|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
18-313 |
2.43e-93 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 282.96 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 18 KVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHR 97
Cdd:pfam00038 19 KVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 98 RATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRA 177
Cdd:pfam00038 98 RTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 178 RYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA 257
Cdd:pfam00038 178 QYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 664806051 258 LKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 313
Cdd:pfam00038 258 LADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-308 |
1.26e-08 |
|
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: 56.99 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREYLYF 135
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------RLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 136 LKHLNEEELGQLQTQASDtsvvLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQVSAQLHGDRMQ 213
Cdd:TIGR02168 752 LSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 214 ETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGElalkDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 293
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*
gi 664806051 294 LSLDVEIATYRRLLE 308
Cdd:TIGR02168 904 RELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-311 |
1.26e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREylyf 135
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 136 LKHLNEEELGQLQTQASDTSVVLSMDNNRyldfssiITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLhgdrmQET 215
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 216 KVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 292
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*....
gi 664806051 293 KLSLDVEIATYRRLLEGEE 311
Cdd:COG1196 458 EEALLELLAELLEEAALLE 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
53-281 |
2.38e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREY 132
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 133 LyflkhlnEEELGQLQTQASDTSVVLSMDNNRYLDFSSIItevrARYEEIARSSKAEAEALYQTKyQELQVSAQLHGDRM 212
Cdd:COG4942 106 L-------AELLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADL-AELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806051 213 QETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLAR 281
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-308 |
1.29e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYF 135
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 136 LKHLNEE----------ELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQV 203
Cdd:TIGR02168 314 LERQLEEleaqleelesKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 204 SAQLHGDRMQETKVQISQLHQEIQRLQSQTENL--KKQNASLQAAITDAEQRGElALKDAQAKVDELEAALRMAKQNLAR 281
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEE-ELEELQEELERLEEALEELREELEE 472
|
250 260
....*....|....*....|....*..
gi 664806051 282 LLCEYQELTSTKLSLDVEIATYRRLLE 308
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-289 |
1.97e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREy 132
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE- 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 133 lyfLKHLNEEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEiARSSKAEAEALYQTKYQELQVSAQLHGD-- 210
Cdd:TIGR02168 776 ---ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN-LRERLESLERRIAATERRLEDLEEQIEEls 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 211 -RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA---LKDAQAKVDELEAALRMAKQNLARLLCEY 286
Cdd:TIGR02168 852 eDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRL 931
|
...
gi 664806051 287 QEL 289
Cdd:TIGR02168 932 EGL 934
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
141-281 |
7.59e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 141 EEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARyeeiARSSKAEAEALyQTKYQELQVSAQLHGDRMQETKVQIS 220
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS----LSAAEAERSRL-QALLAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806051 221 QLHQEIQR-------LQSQTENLKKQNASLQAAITDAEQRGelalKDAQAKVD----ELEAALRMAKQNLAR 281
Cdd:PRK09039 127 SEKQVSARalaqvelLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
176-282 |
7.97e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 176 RARYEEIARSSKAEAEALYQTKYQELQVsAQLHGDRMQE-------TKVQISQLHQEIQRLQSQTENLKKQNASLQAAIT 248
Cdd:COG1566 101 RLEAELGAEAEIAAAEAQLAAAQAQLDL-AQRELERYQAlykkgavSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLR 179
|
90 100 110
....*....|....*....|....*....|....
gi 664806051 249 DAEQrgelaLKDAQAKVDELEAALRMAKQNLARL 282
Cdd:COG1566 180 EEEE-----LAAAQAQVAQAEAALAQAELNLART 208
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-308 |
2.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 52 FEACLDQLRKQLEQLQGERgalDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALRE 131
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRRER---EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 132 YLyflkHLNEEELGQLQTQASDtsvvlsMDNNRYLDFSSIITEVRAryeEIARSSKAEAEalyqtKYQELQVSAQlhgdR 211
Cdd:TIGR02169 266 RL----EEIEQLLEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE-----KERELEDAEE----R 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 212 MQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELTS 291
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250
....*....|....*..
gi 664806051 292 TKLSLDVEIatyRRLLE 308
Cdd:TIGR02169 400 EINELKREL---DRLQE 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-307 |
3.64e-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: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 201 LQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLA 280
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....*..
gi 664806051 281 RLLceyQELTSTKLSLDVEIATYRRLL 307
Cdd:COG4942 87 ELE---KEIAELRAELEAQKEELAELL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-302 |
9.36e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 59 LRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvvlkkdvdgvflsKMELEGKLEALREYLYFLK- 137
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------------IEELEEDLHKLEEALNDLEa 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 138 HLNEEELGQLQTQASDtsvvlsmdnnryldfssiITEVRARYEEIARSSKAEAEALYQTKyqelqvsaQLHGDRMQETKV 217
Cdd:TIGR02169 787 RLSHSRIPEIQAELSK------------------LEEEVSRIEARLREIEQKLNRLTLEK--------EYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 218 QISQLHQEIQRLQSQTENLKKQNASLQAAItdAEQRGELA-----LKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 292
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEEL--EELEAALRdlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250
....*....|
gi 664806051 293 KLSLDVEIAT 302
Cdd:TIGR02169 919 LSELKAKLEA 928
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-288 |
9.60e-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: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvvlkKDVDGVFLSKMELEGKLEALREYLYF 135
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 136 LKHLNEE------ELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAqlHG 209
Cdd:COG4913 687 LAALEEQleeleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA--VE 764
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806051 210 DRMQEtkvqisQLHQEIQRLQSQTENLKKQnasLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQE 288
Cdd:COG4913 765 RELRE------NLEERIDALRARLNRAEEE---LERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEE 834
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-308 |
1.75e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 122 LEGKLEALREYLYFLkhlnEEELGQLQTQASDTSVVLS--MDNNRYLDFSSIITEVRARYEEI------ARSSKAEAEAL 193
Cdd:COG3206 166 LELRREEARKALEFL----EEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELesqlaeARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 194 YQTKYQEL----QVSAQLHGD--------RMQETKVQISQL-------HQEIQRLQSQTENLKKQnasLQAAITDAEQRG 254
Cdd:COG3206 242 LAALRAQLgsgpDALPELLQSpviqqlraQLAELEAELAELsarytpnHPDVIALRAQIAALRAQ---LQQEAQRILASL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664806051 255 ELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTStkLSLDVEIA--TYRRLLE 308
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRR--LEREVEVAreLYESLLQ 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
195-283 |
2.53e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 195 QTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRM 274
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEA 101
|
....*....
gi 664806051 275 AKQNLARLL 283
Cdd:COG4942 102 QKEELAELL 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-308 |
2.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 180 EEIARSSKAEAEAlyQTKYQELQVS-AQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASL--------------Q 244
Cdd:COG4913 309 AELERLEARLDAL--REELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefaalR 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664806051 245 AAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLE 308
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-293 |
3.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 57 DQLRKQLEQLQGERGALDAELKACRDQEEEykskyeeeaHRRatlENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFL 136
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEE---------FRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 137 khlnEEELGQLQTQASDTSVVLSMDNNryldfSSIITEVRARYEEiARSSKAEAEALYQTKYQELQvSAQlhgDRMQETK 216
Cdd:COG3206 239 ----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAE-LEAELAELSARYTPNHPDVI-ALR---AQIAALR 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664806051 217 VQISQLHQEI-QRLQSQTENLKKQNASLQAAITDAEQRGeLALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 293
Cdd:COG3206 305 AQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-311 |
1.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 141 EEELGQLQTQASDTSvvlsmdnnRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQIS 220
Cdd:COG1196 199 ERQLEPLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 221 QLHQEIQRLQSQTENLKKQNASLQAAITDAEQ---RGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLD 297
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170
....*....|....
gi 664806051 298 VEIATYRRLLEGEE 311
Cdd:COG1196 351 EELEEAEAELAEAE 364
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
212-278 |
2.02e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 38.21 E-value: 2.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664806051 212 MQETKVQISQLHQEIQRLQSQTENLKKQnaslqaaitdAEQRGELALKDAQAKV--------DELEAALRMAKQN 278
Cdd:COG0576 1 MEELEAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLaedllpvlDNLERALAAAEED 65
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
56-312 |
2.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 56 LDQLRKQLEQ------------LQGERGALDAELKACRDQEEEYKSKYEE-----EAHRR-----ATLENDFVVLKKDVD 113
Cdd:PRK02224 189 LDQLKAQIEEkeekdlherlngLESELAELDEEIERYEEQREQARETRDEadevlEEHEErreelETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 114 GVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQ-TQASDTSVVLSMDnnrylDFSSIITEVRARYEEIARSSKA---E 189
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARRE-----ELEDRDEELRDRLEECRVAAQAhneE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 190 AEALYQtkyqelqvSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELE 269
Cdd:PRK02224 344 AESLRE--------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER----FGDAPVDLGNAE 411
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 664806051 270 AALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEEC 312
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-282 |
4.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 172 ITEVRARYEEI-ARSSKAEAEALYQTKYQEL-QVSAQLHG--DRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAI 247
Cdd:COG4717 104 LEELEAELEELrEELEKLEKLLQLLPLYQELeALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110
....*....|....*....|....*....|....*
gi 664806051 248 TDAEQRGELALKDAQAKVDELEAALRMAKQNLARL 282
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
193-281 |
4.59e-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: 38.77 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 193 LYQTKYQELQVSAQLhgdRMQETKVQISQLHQEIQRLQSqtenLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAAL 272
Cdd:COG0845 54 LDPPDLQAALAQAQA---QLAAAQAQLELAKAELERYKA----LLKKGAVSQQELDQAKA----ALDQAQAALAAAQAAL 122
|
....*....
gi 664806051 273 RMAKQNLAR 281
Cdd:COG0845 123 EQARANLAY 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
53-280 |
4.94e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREY 132
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 133 LyflkhlnEEELGQLQTQASDTSVVLSMDNNRylDFSSIITEVRARyEEIARSSKAEAEALYQTK--YQELQVSAQLHGD 210
Cdd:COG3883 88 L-------GERARALYRSGGSVSYLDVLLGSE--SFSDFLDRLSAL-SKIADADADLLEELKADKaeLEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 211 RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLA 280
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
157-280 |
5.61e-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: 38.55 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 157 VLSMDNNRYLDFSSI-ITEVRARYEEIARSSKAEAEAlyQTKYQELQvsaqlhgDRMQETKVQISQLHQEIQRLQSQTEN 235
Cdd:TIGR04320 230 FVNFNDSYIADGNKFdKTPIPNPPNSLAALQAKLATA--QADLAAAQ-------TALNTAQAALTSAQTAYAAAQAALAT 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 664806051 236 LKKQNASLQAAitdAEQRGELALKDAQAKVDELEAALRMAKQNLA 280
Cdd:TIGR04320 301 AQKELANAQAQ---ALQTAQNNLATAQAALANAEARLAKAKEALA 342
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
53-250 |
6.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEeykskyeeeAHRRATLENDFVVLKkdvdgvflskmELEGKLEALREy 132
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELD---------ELEAQIRGNGGDRLE-----------QLEREIERLER- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 133 lyflkHLNE--EELGQLQTQASDtsVVLSMDNNRyLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHgd 210
Cdd:COG4913 353 -----ELEEreRRRARLEALLAA--LGLPLPASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-- 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 664806051 211 rmqetkvqisQLHQEIQRLQSQTENLKKQNASLQAAITDA 250
Cdd:COG4913 423 ----------ELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
169-282 |
6.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 169 SSIITEVRARYEEIARSSKAEA-----EALYQTKYQELQVSAQLHGD---RMQETKVQISQLHQEIQRLQSQTENLKKQN 240
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAeaikkEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 664806051 241 ASLQAAITDAEQRgELALKDAQAKVDELEAALRMAKQNLARL 282
Cdd:PRK12704 110 EELEKKEKELEQK-QQELEKKEEELEELIEEQLQELERISGL 150
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
218-282 |
8.95e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 36.52 E-value: 8.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664806051 218 QISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARL 282
Cdd:pfam11559 60 TIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
126-308 |
9.05e-03 |
|
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: 38.16 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 126 LEALREYLYFLKHLNEEELGQLQTQASDTSVVLSmDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQ---------- 195
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK-ENNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnnie 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 196 ---TKYQELQVSAQlhgDRMQETKVQISQLHQEIQRL----QSQTENLKKQNASLQAAITDAEQRGE---LALKDAQAKV 265
Cdd:pfam05483 194 kmiLAFEELRVQAE---NARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKdltFLLEESRDKA 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 664806051 266 DELEAALRMAKQNLARLLCEYQELTS----TKLSLDVEIATYRRLLE 308
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKeledIKMSLQRSMSTQKALEE 317
|
|
|