|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-331 |
6.72e-19 |
|
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: 88.96 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARL-------DNDRLAAALAQVRAERDAL 211
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveqleeRIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQ 291
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18159965 292 YYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-330 |
5.36e-18 |
|
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: 86.26 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAK 298
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
170 180 190
....*....|....*....|....*....|..
gi 18159965 299 YSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-330 |
5.58e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 141 LANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQA 220
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYS 300
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190
....*....|....*....|....*....|
gi 18159965 301 ELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-331 |
4.77e-17 |
|
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: 83.19 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALA-----QVRAERDALRA 213
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 214 QLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYY 293
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18159965 294 SLS-------AKYSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:TIGR02169 886 DLKkerdeleAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-330 |
8.79e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAK 298
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190
....*....|....*....|....*....|..
gi 18159965 299 YSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEE 440
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-331 |
9.44e-17 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 81.99 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLSAQIDQLKQK--IADLQAQLKNKEAQIANLTSLLSAARldndrlaAALAQVRAERDALRA 213
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEAR-------AELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 214 QLEQTQAQLNAVSQ--AKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARL--------SELQQRYDELSK 283
Cdd:COG3206 248 QLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqqeaqrilASLEAELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 284 AEQQLREQYYSLSAKYSELNG---RYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEleaELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-330 |
1.36e-16 |
|
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: 82.03 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR-------LDNDRLAAALAQVRAERDALRAQLEQ 217
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeieeleAQIEQLKEELKALREALDELRAELTL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSK-------AEQQLRE 290
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRS 894
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18159965 291 QYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-326 |
1.73e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 154 DLSAQIDQLKQ-----KIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQA 228
Cdd:COG1196 217 ELKEELKELEAellllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 229 KAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDE 308
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170
....*....|....*...
gi 18159965 309 LSKAYEEARMNLEMLQNR 326
Cdd:COG1196 377 AEEELEELAEELLEALRA 394
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-330 |
2.62e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAV 225
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 226 SQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGR 305
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180
....*....|....*....|....*
gi 18159965 306 YDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEA 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-330 |
3.06e-16 |
|
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: 80.87 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVS 226
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 QAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRY 306
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180
....*....|....*....|....
gi 18159965 307 DELSKAYEEARMNLEMLQNRYSEL 330
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERL 419
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-330 |
4.78e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAV 225
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 226 SQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGR 305
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180
....*....|....*....|....*
gi 18159965 306 YDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-329 |
6.64e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR--LDNDRLAAALAQVRAERDALRAQLEQtqaqLNAVS 226
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER----LDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 QAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQlrEQYYSLSAKYSELNG-- 304
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGda 762
|
170 180
....*....|....*....|....*
gi 18159965 305 RYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEE 787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-331 |
1.16e-15 |
|
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: 78.95 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 163 KQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQ 242
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 243 LEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEM 322
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
....*....
gi 18159965 323 LQNRYSELN 331
Cdd:TIGR02168 836 TERRLEDLE 844
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-315 |
1.18e-15 |
|
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: 78.96 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDN------------------------ 194
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeevsriearlreieq 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 195 --DRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLS 272
Cdd:TIGR02169 820 klNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18159965 273 ELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEE 315
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-339 |
1.58e-15 |
|
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: 78.56 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAK 298
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18159965 299 YSELNGRYDELSKAYEEARMNLEMLQNRYSELNTGFTWALN 339
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-317 |
3.82e-15 |
|
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: 77.40 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQV-------RAERDALRAQLEQTQA 220
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLelqiaslNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEAQLAEtrKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYS 300
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
170
....*....|....*..
gi 18159965 301 ELNGRYDELSKAYEEAR 317
Cdd:TIGR02168 493 SLERLQENLEGFSEGVK 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-331 |
3.85e-15 |
|
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: 77.40 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQ 217
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSA 297
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190
....*....|....*....|....*....|....
gi 18159965 298 KYSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-321 |
4.06e-15 |
|
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: 77.40 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQL-EELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSK----AEQQlreqyy 293
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaAIEE------ 994
|
170 180 190
....*....|....*....|....*....|.
gi 18159965 294 slsakYSELNGRYDELSKAYE---EARMNLE 321
Cdd:TIGR02168 995 -----YEELKERYDFLTAQKEdltEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-330 |
4.28e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 225 VSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNG 304
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180
....*....|....*....|....*.
gi 18159965 305 RYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLL 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
145-316 |
5.90e-15 |
|
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: 77.03 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDAL-------RAQLEQ 217
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyaelKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDEL--------------SGQYTDAQRTIADLQARLSELQQRYD---- 279
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELkreldrlqeelqrlSEELADLNAAIAGIEAKINELEEEKEdkal 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18159965 280 ELSKAEQQL----------REQYYSLSAKYSELNGRYDELSKAYEEA 316
Cdd:TIGR02169 449 EIKKQEWKLeqlaadlskyEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-345 |
7.14e-15 |
|
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: 76.63 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQK---------------------IADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQV 204
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKldelaeelaeleekleelkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKAsyDELSGQYTDAQRTIADLQARLSELQQRYDELSKA 284
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 285 EQQLREQYYSLSAKYSELNGRYDelskayeearmNLEMLQNRYSELNTGFTWALNTATALG 345
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLD-----------SLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
134-390 |
1.42e-14 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 75.44 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSllsaarldndrlAAALAQVRAERDALRA 213
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ------------SPVIQQLRAQLAELEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 214 QLEQTQAQLNAVSQAKAALEAQLAETRKQL-EELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREqy 292
Cdd:COG3206 278 ELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 293 ysLSAKYSELNGRYDELSKAYEEARMNLEMLQNRY------------SELNTGFTWALNTATALGIALLFVIALFFSRKR 360
Cdd:COG3206 356 --LEREVEVARELYESLLQRLEEARLAEALTVGNVrvidpavvplkpVSPKKLLILALGLLLGLLLGLGLALLLELLDRT 433
|
250 260 270
....*....|....*....|....*....|
gi 18159965 361 VQPAPAPAQPPATARGAVIIEEKPKENLVK 390
Cdd:COG3206 434 IEEELELLLLLGLPLLGPLPPLKSKRERRR 463
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-329 |
1.61e-14 |
|
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: 74.42 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQL-------------------------NAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSE 273
Cdd:COG4942 103 KEELaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 274 LQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-316 |
4.51e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIA-------NLTSLLSAARLDNDRLAAALAQVRAERDAL 211
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAeaeeallEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQ 291
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
170 180
....*....|....*....|....*
gi 18159965 292 YYSLSAKYSELNGRYDELSKAYEEA 316
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADY 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-321 |
1.38e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVEDLSAQIDQLKQkIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQvrAERDALRAQLEQTQAQLnavs 226
Cdd:COG4913 239 RAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE--AELEELRAELARLEAEL---- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 qakAALEAQLAETRKQLEELKASYDELSGQ-YTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGR 305
Cdd:COG4913 312 ---ERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170
....*....|....*.
gi 18159965 306 YDELSKAYEEARMNLE 321
Cdd:COG4913 389 AAALLEALEEELEALE 404
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
144-348 |
1.76e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 71.09 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 144 YAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLN 223
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 224 AVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSEln 303
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE-- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18159965 304 gryDELSKAYEEARMNLEMLQNRYSELNTGFTWALNTATALGIAL 348
Cdd:COG4372 183 ---QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-331 |
2.02e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 152 VEDLSAQIDQLKQ--KIA----DLQAQLKNKEAQIAnltsllsaarldndrlAAALAQVRAERDALRAQLEQTQAQLNAV 225
Cdd:COG1196 195 LGELERQLEPLERqaEKAeryrELKEELKELEAELL----------------LLKLRELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 226 SQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGR 305
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180
....*....|....*....|....*.
gi 18159965 306 YDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAE 364
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
157-317 |
2.39e-13 |
|
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: 69.18 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAK------- 229
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 230 --AALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYD----ELSKAEQQLREQYYSLSAKYSEln 303
Cdd:COG1579 97 eiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAAKIPP-- 174
|
170
....*....|....
gi 18159965 304 grydELSKAYEEAR 317
Cdd:COG1579 175 ----ELLALYERIR 184
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-330 |
3.17e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 130 IGRVLPSTYEDLANYAASLEQKVE-DLSAQIDQLKQKIADLQAQLKNKEAQ----------------------------- 179
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEkDLHERLNGLESELAELDEEIERYEEQreqaretrdeadevleeheerreeletle 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 180 --IANLTSLLSAARLDNDRLA-------AALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASY 250
Cdd:PRK02224 258 aeIEDLRETIAETEREREELAeevrdlrERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 251 DELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-317 |
4.13e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDN-DRLAAALAQVRAERDALRAQLEQTQAQLN 223
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 224 AVSQAKAALEAQLAETRKQleelkasydelsgqytdAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELN 303
Cdd:COG4913 370 ALGLPLPASAEEFAALRAE-----------------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
170
....*....|....
gi 18159965 304 GRYDELSKAYEEAR 317
Cdd:COG4913 433 RRKSNIPARLLALR 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-330 |
1.61e-12 |
|
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: 68.25 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 141 LANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLtsllsaarldndrlAAALAQVRAERDALRAQLEQTQA 220
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL--------------LKQLAALERRIAALARRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEAQLAETRKQLEELKASYDEL------SGQY------------TDAQRTIADL-------QARLSELQ 275
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELlralyrLGRQpplalllspedfLDAVRRLQYLkylaparREQAEELR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 276 QRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
149-283 |
4.14e-12 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 66.91 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA---V 225
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSekqV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18159965 226 SQAKAA----LEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARL-SELQQRYDELSK 283
Cdd:PRK09039 132 SARALAqvelLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnVALAQRVQELNR 194
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
190-324 |
4.81e-12 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 66.61 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 190 ARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAvSQAKAALEAQLAETRKQLEELKASYDELSG----------QYTD 259
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavsqqELDE 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 260 AQRTIADLQARLSELQQrydELSKAEQQLREQyyslsAKYSELNGRYDELSKAYEEARMNLEMLQ 324
Cdd:COG1566 153 ARAALDAAQAQLEAAQA---QLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
139-316 |
1.02e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 66.01 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQ--------------- 203
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvsyldvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 204 -----------VRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLS 272
Cdd:COG3883 113 sfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18159965 273 ELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEA 316
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
132-299 |
1.12e-11 |
|
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: 64.18 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 132 RVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARlDNDRLAAALAQV---RAER 208
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEALQKEIeslKRRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 209 DALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELsgqytdaqrtIADLQARLSELQQRYDELSKA-EQQ 287
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE----------LAELEAELEELEAEREELAAKiPPE 175
|
170
....*....|..
gi 18159965 288 LREQYYSLSAKY 299
Cdd:COG1579 176 LLALYERIRKRK 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
146-297 |
2.81e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDN--DRLAAALAQVRAERDALRAQLEQTQAQLN 223
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 224 AVSQAKAALEAQL----AETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELS------KAEQQLREQYY 293
Cdd:COG4717 171 ELAELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneleaaALEERLKEARL 250
|
....
gi 18159965 294 SLSA 297
Cdd:COG4717 251 LLLI 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
140-291 |
4.72e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.65 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 140 DLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDN--DRLAAALAQVRAERD-------- 209
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAelsarytp 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 210 ------ALRAQLEQTQAQLNA-VSQAKAALEAQLAETRKQLEELKASYDELSGQ---YTDAQRTIADLQARLSELQQRYD 279
Cdd:COG3206 289 nhpdviALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYE 368
|
170
....*....|..
gi 18159965 280 ELSKAEQQLREQ 291
Cdd:COG3206 369 SLLQRLEEARLA 380
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-330 |
4.90e-11 |
|
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: 64.70 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADL------------------QAQLKNK----EAQIANLTSLLSAARLDNDRLAAALAQ 203
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeQLRVKEKigelEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 204 VRAERDALRAQ-------LEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQ 276
Cdd:TIGR02169 327 LEAEIDKLLAEieelereIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18159965 277 RYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-321 |
5.34e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQkIADLQAQLKNKEAQIANLTSLLS--AARLDNDRLAAAlaQVRAERDALRAQLE 216
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAerRETIEEKRERAE--ELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 217 QTQAQLNAV-SQAKAALEAqLAETRKQLEELKASYDELsGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSL 295
Cdd:PRK02224 555 EKREAAAEAeEEAEEAREE-VAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
170 180
....*....|....*....|....*.
gi 18159965 296 SAKYSELNGRYDElsKAYEEARMNLE 321
Cdd:PRK02224 633 RERKRELEAEFDE--ARIEEAREDKE 656
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
143-317 |
6.46e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 143 NYAASLEQKVEDLSA---QIDQLKQKIADLQAQLKNKEAQIANLTSLL----------SAARLD-----NDRLAAALAQV 204
Cdd:PRK04863 918 NALAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVqrrahfsyedAAEMLAknsdlNEKLRQRLEQA 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTD--AQRTIAD---LQARLSELQQRYD 279
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgaEERARARrdeLHARLSANRSRRN 1077
|
170 180 190
....*....|....*....|....*....|....*...
gi 18159965 280 ELSKaeqqlreQYYSLSAKYSELNGRYDELSKAYEEAR 317
Cdd:PRK04863 1078 QLEK-------QLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-383 |
6.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLdndrlAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-----YQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 225 VSQA---KAALEAQLAETRKQLEELKASYD-ELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKY- 299
Cdd:COG4717 158 LRELeeeLEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELe 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 300 -SELNGRYDELSKAYEEARMNLEMLQNRYSELNTGFTWAlnTATALGIALLFVIALFFSRKRVQPAPAPAQPPATARGAV 378
Cdd:COG4717 238 aAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA--GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
....*
gi 18159965 379 IIEEK 383
Cdd:COG4717 316 LEEEE 320
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
139-330 |
9.01e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIA---DLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAER---DALR 212
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKA--------------------SYDELSG---QYTDAQRTI----A 265
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKeieeleekvkelkelkekaeEYIKLSEfyeEYLDELREIekrlS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 266 DLQARLSELQQRYDELSKAEQQLREqyysLSAKYSELNGRYDELS---KAYEEARMNLEMLQNRYSEL 330
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRL 381
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-317 |
1.22e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIADLQAQLKNKEAQiANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQL 236
Cdd:COG4717 347 EELQELLREAEELEEELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 237 --AETRKQLEELKASYDELSGQYTDAQRTIADLQARLSEL--QQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKA 312
Cdd:COG4717 426 deEELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELLEEA 505
|
....*
gi 18159965 313 YEEAR 317
Cdd:COG4717 506 REEYR 510
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
150-296 |
1.23e-10 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 61.99 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVE--DLSAQID--QLKQKIADLQAQLKNKEAQIANLTSLLSAarldndrlAAALAQVRAERDALRAQLEQTQAQLNAV 225
Cdd:COG1566 65 DRVKkgQVLARLDptDLQAALAQAEAQLAAAEAQLARLEAELGA--------EAEIAAAEAQLAAAQAQLDLAQRELERY 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 226 SQakaaLEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYD---ELSKAEQQLREQYYSLS 296
Cdd:COG1566 137 QA----LYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAaqaQVAQAEAALAQAELNLA 206
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
149-321 |
1.99e-10 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 60.36 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR--LDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVs 226
Cdd:pfam15934 47 EQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLQSMITGYSdiSENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQ- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 qakaalEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRY 306
Cdd:pfam15934 126 ------EEQRVELCDKYESLLGSFEEQCQELKRANRRVQSLQTRLSQVEKLQEELRTERKILREEVIALKEKDAKSNGRE 199
|
170
....*....|....*
gi 18159965 307 DELSKAYEEARMNLE 321
Cdd:pfam15934 200 RALQDQLKCCQTEIE 214
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
162-311 |
2.09e-10 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 61.52 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 162 LKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRK 241
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 242 QLEELKASYDELSGQYTDAQRTIADLQARLSELQqryDELSKAEQQLREQYYSLSAKYSELN----GRYDELSK 311
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALRRQLAALE---AALDASEKRDRESQAKIADLGRRLNvalaQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
183-332 |
3.32e-10 |
|
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: 61.32 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 183 LTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQR 262
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 263 TIADLQARLSELQQRYDELSKAEQQLREQYYS---LSAKYSELNGRYDELSKAYEEARMN-LEMLQNRYSELNT 332
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAA 164
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
150-330 |
6.32e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDLSAQIDQLKQKIADLQAQLKNKEAQIanltsllsaarldnDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAK 229
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKR--------------DELNEELKELAEKRDELNAQVKELREEAQELREKR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 230 AALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQAR---LSELQQRYDEL----------SKAEQQLREQYYSLS 296
Cdd:COG1340 67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLewrqqtevlsPEEEKELVEKIKELE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18159965 297 AKYS------ELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1340 147 KELEkakkalEKNEKLKELRAELKELRKEAEEIHKKIKEL 186
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
148-332 |
1.41e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR-------LDNDRLAAALAQVRAERDALRAQLEQTQA 220
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEaQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDEL-SKAEQQ------------ 287
Cdd:PRK02224 490 EVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELeAEAEEKreaaaeaeeeae 568
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18159965 288 -LREQYYSLSAKYSELNGRYDELSK------AYEEARMNLEMLQNRYSELNT 332
Cdd:PRK02224 569 eAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAE 620
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
213-306 |
1.46e-09 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 55.28 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASyDELSGQY---------TDAQRTIADLQARLSELQQRYDELSK 283
Cdd:COG1382 14 AQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKL-PDDAEVYksvgnllvkTDKEEVIKELEEKKETLELRLKTLEK 92
|
90 100
....*....|....*....|...
gi 18159965 284 AEQQLREQYYSLSAKYSELNGRY 306
Cdd:COG1382 93 QEERLQKQLEELQEKLQEALSGA 115
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
139-386 |
1.73e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLS-----ELQQRYDELSKAEQQLREQYY 293
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 294 SLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNTGFTWALNTATALGIALLFVIALFFSRKRVQPAPAPAQPPAT 373
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250
....*....|...
gi 18159965 374 ARGAVIIEEKPKE 386
Cdd:COG4372 281 AALELEALEEAAL 293
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-292 |
2.26e-09 |
|
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: 59.42 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQY 292
Cdd:pfam01576 509 EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
149-330 |
2.31e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR--------LDNDRLAAALAQVRAERDALR-------- 212
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlnlLADETLADRVEEIREQLDEAEeakrfvqq 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 -----AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSG--------QYTDAQRTIADLQARLSELQQRYD 279
Cdd:PRK04863 916 hgnalAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQRLE 995
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 280 ELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
201-330 |
2.41e-09 |
|
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: 57.24 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 201 LAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQ-QR-Y 278
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKeY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18159965 279 DELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
148-330 |
2.91e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKN----KEAQIANLTSLLSAARLDNDRLAAALAQV---RAERDALRAQLEQTQA 220
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKElaekRDELNAQVKELREEAQELREKRDELNEKVkelKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QL-----------------NAVSQAKAALE-----------------AQLAETRKQLEELKASyDELSGQYTDAQRTIAD 266
Cdd:COG1340 93 ELdelrkelaelnkaggsiDKLRKEIERLEwrqqtevlspeeekelvEKIKELEKELEKAKKA-LEKNEKLKELRAELKE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 267 LQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-291 |
3.34e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQL-N 223
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeE 773
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 224 AVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQryDELSKAEQQLREQ 291
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE--DGLPEYEERFKEL 839
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-274 |
4.50e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDN-----DRLAAALAQVRAERDALR 212
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLE 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 213 AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSG------QYTDAQRTIADLQARLSEL 274
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSGILGVLSEL 528
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
148-302 |
5.67e-09 |
|
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: 58.26 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQaQLKNK-EAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLnavs 226
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLS-KLKNKhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI---- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 qakAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDE----LSKAEQQLREQYYSLSAKYSEL 302
Cdd:pfam01576 232 ---AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESeraaRNKAEKQRRDLGEELEALKTEL 308
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
193-340 |
5.71e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 193 DNDRLAAALaqvRAERDALRAQLEQTQAQLNAVSQAKAALEAQLaETRKQLEELKASYDELSGqytdAQRTIADLQARLS 272
Cdd:COG4913 607 DNRAKLAAL---EAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEIDVAS----AEREIAELEAELE 678
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 273 ELQQRYDELSKAEQQL---REQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNTGFTWALNT 340
Cdd:COG4913 679 RLDASSDDLAALEEQLeelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-280 |
6.02e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYA------ASLEQKVEDLSAQIDQLKQKIADLQAQlknkEAQIANLTSLLSAARLDNDRLAAALAQVRAERD 209
Cdd:COG4913 648 EALQRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 210 ALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDE----LSGQYTDAQRTIADLQARLSELQQRYDE 280
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElrenLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-266 |
6.92e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQ--------IDQLKQKIADLQAQLKNKEAQIANLTSLLSAARL----DNDRLAAALAQVRA 206
Cdd:COG4913 312 ERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLplpaSAEEFAALRAEAAA 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 207 ERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIAD 266
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
148-330 |
7.06e-09 |
|
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: 57.88 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQvraerdaLRAQLEQTQAQLNAVSQ 227
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS-------LESQLQDTQELLQEETR 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 228 AKAALEAQLaetrKQLEELKASYDELSGQYTDAQRT----IADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELN 303
Cdd:pfam01576 483 QKLNLSTRL----RQLEDERNSLQEQLEEEEEAKRNverqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
170 180
....*....|....*....|....*..
gi 18159965 304 GRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-317 |
7.21e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANltsllsaARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD-------APVDLGNAEDFLEELREERDELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQL----NAVSQAKAALEA-----------------QLAETRKQLEELKASYDELSGQYTDAQRTI------ADLQARL 271
Cdd:PRK02224 432 EATLrtarERVEEAEALLEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLeraedlVEAEDRI 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18159965 272 SELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEAR 317
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
146-330 |
9.72e-09 |
|
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: 57.27 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLL-SAARLDNDRLAAALAQVRAERDalraQLEQTQAQLNA 224
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELD----AAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 225 VSQAKAALEAQLAETRK---QLEELKASYDELSGQYTDAQRTI---------------ADLQARLSE-------LQQRYD 279
Cdd:COG3096 915 HGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIfalsevvqrrphfsyEDAVGLLGEnsdlnekLRARLE 994
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 280 ELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
139-317 |
1.23e-08 |
|
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: 57.27 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLT--------SLLSAARLDNDRLAAALAQVRAERDA 210
Cdd:COG3096 923 EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavGLLGENSDLNEKLRARLEQAEEARRE 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 211 LRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTD-----AQRTIADLQARLSELQQRYDELSKae 285
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeaeerARIRRDELHEELSQNRSRRSQLEK-- 1080
|
170 180 190
....*....|....*....|....*....|..
gi 18159965 286 qqlreQYYSLSAKYSELNGRYDELSKAYEEAR 317
Cdd:COG3096 1081 -----QLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
158-316 |
1.26e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 158 QIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLN---------AVSQA 228
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerreelgerARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 229 KA------------------------ALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKA 284
Cdd:COG3883 97 RSggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|..
gi 18159965 285 EQQLREQYYSLSAKYSELNGRYDELSKAYEEA 316
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
147-331 |
1.96e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 55.31 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVEDLSAQIDQLKQK---------------IADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDAL 211
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDE----LSGQYTDAQRTIA-------DLQARLSELQQRYDE 280
Cdd:pfam00038 102 ENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevreLQAQVSDTQVNVEmdaarklDLTSALAEIRAQYEE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 281 LSKAEQQLREQYYslSAKYSELNgrydelskayEEARMNLEMLQNRYSELN 331
Cdd:pfam00038 182 IAAKNREEAEEWY--QSKLEELQ----------QAAARNGDALRSAKEEIT 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-290 |
2.50e-08 |
|
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: 56.23 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELK------ASYDELSGQYTDAQRTIADL--------------QARLSELQQRY 278
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEeipeeeLSLEDVQAELQRVEEEIRALepvnmlaiqeyeevLKRLDELKEKR 995
|
170
....*....|..
gi 18159965 279 DELSKAEQQLRE 290
Cdd:TIGR02169 996 AKLEEERKAILE 1007
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
125-258 |
2.70e-08 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 55.12 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 125 SYNYYIGRVLPSTYEDLANYAAsleQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQV 204
Cdd:TIGR04320 225 GVTIHFVNFNDSYIADGNKFDK---TPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATA 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 205 RAERDALRAQLEQT-QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYT 258
Cdd:TIGR04320 302 QKELANAQAQALQTaQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| gimC_beta |
TIGR02338 |
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ... |
213-302 |
3.08e-08 |
|
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.
Pssm-ID: 131391 [Multi-domain] Cd Length: 110 Bit Score: 51.20 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDEL-----SGQY---TDAQRTIADLQARLSELQQRYDELSKA 284
Cdd:TIGR02338 10 AQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTpvyksVGNLlvkTDKEEAIQELKEKKETLELRVKTLQRQ 89
|
90
....*....|....*...
gi 18159965 285 EQQLREQYYSLSAKYSEL 302
Cdd:TIGR02338 90 EERLREQLKELQEKIQEA 107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-315 |
3.12e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAA----RLDN--DRLAAALAQVRAERDALRAQLEQTQ 219
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyiKLSEfyEEYLDELREIEKRLSRLEEEINGIE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAKAALEaqlaETRKQLEELKASYDELSGQ---YTDAQRTIADLQ---ARLS-----ELQQRYDELSKAEQQL 288
Cdd:PRK03918 328 ERIKELEEKEERLE----ELKKKLKELEKRLEELEERhelYEEAKAKKEELErlkKRLTgltpeKLEKELEELEKAKEEI 403
|
170 180
....*....|....*....|....*..
gi 18159965 289 REQYYSLSAKYSELNGRYDELSKAYEE 315
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEE 430
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
164-321 |
3.71e-08 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 54.86 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 164 QKIAdlQAQLKNKEAQIANLTsllsaARLDNDRLAAALAQV-RAERDALRAQLEQTQAQ-----LNAVSQAK------AA 231
Cdd:COG3524 153 QAIA--EALLAESEELVNQLS-----ERAREDAVRFAEEEVeRAEERLRDAREALLAFRnrngiLDPEATAEallqliAT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 232 LEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYdelskAEQQLREQYYSLSAKYSELNGRYDELSK 311
Cdd:COG3524 226 LEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARL-----TGASGGDSLASLLAEYERLELEREFAEK 300
|
170
....*....|
gi 18159965 312 AYEEARMNLE 321
Cdd:COG3524 301 AYTSALAALE 310
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
134-330 |
4.27e-08 |
|
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: 55.51 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYAASLEQK---VEDLSAQIDQLKQKIaDLQAQ----LKNKEAQIANLTSLLSAARL---DNDRLAAALAQ 203
Cdd:pfam15921 491 LESSERTVSDLTASLQEKeraIEATNAEITKLRSRV-DLKLQelqhLKNEGDHLRNVQTECEALKLqmaEKDKVIEILRQ 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 204 VRAERDALRAQLEQTQAqlnAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQ-----------ARL- 271
Cdd:pfam15921 570 QIENMTQLVGQHGRTAG---AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagsERLr 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 272 --SELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEM-LQNRYSEL 330
Cdd:pfam15921 647 avKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSEL 708
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-313 |
4.97e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIAN--------------LTSLLSAARLDN--------- 194
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyLDVLLGSESFSDfldrlsals 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 195 ----------DRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTI 264
Cdd:COG3883 126 kiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18159965 265 ADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAY 313
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
154-296 |
5.38e-08 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 53.97 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 154 DLSAQIDQLKQKIADLQAQLKNKEAQIANLTSL---LSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAV---SQ 227
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALeseLAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRrvlAP 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 228 AKAALEAQLAETRKQLEELKASYDELSGQ----YTDAQRTIADLQA-RLSELQQRYDELSKAEQQLREQYYSLS 296
Cdd:pfam00529 135 IGGISRESLVTAGALVAQAQANLLATVAQldqiYVQITQSAAENQAeVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
238-323 |
5.60e-08 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 53.58 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 238 ETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEAR 317
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEV 211
|
....*.
gi 18159965 318 MNLEML 323
Cdd:COG4026 212 FSLEEL 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-332 |
8.27e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 133 VLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQI--------------ANLTSLLSAARLDNDRLA 198
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneekkeleekvKDLTKKISSLKEKIEKLE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 199 AALAQVRAERDALRAQLEQTQAQLNavsqaKAALEAQLAETRKQLEELKASYDELsgqyTDAQrtiadlqarlSELQQRY 278
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSL----KKKQ----------EEKQELI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18159965 279 DELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
152-339 |
1.08e-07 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 52.05 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 152 VEDLSAQIDQLKQKIADLQAQLKNkeaqianLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAvsqakaa 231
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQN-------LLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKD------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 232 LEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYyslSAKYSELNGRYDELSK 311
Cdd:pfam17078 71 LEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHY---QQEINTLQESLEDLKL 147
|
170 180
....*....|....*....|....*...
gi 18159965 312 ayeEARMNLEMLQNRYSELNTGFTWALN 339
Cdd:pfam17078 148 ---ENEKQLENYQQRISSNDKDIDTKLD 172
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
148-304 |
1.37e-07 |
|
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: 53.64 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAArldnDRlaaALAQVRAERDALRAQLEQTQAQLNAVSQ 227
Cdd:pfam01576 810 LQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAAS----ER---ARRQAQQERDELADEIASGASGKSALQD 882
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 228 AKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNG 304
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
139-303 |
1.39e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKV-EDLSAQ-IDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLE 216
Cdd:PRK11281 101 AELEALKDDNDEETrETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 217 QT---QAQLNAVSQAK-----AALEAQLAETRKQLEE-------LKASYDELSGQYTDAQRTIADLQA-----RLSELQQ 276
Cdd:PRK11281 181 GGkvgGKALRPSQRVLlqaeqALLNAQNDLQRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQEainskRLTLSEK 260
|
170 180
....*....|....*....|....*..
gi 18159965 277 RYDELSKAEQQLREQYYSLSAKYSELN 303
Cdd:PRK11281 261 TVQEAQSQDEAARIQANPLVAQELEIN 287
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
145-291 |
1.71e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 51.92 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQ-IDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLN 223
Cdd:pfam12795 65 AKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 224 AVSQAK--------AALEAQLAETRKQL-------EELKASYDELSGQYTDAQRTIADLQARLSELQQrydelSKAEQQL 288
Cdd:pfam12795 145 PLSEAQrwalqaelAALKAQIDMLEQELlsnnnrqDLLKARRDLLTLRIQRLEQQLQALQELLNEKRL-----QEAEQAV 219
|
...
gi 18159965 289 REQ 291
Cdd:pfam12795 220 AQT 222
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
138-325 |
1.75e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 52.93 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVED-----------LSAQIDQLKQKIADLQAQ------------LKNKEAQIANLTSLLsaARLDN 194
Cdd:pfam06160 181 LEKLEEETDALEELMEDipplyeelkteLPDQLEELKEGYREMEEEgyalehlnvdkeIQQLEEQLEENLALL--ENLEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 195 DRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYT---DAQRTIADLQARL 271
Cdd:pfam06160 259 DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTlneNELERVRGLEKQL 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 272 SELQQRYDELskaEQQLREQ---YYSLSAKYSELNGRYDELSKAYEEARmnlEMLQN 325
Cdd:pfam06160 339 EELEKRYDEI---VERLEEKevaYSELQEELEEILEQLEEIEEEQEEFK---ESLQS 389
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
139-319 |
1.83e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLT--SLLSAARLD--NDRLAAALAQVR---AERDAL 211
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTqrVLERETELErmKERAKKAGAQRKeeeAERKQL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQ---L 288
Cdd:pfam07888 177 QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKvegL 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18159965 289 REQYYSLSAKYS--------------ELNGRYDELSKAYEEARMN 319
Cdd:pfam07888 257 GEELSSMAAQRDrtqaelhqarlqaaQLTLQLADASLALREGRAR 301
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
148-330 |
1.97e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVED---LSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRA------ERDALRAQ-LEQ 217
Cdd:PRK03918 520 LEKKAEEyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesvEELEERLKeLEP 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRtiadLQARLSELQQRYDElsKAEQQLREQYYSLSA 297
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE----LRKELEELEKKYSE--EEYEELREEYLELSR 673
|
170 180 190
....*....|....*....|....*....|...
gi 18159965 298 KYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| Prefoldin_beta_GimC |
cd23162 |
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ... |
213-298 |
2.65e-07 |
|
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467478 [Multi-domain] Cd Length: 102 Bit Score: 48.24 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDElSGQY---------TDAQRTIADLQARLSELQQRYDELSK 283
Cdd:cd23162 4 AQLQQLQQQLQAVLLQKQQLEAELREIERALEELEKLPDD-AEVYksvgtilvkVDKEEVIKELKERKETLELRLKTLEK 82
|
90
....*....|....*
gi 18159965 284 AEQQLREQYYSLSAK 298
Cdd:cd23162 83 QEERLRKQLEELQKK 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
132-329 |
3.00e-07 |
|
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: 52.48 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 132 RVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIAN-------LTSLLSAAR--LDNDRLAAALA 202
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNalkkireLEAQISELQedLESERAARNKA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 203 QVR-----AERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYD----ELSGQYTDAqrtIADLQARLSE 273
Cdd:pfam01576 291 EKQrrdlgEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEaqlqEMRQKHTQA---LEELTEQLEQ 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 274 LQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
148-331 |
4.00e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSllsaarldndrlaaalaqvraERDALRAQLEQTQAQLNAVSQ 227
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD---------------------EQNKIKKQLSEKQKELEQNNK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 228 AKAALEAQLAETRKQLEELKASYD-----ELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSL----SAK 298
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesenSEK 361
|
170 180 190
....*....|....*....|....*....|...
gi 18159965 299 YSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-245 |
4.75e-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: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 135 PSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQ 214
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
90 100 110
....*....|....*....|....*....|.
gi 18159965 215 LEQTQAQLNAVSQAKAALEAQLAETRKQLEE 245
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
112-316 |
4.99e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.55 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 112 LLEIWIYLPNYTLSYNYYigRVLPSTYEDLANYAASLEQKV-------EDLSAQ----IDQLKQKIADLQAQLKNKEAQI 180
Cdd:PHA02562 159 LLDISVLSEMDKLNKDKI--RELNQQIQTLDMKIDHIQQQIktynkniEEQRKKngenIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 181 ANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLN---------AVSQakaaleaQLAETRKQLEELKASYD 251
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQ-------QISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 252 ELSGQYTDAQRTIADLQARLSElqqrYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEA 316
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDE----FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-332 |
6.15e-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: 51.60 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANyaaSLEQKVEDLSAQIDQlKQKIADLQAQLKNKEAQianltslLSAARLDndrlaaalaqvraerdALRAQLEQT 218
Cdd:TIGR02168 192 EDILN---ELERQLKSLERQAEK-AERYKELKAELRELELA-------LLVLRLE----------------ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASydelsgqytdaqrtIADLQARLSELQQRYDEL----SKAEQQ---LREQ 291
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLE--------------VSELEEEIEELQKELYALaneiSRLEQQkqiLRER 310
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18159965 292 YYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
137-298 |
6.16e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 137 TYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLknkeAQIANLTSLLSAARLDNDRLAA------ALAQVRAERdA 210
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH----SQFEQAYQLVRKIAGEVSRSEAwdvareLLRRLREQR-H 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 211 LRAQLEQTQAQLNAVSQA---KAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQ 287
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRlrqQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
170
....*....|.
gi 18159965 288 LREQYYSLSAK 298
Cdd:PRK04863 591 LQARIQRLAAR 601
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
139-330 |
6.72e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAA------SLEQKVEDLSAQIDQLKQKIADLQAQLKnkEaqianltslLSAARLDNDrlaaALAQVRAERDALR 212
Cdd:COG0497 155 ELLEEYREayrawrALKKELEELRADEAERARELDLLRFQLE--E---------LEAAALQPG----EEEELEEERRRLS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 -AQ--LEQTQAQLNAVSQAKAALEAQLAETRKQLEELK---ASYDELSGQYTDAQRTIADLQARLSELQQRYD----ELS 282
Cdd:COG0497 220 nAEklREALQEALEALSGGEGGALDLLGQALRALERLAeydPSLAELAERLESALIELEEAASELRRYLDSLEfdpeRLE 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18159965 283 KAEQQLrEQYYSLSAKYselNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG0497 300 EVEERL-ALLRRLARKY---GVTVEELLAYAEELRAELAELENSDERL 343
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
155-315 |
6.85e-07 |
|
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: 51.49 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 155 LSAQIDQLKQKIADLQAQLknkeAQIANLTSLLsaarldnDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEA 234
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRL----RQQQNAERLL-------EEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 235 QLAETRKQLEELKASYDELSGQ---YTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSK 311
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARapaWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
....
gi 18159965 312 AYEE 315
Cdd:COG3096 659 QIER 662
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
150-325 |
7.23e-07 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 50.50 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVE--DLSAQIDQlkqkiADLQAQLKNKEAQIANLTSLLSAARLDNDRLAA---ALAQVRAERDALRAQLEQTQAQlna 224
Cdd:pfam00529 40 DRVKagDVLFQLDP-----TDYQAALDSAEAQLAKAQAQVARLQAELDRLQAlesELAISRQDYDGATAQLRAAQAA--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 225 VSQAKAALEAqlaeTRKQLE--ELKASYDELSGQ-YTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAkySE 301
Cdd:pfam00529 112 VKAAQAQLAQ----AQIDLArrRVLAPIGGISREsLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR--SE 185
|
170 180
....*....|....*....|....
gi 18159965 302 LNGRYDELSKAYEEARMNLEMLQN 325
Cdd:pfam00529 186 LSGAQLQIAEAEAELKLAKLDLER 209
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
137-330 |
7.86e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 137 TYEDLANYAASLEQKVED-----------LSAQIDQLKQKIADLQAQ------------LKNKEAQIANLTSLLSaaRLD 193
Cdd:PRK04778 199 ILDQLEEELAALEQIMEEipellkelqteLPDQLQELKAGYRELVEEgyhldhldiekeIQDLKEQIDENLALLE--ELD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 194 NDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKA-------SY---------------- 250
Cdd:PRK04778 277 LDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEeidrvkqSYtlneselesvrqlekq 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 251 -DELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELngRYDELskayeEARMNLEMLQNRYSE 329
Cdd:PRK04778 357 lESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGL--RKDEL-----EAREKLERYRNKLHE 429
|
.
gi 18159965 330 L 330
Cdd:PRK04778 430 I 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-331 |
8.11e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIAD--LQAQLKNKEAQ-----IANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQ 217
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrVAAQAHNEEAEslredADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQ------------------RYD 279
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegspHVE 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 280 ELSKAEQQ---LREQYYSLSAKYSELNGRYDELSKAYEEARmNLEMLQNRYSELN 331
Cdd:PRK02224 469 TIEEDRERveeLEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLE 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
146-331 |
8.59e-07 |
|
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: 51.11 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLS---AARLDNDRlAAALAQVRAERDALRAQLEQTQAQL 222
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGghlAVAFAPDP-EAELAALRQRRSELERELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 223 NAVSQAKAALEAQLAETRKQL--------EELKASYDELSGQYTDAQ----------RTIADLQARLS----------EL 274
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQeaqafiqqhgKALAQLEPLVAvlqsdpeqfeQL 939
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18159965 275 QQRYDELSKAEQQLREQYYSLS------------------AKYSELN----GRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSevvqrrphfsyedavgllGENSDLNeklrARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-332 |
9.25e-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: 51.21 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 187 LSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKaalEAQLAETRKQLEELKASYDELSGQYTDAQRTIAD 266
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELR---ELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 267 LQARLSELQQRYDELskaeqqlREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:TIGR02168 258 LTAELQELEEKLEEL-------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
138-290 |
9.30e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQL-----------KNKEAQIANLTSLLSAARL----DNDR---LAA 199
Cdd:pfam00038 91 YEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIeslkeelaflkKNHEEEVRELQAQVSDTQVnvemDAARkldLTS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 200 ALAQVRAERDAL----RAQLEQT------QAQLNAVSQAKAALEAQ--LAETRKQLEELKASYDELSGQYTDAQRTIADL 267
Cdd:pfam00038 171 ALAEIRAQYEEIaaknREEAEEWyqskleELQQAAARNGDALRSAKeeITELRRTIQSLEIELQSLKKQKASLERQLAET 250
|
170 180
....*....|....*....|....
gi 18159965 268 QARLS-ELQQRYDELSKAEQQLRE 290
Cdd:pfam00038 251 EERYElQLADYQELISELEAELQE 274
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
138-325 |
1.06e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDlSAQIDQLKQKIADLQAQL------KNKE----AQIANLTSLLSAARlDNDRLAAALAQVRAE 207
Cdd:COG1340 91 REELDELRKELAELNKA-GGSIDKLRKEIERLEWRQqtevlsPEEEkelvEKIKELEKELEKAK-KALEKNEKLKELRAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 208 RDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAqrtiadlQARLSELQQRYDELSKAEQQ 287
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA-------QEKADELHEEIIELQKELRE 241
|
170 180 190
....*....|....*....|....*....|....*...
gi 18159965 288 LREQYYSLSAKYSELnGRYDELSKAYEEARMNLEMLQN 325
Cdd:COG1340 242 LRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKK 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
145-290 |
1.18e-06 |
|
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: 50.72 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAArldNDRLAAALAQVRAER--DALRAQLEQTQAQL 222
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA---SDHLNLVQTALRQQEkiERYQEDLEELTERL 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 223 NAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLRE 290
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGL 431
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
139-322 |
1.31e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 50.10 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKN----KEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQ 214
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKElylaKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 215 L---EQTQAQlnAVSQAK-------AALEAQLAET--------RKQLEELKASYdelsGQYTD-AQRTIADLQARLSELQ 275
Cdd:pfam03528 84 AtvsENTKQE--AIDEVKsqwqeevASLQAIMKETvreyevqfHRRLEQERAQW----NQYREsAEREIADLRRRLSEGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 276 QRY---DELSKAE---QQLR-------EQYYSLSAKYSELNGRYDELS-----------KAYEEARMNLEM 322
Cdd:pfam03528 158 EEEnleDEMKKAQedaEKLRsvvmpmeKEIAALKAKLTEAEDKIKELEaskmkelnhylEAEKSCRTDLEM 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
145-345 |
1.32e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLknkEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQ--LEQTQAQL 222
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMAREL---AELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQadLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 223 NAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLreQYYSLSAKysEL 302
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLC--GLPDLTAD--NA 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18159965 303 NGRYDELSKAYEEARMNLEMLQNRYS---ELNTGFTWALNTATALG 345
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSvaqAAHSQFEQAYQLVRKIA 486
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
160-330 |
1.65e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 49.37 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 160 DQLKQKIAD--LQAQ--LKNKEAQIANLTSLLSAARLDNDR-LAAALAQVRAERDALRAQLEQTQAQLNAVS------QA 228
Cdd:pfam09787 3 ESAKQELADykQKAAriLQSKEKLIASLKEGSGVEGLDSSTaLTLELEELRQERDLLREEIQKLRGQIQQLRtelqelEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 229 KAALEA-----QLAETRKQLEELKASY----DELSGQYTDAQRTIADLQ----ARLSELQQRYDELSKAEQQLREQYYSL 295
Cdd:pfam09787 83 QQQEEAessreQLQELEEQLATERSARreaeAELERLQEELRYLEEELRrskaTLQSRIKDREAEIEKLRNQLTSKSQSS 162
|
170 180 190
....*....|....*....|....*....|....*
gi 18159965 296 SAKySELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:pfam09787 163 SSQ-SELENRLHQLTETLIQKQTMLEALSTEKNSL 196
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-312 |
1.66e-06 |
|
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: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 170 QAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKAS 249
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 250 YDELSGQYTDAQRTIADLQARLSELQQRYDELSK----AEQQLREqyysLSAKYSELNGRYDELSKA 312
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEALGPvnllAIEEYEE----LEERYDFLSEQREDLEEA 810
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-332 |
1.72e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQ------------LKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLE 216
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 217 QTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLRE------ 290
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknn 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18159965 291 -QYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:TIGR04523 440 sEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-290 |
1.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 153 EDLSAQIDQLKQKIaDLQAQLKNKEAQIANLTSLLSAARLDNDRlaaalaqvraerDALRAQLEQTQAQLNAVSQAKAAL 232
Cdd:COG4717 385 EELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDE------------EELEEELEELEEELEELEEELEEL 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 233 EAQLAETRKQLEELkasydELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLRE 290
Cdd:COG4717 452 REELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
163-279 |
1.83e-06 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 49.34 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 163 KQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVsQAKAALEAQlaetrKQ 242
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANA-QAQALQTAQ-----NN 319
|
90 100 110
....*....|....*....|....*....|....*..
gi 18159965 243 LEELKASYDELSGQYTDAQRTIADLQARLSELQQRYD 279
Cdd:TIGR04320 320 LATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
158-248 |
1.85e-06 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 48.89 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 158 QIDQLKQKIADLQAQLKNKEAQIANLTSLLSAArldndrlaAALAQVRAERDALRAQLEQTQAQLNAvsQAKAALEAQLA 237
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAA--------AATAALEARLAALRAALAAAREAVAA--AAAAALEARLA 70
|
90
....*....|.
gi 18159965 238 ETRKQLEELKA 248
Cdd:COG4223 71 ALEAKAAAPEA 81
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-330 |
1.85e-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: 50.07 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQvrAER-DALRAQLEQTQAQLnaVSQAKAALEAQ 235
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK--AERyQALLKEKREYEGYE--LLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 236 LAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQ-QLREQYYSLSAKYSELNGRYDELSKAYE 314
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELE 318
|
170
....*....|....*.
gi 18159965 315 EARMNLEMLQNRYSEL 330
Cdd:TIGR02169 319 DAEERLAKLEAEIDKL 334
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
145-331 |
1.90e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.45 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIanltsllsAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:pfam12795 39 AAAYQKALDDAPAELRELRQELAALQAKAEAAPKEI--------LASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 225 VSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRT-IADLQARLSELQQRYDELsKAEQQlreqyySLSAKYSELN 303
Cdd:pfam12795 111 LQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAqRWALQAELAALKAQIDML-EQELL------SNNNRQDLLK 183
|
170 180
....*....|....*....|....*...
gi 18159965 304 GRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:pfam12795 184 ARRDLLTLRIQRLEQQLQALQELLNEKR 211
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
150-240 |
2.10e-06 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 49.17 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVE--DLSAQIDQlkqkiADLQAQLKNKEAQIANLTSLLSAARLDNDR---LAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:COG0845 43 DRVKkgQVLARLDP-----PDLQAALAQAQAQLAAAQAQLELAKAELERykaLLKKGAVSQQELDQAKAALDQAQAALAA 117
|
90
....*....|....*....
gi 18159965 225 vsqAKAALE---AQLAETR 240
Cdd:COG0845 118 ---AQAALEqarANLAYTT 133
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-338 |
2.16e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSaarldndrlaaalaQVRAERDALRAQLEQT 218
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE--------------LLEKEIERLKETIIKN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAK 298
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18159965 299 YSELNGRYDELSKAYEEARMNLEMLQNRYSELNTGFTWAL 338
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
188-290 |
2.26e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 49.69 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 188 SAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAA-LEAQLAETRKQLEELKAsydelsgQYTDAQRTIAD 266
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAeLRDELAELEEELEALKA-------RWEAEKELIEE 472
|
90 100
....*....|....*....|....
gi 18159965 267 LQARLSELQQRYDELSKAEQQLRE 290
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAE 496
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
159-283 |
2.26e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 47.98 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 159 IDQLKQKIADLQAQLKNKEaqianltSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQlnavSQAKAALEAQLAE 238
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNE-------KLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLKV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18159965 239 TRKQLEELKASYDelsgqytdaqrtiaDLQARLSELQQRYDELSK 283
Cdd:pfam13851 97 LEKELKDLKWEHE--------------VLEQRFEKVERERDELYD 127
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
157-254 |
2.32e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 49.69 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIAdlqaQLKNKEAQIANLTSLLSAARLDndRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQ- 235
Cdd:COG0542 411 EELDELERRLE----QLEIEKEALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRy 484
|
90 100
....*....|....*....|.
gi 18159965 236 --LAETRKQLEELKASYDELS 254
Cdd:COG0542 485 gkIPELEKELAELEEELAELA 505
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
137-277 |
2.75e-06 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.57 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 137 TYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLdndrLAAALAQVRAERDALRAQLE 216
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV----LAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 217 QTQAQLNAVSQAKAALEAQLAETRKQLEElkasydELSGQYTDAQRTIADLQARLSELQQR 277
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQA------EVRSELSGAQLQIAEAEAELKLAKLD 206
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
143-332 |
2.90e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 143 NYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQL 222
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 223 NAVSQAKAALEAQLAETRKQLEELKASYDE----LSGQ----------YTDAQRTIADLQARLSELQQRYDELSKAEQQL 288
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEALLEAgkcpECGQpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18159965 289 rEQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:PRK02224 502 -EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
118-289 |
3.18e-06 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 48.91 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 118 YLPNYTLSYNYYIGRVLPSTYE------DLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR 191
Cdd:TIGR01844 40 LLPQLGLTANYGYSNTYPTESRgrntdlNSGSSTLTLSQPLFDGGSTWNAVRAAEAAALAARETLRATAQDLILRTAEAY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 192 LDNDRLAAALAQVRAERDALRAQLEQTQAQLNA-------VSQAKAAL---EAQLAETRKQLEELKASYDELSGQYTDAQ 261
Cdd:TIGR01844 120 MEVLRAQEILALAEANLAALKEQLDLARARFDVglgtrtdVLQAEARYasaRAQLIQAQNNLDDAKAQLRRLVGQPELAP 199
|
170 180
....*....|....*....|....*...
gi 18159965 262 RTIADLQArlsELQQRYDELSKAEQQLR 289
Cdd:TIGR01844 200 LAVPSFPA---ELPEPLDQLLEIAEASN 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-290 |
4.48e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 225 VSQAKAALEAQLAETRKQLEELKASYDELsG--------QYtdaqrtiADLQARLSELQQRYDELSKAEQQLRE 290
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEAL-GpvnllaieEY-------EELEERYDFLSEQREDLEEARETLEE 816
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-276 |
4.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIA---DLQAQLKNKEAQIANLtsllsaarldNDRLAAALAQVRAERdalRAQ 214
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAEL----------QEELEELLEQLSLAT---EEE 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 215 LEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSgqytdAQRTIADLQARLSELQQ 276
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-----NELEAAALEERLKEARL 250
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
153-291 |
4.66e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.54 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 153 EDLSAQIDQLKQKIADLQAQlknKEAQIANLTSLLSAA-----------------RLDNDRLAAALAQVRAERDALRAQL 215
Cdd:PRK11637 99 NQLNKQIDELNASIAKLEQQ---QAAQERLLAAQLDAAfrqgehtglqlilsgeeSQRGERILAYFGYLNQARQETIAEL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 216 EQTQAQLnavSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQ 291
Cdd:PRK11637 176 KQTREEL---AAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS 248
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
140-292 |
5.12e-06 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 46.96 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 140 DLANYAASLEQKVEdlsaQIDQLKQK-IADLQAQLKNKEAQIANLTSLLSaarldnDRLAAALAQVRAERDALRAQLEQ- 217
Cdd:pfam15665 50 DLKRRIQTLEESLE----QHERMKRQaLTEFEQYKRRVEERELKAEAEHR------QRVVELSREVEEAKRAFEEKLESf 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADL-QARLSELQQRYDELSKAEQQLREQY 292
Cdd:pfam15665 120 EQLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLAEQEKLEELhKAELESLRKEVEDLRKEKKKLAEEY 195
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
206-302 |
5.25e-06 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 45.45 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 206 AERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKaSYDELSGQY---------TDAQRTIADLQARLSELQQ 276
Cdd:PRK09343 7 PEVQAQLAQLQQLQQQLERLLQQKSQIDLELREINKALEELE-KLPDDTPIYkivgnllvkVDKTKVEKELKERKELLEL 85
|
90 100
....*....|....*....|....*.
gi 18159965 277 RYDELSKAEQQLREQYYSLSAKYSEL 302
Cdd:PRK09343 86 RSRTLEKQEKKLREKLKELQAKINEM 111
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-331 |
5.63e-06 |
|
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: 48.63 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 154 DLSAQIDQLKQKIADLQAQLKNKEAQianltsllsaarLDNDRLAAALAQvrAERDALRAQLEQTQAQLNAVSQAK---- 229
Cdd:pfam01576 732 DLQARDEQGEEKRRQLVKQVRELEAE------------LEDERKQRAQAV--AAKKKLELDLKELEAQIDAANKGReeav 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 230 ---AALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQrydELSKAEQQ----------LREQYYSLS 296
Cdd:pfam01576 798 kqlKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE---DLAASERArrqaqqerdeLADEIASGA 874
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18159965 297 AKYS-------ELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:pfam01576 875 SGKSalqdekrRLEARIAQLEEELEEEQSNTELLNDRLRKST 916
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
158-322 |
5.83e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 158 QIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVR---AERD----ALRAQLEQTQAQLnavsqaka 230
Cdd:pfam10174 395 KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEriieRLKEQREREDRER-------- 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 231 aLEaQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRydeLSKAEQQLREQYYSLSAKYSELNGRYDELS 310
Cdd:pfam10174 467 -LE-ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASS---GLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
|
170
....*....|....*
gi 18159965 311 KAYE---EARMNLEM 322
Cdd:pfam10174 542 KAHNaeeAVRTNPEI 556
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
140-330 |
5.93e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.20 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 140 DLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQianltsllsaarldNDRLAAALAQVRAERDALRAQLEQTQ 219
Cdd:pfam05557 301 SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL--------------VRRLQRRVLLLTKERDGYRAILESYD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAvSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELsKAEQQLREQYYSlsaky 299
Cdd:pfam05557 367 KELTM-SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-RQQESLADPSYS----- 439
|
170 180 190
....*....|....*....|....*....|.
gi 18159965 300 selNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:pfam05557 440 ---KEEVDSLRRKLETLELERQRLREQKNEL 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-302 |
6.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQ---LKQKIADLQAQLKNKEAQIANLTSLL-----SAARLDNDRLAA---------A 200
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKElepfyneylE 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 201 LAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDE-----LSGQYTDAQRTIADLQARLSELQ 275
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELE 686
|
170 180
....*....|....*....|....*..
gi 18159965 276 QRYDELSKAEQQLREQYYSLSAKYSEL 302
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
141-336 |
6.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 141 LANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVR-AERDALRAQLEQTQ 219
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEeLEEELQLEELEQEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAKAALE-AQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLS--ELQQRYDELSKAEQQLREQYYSLS 296
Cdd:COG4717 373 AALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELR 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18159965 297 AKYSELN---------GRYDELSKAYEEARMNLEMLQNRYSELNTGFTW 336
Cdd:COG4717 453 EELAELEaeleqleedGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
138-302 |
7.61e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDL-ANYAASLEQKVEDLSAQIDQL-----KQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDAL 211
Cdd:PRK04778 73 WDEIvTNSLPDIEEQLFEAEELNDKFrfrkaKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 RAQLEQTQAQLnavSQAKAALEAQLAetrkQLEELKASYDEL--SGQYTDAQRTIADLQARLSELQQRYDE----LSKAE 285
Cdd:PRK04778 153 RKSLLANRFSF---GPALDELEKQLE----NLEEEFSQFVELteSGDYVEAREILDQLEEELAALEQIMEEipelLKELQ 225
|
170
....*....|....*..
gi 18159965 286 QQLREQYYSLSAKYSEL 302
Cdd:PRK04778 226 TELPDQLQELKAGYREL 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-331 |
8.27e-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: 48.13 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 211 LRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKAS------YDELSGQYTDAQRTIadLQARLSELQQRYDELSKA 284
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQaekaerYKELKAELRELELAL--LVLRLEELREELEELQEE 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18159965 285 EQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
153-290 |
9.29e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 153 EDLSAQIDQLKqKIADLQAQLKnkeAQIANLTSLLsaarldndRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAAL 232
Cdd:PRK11281 39 ADVQAQLDALN-KQKLLEAEDK---LVQQDLEQTL--------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 233 EAQLAETRKQ------LEELKASYDELSGQYTDAQRTIADLQARLSELQQRYD----ELSKAEQQLRE 290
Cdd:PRK11281 107 KDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaALYANSQRLQQ 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-277 |
1.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEqKVEDLSAQIDQLKQKIADLQA-------QLKNKEAQIANLTSLLSAARL-----DNDRLAAALAQVRA 206
Cdd:PRK02224 589 ESLERIRTLLA-AIADAEDEIERLREKREALAElnderreRLAEKRERKRELEAEFDEARIeeareDKERAEEYLEQVEE 667
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 207 ERDALRAQLEQTQAQLNAVSQAKAALEAqLAETRKQLEELKASYDELSGQYTDAQRTIADLQArlsELQQR 277
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEELEE-LRERREALENRVEALEALYDEAEELESMYGDLRA---ELRQR 734
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
196-330 |
1.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 196 RLAAALAQVRAERDALRAQLEQTQAQLNA-------VSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQ 268
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQlreeleqAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 269 ARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
145-322 |
1.12e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDlsaQIDQLKQKIADLQAQLKnkeaqianltsllsaarldndRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:COG1842 14 INALLDKAED---PEKMLDQAIRDMEEDLV---------------------EARQALAQVIANQKRLERQLEELEAEAEK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 225 V-SQAKAALEA---QLAetRKQLEElkasydelsgqytdaqrtIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYS 300
Cdd:COG1842 70 WeEKARLALEKgreDLA--REALER------------------KAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLE 129
|
170 180
....*....|....*....|..
gi 18159965 301 ELNGRYDELSKAYEEARMNLEM 322
Cdd:COG1842 130 ELKAKKDTLKARAKAAKAQEKV 151
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
136-245 |
1.13e-05 |
|
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: 47.64 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQL 215
Cdd:COG3096 550 DAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
|
90 100 110
....*....|....*....|....*....|
gi 18159965 216 EQTQAQLNAVSQAKaALEAQLAETRKQLEE 245
Cdd:COG3096 630 AAMQQLLEREREAT-VERDELAARKQALES 658
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
150-292 |
1.15e-05 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 45.80 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDLSAQIDQLKQKIADLqaqlknkEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALrAQLEQTQAQLNAVSQAK 229
Cdd:pfam15035 16 QLVQKLQAKVLQYKKRCSEL-------EQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHS-ADLEEALIRLEEERQRS 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18159965 230 AALEAQLAETRKQLEELKASYDELSgqyTDAQRTIADLQARLSELQQRYDELSKAEQQLREQY 292
Cdd:pfam15035 88 ESLSQVNSLLREQLEQASRANEALR---EDLQKLTNDWERAREELEQKESEWRKEEEAFNEYL 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-274 |
1.19e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 132 RVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAAL-AQVRAERDA 210
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEE 969
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 211 LRAQLEQTQAQLNAVSQAK-AALEaqlaetrkQLEELKASYDELSGQYTDAQRTIADLQARLSEL 274
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNlAAIE--------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
185-331 |
1.19e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 185 SLLSAAR----LDN-DRLAAALAQVRAERDALRaqleQTQAQLNAVSQAKAALEAQLAETRKQLEELKA----------- 248
Cdd:COG0497 136 SLLDPDAqrelLDAfAGLEELLEEYREAYRAWR----ALKKELEELRADEAERARELDLLRFQLEELEAaalqpgeeeel 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 249 -------------------SYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDEL 309
Cdd:COG0497 212 eeerrrlsnaeklrealqeALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSL 291
|
170 180
....*....|....*....|..
gi 18159965 310 SkaYEEARmnLEMLQNRYSELN 331
Cdd:COG0497 292 E--FDPER--LEEVEERLALLR 309
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
125-324 |
1.70e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 125 SYNYYIGRVLPSTYEDLANYaaslEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQV 204
Cdd:PHA02562 199 TYNKNIEEQRKKNGENIARK----QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALR---------AQLEQTQAQLNAVSQAKAALEAQLA---ETRKQLEELKASYDELSGQYTDAQRTIADLQARLS 272
Cdd:PHA02562 275 QKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEkldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLI 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18159965 273 ELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQ 324
Cdd:PHA02562 355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
133-324 |
1.76e-05 |
|
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: 47.14 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 133 VLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLT------------SLLSAARLDNDRLAAA 200
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFdekqsekdkknkALAERKDSANERLNSL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 201 LAQVRAERDALRAQLEQTQ----------------------AQLNAVSQAKAALEAQLAETRKQLEELKASydELSGQYT 258
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEEQKeqkreartekqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKR--DLASLGV 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 259 DAQ------RTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSElngRYDELSKAYEEARMNLEMLQ 324
Cdd:pfam12128 766 DPDviaklkREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT---QLSNIERAISELQQQLARLI 834
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
111-317 |
1.84e-05 |
|
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: 47.04 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 111 ILLEIWIYLPNYTLSYNYYIGRVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIAN-------- 182
Cdd:pfam15921 185 VLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkielllqq 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 183 ----LTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQL---NAVSQAK-AALEAQLAETRKQLEELKASYDEls 254
Cdd:pfam15921 265 hqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqNSMYMRQlSDLESTVSQLRSELREAKRMYED-- 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18159965 255 gQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAkysELNGRYDELSKAYEEAR 317
Cdd:pfam15921 343 -KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA---DLHKREKELSLEKEQNK 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-330 |
2.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 185 SLLSAARLDNDRLAAALAQVRAER--DALRAQLEQTQAQLNAVSQAKaaLEAQLAETRKQLEELKASYDELSGQYTDAQR 262
Cdd:PRK02224 157 DLLQLGKLEEYRERASDARLGVERvlSDQRGSLDQLKAQIEEKEEKD--LHERLNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 263 TIADLQARLSELQQRYDELSKAEQQLREqyysLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEELEEERDDL 298
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-287 |
2.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 197 LAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQ 276
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90
....*....|.
gi 18159965 277 RYDELSKAEQQ 287
Cdd:COG3883 87 ELGERARALYR 97
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
141-332 |
2.49e-05 |
|
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: 46.21 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 141 LANYAASLEQKVEDLSAQIDQLKQKIA----DLQAQLKNKEAQIANLTSL----------LSAARLDNDRLAAALAQVRA 206
Cdd:pfam19220 144 LREEAQAAEKALQRAEGELATARERLAlleqENRRLQALSEEQAAELAELtrrlaeletqLDATRARLRALEGQLAAEQA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 207 ERDALRAQLEQTQAQ-----------LNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQ 275
Cdd:pfam19220 224 ERERAEAQLEEAVEAhraeraslrmkLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLE 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 276 QrydELSKAEQQLREqyysLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:pfam19220 304 A---DLERRTQQFQE----MQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
135-246 |
2.57e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 135 PSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAE---RDAL 211
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEfedSQDV 629
|
90 100 110
....*....|....*....|....*....|....*
gi 18159965 212 RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEEL 246
Cdd:PRK04863 630 TEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
193-292 |
2.58e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 45.87 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 193 DNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQ-YTDAQRTIADLQARL 271
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNnLATAQAALANAEARL 334
|
90 100
....*....|....*....|.
gi 18159965 272 SELQQRYDELSKAEQQLREQY 292
Cdd:TIGR04320 335 AKAKEALANLNADLAKKQAAL 355
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
146-240 |
2.94e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSA------QIDQLKQKIADLQAQLKNKEAQIANLTSLL-----SAARLDNDR---------LAAALAQVR 205
Cdd:COG1566 93 AAAEAQLARLEAelgaeaEIAAAEAQLAAAQAQLDLAQRELERYQALYkkgavSQQELDEARaaldaaqaqLEAAQAQLA 172
|
90 100 110
....*....|....*....|....*....|....*..
gi 18159965 206 AERDALR--AQLEQTQAQLNAVSQAKAALEAQLAETR 240
Cdd:COG1566 173 QAQAGLReeEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-231 |
3.06e-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: 45.53 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQT 218
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
90
....*....|...
gi 18159965 219 QAQLNAVSQAKAA 231
Cdd:COG4942 233 EAEAAAAAERTPA 245
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
149-348 |
3.12e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLD------NDRLAAALAQVRAERDALR------AQLE 216
Cdd:PRK10929 64 LERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEqeilqvSSQLLEKSRQAQQEQDRAReisdslSQLP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 217 QTQA----QLNAVSQAKAAL--------EAQLAETRKQLEELKASYDELS-GQYTDAQRT-IADLQARLseLQQRYDELS 282
Cdd:PRK10929 144 QQQTearrQLNEIERRLQTLgtpntplaQAQLTALQAESAALKALVDELElAQLSANNRQeLARLRSEL--AKKRSQQLD 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 283 KAEQQLREQYYSLsakyselngRYDELSKAYEearmNLEMLQNRYSELNTGFTWALNTATALGIAL 348
Cdd:PRK10929 222 AYLQALRNQLNSQ---------RQREAERALE----STELLAEQSGDLPKSIVAQFKINRELSQAL 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
155-297 |
3.17e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 155 LSAQIDQLKQKIADLQAQLKNKEAQIANLTSLlsAARLDNDRLAAALAQvraerdALRAQLEqtqAQLNAVSQAKAALEA 234
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEF--CKRLGKNLDDEDELE------QLQEELE---ARLESLSESVSEARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 235 QLAETRKQLEELKASYDELSGQ---------------------YTDAQR---TIADLQARLSELQQRYDELSKAEQQLRE 290
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARapawlaaqdalarlreqsgeeFEDSQDvteYMQQLLERERELTVERDELAARKQALDE 659
|
....*..
gi 18159965 291 QYYSLSA 297
Cdd:PRK04863 660 EIERLSQ 666
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
190-272 |
3.49e-05 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 45.38 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 190 ARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNavsQAKaALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQA 269
Cdd:TIGR01730 55 ARLDDDDYQLALQAALAQLAAAEAQLELAQRSFE---RAE-RLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQL 130
|
...
gi 18159965 270 RLS 272
Cdd:TIGR01730 131 NLR 133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
146-265 |
3.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAV 225
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18159965 226 SQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIA 265
Cdd:COG3883 223 AAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
154-290 |
4.15e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 154 DLSAQIDqLKQKIADLQAQL-----KNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQA 228
Cdd:pfam00038 161 DAARKLD-LTSALAEIRAQYeeiaaKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 229 KAALEAQLAETRkqleelkasyDELSGQYTDAQRTIADLQArlsELQQRYDELskaEQQLRE 290
Cdd:pfam00038 240 KASLERQLAETE----------ERYELQLADYQELISELEA---ELQETRQEM---ARQLRE 285
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
183-281 |
4.47e-05 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 42.77 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 183 LTSLLSAARLDNDRLAAALAQVRaerdalraQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQR 262
Cdd:pfam04871 10 ASSLKNENTELKAELQELSKQYN--------SLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELDDLLL 81
|
90
....*....|....*....
gi 18159965 263 TIADLQARLSELQQRYDEL 281
Cdd:pfam04871 82 LLGDLEEKVEKYKARLKEL 100
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
150-256 |
4.47e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDR-------LAAALAQVRAERDALRAQLEQTQAQL 222
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERelvlhaeDIKALQALREELNELKAEIAELKAEA 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 18159965 223 NAVSQAKAALEAQLAETRKQLE----ELKASYDELSGQ 256
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEkelsELEKRIEDLNEQ 118
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
208-332 |
4.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 208 RDALRAQLEQTQAQLNAVSQAKAALE----AQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSK 283
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlkelKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 18159965 284 AEQ--QLREQYYSLSAKYSELNGRYDELS---KAYEEARMNLEMLQNRYSELNT 332
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQE 177
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
148-297 |
4.85e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 44.29 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLlsAARLDNDrlaAALAQVRAERDALRAQLEQTQaqlNAVSQ 227
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQ--AKKLEEK---AQAALTKGNEELAREALAEKK---SLEKQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 228 AkAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSElqqrydelSKAEQQLREQYYSLSA 297
Cdd:pfam04012 99 A-EALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKA--------AKAQEAVQTSLGSLST 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
139-335 |
5.48e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEA--QIANLTSLLSAARLDN-DRLAAALAQVRAERDALRAQ- 214
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEi 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 215 --LEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQytdaqrTIADLQARLSELQ---QRYDELSKAEQQLR 289
Cdd:PRK03918 542 ksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE------SVEELEERLKELEpfyNEYLELKDAEKELE 615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18159965 290 EQYYSLSAKYSELNGRYDELSKAYEEarmnLEMLQNRYSELNTGFT 335
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKR----LEELRKELEELEKKYS 657
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
160-295 |
6.01e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 160 DQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQtQAQlNAVSQAKAALEAQLAET 239
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK-EAQ-QAIKEAKKEADEIIKEL 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 240 RKQLEELKASYDElsgqytdaqrtiADLQARLSELQQRYDELSKAEQQLREQYYSL 295
Cdd:PRK00409 594 RQLQKGGYASVKA------------HELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
135-269 |
6.40e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 135 PSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAarlDNDRLAAALAQvrAERDALRAQ 214
Cdd:cd22656 106 ATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET---LEKALKDLLTD--EGGAIARKE 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 215 LEQTQAQLnavsqaKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQA 269
Cdd:cd22656 181 IKDLQKEL------EKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTA 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-305 |
7.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 192 LDNDRLAAALAQVRAERDAL---RAQLEQTQAQLNAVSQAKAALE--AQLAETRKQLEELKA--SYDELSGQYTDAQRTI 264
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLeraHEALEDAREQIELLEPIRELAEryAAARERLAELEYLRAalRLWFAQRRLELLEAEL 297
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18159965 265 ADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGR 305
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD 338
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
136-330 |
7.41e-05 |
|
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: 45.17 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQ----------------------------AQLKNKEAQIANLTSLL 187
Cdd:pfam01576 566 AAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEkkqkkfdqmlaeekaisaryaeerdraeAEAREKETRALSLARAL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 188 SAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKasyDELSG------------ 255
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELE---DELQAtedaklrlevnm 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 256 QYTDAQRTiADLQARLSELQQRYDELSKA--------EQQLREQYYSLSAK------YSELNGRYDELSKAYEEARMNLE 321
Cdd:pfam01576 723 QALKAQFE-RDLQARDEQGEEKRRQLVKQvreleaelEDERKQRAQAVAAKkkleldLKELEAQIDAANKGREEAVKQLK 801
|
....*....
gi 18159965 322 MLQNRYSEL 330
Cdd:pfam01576 802 KLQAQMKDL 810
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
140-288 |
7.77e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 140 DLANYAASLEQKVEDlSAQIDQLKQKIADLQAQLKNKEAQIANLTSllsaarldnDRLAAALAQVRAERdALRAQLEQTQ 219
Cdd:PRK10246 364 ELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPAITLTLTA---------DEVAAALAQHAEQR-PLRQRLVALH 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18159965 220 AQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQArLSELQQRYDELSKAEQQL 288
Cdd:PRK10246 433 GQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT-ICEQEARIKDLEAQRAQL 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
207-329 |
7.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 207 ERDALRAQLEQTQAQLNAVSQAKAALEaQLAETRKQLEELKASYDElsgqYTDAQRTIADLQARLSEL-----QQRYDEL 281
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALE-DAREQIELLEPIRELAER----YAAARERLAELEYLRAALrlwfaQRRLELL 293
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 18159965 282 SKAEQQLREQYyslsakySELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:COG4913 294 EAELEELRAEL-------ARLEAELERLEARLDALREELDELEAQIRG 334
|
|
| DUF4349 |
pfam14257 |
Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. ... |
147-215 |
8.12e-05 |
|
Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important. The N-terminus contains a lipoprotein signal peptide sequence.
Pssm-ID: 464117 [Multi-domain] Cd Length: 213 Bit Score: 43.31 E-value: 8.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 147 SLEQKVEDLSAQIdqlkqkiADLQAQLKNKEAQIANLTSLLSAARLDNDRLAA--ALAQVRAERDALRAQL 215
Cdd:pfam14257 75 SRSISAEDVTEQY-------VDLEARLKALRASEDRLLALLERAGSVEDLLAVerELSEVQAELESLEGQL 138
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
138-291 |
9.97e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQkiADLQA----QLKNKEAQIANLTSLLSAAR-----LDN------DRLAAA-- 200
Cdd:COG0497 174 LEELRADEAERARELDLLRFQLEELEA--AALQPgeeeELEEERRRLSNAEKLREALQealeaLSGgeggalDLLGQAlr 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 201 ----LAQVRAERDALRAQLEQTQAQLNAVS--------------QAKAALEAQLAE----TRK---QLEELKASYDELSG 255
Cdd:COG0497 252 alerLAEYDPSLAELAERLESALIELEEAAselrryldslefdpERLEEVEERLALlrrlARKygvTVEELLAYAEELRA 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 18159965 256 QY---TDAQRTIADLQARLSELQQRYDELSKAEQQLREQ 291
Cdd:COG0497 332 ELaelENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
145-325 |
1.25e-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: 44.17 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLknkeaqianltSLLSAARLDNDRLAAALAQVRAERDALRA-----QLEQTQ 219
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKL-----------SVADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRY 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAKAALEAQLAETRKQLEELKasydelsgqytDAQRTIADLQAR--------------LSELQQRYDELSKAE 285
Cdd:COG3096 505 RSQQALAQRLQQLRAQLAELEQRLRQQQ-----------NAERLLEEFCQRigqqldaaeeleelLAELEAQLEELEEQA 573
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18159965 286 QQLREQYYSLSAKYSELNGRYDELSK---AYEEARMNLEMLQN 325
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLRE 616
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
160-291 |
1.26e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 160 DQLKQKIADLQAQLKN----KEAQ-------------IANLTSLLSAARLDNDRLAAALAQVRAErdaLRAQLEQTQA-- 220
Cdd:pfam15921 377 DQLQKLLADLHKREKElsleKEQNkrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSE---CQGQMERQMAai 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 221 -----QLNAVSQAKAALEAQLAETRKQLEELKASYDELSgqytDAQRTIADLQARLSElQQRYDELSKAE-QQLREQ 291
Cdd:pfam15921 454 qgkneSLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE----SSERTVSDLTASLQE-KERAIEATNAEiTKLRSR 525
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
146-326 |
1.32e-04 |
|
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: 44.06 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQidqLKQKIADLQAQLKNKeaqIANLTSLLSAARldndrlaAALAQVRAERDALRAQ----------- 214
Cdd:pfam12128 275 ASRQEERQETSAE---LNQLLRTLDDQWKEK---RDELNGELSAAD-------AAVAKDRSELEALEDQhgafldadiet 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 215 -------LEQTQAQLNAVSQAKAALEA------QLAETRKQL-------------EELKASYDELSGQYTDAQrtiADLQ 268
Cdd:pfam12128 342 aaadqeqLPSWQSELENLEERLKALTGkhqdvtAKYNRRRSKikeqnnrdiagikDKLAKIREARDRQLAVAE---DDLQ 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 269 ARLSELQqryDELSKAEQQLREQYYSLSAKYSELNGRYDELSkAYEEARMNLEMLQNR 326
Cdd:pfam12128 419 ALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT-ATPELLLQLENFDER 472
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
148-288 |
1.35e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQK-------------------IADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAER 208
Cdd:COG1842 56 LERQLEELEAEAEKWEEKarlalekgredlarealerKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 209 DALRAQLEQTQAQ------LNAVSQAKAALEAQLAETRKQLEELKA-SYDELSGQytdaqrtiADLQARLSELQQRydel 281
Cdd:COG1842 136 DTLKARAKAAKAQekvneaLSGIDSDDATSALERMEEKIEEMEARAeAAAELAAG--------DSLDDELAELEAD---- 203
|
....*..
gi 18159965 282 SKAEQQL 288
Cdd:COG1842 204 SEVEDEL 210
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-262 |
1.46e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQL 215
Cdd:COG3883 112 ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18159965 216 EQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQR 262
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
197-288 |
1.53e-04 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 42.99 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 197 LAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELsgqytdaQRTIADLQARLSELQQ 276
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQL-------ERLVASQEQEIASLER 83
|
90
....*....|..
gi 18159965 277 RYDELSKAEQQL 288
Cdd:pfam11932 84 QIEEIERTEREL 95
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
131-335 |
1.62e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 131 GRVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQ------------------KIADLQAQLKN--------KEAQIANLT 184
Cdd:cd22656 18 GLLLPTTEEEYRKRLGISSDIDDKLSSDFDPLLDayksikdhctdfkddtypSIVSLAGDIYNyaqnaggtIDSYYAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 185 SLLSAARL--DNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQY--TDA 260
Cdd:cd22656 98 ELIDDLADatDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEggAIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 261 QRTIADLQARLSELQQRY-DELSKAEQQLREQYYSLSAK----------YSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:cd22656 178 RKEIKDLQKELEKLNEEYaAKLKAKIDELKALIADDEAKlaaalrliadLTAADTDLDNLLALIGPAIPALEKLQGAWQA 257
|
....*.
gi 18159965 330 LNTGFT 335
Cdd:cd22656 258 IATDLD 263
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
146-243 |
1.73e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSA--ARLDNDRLAAALAQVRAERDalRAQLEQTQAQLn 223
Cdd:COG3524 224 ATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAerARLTGASGGDSLASLLAEYE--RLELEREFAEK- 300
|
90 100
....*....|....*....|
gi 18159965 224 AVSQAKAALEAQLAETRKQL 243
Cdd:COG3524 301 AYTSALAALEQARIEAARQQ 320
|
|
| DAHL |
pfam19443 |
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic ... |
131-292 |
1.76e-04 |
|
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic sensory domain, which is found in major types of bacterial signal transduction proteins: histidine kinases and diguanylate cyclases/phosphodiesterases, and, occasionally in chemoreceptors. The majority of the DAHL domain-containing proteins were found in alpha-, beta-, gamma- and epsilonproteobacteria. It is also present in some cyanobacterial species. Secondary structure prediction suggested that DAHL consists predominantly of alpha-helical regions. The DAHL domain was identified in the Tlp10 chemoreceptor from the human pathogen Campylobacter jejuni and in the VirA sensor histidine kinase from a plant pathogen Agrobacterium tumefaciens. This domain recognizes Asp, Ile, purine, fumarate, malate, alpha-ketoglutarate, mannose, rhamnose, fucose, sialic acid, Arg, thiamine and galactose (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 466085 [Multi-domain] Cd Length: 222 Bit Score: 42.43 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 131 GRVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIAdlqaQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAE--- 207
Cdd:pfam19443 59 SFLLAGDSAELDAALAALRAALQEKEELVERFKSQNA----LLRNSLAYFPTLVDELLAASPAEPALAAALNELLRAvll 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 208 --------RDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEeLKASYDELSGQYTDAqrtiaDLQARLSELQQRYD 279
Cdd:pfam19443 135 ynlssdpaLAEIEALLERLEALAESAPALRAALQLLLAHARLILR-LLPQVDALLQEILAL-----PTAAALEALEAAYL 208
|
170
....*....|...
gi 18159965 280 ELSKAEQQLREQY 292
Cdd:pfam19443 209 AAYQQALARAERY 221
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
155-321 |
1.78e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 155 LSAQIDQLKQKIADLQAQL----KNKEAQIANLTSLLSaARLDNDrLAAALAQVRAERDALRAQL----EQTQAQLNAVS 226
Cdd:pfam01442 2 LEDSLDELSTYAEELQEQLgpvaQELVDRLEKETEALR-ERLQKD-LEEVRAKLEPYLEELQAKLgqnvEELRQRLEPYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 QA-KAALEAQLAETRKQLEELKASYDELSGQYTDAQRtiADLQARLSELQQRYDE-LSKAEQQLREQYYSLSAKyseLNG 304
Cdd:pfam01442 80 EElRKRLNADAEELQEKLAPYGEELRERLEQNVDALR--ARLAPYAEELRQKLAErLEELKESLAPYAEEVQAQ---LSQ 154
|
170
....*....|....*..
gi 18159965 305 RYDELSKAYEEARMNLE 321
Cdd:pfam01442 155 RLQELREKLEPQAEDLR 171
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
150-330 |
1.79e-04 |
|
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: 43.63 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDLSAQIDQLKQKIADLQ---AQLKNKEAQIANLTSLLSAARLDNDRlaaalaqvraERDALRAQLEQTQAQLNAVS 226
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEH----------KRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 QAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRY 306
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL 505
|
170 180
....*....|....*....|....
gi 18159965 307 DELSKAYEEARMNLEMLQNRYSEL 330
Cdd:pfam01576 506 EEEEEAKRNVERQLSTLQAQLSDM 529
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
139-272 |
1.82e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYA----ASLEQKVEDLSAQIDQ----LKQKIADLQAQLKNK--------EAQIANLTS-LLSAARLDNDRLAAAL 201
Cdd:pfam01442 18 EQLGPVAqelvDRLEKETEALRERLQKdleeVRAKLEPYLEELQAKlgqnveelRQRLEPYTEeLRKRLNADAEELQEKL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 202 AQVRAE-RDALRAQLEQTQAQLNAVS-QAKAALEAQLAETRKQLEELKASY-DELSGQYTDAQRTIA----DLQARLS 272
Cdd:pfam01442 98 APYGEElRERLEQNVDALRARLAPYAeELRQKLAERLEELKESLAPYAEEVqAQLSQRLQELREKLEpqaeDLREKLD 175
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
135-237 |
1.82e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 43.32 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 135 PSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKE-------AQIANLTSLLSAARLD-------------- 193
Cdd:PRK12472 189 PARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLErakaradAELKRADKALAAAKTDeakaraeerqqkaa 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 194 ------NDRLAAALAQVRAERDALRAQLEQ-TQAQLNAVSQAKAALEAQLA 237
Cdd:PRK12472 269 qqaaeaATQLDTAKADAEAKRAAAAATKEAaKAAAAKKAETAKAATDAKLA 319
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-325 |
1.87e-04 |
|
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: 43.63 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 141 LANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQA 220
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQ-------LREQYY 293
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdLQEQIA 225
|
170 180 190
....*....|....*....|....*....|....*..
gi 18159965 294 SLSAKYSELNGrydELSKAYEE-----ARMNLEMLQN 325
Cdd:pfam01576 226 ELQAQIAELRA---QLAKKEEElqaalARLEEETAQK 259
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
134-330 |
2.11e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYaasLEQKVEDLSAQIDQLK------------QKIADLQAQLKNKEAQIANLTslLSAARLDNDRLAAAL 201
Cdd:pfam06160 198 IPPLYEELKTE---LPDQLEELKEGYREMEeegyalehlnvdKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 202 AQ----VRAERDA-----------------LRAQLEQTQAQLNAVSQAKAALEAQLAETR---KQLEELKASYDELSGQY 257
Cdd:pfam06160 273 DQlydlLEKEVDAkkyveknlpeiedylehAEEQNKELKEELERVQQSYTLNENELERVRgleKQLEELEKRYDEIVERL 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18159965 258 TDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLsakyselngRYDELskayeEARMNLEMLQNRYSEL 330
Cdd:pfam06160 353 EEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSL---------RKDEL-----EAREKLDEFKLELREI 411
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
194-309 |
2.22e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 194 NDRLAAALAQVRA---ERDALRAQLEQTQAQLNA-VSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQA 269
Cdd:pfam00038 10 NDRLASYIDKVRFleqQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQ 89
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18159965 270 RLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDEL 309
Cdd:pfam00038 90 KYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESL 129
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
148-332 |
2.23e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQA-------QLKNKEAQIANLTSllsaarldndrlaaalaqvraERDALRAQLEQTQA 220
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSdlskinsEIKNDKEQKNKLEV---------------------ELNKLEKQKKENKK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEAQLA-------ETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQqlreQYY 293
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNK 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 18159965 294 SLSAKYSELNGRYDELSKayeearmNLEMLQNRYSELNT 332
Cdd:TIGR04523 215 SLESQISELKKQNNQLKD-------NIEKKQQEINEKTT 246
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
200-330 |
2.52e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 200 ALAQVRAERD----ALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRtiadlQARLSELQ 275
Cdd:pfam15905 84 ALVQERGEQDkrlqALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGT-----QKKMSSLS 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 276 QrydELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:pfam15905 159 M---ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST 210
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-311 |
2.53e-04 |
|
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: 43.24 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLAN---YAASLEQKVEDLSAQIDQLKQKIAD------LQAQLKNKEAQiaNLTSLLSAARLDNDRLAAALAQVRAER- 208
Cdd:pfam01576 278 EDLESeraARNKAEKQRRDLGEELEALKTELEDtldttaAQQELRSKREQ--EVTELKKALEEETRSHEAQLQEMRQKHt 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 209 ---DALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAE 285
Cdd:pfam01576 356 qalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
|
170 180
....*....|....*....|....*.
gi 18159965 286 QQLREQYYSLSAKYSELNGRYDELSK 311
Cdd:pfam01576 436 SKLQSELESVSSLLNEAEGKNIKLSK 461
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
134-291 |
2.66e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYAASLEQKvedlSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAA---ALAQVRAERDA 210
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQR----DTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAserKVEGLGEELSS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 211 LRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYdelSGQYTDAQRTIADLQARLSELQqryDELSKAEQQLRE 290
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARW---AQERETLQQSAEADKDRIEKLS---AELQRLEERLQE 336
|
.
gi 18159965 291 Q 291
Cdd:pfam07888 337 E 337
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-290 |
2.82e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVED---LSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAaalaQVRAERDALRAQLEQTQAQLN 223
Cdd:PRK03918 287 ELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 224 AVSQAKAaLEAQLAETRKQL-----EELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLRE 290
Cdd:PRK03918 363 LYEEAKA-KKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
151-270 |
2.90e-04 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 42.30 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 151 KVEDLSAQIDQlkqkiADLQAQLKNKEAQIANLTSLLSAARLDNDRlAAALAQV----RAERDALRAQLEQTQAQLNAVS 226
Cdd:TIGR01730 49 KKGQVLARLDD-----DDYQLALQAALAQLAAAEAQLELAQRSFER-AERLVKRnavsQADLDDAKAAVEAAQADLEAAK 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 227 QAKAALEAQLAETrkqleELKASYDEL-------SGQYTDAQRTIADLQAR 270
Cdd:TIGR01730 123 ASLASAQLNLRYT-----EIRAPFDGTigrrlveVGAYVTAGQTLATIVDL 168
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
157-329 |
3.09e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQL 236
Cdd:COG1538 128 AQLAQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 237 AETRKQLE---ELKASYDELSGQYT-------------------DAQRTIADLQARLSELQQRYDELSKAEQQLREQYYS 294
Cdd:COG1538 208 GVARAAFLpslSLSASYGYSSSDDLfsggsdtwsvglslslplfDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQEVED 287
|
170 180 190
....*....|....*....|....*....|....*
gi 18159965 295 LSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:COG1538 288 ALAALRAAREQLEALEEALEAAEEALELARARYRA 322
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
149-278 |
3.29e-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: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAArldndrlAAALAQVRAERDALRAQLEQTQAQLNAVSQA 228
Cdd:COG3524 206 RNGILDPEATAEALLQLIATLEGQLAELEAELAALRSYLSPN-------SPQVRQLRRRIAALEKQIAAERARLTGASGG 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18159965 229 KAaleaqLAETRKQLEELKASYDELSGQYTDAQrtIADLQARL-SELQQRY 278
Cdd:COG3524 279 DS-----LASLLAEYERLELEREFAEKAYTSAL--AALEQARIeAARQQRY 322
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
150-237 |
3.36e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.54 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDlsaQIDQLKQKIADLQAQLKNKEAQIAnltslLSAARLDN---------------DRLAAALAQVRAERDALRAQ 214
Cdd:pfam03148 268 KKTLQ---EIAELEKNIEALEKAIRDKEAPLK-----LAQTRLENrtyrpnvelcrdeaqYGLVDEVKELEETIEALKQK 339
|
90 100
....*....|....*....|...
gi 18159965 215 LEQTQAQLNAVSQAKAALEAQLA 237
Cdd:pfam03148 340 LAEAEASLQALERTRLRLEEDIA 362
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
168-264 |
3.47e-04 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 168 DLQAQLKNKEAQIANLtsllsAARLDNDRLAAALAqVRAERDALRAQLEQTQAQLNAVS----QAKA------ALEAQLA 237
Cdd:PRK05431 3 DIKLIRENPEAVKEAL-----AKRGFPLDVDELLE-LDEERRELQTELEELQAERNALSkeigQAKRkgedaeALIAEVK 76
|
90 100
....*....|....*....|....*..
gi 18159965 238 ETRKQLEELKASYDELSGQYTDAQRTI 264
Cdd:PRK05431 77 ELKEEIKALEAELDELEAELEELLLRI 103
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
205-332 |
3.71e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLseLQQRYdELSKA 284
Cdd:PRK04778 90 EAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL--LANRF-SFGPA 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18159965 285 EQQLREQYYSLSAKYSElngrYDELSKA--YEEARMNLEMLQNRYSELNT 332
Cdd:PRK04778 167 LDELEKQLENLEEEFSQ----FVELTESgdYVEAREILDQLEEELAALEQ 212
|
|
| ClyA_XaxA-like |
cd22657 |
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ... |
138-289 |
3.95e-04 |
|
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and similar proteins; This model includes Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, both parts of two-component alpha-helical pore-forming toxins (alpha-PFTs). The xaxAB genes encoding the XaxAB toxin have also been also identified in various plant and human pathogens. XaxAB triggers necrosis and apoptosis in both insect hemocytes and mammalian cells. Structure studies show that component A binds to component B's back, forming a subunit; twelve to fifteen of these subunits then conjoin as the pore-forming toxin. Component A stabilizes each subunit on the membrane and activates component B, which then punctures the membrane by swinging out its lower end. Similarly, Yersinia enterocolitica YaxA, encoded by the yaxAB gene, forms a pore predominantly composed of decamers of YaxA-YaxB heterodimers. Although both subunits bear membrane-active moieties, only YaxA is capable of binding to membranes by itself and YaxB is subsequently recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices; pore formation then progresses by further oligomerization of YaxA-YaxB dimers. YaxAB has been found to be strongly upregulated by the Yersinia master regulator RovA, a transcriptional activator of Yersinia outer membrane protein invasion which is involved in bacterial attachment and invasion across the intestinal epithelium.
Pssm-ID: 439155 [Multi-domain] Cd Length: 306 Bit Score: 41.80 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEA-QIANLTSLLSAARLDNDrlaaaLAQVRAERDALRAQLE 216
Cdd:cd22657 90 ISDLGEYLEDIKEDIKEYSKSTEEVKARLDDFRDELREELIpEVKLKLKLIDRNDLDEE-----IEELNEEIDELDEEID 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 217 QTQAQLNAVSQAKAA---------------LEAQLAETRKQLEELKASYDELSGQYTDAQRTIA---DLQARLSELQQRY 278
Cdd:cd22657 165 ELNKEYKKLVGLAFTglaggpigllitggiFGVKAEKIRKERNELIAEREELIQKLKSKNRLLGsleRLETDLQDLDIRM 244
|
170
....*....|.
gi 18159965 279 DELSKAEQQLR 289
Cdd:cd22657 245 IDAEVATKNLE 255
|
|
| LXG |
pfam04740 |
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ... |
152-335 |
4.18e-04 |
|
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of polymorphic toxin proteins in bacteria. It is predicted to use Type VII secretion pathway to mediate export of bacterial toxins.
Pssm-ID: 428100 [Multi-domain] Cd Length: 202 Bit Score: 41.08 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 152 VEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLlsaarldNDRL---AAalaqvraerDALRAQLEQTQAQ-LNAVSQ 227
Cdd:pfam04740 5 VSELIEGIDQTISELKELRDQLEKVKKAIEGLANL-------EDSLkgkGG---------EAIKNFYSELHLPfLDFLQD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 228 AKAALEAQLAETRKQLEELKASYD----------ELSGQYTDAQRTIADLQARLSELQQRY---------------DELS 282
Cdd:pfam04740 69 FIDEYIEFLEQIKAALESFEPSSNafidesflehELENGLKKAKEKTEELTDEINSILASVsdivslpklsdsevqDSLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 283 KAEQQLR---EQYYSLSAkyselngrydELSKAYEEARMNLEMLQNRYSELNTGFT 335
Cdd:pfam04740 149 KAKKKVKdtiEKLYDFDQ----------EQTSELSELEADLQALKTYVSELEEMTS 194
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
141-317 |
4.21e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 141 LANYAASLE---QKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANL--TSLLSAARLDNDRlaAALAQVRAERDALR--- 212
Cdd:PRK10246 285 LAQPARQLRphwERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhHAAKQSAELQAQQ--QSLNTWLAEHDRFRqwn 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 ---AQLEQTQAQLNAVSQAKAALEAQLAETRKQL------------EELKASYDELSGQYTDAQRtIADLQARLSELQQR 277
Cdd:PRK10246 363 nelAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLnalpaitltltaDEVAAALAQHAEQRPLRQR-LVALHGQIVPQQKR 441
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18159965 278 YDELSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEAR 317
Cdd:PRK10246 442 LAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK 481
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
158-291 |
4.84e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.55 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 158 QIDQLKQKIADLQA---QLKNKEAQIANLTSLLSA--ARLDND---RLAAALAQVRAERDALRAQLEQTQAQLNAVSQak 229
Cdd:pfam04849 165 QLDALQEKLRGLEEenlKLRSEASHLKTETDTYEEkeQQLMSDcveQLSEANQQMAELSEELARKMEENLRQQEEITS-- 242
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 230 aaLEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDE----LSKAEQQLREQ 291
Cdd:pfam04849 243 --LLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAEclgmLHEAQEELKEL 306
|
|
| LTXXQ |
pfam07813 |
LTXXQ motif family protein; This protein family includes two copies of a five residue motif is ... |
166-266 |
4.94e-04 |
|
LTXXQ motif family protein; This protein family includes two copies of a five residue motif is found in a number of bacterial proteins bearing similarity to the protein CpxP. This is a periplasmic protein that aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to alkaline pH. Another member of this family, Spy is also a periplasmic protein that may be involved in the response to stress. The homology between CpxP and Spy may indicate that these two proteins are functionally related.
Pssm-ID: 429675 Cd Length: 97 Bit Score: 38.88 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 166 IADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAqleqtQAQLNAVSQAKAALEAQLAETRKQLEE 245
Cdd:pfam07813 3 IAFIKAELKLTDAQRAQLDALRDAARAQAKPLKASCEEMRAMRKANFD-----ETAPRRLAAMEQMLEARLEAVKARAEA 77
|
90 100
....*....|....*....|.
gi 18159965 246 LKASYDELsgqyTDAQRTIAD 266
Cdd:pfam07813 78 LKQFYAIL----TPEQKAQFD 94
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
192-291 |
5.01e-04 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 41.03 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 192 LDNDRLAA--ALAQVRAERDALRAQLEQTQAQLNAVSQakaaleaqlaetRKQLEELKASYDELsGQYTDAQRTIADLQA 269
Cdd:NF038305 99 LNNTRRLStqALQQINQQAGQQETQLQQQLNQLQAQTS------------PQQLNQLLKSEQKQ-GQALASGQLPEEQKE 165
|
90 100
....*....|....*....|..
gi 18159965 270 RLSELQQRYDELSKAEQQLREQ 291
Cdd:NF038305 166 QLQQFKSNPQALDKFLAQQLTQ 187
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
142-329 |
5.09e-04 |
|
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: 42.25 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 142 ANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQI-ANLTSLLSAARLDndRLAAALAQVRAERDALRAQLEQT-Q 219
Cdd:COG5185 321 AEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIkEEIENIVGEVELS--KSSEELDSFKDTIESTKESLDEIpQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKA--EQQLREQYYSLSA 297
Cdd:COG5185 399 NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSrlEEAYDEINRSVRS 478
|
170 180 190
....*....|....*....|....*....|..
gi 18159965 298 KYSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:COG5185 479 KKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| DUF5930 |
pfam19353 |
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ... |
160-245 |
5.12e-04 |
|
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.
Pssm-ID: 466052 [Multi-domain] Cd Length: 320 Bit Score: 41.70 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 160 DQLKQKIADLQAQLKNKEAQIANLTSLLSAARldnDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAET 239
Cdd:pfam19353 150 DAARAELAALQAELEGGGAAAAARAADADATL---DFLTAALAETAAERDQIAADAQDALAEADELALEIRLMEERNDQI 226
|
....*.
gi 18159965 240 RKQLEE 245
Cdd:pfam19353 227 FRQLEE 232
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
151-331 |
5.53e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 151 KVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSL-LSAARLDNDRLAAALAQVRA-ERDALRAQLEQTQAQLNAVSQA 228
Cdd:PRK01156 523 KIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 229 KAALEAQLAE----TRKQLEELKASYDELSGQYTDAQ---RTIADLQARLSELQQRYDELSKAEQQLREqyysLSAKYSE 301
Cdd:PRK01156 603 LQEIEIGFPDdksyIDKSIREIENEANNLNNKYNEIQenkILIEKLRGKIDNYKKQIAEIDSIIPDLKE----ITSRIND 678
|
170 180 190
....*....|....*....|....*....|....*..
gi 18159965 302 LNGRYDELSKAYEEARMNL-------EMLQNRYSELN 331
Cdd:PRK01156 679 IEDNLKKSRKALDDAKANRarlestiEILRTRINELS 715
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
147-251 |
5.63e-04 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.67 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQA-QLNAV 225
Cdd:pfam10186 54 QLEDNIGNKKLKLRLLKSEVAISNERLNEIKDKLDQLRREIAEKKKKIEKLRSSLKQRRSDLESASYQLEERRAsQLAKL 133
|
90 100 110
....*....|....*....|....*....|....
gi 18159965 226 SQA-------KAALEAQLAETRKQL-EELKASYD 251
Cdd:pfam10186 134 QNSikrikqkWTALHSKTAESRSFLcRELAKLYG 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
134-287 |
6.07e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSaarlDNDRLAAALAQVRAERDALRA 213
Cdd:TIGR04523 157 LNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 214 QLEQTQAQLNAvsqakaaLEAQLAETRKQLEELKASYDELSGQYTDAQ-------RTIADLQARLSELQQRYDELSKAEQ 286
Cdd:TIGR04523 233 NIEKKQQEINE-------KTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnKKIKELEKQLNQLKSEISDLNNQKE 305
|
.
gi 18159965 287 Q 287
Cdd:TIGR04523 306 Q 306
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
180-317 |
6.31e-04 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 39.95 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 180 IANLTSLLSAARLDndrlaaalaQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTD 259
Cdd:pfam16535 8 LGNLMSLLGEVSLS---------QLESRIAAWKAMQEAQQQKGLELSDEFQTALSEAEEATDAYEKAINKLKNAKSKAKA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 260 AQRTIADLQARLSEL---QQRYDELSKAEQQLREQYYSLSAKySELNGRYDELSKAYEEAR 317
Cdd:pfam16535 79 AEKKIDQAQTRLQSLapdSPGKAKLEAAEQQAGIKKDALQAD-RTLDKALDAASKLTTKAM 138
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
146-330 |
6.34e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLqaqlknkEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAV 225
Cdd:pfam17078 48 ASLKHENDNLSSMLNRKERRLKDL-------EDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 226 SQA----KAALEAQLAETRKQLEELKAsydELSGQYTDAQRTIA----DLQARLSELQQRYDELSKAEQQlreqyyslsa 297
Cdd:pfam17078 121 VDSqneyKDHYQQEINTLQESLEDLKL---ENEKQLENYQQRISsndkDIDTKLDSYNNKFKNLDNIYVN---------- 187
|
170 180 190
....*....|....*....|....*....|...
gi 18159965 298 KYSELNGRYDELSkayeeARMNLEMLQNRYSEL 330
Cdd:pfam17078 188 KNNKLLTKLDSLA-----QLLDLPSWLNLYPES 215
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
148-297 |
6.37e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRA--ERDALRAQLEQTQAQLNAV 225
Cdd:PRK10246 424 LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTicEQEARIKDLEAQRAQLQAG 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 226 S-------------QAKAALE-----AQLAETRKQLEELKASYDELSGQytdaqrtiadLQARLSELQQRYDE---LSKA 284
Cdd:PRK10246 504 QpcplcgstshpavEAYQALEpgvnqSRLDALEKEVKKLGEEGAALRGQ----------LDALTKQLQRDESEaqsLRQE 573
|
170
....*....|...
gi 18159965 285 EQQLREQYYSLSA 297
Cdd:PRK10246 574 EQALTQQWQAVCA 586
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
146-332 |
6.46e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQlKNKEAQIANLTSLLSaaRLDNDRLAAALAQVRAERDALRAQ--LEQTQAQLN 223
Cdd:pfam15905 125 ASLEKQLLELTRVNELLKAKFSEDGTQ-KKMSSLSMELMKLRN--KLEAKMKEVMAKQEGMEGKLQVTQknLEHSKGKVA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 224 AVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELN 303
Cdd:pfam15905 202 QLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLN 281
|
170 180 190
....*....|....*....|....*....|
gi 18159965 304 GRYDELSKAYEE-ARMNLEMLQNRYSELNT 332
Cdd:pfam15905 282 EKCKLLESEKEElLREYEEKEQTLNAELEE 311
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
139-327 |
6.48e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 41.35 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLA-NYAASLEQKVEDLSAQIDQLKQKIADLQAQL-KNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLE 216
Cdd:pfam09755 95 ETLAmNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLeQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 217 QTQAQL--------NAVSQAKAALEAQLAE------TRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDE-- 280
Cdd:pfam09755 175 QEQEALvnrlwkrmDKLEAEKRLLQEKLDQpvsappSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEkm 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18159965 281 --LSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRY 327
Cdd:pfam09755 255 aqYAQEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERY 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-329 |
6.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLS--- 296
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqei 753
|
90 100 110
....*....|....*....|....*....|....*..
gi 18159965 297 ----AKYSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:TIGR02169 754 envkSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
228-303 |
6.68e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 39.30 E-value: 6.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 228 AKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELN 303
Cdd:pfam04871 2 KKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELD 77
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
139-331 |
7.14e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLsaaRLDNDRLAAALAQVRAerdaLRAQLEQT 218
Cdd:pfam05483 317 EDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL---RTEQQRLEKNEDQLKI----ITMELQKK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 219 QAQLNAVSQAKAALEAQLAETRKQL-----------------EELKASYDELSGQYTDAQRTIADLQARLSELQQRYDEL 281
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILaedeklldekkqfekiaEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 282 SKAEQQLREQYYSLSAKYSELNGRYDELS----KAYEEAR-MNLEmLQNRYSELN 331
Cdd:pfam05483 470 LKEVEDLKTELEKEKLKNIELTAHCDKLLlenkELTQEASdMTLE-LKKHQEDII 523
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
161-332 |
7.38e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 161 QLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETR 240
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 241 KQLEELKASYDELSGQYTDAQrTIADLQARLSELQQRYDE---------LSKAEQQLREQYYSLSAKYSELNGRYDELSK 311
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIAQqaaklqgsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180
....*....|....*....|.
gi 18159965 312 AYEEARMNLEMLQNRYSELNT 332
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKS 871
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
134-330 |
7.54e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLaaalaqvRAERDALRA 213
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-------DNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 214 QLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQytdaqrtIADLQARLSELQQRYDELSKAEQQLREQYY 293
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK-------VKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
170 180 190
....*....|....*....|....*....|....*....
gi 18159965 294 SLSAKYSELNGR--YDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:TIGR04523 542 DLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSL 580
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
238-322 |
8.01e-04 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 38.32 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 238 ETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDEL-----SKA 312
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELverwmAKK 80
|
90
....*....|.
gi 18159965 313 YEEA-RMNLEM 322
Cdd:cd22887 81 QQEAdKMNEAN 91
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
148-289 |
9.94e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQIDQLKQKIADLQAQLKNkeaqianltsllsaarldndrLAAALAQVRAERDALRAQLEQTQAQLNAVSQ 227
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEELEEKYKE---------------------LSASSEELSEEKDALLAQRAAHEARIRELEE 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 228 AKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLR 289
Cdd:pfam07888 137 DIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
178-311 |
1.00e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.77 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 178 AQIANLTSLLSAARLDNDRLAAALAQVRAErdaLRAQLEQTQAqlnavSQAKAALEAQL-AETRKQLEELKASYDELsgq 256
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQED---LEKQAEIARE-----AQQNYERELVLhAEDIKALQALREELNEL--- 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 257 ytdaQRTIADLQARLSELQQrydELSKAEQQLREQYYSLSAKYSELNGRYDELSK 311
Cdd:pfam07926 70 ----KAEIAELKAEAESAKA---ELEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
136-327 |
1.06e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 40.83 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNkeaQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQL 215
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSV---QLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 216 EQTQAQLNAVSqAKAALEAQLAETRK-----------QLEE-LKASYDELSGQYTdaqrtiaDLQARLSELQQRYDELSK 283
Cdd:pfam04108 80 EETLDKLRNTP-VEPALPPGEEKQKTlldfidedsveILRDaLKELIDELQAAQE-------SLDSDLKRFDDDLRDLQK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18159965 284 AEQQLREQYYSLSAKYSELngryDELSKAYEEARMNLEMLQNRY 327
Cdd:pfam04108 152 ELESLSSPSESISLIPTLL----KELESLEEEMASLLESLTNHY 191
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
113-270 |
1.20e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 113 LEIWiYLPNYTLSYNYYIGR-VLPstyEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLknkEAQIANLTSLlsaar 191
Cdd:PRK11448 115 LAVW-FHRTYGKDWDFKPGPfVPP---EDPENLLHALQQEVLTLKQQLELQAREKAQSQALA---EAQQQELVAL----- 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18159965 192 ldnDRLAAALAQVRAErdaLRAQLEQTQAQLNAVSQakaaleaQLAETRKQLEELKASYDELSGQYTdaqRTIADLQAR 270
Cdd:PRK11448 183 ---EGLAAELEEKQQE---LEAQLEQLQEKAAETSQ-------ERKQKRKEITDQAAKRLELSEEET---RILIDQQLR 245
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
145-288 |
1.24e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 40.79 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAAR----------LDNDRLAAALAQVRAERDALRAQ 214
Cdd:COG1538 64 EADLRAARLDLAAEVAQAYFDLLAAQEQLALAEENLALAEELLELARaryeaglasrLDVLQAEAQLAQARAQLAQAEAQ 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159965 215 LEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELsgqYTDAQRTIADLQARLSELQQRYDELSKAEQQL 288
Cdd:COG1538 144 LAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGL---PSEALERRPDLRAAEAQLEAAEAEIGVARAAF 214
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
186-331 |
1.29e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 186 LLSAARLDNDrLAAALAQVRAErdaLRAQLEQTQAQLNA----VSQAKAALEAQLAETRKQLEELKASYDELsgqytdaQ 261
Cdd:pfam03148 217 RAASAQLREL-IDSILEQTAND---LRAQADAVNFALRKrieeTEDAKNKLEWQLKKTLQEIAELEKNIEAL-------E 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 262 RTIADL-------QARLSELQQRydelSKAEQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:pfam03148 286 KAIRDKeaplklaQTRLENRTYR----PNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLE 358
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
140-328 |
1.35e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 140 DLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQ 219
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAK---AALEAQLAETRKQLEELKASYDElsgQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYysLS 296
Cdd:TIGR00606 899 SLIREIKDAKeqdSPLETFLEKDQQEKEELISSKET---SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY--LK 973
|
170 180 190
....*....|....*....|....*....|...
gi 18159965 297 AKYSELNGRYDELSKAYE-EARMNLEMLQNRYS 328
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKhQEKINEDMRLMRQD 1006
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-242 |
1.36e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARldnDRLAAALAQVRAERDALRAQLEQ 217
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELAAELAE 217
|
90 100
....*....|....*....|....*
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQ 242
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
149-286 |
1.38e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALaqvRAERDALRAQLEQTQAQLNAVSQA 228
Cdd:PRK10636 502 DGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSAQARKDQKRREAEL---RTQTQPLRKEIARLEKEMEKLNAQ 578
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18159965 229 KAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQ 286
Cdd:PRK10636 579 LAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQ 636
|
|
| T4SS |
pfam07996 |
Type IV secretion system proteins; Members of this family are components of the type IV ... |
140-291 |
1.47e-03 |
|
Type IV secretion system proteins; Members of this family are components of the type IV secretion system. They mediate intracellular transfer of macromolecules via a mechanism ancestrally related to that of bacterial conjugation machineries.
Pssm-ID: 429777 [Multi-domain] Cd Length: 189 Bit Score: 39.25 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 140 DLANYAASLEQKVEdLSAQIDQLKQKIADLQAQLkNKEAQIANLTSLLSAARLdNDRLAAALAQVRAERDALRA------ 213
Cdd:pfam07996 6 DAAAIAQAIAQVVE-AIAQLTQLKQQINQYKQQY-NSLTGARGLGDILNNPAL-RNYLPADWQDIYDLVKSGGSygslss 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 214 -------------------QLEQTQAQLNAVSQAKAALEAQLAETRKQLEELkasyDELSGQYTDAQ--RTIADLQARLS 272
Cdd:pfam07996 83 aaqslrdanklydvctdddRADACQQAANKAAQDKAFAEQAYDTATQRLDQI----QQLMDQINTATdpKAIADLQARIQ 158
|
170 180
....*....|....*....|....*....
gi 18159965 273 ----ELQ------QRYDELSKAEQQLREQ 291
Cdd:pfam07996 159 aeqaMLQneqtrlQMLQMLAEAEDRLAEQ 187
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
142-256 |
1.68e-03 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 39.94 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 142 ANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTslLSAARLDN-----DRLAAALAQVRAERDALRAQLE 216
Cdd:cd22654 214 NGIGNASDDEVKEAANKIQQKQKELVDLIKKLSDAEIQATQLT--LVEDQVNGfteliKRQIATLENLVEDWEMLNQNMN 291
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18159965 217 QTQAQLNAVSQAKAALEaqlaetrKQLEELKASYDELSGQ 256
Cdd:cd22654 292 QLQTNVNSGKIDSKLLQ-------KQLKQIKKISDELNKQ 324
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
139-290 |
1.73e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSAQIDQLKQKIADL-----QAQLKNKEAQIANLTSLLSAARLDN--DRLAAALAQVRAERDAL 211
Cdd:pfam06008 78 ERTLGHAKELAEAIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDfgTQLQNAEAELKAAQDLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 ---RAQLEQTQAQLNAVsqaKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQL 288
Cdd:pfam06008 158 sriQTWFQSPQEENKAL---ANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQL 234
|
..
gi 18159965 289 RE 290
Cdd:pfam06008 235 EE 236
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
195-291 |
1.78e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 195 DRLAAALAQVRAERDAL-RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSE 273
Cdd:COG0542 414 DELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90
....*....|....*...
gi 18159965 274 LQQRYDELSKAEQQLREQ 291
Cdd:COG0542 494 LAELEEELAELAPLLREE 511
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
134-239 |
1.80e-03 |
|
Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.
Pssm-ID: 312712 [Multi-domain] Cd Length: 107 Bit Score: 37.68 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 134 LPSTYEDLANYAASLEQKVE-------DLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAA--RLDNDRLAaalaqv 204
Cdd:pfam09304 7 LEASKNSLANKLAGLENSLEsektsreQLIKQKDELESLLASLEQENAEREKRLRELEAKLDEAlkNLELEKLA------ 80
|
90 100 110
....*....|....*....|....*....|....*
gi 18159965 205 raerdalRAQLEqtqAQLNAVSQAKAALEAQLAET 239
Cdd:pfam09304 81 -------RMELE---SRLSKTEKDKAILELKLAEA 105
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
221-332 |
1.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 221 QLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQytdaqrtIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKYS 300
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEE-------LKELAEKRDELNAQVKELREEAQELREKRDELNEKVK 74
|
90 100 110
....*....|....*....|....*....|..
gi 18159965 301 ELNGRYDELSKAYEEARMNLEMLQNRYSELNT 332
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAELNK 106
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
197-297 |
1.87e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 40.47 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 197 LAAALAQVRAERDALRAQLEQTQAQLnavSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQ 276
Cdd:PRK06975 330 VVVLACAAAVGGYALNRKVDRLDQEL---VQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADAQSAQQALEQ 406
|
90 100
....*....|....*....|...
gi 18159965 277 RYDELSKAEQ--QLREQYYSLSA 297
Cdd:PRK06975 407 QYQDLSRNRDdwMIAEVEQMLSS 429
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
139-291 |
1.91e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 40.43 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVED---LSAQIDQ----LKQKIADLQAQLKNKEA---QIANLTSLLsaarldnDRLAAALAQVRAER 208
Cdd:pfam15070 211 EELGELKETLELKSQEaqsLQEQRDQylahLQQYVAAYQQLASEKEElhkQYLLQTQLM-------DRLQHEEVQGKVAA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 209 DALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIA-DLQAR-------LSELQQRYDE 280
Cdd:pfam15070 284 EMARQELQETQERLEALTQQNQQLQAQLSLLANPGEGDGLESEEEEEEAPRPSLSIPeDFESReamvaffNSALAQAEEE 363
|
170
....*....|.
gi 18159965 281 LSKAEQQLREQ 291
Cdd:pfam15070 364 RAELRRQLKEQ 374
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
212-304 |
1.92e-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: 40.71 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 212 RAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQY------TDAQRTIADLQARLSELQQRYDELSKAE 285
Cdd:COG3096 780 RAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHlavafaPDPEAELAALRQRRSELERELAQHRAQE 859
|
90
....*....|....*....
gi 18159965 286 QQLREQYYSLSAKYSELNG 304
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNK 878
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
152-236 |
1.92e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 39.16 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 152 VEDLSAQIDQLKQKIADLQAQLKNKEAQIANLtsllsaarldndrlaaalaqvraerDALRAQLEQTQAQLnavsqakAA 231
Cdd:COG3167 41 ISPQLEELEELEAEEAQLKQELEKKQAKAANL-------------------------PALKAQLEELEQQL-------GE 88
|
....*
gi 18159965 232 LEAQL 236
Cdd:COG3167 89 LLKQL 93
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
179-290 |
1.99e-03 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 38.58 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 179 QIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAET------------------- 239
Cdd:pfam09486 2 RASAWRTLVERRTRRYQRLRAELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLttggspfsaadylacrayr 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 240 ----------RKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLRE 290
Cdd:pfam09486 82 dvlegrvgaaEAALAAARQALDAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERARE 142
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
146-330 |
2.03e-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: 40.32 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 146 ASLEQKVEDLSAQIDQLKQKIADLQAQLknkEAQ-------------IANLTSLLSAARLDNDRLAAALAQVRAERDALR 212
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQAL---DVQqtraiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 AQLEQTQAQLN----AVSQAKAALEA-----------QLAETRKQLEELKASYDELSGQytdaqrtIADLQARLSELQQR 277
Cdd:COG3096 455 EEVLELEQKLSvadaARRQFEKAYELvckiageversQAWQTARELLRRYRSQQALAQR-------LQQLRAQLAELEQR 527
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 278 YDELSKAEQQLRE-------QYYS---LSAKYSELNGRYDELSKAYEEA-------RMNLEMLQNRYSEL 330
Cdd:COG3096 528 LRQQQNAERLLEEfcqrigqQLDAaeeLEELLAELEAQLEELEEQAAEAveqrselRQQLEQLRARIKEL 597
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
131-256 |
2.25e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.04 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 131 GRVLPSTYEDLANYAASLEQKVEDLSAQIDQLKQKIAD-------LQAQLKNKEAQIANLTSLLSAARLDNdRLAAALAQ 203
Cdd:pfam05911 669 GPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASctenlesTKSQLQESEQLIAELRSELASLKESN-SLAETQLK 747
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 204 VRAE--RDaLRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQ 256
Cdd:pfam05911 748 CMAEsyED-LETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQ 801
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
150-251 |
2.29e-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: 40.32 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSA------------ARLDNDRLAAALAQVRAERDALRAQLEQ 217
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeaeerARIRRDELHEELSQNRSRRSQLEKQLTR 1084
|
90 100 110
....*....|....*....|....*....|....
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYD 251
Cdd:COG3096 1085 CEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWC 1118
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
125-247 |
2.43e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 125 SYN-YYIGRVlpstyEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRlaaaLAQ 203
Cdd:PRK01156 615 SYIdKSIREI-----ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDN----LKK 685
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18159965 204 VRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELK 247
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
198-303 |
2.48e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 198 AAALAQVRAERDALRAQLEQtqaQLNAVSQAKAALEAQlAETRKQLEELKASYDElsgqytdaqrTIADLQARLSELQQR 277
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLEL---QAREKAQSQALAEAQ-QQELVALEGLAAELEE----------KQQELEAQLEQLQEK 206
|
90 100
....*....|....*....|....*.
gi 18159965 278 YDELSKAEQQLREQYYSLSAKYSELN 303
Cdd:PRK11448 207 AAETSQERKQKRKEITDQAAKRLELS 232
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
129-329 |
2.50e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 129 YIGRVLPSTYEDLANYAASLEQ----------KVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLA 198
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADdekshsitlkEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 199 AALAQVraerdalrAQLEQTQAQLNAVSQAKA-----------ALEAQLAETRKQLEELKAsydELSgQYTDAQRTIADL 267
Cdd:PRK01156 267 MELEKN--------NYYKELEERHMKIINDPVyknrnyindyfKYKNDIENKKQILSNIDA---EIN-KYHAIIKKLSVL 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 268 QARLSE---LQQRYDELSKAEQQLREqYYSlsaKYSELNGRYDELSKAYEEARMNLEMLQNRYSE 329
Cdd:PRK01156 335 QKDYNDyikKKSRYDDLNNQILELEG-YEM---DYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
171-313 |
2.50e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 171 AQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVrAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASY 250
Cdd:PRK01156 149 AQRKKILDEILEINSLERNYDKLKDVIDMLRAEI-SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 251 DELSGQYTDAQRTIADLQArLSELQQRYD-ELSKAEQQLREQYYSlSAKYSELNGRYDEL--SKAY 313
Cdd:PRK01156 228 NNAMDDYNNLKSALNELSS-LEDMKNRYEsEIKTAESDLSMELEK-NNYYKELEERHMKIinDPVY 291
|
|
| ClyA_MakA-like |
cd22655 |
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
157-239 |
2.51e-03 |
|
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.
Pssm-ID: 439153 [Multi-domain] Cd Length: 342 Bit Score: 39.57 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARL---DNDRLAAALAQVRAERDALRAQLeqtQAQLNAVSQAKAALE 233
Cdd:cd22655 230 SKINDYQDEIAKDQKELSDDQRQIAALQGLSMSSSQavsDIDTATSALSDVRTSWAVFSGEL---QGVIDKLEKAEDALS 306
|
....*.
gi 18159965 234 AQLAET 239
Cdd:cd22655 307 IIVAKA 312
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
153-331 |
2.52e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 153 EDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARL-----DNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQ 227
Cdd:PRK10246 253 DELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLrphweRIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 228 AKAALEAQLAETRKQLEELKASYD-------ELSG------QYTDAQRTIADLQARLSELQQRY------------DELS 282
Cdd:PRK10246 333 HAAKQSAELQAQQQSLNTWLAEHDrfrqwnnELAGwraqfsQQTSDREQLRQWQQQLTHAEQKLnalpaitltltaDEVA 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18159965 283 KAEQQLREQyYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELN 331
Cdd:PRK10246 413 AALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN 460
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
136-321 |
2.59e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 38.97 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLS-----AQIDQLKQKIADLQAQLKNKEAQIANLTSLlsAARLdndrlaaaLAQVRAERDA 210
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTDygddlESVEALLKKHEALEAELAAHEERVEALNEL--GEQL--------IEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 211 LRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELS------------------GQYTDAQRTIADLQARLS 272
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQwleekeaalasedlgkdlESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18159965 273 ELQQRYDELSKAEQQLREQYYSLSAKY-----SELNGRYDELSKAYEEARMNLE 321
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEieeklEELNERWEELLELAEERQKKLE 210
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
145-287 |
2.60e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 39.93 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQidqLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAAlaqvRAERDALRAQLEQTQAQLNA 224
Cdd:PRK05035 470 EARHKKAAEARAAK---DKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAA----REARKAQARARQAEKQAAAA 542
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 225 VSQAKAALEAQLAETRKQLEELKASYDELSGQYTD----AQRTIADLQARLSELQQRYDELSKAEQQ 287
Cdd:PRK05035 543 ADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPkkaaVAAAIARAKAKKAAQQAASAEPEEQVAE 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-245 |
2.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 137 TYEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQianltsllsaarldndrlaAALAQVRAERDALRAQLE 216
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-------------------GELAELLQELEELKAELR 486
|
90 100
....*....|....*....|....*....
gi 18159965 217 QTQAQLNAVSQAKAALEaqlaETRKQLEE 245
Cdd:COG4717 487 ELAEEWAALKLALELLE----EAREEYRE 511
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
205-332 |
3.05e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLseLQQRYdELSKA 284
Cdd:pfam06160 71 EAEELNDKYRFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTL--LANRF-SYGPA 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18159965 285 EQQLREQYYSLSAKYSElngrYDELSKA--YEEARMNLEMLQNRYSELNT 332
Cdd:pfam06160 148 IDELEKQLAEIEEEFSQ----FEELTESgdYLEAREVLEKLEEETDALEE 193
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
145-256 |
3.28e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 37.66 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:pfam10473 19 ADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSE 98
|
90 100 110
....*....|....*....|....*....|....*.
gi 18159965 225 VSQAKAALEAQL----AETRKQLEELKASYDELSGQ 256
Cdd:pfam10473 99 LESLNSSLENLLeekeQEKVQMKEESKTAVEMLQTQ 134
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
196-308 |
3.31e-03 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 37.47 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 196 RLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAqlaetrkqLEELKASYDEL----SGQY-----TDAQRTIAD 266
Cdd:cd23160 4 RLLAELQQLEQQAEALQQQIELLQASINELNRAKETLEE--------LKKLKEGTEILvpigGGSFvkakiKDTDKVLVN 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18159965 267 LQAR----------LSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRYDE 308
Cdd:cd23160 76 IGAGvvvektideaIEILEKRIKELEKALEKLQEQLQQIAQRLEELEAELQE 127
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
161-256 |
3.31e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 36.82 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 161 QLKQKIADLQAQLKNKEAQIANLTSLLSA-ARLDNDRLAAAL---AQVRAERDALRAQLEQTQAQLNAVSQAkaaLEAQL 236
Cdd:pfam01920 6 QLQQQLQLLAQQIKQLETQLKELELALEElELLDEDTKVYKLigdVLVKQDKEEVKEQLEERKETLEKEIKT---LEKQL 82
|
90 100
....*....|....*....|
gi 18159965 237 AETRKQLEELKASYDELSGQ 256
Cdd:pfam01920 83 EKLEKELEELKEELYKKFGQ 102
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
147-249 |
3.65e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.35 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVEDLSAQIDQLKQKIAD---LQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDALRAQLEQ------ 217
Cdd:pfam13851 58 RLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAaiqdvq 137
|
90 100 110
....*....|....*....|....*....|....
gi 18159965 218 --TQAQLNAVSQAKAALEAQLAETRKQLEELKAS 249
Cdd:pfam13851 138 qkTGLKNLLLEKKLQALGETLEKKEAQLNEVLAA 171
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
218-316 |
3.65e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.94 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYY-SLS 296
Cdd:TIGR04320 245 DKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLaTAQ 324
|
90 100
....*....|....*....|
gi 18159965 297 AKYSELNGRYDELSKAYEEA 316
Cdd:TIGR04320 325 AALANAEARLAKAKEALANL 344
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
148-302 |
3.70e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 148 LEQKVEDLSAQiDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRL-----AAALAQVRAERDALRAQLEQTQAQL 222
Cdd:TIGR00618 245 LTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 223 NAVSQAKAALEAQ---LAETRKQLEELKASYDELSgQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKY 299
Cdd:TIGR00618 324 AKLLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
...
gi 18159965 300 SEL 302
Cdd:TIGR00618 403 DIL 405
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
201-290 |
3.72e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.16 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 201 LAQVRAErdALRAQLEQTQAQLnavsqakAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDE 280
Cdd:COG0845 51 LARLDPP--DLQAALAQAQAQL-------AAAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAA 121
|
90
....*....|
gi 18159965 281 LSKAEQQLRE 290
Cdd:COG0845 122 LEQARANLAY 131
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
204-312 |
4.17e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 38.75 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 204 VRAERDALRAQ--LEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQY-TDAQRT-----IADLQARLSELQ 275
Cdd:pfam13949 6 LREKAEEVRQQggIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYgTRWTRPpsselTATLRAEIRKYR 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 18159965 276 QRYDELSKAEQQLREQYYSLSAKYSELNGRYDELSKA 312
Cdd:pfam13949 86 EILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAF 122
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
149-242 |
4.23e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 39.16 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAerdALRAQLEQTQAQLNAVSQA 228
Cdd:PRK05035 600 SAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKA---RKAAQQQANAEPEEAEDPK 676
|
90
....*....|....*.
gi 18159965 229 KAALEAQLA--ETRKQ 242
Cdd:PRK05035 677 KAAVAAAIAraKAKKA 692
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
185-268 |
4.40e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 39.56 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 185 SLLSAAR--LDNDRLAAALAQVRAERDALRAQLEQTQAqlnAVSQAKAALEAQLAETRKQL---EELKASYDElsgqytd 259
Cdd:PRK12316 1124 SLLLQARqpLDPDRLGRALERLVAHHDALRLRFREEDG---GWQQAYAAPQAGEVLWQRQAaseEELLALCEE------- 1193
|
....*....
gi 18159965 260 AQRTIaDLQ 268
Cdd:PRK12316 1194 AQRSL-DLE 1201
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
190-330 |
4.53e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 190 ARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKasydelsgqytdaqRTIADLQA 269
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD--------------ERIERLER 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159965 270 RLSELQQRydelskAEQQLREqyyslSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSEL 330
Cdd:COG2433 449 ELSEARSE------ERREIRK-----DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
256-344 |
4.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 256 QYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQY--YSLSAKYSELNGRYDELSKAYEEARMNLEMLQNRYSELNTG 333
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90
....*....|.
gi 18159965 334 FTWALNTATAL 344
Cdd:COG3206 249 LGSGPDALPEL 259
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
147-317 |
4.77e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.28 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 147 SLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSaarldndrlaaalaQVRAERDALRAQLEQTQAQLNAVS 226
Cdd:pfam12718 4 SLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQ--------------QLEEEVEKLEEQLKEAKEKAEESE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 227 QAKAALEAqLAETRKQLEElkasydelsgqytDAQRTiadlQARLSELQQRYDELSKAEQQLREQYYSLSAKYSELNGRY 306
Cdd:pfam12718 70 KLKTNNEN-LTRKIQLLEE-------------ELEES----DKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKY 131
|
170
....*....|.
gi 18159965 307 DELSKAYEEAR 317
Cdd:pfam12718 132 EELEEKYKEAK 142
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
136-288 |
5.05e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 38.16 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 136 STYEDLANYAASLEQKVEDLSAQID-----------QLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQV 204
Cdd:cd21116 59 SLPNDIIGYNNTFQSYYPDLIELADnlikgdqgakqQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIAD--LQARLSELQQRYDELS 282
Cdd:cd21116 139 ATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAafLQADLKAAKADWNQLY 218
|
....*.
gi 18159965 283 KAEQQL 288
Cdd:cd21116 219 EQAKSL 224
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
145-278 |
5.31e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 38.67 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAqianltsllsAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:TIGR02794 138 AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA----------KKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAA 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 225 VSQAKAALEAQL---AETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRY 278
Cdd:TIGR02794 208 EAAAKAEAEAAAaaaAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKY 264
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
157-251 |
5.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 157 AQIDQLKQKIADLQAQLKNKEAQIANLTSLLSA------------ARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNA 224
Cdd:PRK04863 1013 AQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgaeerARARRDELHARLSANRSRRNQLEKQLTFCEAEMDN 1092
|
90 100
....*....|....*....|....*..
gi 18159965 225 VSQAKAALEAQLAETRKQLEELKASYD 251
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQVVNAKAGWC 1119
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
138-324 |
5.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 138 YEDLANYAASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSA-----ARLDNDRLAAALAQVRAERDALR 212
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESlqeelAALEQELQALSEAEAEQALDELL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 213 AQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIA--DLQARLSELQQRYDELSKAEQQLRE 290
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALelEEDKEELLEEVILKEIEELELAILV 269
|
170 180 190
....*....|....*....|....*....|....
gi 18159965 291 QYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQ 324
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLN 303
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
205-326 |
5.78e-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: 39.05 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 205 RAERDALRAQLEQTQAQlnAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYdelska 284
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAI--AGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAEL------ 288
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 18159965 285 EQQLREQYYSLSAKYSELNGRYDELSKAYEEARMNLEMLQNR 326
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ 330
|
|
| Imelysin-like_EfeO |
cd14656 |
EfeO is a component of the EfeUOB operon; This family includes the EfeO domain, an essential ... |
150-273 |
5.80e-03 |
|
EfeO is a component of the EfeUOB operon; This family includes the EfeO domain, an essential component of the EfeUOB operon which is highly conserved in bacteria. However, its biochemical function is unknown. EfeO contains an N-terminal cupredoxin (CUP)-like domain and C-terminal imelysin-like domain that may bind iron. Algp7, a member of EfeO family protein from Sphingomonas sp. A1, is found to bind alginate at neutral pH, but does not contain the CUP domain, thus having a role that does not seem to be related to iron uptake. Some members of this family are fused to an N-terminal putative EfeU ion permease domain. The imelysin-like domain of this family also contains the GxHxxE sequence motif and a highly conserved functional site, suggesting a similar role to other imelysin family proteins containing the same motif.
Pssm-ID: 271139 Cd Length: 239 Bit Score: 38.00 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 150 QKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTslLSAARLDNDrlaAALAQVRAERDA--------LRAQLEQTQAQ 221
Cdd:cd14656 96 KSTAGLAPVADQLVADVKALRARLRTLDLDPADLA--NGAHELLEE---VATSKITGEEDRyshtdladFAANLEGARKA 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18159965 222 LNA----VSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSE 273
Cdd:cd14656 171 LDLlrplLEKKDPALLAQIDAAFAALDALLAAYRTGGGGYVPYDALTAADRKALAA 226
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
130-251 |
5.90e-03 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 38.40 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 130 IGRVLPSTYEDLANYAaslEQKVEDLSAQIDQLK-----QKIADLQAQLKNKEAQIANLTSLL------------SAARL 192
Cdd:PRK03598 71 LGELDAAPYENALMQA---KANVSVAQAQLDLMLagyrdEEIAQARAAVKQAQAAYDYAQNFYnrqqglwksrtiSANDL 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 193 DNDRLA--AALAQVRAERDALRaQLE---------QTQAQLNavsQAKAALeAQlAETRKQLEELKASYD 251
Cdd:PRK03598 148 ENARSSrdQAQATLKSAQDKLS-QYRegnrpqdiaQAKASLA---QAQAAL-AQ-AELNLQDTELIAPSD 211
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
160-328 |
7.20e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 38.41 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 160 DQLKQKIADLQAQLKNKEAQIA--NLTSLLSAARldnDRLAAA------------------LAQVRAERDALRAQLEQTQ 219
Cdd:PRK15374 43 DVVATKAGDLKAGTKSGESAINtvGLKPPTDAAR---EKLSSEgqltlllgklmtllgdvsLSQLESRLAVWQAMIESQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 220 AQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKAEQQLREQYYSLSAKY 299
Cdd:PRK15374 120 EMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPADPGYAQAEAAVEQAGKEATEAK 199
|
170 180
....*....|....*....|....*....
gi 18159965 300 SELNGRYDELSKAYEEARMNLEMLQNRYS 328
Cdd:PRK15374 200 EALDKATDATVKAGTDAKAKAEKADNILT 228
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
187-287 |
7.31e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 37.85 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 187 LSAARLDNDRLAAALAQVRAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASydelSGQYTDAQRTIAD 266
Cdd:PRK06991 166 LRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAIIAAALERARKKKEELAAQ----GAGPKNTEGVSAA 241
|
90 100
....*....|....*....|.
gi 18159965 267 LQARLSELQQRYDELSKAEQQ 287
Cdd:PRK06991 242 VQAQIDAAEARRKRLAEQRDA 262
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
139-284 |
7.40e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 38.34 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 139 EDLANYAASLEQKVEDLSA---QIDQLKQKIADLQAQLKNKEAQIA-NLTSLLSAARLDNDRLAAALAQVRAERDALraQ 214
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALREGRARWAqERETLQQSAEADKDRIEKLSAELQRLEERL--Q 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 215 LEQTQAQLNAV--SQAKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQARLSELQQRYDELSKA 284
Cdd:pfam07888 336 EERMEREKLEVelGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
205-281 |
7.73e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 35.62 E-value: 7.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18159965 205 RAERDALRAQLEQTQAQLNAVSQAKAALEAQLAETRKQLEELKASYDELSGQYTdaqrtiaDLQARLSELQQRYDEL 281
Cdd:cd22887 3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENN-------LLEEKLRKLQEENDEL 72
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
149-248 |
8.26e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 38.25 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 149 EQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSA---ARLDNDRLAAALAQVRAERDAlraqLEQTQAQLNAV 225
Cdd:PRK09510 105 QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAkakAEAEAKRAAAAAKKAAAEAKK----KAEAEAAKKAA 180
|
90 100
....*....|....*....|...
gi 18159965 226 SQAKAALEAQLAETRKQLEELKA 248
Cdd:PRK09510 181 AEAKKKAEAEAAAKAAAEAKKKA 203
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
147-211 |
8.36e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 35.23 E-value: 8.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18159965 147 SLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSAARLDNDRLAAALAQVRAERDAL 211
Cdd:cd22887 8 ELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDEL 72
|
|
| Mtu_fam_mce |
TIGR00996 |
virulence factor Mce family protein; Members of this paralogous family are found as six tandem ... |
145-253 |
8.41e-03 |
|
virulence factor Mce family protein; Members of this paralogous family are found as six tandem homologous proteins in the same orientation per cassette, in four separate cassettes in Mycobacterium tuberculosis. The six members of each cassette represent six subfamilies. One subfamily includes the protein mce (mycobacterial cell entry), a virulence protein required for invasion of non-phagocytic cells. [Cellular processes, Pathogenesis]
Pssm-ID: 273384 [Multi-domain] Cd Length: 291 Bit Score: 37.65 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 145 AASLEQKVEDLSAQIDQLKQKIADLQAQLKNKEAQIANLTSLLSA-----ARLD--NDRLAAALAQVRAERDALRAQLEQ 217
Cdd:TIGR00996 159 AQALAGQGPQLRNLLDGLAQLTAALNERDGDIGELIRNLNRVLDVladrsDQLDrlLDNLPTLIATLADRSDALDDALAA 238
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18159965 218 TQAQLNAVSQAKAALEAQLAETRKQL----EELKASYDEL 253
Cdd:TIGR00996 239 LSAASAQVRDLLAENRPNLGQALANLapvlTLLVDYSPEL 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
198-333 |
8.93e-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: 38.39 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 198 AAALAQVRAERDALRAQ-LEQTQAQLNAVSQaKAALEAQLAETRKQLEELKASYDELSGQYTDAQRTIADLQA--RLSEL 274
Cdd:COG3096 270 AADYMRHANERRELSERaLELRRELFGARRQ-LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159965 275 QQRY-DELSKAEQQLREQyyslsakyselNGRYDELSKAYEEARMNLEMLQNRYSELNTG 333
Cdd:COG3096 349 IERYqEDLEELTERLEEQ-----------EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQ 397
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
205-276 |
9.45e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 37.23 E-value: 9.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159965 205 RAERDALRAQLEQTQAQLnavsQAKAALEAQLAETRKQLEELKASYDELSGQYTDaQRTIADLqarLSELQQ 276
Cdd:COG3167 45 LEELEELEAEEAQLKQEL----EKKQAKAANLPALKAQLEELEQQLGELLKQLPS-KAEVPAL---LDDISQ 108
|
|
| |
