-313 |
1.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSWATALAEGERDALRReLRELQRLDAEERAARGRLDA-ELGAQQRELQEALGARAALEALLGRLQAE 140
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 141 RRGLDAAherdVRELRARAASLtmhfraratgpaappprlrevhdsyallvaeswretvqlyEDEVRELEEALRR---GQ 217
Cdd:COG4913 304 LARLEAE----LERLEARLDAL----------------------------------------REELDELEAQIRGnggDR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 218 ESRLQAEEETRlcAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDL 297
Cdd:COG4913 340 LEQLEREIERL--ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
250
....*....|....*.
gi 112382237 298 LQVKTGLSLEVATYRA 313
Cdd:COG4913 418 RRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-262 |
1.47e-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: 46.59 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 45 GRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEAL 124
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 125 GARAALEALLGRLQAERRGLdaahERDVRELRARAASLTMHF---RARATGPAAPPPRLREVHDSYALLVAESWRETVQL 201
Cdd:TIGR02168 365 AELEELESRLEELEEQLETL----RSKVAQLELQIASLNNEIerlEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112382237 202 YEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALG-LEQLRARLeDALLRMREEY 262
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEReLAQLQARL-DSLERLQENL 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-289 |
1.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 85 RDALRRELRELQRLDAEERAargRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAhERDVRELRARAASLTm 164
Cdd:COG4717 48 LERLEKEADELFKPQGRKPE---LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-EAELEELREELEKLE- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 165 hfraratgpaapppRLREVHDSYallvaESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGL 244
Cdd:COG4717 123 --------------KLLQLLPLY-----QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 112382237 245 EQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMAD 289
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
54-316 |
1.60e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.50 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 54 AEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEAL 133
Cdd:COG4995 189 AALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAAALLLLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 134 LGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEAL 213
Cdd:COG4995 269 ALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAAALLAAA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 214 RRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRD 293
Cdd:COG4995 349 LAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAA 428
|
250 260
....*....|....*....|....*....
gi 112382237 294 YQDLLQ------VKTGLSLEVATYRALLE 316
Cdd:COG4995 429 RLALLAlieyiiLPDRLYAFVQLYQLLIA 457
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
62-260 |
2.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSWATALAEGERDALRRELREL--QRLDAEERAARGRLDAELGAQQrelQEALGARaaLEALLGRLQA 139
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLreRLEELEEERDDLLAEAGLDDAD---AEAVEAR--REELEDRDEE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 140 ERRGLD------AAHERDVRELRARAASLtmhfRARATGPAAPPPRLREVHDSYALLVAESwRETVQLYEDEVRELEEAL 213
Cdd:PRK02224 326 LRDRLEecrvaaQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERF 400
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 112382237 214 RRGQESRLQAEEETRLCAQEAEALRREalgLEQLRARLEDALLRMRE 260
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELRER---EAELEATLRTARERVEE 444
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
59-282 |
3.66e-04 |
|
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: 45.11 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 59 RCAEEARSLRQQLDELSwATALAEGERDALRRElRELQRLDAEERAARgrldaelgaQQRELQEALGARAALEALLGRLQ 138
Cdd:pfam17380 316 RKLEEAEKARQAEMDRQ-AAIYAEQERMAMERE-RELERIRQEERKRE---------LERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 139 AERRgldAAHERDVRELRA-RAASLTMHFRARATgpaapPPRLREVHDSYALLVAESWRETVQLYEDEVRELE-----EA 212
Cdd:pfam17380 385 MERQ---QKNERVRQELEAaRKVKILEEERQRKI-----QQQKVEMEQIRAEQEEARQREVRRLEEERAREMErvrleEQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112382237 213 LRRGQESRL-QAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKAT 282
Cdd:pfam17380 457 ERQQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
57-282 |
4.27e-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: 45.33 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 57 QARCA-EEARSLrQQLDELSWATAlaEGERDALRRELREL--QRLDAEERAArgrlDAELGAQQRElqEALgarAALEAL 133
Cdd:COG3096 417 QAVQAlEKARAL-CGLPDLTPENA--EDYLAAFRAKEQQAteEVLELEQKLS----VADAARRQFE--KAY---ELVCKI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 134 LGRLQAERRGlDAAHE--RDVRELRARAASLTmHFRARAtgpAAPPPRLREVHDSYALLVAESWRETVQLyeDEVRELEE 211
Cdd:COG3096 485 AGEVERSQAW-QTAREllRRYRSQQALAQRLQ-QLRAQL---AELEQRLRQQQNAERLLEEFCQRIGQQL--DAAEELEE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 212 ALRRGQESRLQAEEETRLCAQEAEALRREalgLEQLRAR-------------LEDALLRMREEYGIQAEERQRVIDC--- 275
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAVEQRSELRQQ---LEQLRARikelaarapawlaAQDALERLREQSGEALADSQEVTAAmqq 634
|
....*...
gi 112382237 276 -LEDEKAT 282
Cdd:COG3096 635 lLEREREA 642
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-594 |
4.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 192 AESWRETVQLYEDEVRELEEALRRGQESRlQAEEETRlcAQEA----EALRREALGLEQLRARLEDAllrMREEYGIQAE 267
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDAR-KAEEARK--AEDArkaeEARKAEDAKRVEIARKAEDA---RKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 268 ERQRVidclEDEKATLTLAMADWLRDYQDLLQVKTGLSLE---VATYRALLEGESNPEIVIWAEHVENMPSEFRnksyhy 344
Cdd:PTZ00121 1174 DAKKA----EAARKAEEVRKAEELRKAEDARKAEAARKAEeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK------ 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 345 tdsllQRENERNLFSRQKAPLASFNHSSALYSNLSGHrgsqtgtsiggDARRgflgsgySSSATTQQENSYGKAVSSQTN 424
Cdd:PTZ00121 1244 -----KAEEERNNEEIRKFEEARMAHFARRQAAIKAE-----------EARK-------ADELKKAEEKKKADEAKKAEE 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 425 VRTFSPtygLLRNTEAQVKTFPDRPKAGDTREVPVYIGEDSTIARESYRDRRDKVAAGASESTRSNErtvilgKKTEVKA 504
Cdd:PTZ00121 1301 KKKADE---AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE------KAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 505 TREQERNRPETIRTKPEE-KMFDSKEKASEERNLRWEELTKldKEARQRESQQMKEKAKEK---DSPKEKSVREREV-PI 579
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEkKKADEAKKKAEEDKKKADELKK--AAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKAdEA 1449
|
410
....*....|....*
gi 112382237 580 SLEVSQDRRAEVSPK 594
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKK 1464
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-163 |
6.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 57 QARCAEEARSLRQQLDELSWAtalAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGR 136
Cdd:COG4913 354 LEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
90 100
....*....|....*....|....*..
gi 112382237 137 LQAeRRGLDAAHERDVRELRARAASLT 163
Cdd:COG4913 431 LER-RKSNIPARLLALRDALAEALGLD 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
58-262 |
7.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 58 ARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLD-AELGAQQRELQEALGArAALEALLGR 136
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAGV-EDEEELRAA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 137 LQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLvaeswRETVQLYEDEVRELEEALRR- 215
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL-----EEELEELREELAELEAELEQl 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 112382237 216 ---GQESRLQAEEETRLcaQEAEALRREALGLEQLRARLEDALLRMREEY 262
Cdd:COG4717 466 eedGELAELLQELEELK--AELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
53-295 |
8.94e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 44.06 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 53 WAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEA 132
Cdd:COG0553 2 LLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 133 LLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEA 212
Cdd:COG0553 82 LLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 213 LRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQR--VIDCLEDEKATLTLAMADW 290
Cdd:COG0553 162 LLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDafRLRRLREALESLPAGLKAT 241
|
....*
gi 112382237 291 LRDYQ 295
Cdd:COG0553 242 LRPYQ 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
62-251 |
1.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSWATALAEGERDALRRELRELQRLDA--EERAARGRLDAELGAQQRELQEALGARAALEALLGRLQa 139
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELE- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 140 errgldaAHERDVRELRARAASLTMHFRARAtgpaappprlrEVHDSYALLVAESWRETVQLYEDEVRELEEALRRgQES 219
Cdd:COG4717 167 -------ELEAELAELQEELEELLEQLSLAT-----------EEELQDLAEELEELQQRLAELEEELEEAQEELEE-LEE 227
|
170 180 190
....*....|....*....|....*....|..
gi 112382237 220 RLQAEEETRLCAQEAEALRREALGLEQLRARL 251
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAAALL 259
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
55-258 |
1.02e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 55 EGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQrldAEERaargRLDAELGAQQRELQEALGARAALEALL 134
Cdd:pfam15921 755 EAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR---SQER----RLKEKVANMEVALDKASLQFAECQDII 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 135 GRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREV--HDSYALLVAESWRETVQLYEDEVRELEEA 212
Cdd:pfam15921 828 QRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVpsSQSTASFLSHHSRKTNALKEDPTRDLKQL 907
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 112382237 213 LrrgQESRLQAEEETRLCAQEAEALRReALGLEQLRARLEDALLRM 258
Cdd:pfam15921 908 L---QELRSVINEEPTVQLSKAEDKGR-APSLGALDDRVRDCIIES 949
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
62-253 |
1.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSwatALAEgERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEAlgarAALEALLGRLQAER 141
Cdd:PRK04863 496 DVARELLRRLREQR---HLAE-QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 142 RGLDAAherdVRELRARAASLTMH---FRARATGPAAPPPRLREVHDSYALLVAESWR--ETVQLYEDEVRELEEALRRG 216
Cdd:PRK04863 568 ESLSES----VSEARERRMALRQQleqLQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQDVTEYMQQLLEREREL 643
|
170 180 190
....*....|....*....|....*....|....*...
gi 112382237 217 QESRLQAEEETRLCAQEAEAL-RREALGLEQLRARLED 253
Cdd:PRK04863 644 TVERDELAARKQALDEEIERLsQPGGSEDPRLNALAER 681
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
61-163 |
1.44e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 61 AEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARG---------RLDAELGAQQRELQEALG------ 125
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPellqspviqQLRAQLAELEAELAELSArytpnh 290
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 112382237 126 -----ARAALEALLGRLQAERRGLDAAHERDVRELRARAASLT 163
Cdd:COG3206 291 pdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQ 333
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
62-298 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 62 EEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAER 141
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 142 RGLDAAH-ERDVRELRARAASLTMHFRARATGPAAPPPRLREVHD-SYALLVAESWRETVQ---LYEDEVRELEEALRRG 216
Cdd:COG4372 174 QALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEeLLEAKDSLEAKLGLAlsaLLDALELEEDKEELLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 217 QESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQD 296
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
..
gi 112382237 297 LL 298
Cdd:COG4372 334 IL 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-280 |
1.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 54 AEGQARCAEEAR---SLRQQLDELSWATALAEGERDAlRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAAL 130
Cdd:PTZ00121 1459 AEEAKKKAEEAKkadEAKKKAEEAKKADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 131 EAllgRLQAERRGLD----------AAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYallvaeswRETVQ 200
Cdd:PTZ00121 1538 EA---KKAEEKKKADelkkaeelkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY--------EEEKK 1606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 201 LYEDEVRELEEALRRGQESRlQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEK 280
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
137-290 |
1.98e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 42.66 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 137 LQAERRGL-DAAH---ERDVRELRARAASLTMHFRARAtgPAAPPPRLREVHDSYALLVAEswRETVQLYEDEVRELEEA 212
Cdd:pfam04632 508 LRALRRDLaRAARrraAGARARFESRMLDRLAQLAPRL--AAAPPARRRALRDGLAALRLG--RAVIRLRRALARALPAP 583
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112382237 213 LRRGQESRLQAEEETRLCAQEAEALRRealgLEQLRARLEDALLRMREEygIQAEERQRVIDCLEDekatLTLAMADW 290
Cdd:pfam04632 584 ARAALDRVLRALARAPAAGRLARRLRA----PARLLRELDAALAALAAD--GAPSALRRALAALHF----LRLALLDP 651
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-261 |
2.17e-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: 42.74 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 3 SWRLQTGPEKAELQELNARLYDYVCRVRELERENllleeelrgrrgreglwaegqARCAEEARSLRQQLDELSWATALAE 82
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRI---------------------AATERRLEDLEEQIEELSEDIESLA 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 83 GERDALRRELRELQR-------LDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERrgldAAHERDVREL 155
Cdd:TIGR02168 859 AEIEELEELIEELESeleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGL 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 156 RARAASLTMHFRARATGPAAPPPRLrevhdsYALLVAESwretvQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAE 235
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEAL------ENKIEDDE-----EEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
250 260
....*....|....*....|....*.
gi 112382237 236 ALRREALGLEQLRARLEDALLRMREE 261
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
53-311 |
2.39e-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: 42.52 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 53 WAEGQARCAEEARSLRQQldelswATALAEGERDAlrrelrELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEA 132
Cdd:pfam12128 701 WLEEQKEQKREARTEKQA------YWQVVEGALDA------QLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 133 LLGRLQAERRGLDAAHErdvrelraraasltmhfRARATGPAAppprlREVHDSYallvAESWRETVQLYEDEVRELEEA 212
Cdd:pfam12128 769 VIAKLKREIRTLERKIE-----------------RIAVRRQEV-----LRYFDWY----QETWLQRRPRLATQLSNIERA 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 213 LR--RGQESRLQAEEETRLCAqeaealrrealgLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKA-TLTLAMAD 289
Cdd:pfam12128 823 ISelQQQLARLIADTKLRRAK------------LEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSeQAQGSIGE 890
|
250 260
....*....|....*....|..
gi 112382237 290 WLRDYQDLLQVKTGLSLEVATY 311
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVKKY 912
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
53-256 |
2.50e-03 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 41.82 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 53 WAEGQARCAEEA--RSLRQQLDELSWATALAE-----GERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALg 125
Cdd:COG3071 27 LAEGRYARAEKLlsKAAEHSEAPLLAYLLAARaaqalGDYERRDEYLAQALELAPEAELAVLLTRAELLLDQGQAEQAL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 126 arAALEALLG-----------RLQAER---------------RGLDAAHERDVRELRARAAslTMHFRARATGPAAP--- 176
Cdd:COG3071 106 --ATLEALRAgaprhpqvlrlLLQAYRqlgdweellellpalRKHKALSAEEAQALERRAY--LGLLRQAARDAEALkal 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 177 ----PPRLREvHDSYALLVAESWREtVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRRealgLEQ-LRARL 251
Cdd:COG3071 182 wkalPRAERR-DPELAAAYARALIA-LGDHDEAERLLREALKRQWDPRLVRLYGRLQGGDPAKQLKR----AEKwLKKHP 255
|
....*
gi 112382237 252 EDALL 256
Cdd:COG3071 256 NDPDL 260
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
57-615 |
2.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 57 QARCAEEARslRQQLDELSWATALAEGERDA-LRRELRELQRLDAEERAARGRLDAELgaqqRELQEALGARAALEAL-L 134
Cdd:PTZ00121 1138 DARKAEEAR--KAEDAKRVEIARKAEDARKAeEARKAEDAKKAEAARKAEEVRKAEEL----RKAEDARKAEAARKAEeE 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 135 GRLQAERRGLDAAHERDVREL-----RARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETvqlyeDEVREL 209
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-----DELKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 210 EEaLRRGQESRlQAEEETRlcAQEAEALRREALGLEQLRARLEDALlRMREEYGIQAEERQRVIDCL--EDEKATLTLAM 287
Cdd:PTZ00121 1287 EE-KKKADEAK-KAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAK-KKADAAKKKAEEAKKAAEAAkaEAEAAADEAEA 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 288 ADWLRDYQDLLQVKTGLSLEVATYRAllegesnpEIVIWAEHVENMPSEFRNKSyhytDSLLQRENERNLFSRQKAPLAS 367
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKA--------EEKKKADEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEE 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 368 FNHSSALYSNLSGHRGSQTGTSIGGDARRGFLGSGYSSSATTQQE-----NSYGKAVSSQTNVRTFSPTYGLLRNTEAQV 442
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 443 KTFPDRPKAGDTREV-PVYIGEDSTIARESYRDRRDKVA---------------AGASESTRSNERTVILGKKTEVKATR 506
Cdd:PTZ00121 1510 KKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKAdelkkaeelkkaeekKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 507 EQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKlDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEV--- 583
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeak 1668
|
570 580 590
....*....|....*....|....*....|....*
gi 112382237 584 ---SQDRRAEVSPKGLQTPVKDAGGGTGREAEARE 615
Cdd:PTZ00121 1669 kaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
66-298 |
2.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 66 SLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQA------ 139
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 140 ERRGLDAAHERDVRE----LRARAASLTMHFR--------ARATGPAAPPPRL-REVHDSYALLVAESWRETVQLYEDEV 206
Cdd:PRK02224 405 VDLGNAEDFLEELREerdeLREREAELEATLRtarerveeAEALLEAGKCPECgQPVEGSPHVETIEEDRERVEELEAEL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 207 RELE-----------------EALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMRE------EYG 263
Cdd:PRK02224 485 EDLEeeveeveerleraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkreaaaEAE 564
|
250 260 270
....*....|....*....|....*....|....*
gi 112382237 264 IQAEERQRVIDCLEDEKATLTLAMaDWLRDYQDLL 298
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERI-ESLERIRTLL 598
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
58-156 |
2.86e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 58 ARCAEEARSLR----QQLDELSWATALA---EGERDALRRELRELQRLDAEERAARGRLDAELGAQ----------QREL 120
Cdd:pfam19220 170 ALLEQENRRLQalseEQAAELAELTRRLaelETQLDATRARLRALEGQLAAEQAERERAEAQLEEAveahraerasLRMK 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 112382237 121 QEALGAR-AALEALLGRLQ------------AERRGLDAAHERDVRELR 156
Cdd:pfam19220 250 LEALTARaAATEQLLAEARnqlrdrdeairaAERRLKEASIERDTLERR 298
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-210 |
2.99e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 57 QARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLgR 136
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE-R 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112382237 137 LQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLrEVHDSYALLVAESWRETVQLYEDEVRELE 210
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPDLEELERELERLEREIEALG 780
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
28-240 |
3.15e-03 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 41.81 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 28 RVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARG 107
Cdd:COG3920 89 LLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 108 RLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSY 187
Cdd:COG3920 169 ALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRAR 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 112382237 188 ALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRRE 240
Cdd:COG3920 249 GLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRE 301
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-576 |
3.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 54 AEGQARCAEEARslrqQLDELSWATALAEGERDALRRELRELQRLD----AEERAARGRLDAELGAQQRELQEALGARAA 129
Cdd:PTZ00121 1304 ADEAKKKAEEAK----KADEAKKKAEEAKKKADAAKKKAEEAKKAAeaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 130 LEALLGRLQAERRGLDAahERDVRELRARAASLTMHFRARATGPAAPPPrlrevhdsyallvAESWRETvqlyeDEVREL 209
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEA--KKKAEEDKKKADELKKAAAAKKKADEAKKK-------------AEEKKKA-----DEAKKK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 210 EEALRRGQESRLQAEEETRlcAQEAEALRREALGLEQLRARLEDAllRMREEYGIQAEERQRVIDclEDEKATLTLAMAD 289
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKK--AEEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKAD--EAKKAAEAKKKAD 1513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 290 WLRDYQdllQVKTGLSLEVATYRALLEGESNPEIVIWAEHVENMPSEFRNKSYHYTDSLLQRENERNLFSRQ-----KAP 364
Cdd:PTZ00121 1514 EAKKAE---EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeakKAE 1590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 365 LASFNHSSALYSNLSGHRGSQtgtsiggdARRgflgsgysssatTQQENSYGKAVSSQTNVRtfSPTYGLLRNTEAQVKt 444
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEE--------AKK------------AEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKK- 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 445 fpdrpKAGDTREvpvyigedstiARESYRDRRDKVAAGASESTRSNErtvilgkktEVKATREQERNRPETIRTKPEEKM 524
Cdd:PTZ00121 1648 -----KAEELKK-----------AEEENKIKAAEEAKKAEEDKKKAE---------EAKKAEEDEKKAAEALKKEAEEAK 1702
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 112382237 525 FDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVRERE 576
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
|
| DICT |
pfam10069 |
Sensory domain in DIguanylate Cyclases and Two-component system; DICT is a sensory domain ... |
1115-1196 |
3.96e-03 |
|
Sensory domain in DIguanylate Cyclases and Two-component system; DICT is a sensory domain found associated with GGDEF, EAL, HD-GYP, STAS, and two component systems (histidine-kinase type). It assumes an alpha+beta fold with a 4-stranded beta-sheet and might have a role in light response (Natural history of sensor domains in bacterial signaling systems by Aravind L, LM Iyer, Anantharaman V, from 'Sensory Mechanisms in Bacteria: Molecular Aspects of Signal Recognition.' Caister Academic Press. 2010) - see (http://de.scribd.com/doc/28576661/Bacterial-Signaling-Chapter)
Pssm-ID: 431029 Cd Length: 126 Bit Score: 39.15 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 1115 QVLEDVSQAARHIKLGPSEVWRTERMSYE--GPTAEVVEVSAGGDlSQAASPTGASRSVRHVTLGPGQSPLSRE--VIFL 1190
Cdd:pfam10069 37 LLIEQQIPATVWAKFQRGKFYRQEADRYQqlAQKSRQIYVCAAPE-SEFAEPDSSSDNVETVALDPNSDPLRREwfLIVL 115
|
....*.
gi 112382237 1191 GPAPAC 1196
Cdd:pfam10069 116 SPQFCS 121
|
|
| CHAD |
COG5607 |
CHAD domain, binds inorganic polyphosphates [Function unknown]; |
65-296 |
4.26e-03 |
|
CHAD domain, binds inorganic polyphosphates [Function unknown];
Pssm-ID: 444338 [Multi-domain] Cd Length: 284 Bit Score: 40.84 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 65 RSLRQQLdelswATALAEGERDALRRELRELQRL-----DAEerAARGRLDAELGAQQRELQEALgaraalEALLGRLQA 139
Cdd:COG5607 47 RSLLRLF-----RPVLPRPKLAALRRELRDLARAlgplrDLD--VLLETLEALAAALPEEERPAL------ARLLARLEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 140 ERRgldAAHERDVRELR-ARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWREtVQLYEDEVRELEEA-----L 213
Cdd:COG5607 114 RRE---AARAKLLAALDsARYQRLLAALEEWLARPPWRDRADKPLRDLLAKRLARRYRR-LRKAGAALDLDADDeelheL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 214 R-RGQESRLQAEEETRLCAQEAEALRR------EALGLEQ----LRARLEDALLRMREEygIQAEERQRVIDCLEDEKAT 282
Cdd:COG5607 190 RkAAKRLRYALELFAPLYPEKLKALLKalkalqDLLGDHHdlavLRELLRDLAAEAGLA--PELPALGALLALLRARRER 267
|
250
....*....|....
gi 112382237 283 LTLAMADWLRDYQD 296
Cdd:COG5607 268 LRAELLELWRRLLA 281
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-317 |
4.44e-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: 41.98 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 67 LRQQLDELSWATALAEgERDALRRELRELQrldAEERAArgrldaELGAQQRELQEALGARAALEALLGRLQAERRGLD- 145
Cdd:TIGR02169 196 KRQQLERLRREREKAE-RYQALLKEKREYE---GYELLK------EKEALERQKEAIERQLASLEEELEKLTEEISELEk 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 146 --AAHERDVRELRARAASLTMHFRARATgpaappPRLREVHDSYALLvaeswretvqlyEDEVRELEEALRRGQESRLQA 223
Cdd:TIGR02169 266 rlEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGELEAEIASL------------ERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 224 EEETRLCAQEAEAL---------RREALG--LEQLRARLEDALLRMREEYGIQAEERQRVIDcLEDEKATLTLAMADWLR 292
Cdd:TIGR02169 328 EAEIDKLLAEIEELereieeerkRRDKLTeeYAELKEELEDLRAELEEVDKEFAETRDELKD-YREKLEKLKREINELKR 406
|
250 260
....*....|....*....|....*
gi 112382237 293 DYQDLLQVKTGLSLEVATYRALLEG 317
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAG 431
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
200-288 |
4.91e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 200 QLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRvidcLEDE 279
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ----LEAE 84
|
....*....
gi 112382237 280 KATLTLAMA 288
Cdd:pfam20492 85 LAEAQEEIA 93
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
61-156 |
6.14e-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: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 61 AEEARS-----LRQQLDELSWATAL---AEGERDALRRELRELQR----------LDAEERAARGRldaelgaqqRELQE 122
Cdd:COG3096 996 AEEARReareqLRQAQAQYSQYNQVlasLKSSRDAKQQTLQELEQeleelgvqadAEAEERARIRR---------DELHE 1066
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 112382237 123 AL----GARAALEALLGRLQAERRGLDA---AHERDVRELR 156
Cdd:COG3096 1067 ELsqnrSRRSQLEKQLTRCEAEMDSLQKrlrKAERDYKQER 1107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
469-603 |
6.84e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 469 RESYRDRRDKVAAGAsESTRSNERTVILGKKTEVKATR----EQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTK 544
Cdd:PTZ00121 1575 DKNMALRKAEEAKKA-EEARIEEVMKLYEEEKKMKAEEakkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 112382237 545 LDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRAEVSPKGLQTPVKDA 603
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
61-298 |
8.52e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.00 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 61 AEEARSLRQQLDELSWAT-ALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALE-------- 131
Cdd:COG3899 712 ARRALARGAYAEALRYLErALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALrhgnppas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 132 ---------ALLGRL----QAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSyALLVAESWRET 198
Cdd:COG3899 792 arayanlglLLLGDYeeayEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEA-GLETGDAALAL 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112382237 199 VQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLED 278
Cdd:COG3899 871 LALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAA 950
|
250 260
....*....|....*....|
gi 112382237 279 EKATLTLAMADWLRDYQDLL 298
Cdd:COG3899 951 AAALAAALALAAAAAAAAAA 970
|
|
| |
