|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
110-423 |
2.72e-108 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 325.34 E-value: 2.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 110 QETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKA 189
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 190 CRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQTQASDTSVVLS 269
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 270 MDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQ 349
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89357932 350 NASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 423
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
43-107 |
1.92e-18 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 82.40 E-value: 1.92e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89357932 43 SFGGCleGSRGSTWGSGGRLGVRFGE----WSGGPGLSLCPPGGIQEVTINQNLLTPLKIEIDPQFQVV 107
Cdd:pfam16208 90 GFGGG--GGFGGGFGGGGYGGGGFGGggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-418 |
2.50e-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: 60.07 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREYLYF 245
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------RLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 246 LKHLNEEELGQLQTQASDtsvvLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQVSAQLHGDRMQ 323
Cdd:TIGR02168 752 LSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 324 ETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGElalkDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 403
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*
gi 89357932 404 LSLDVEIATYRRLLE 418
Cdd:TIGR02168 904 RELESKRSELRRELE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-399 |
2.86e-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: 56.60 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 107 VRTQETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWHLLqqqglsgsqqglepvfEACLDQLRKQLEQLQGERGALDAE 186
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL----------------EEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 187 LKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALreylyflkhlnEEELGQLQTQASDTSV 266
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-----------EAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 267 VLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQlhgdrMQETKVQISQLHQEIQRLQSQTENL 346
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-----IESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 89357932 347 KKQNASLQAAITDAEQRGELA---LKDAQAKVDELEAALRMAKQNLARLLCEYQEL 399
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-421 |
2.89e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREylyf 245
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 246 LKHLNEEELGQLQTQASDTSVVLSMDNNRyldfssiITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLhgdrmQET 325
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 326 KVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 402
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*....
gi 89357932 403 KLSLDVEIATYRRLLEGEE 421
Cdd:COG1196 458 EEALLELLAELLEEAALLE 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-391 |
5.20e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREY 242
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 243 LyflkhlnEEELGQLQTQASDTSVVLSMDNNRYLDFSSIItevrARYEEIARSSKAEAEALYQTKyQELQVSAQLHGDRM 322
Cdd:COG4942 106 L-------AELLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADL-AELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89357932 323 QETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLAR 391
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-418 |
2.54e-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: 53.52 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYF 245
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 246 LKHLNEE----------ELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEiARSSKAEAEALYQT---KYQELQ 312
Cdd:TIGR02168 314 LERQLEEleaqleelesKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE-LESRLEELEEQLETlrsKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 313 VSAQLHGDRMQETKVQISQLHQEIQRLQSQTENL--KKQNASLQAAITDAEQRGElALKDAQAKVDELEAALRMAKQNLA 390
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEE-ELEELQEELERLEEALEELREELE 471
|
250 260
....*....|....*....|....*...
gi 89357932 391 RLLCEYQELTSTKLSLDVEIATYRRLLE 418
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-418 |
1.08e-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: 51.61 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 162 FEACLDQLRKQLEQLQGERgaLDAE-LKACRDQeeEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALR 240
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRRER--EKAErYQALLKE--KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 241 EYLyflkHLNEEELGQLQTQASDtsvvlsMDNNRYLDFSSIITEVRAryeEIARSSKAEAEalyqtKYQELQVSAQlhgd 320
Cdd:TIGR02169 265 KRL----EEIEQLLEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE-----KERELEDAEE---- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 321 RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELT 400
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250
....*....|....*...
gi 89357932 401 STKLSLDVEIatyRRLLE 418
Cdd:TIGR02169 399 REINELKREL---DRLQE 413
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
277-392 |
1.64e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.05 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 277 DFSSIITEVRARYEEiARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQ--------------ISQlhQEIQRLQSQ 342
Cdd:COG1566 80 DLQAALAQAEAQLAA-AEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQreleryqalykkgaVSQ--QELDEARAA 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 89357932 343 TENLKKQNASLQAAITDAEQ--RGELALKDAQAKVDELEAALRMAKQNLARL 392
Cdd:COG1566 157 LDAAQAQLEAAQAQLAQAQAglREEEELAAAQAQVAQAEAALAQAELNLART 208
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-421 |
1.91e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQLQGERG------ALDAELKACRdqeeeykskYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEAL 239
Cdd:COG1196 195 LGELERQLEPLERQAEkaeryrELKEELKELE---------AELLLLKLRELEAELEELEAELE-------ELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 240 reylyflkhlnEEELGQLQTQasdtsvvlsmdnnryldfssiITEVRARYEEIARSSKAEAEALYQ--TKYQELQVSAQL 317
Cdd:COG1196 259 -----------EAELAELEAE---------------------LEELRLELEELELELEEAQAEEYEllAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 318 HGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLC 394
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260
....*....|....*....|....*..
gi 89357932 395 EYQELTSTKLSLDVEIATYRRLLEGEE 421
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
251-391 |
4.78e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 251 EEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARyeeiARSSKAEAEALyQTKYQELQVSAQLHGDRMQETKVQIS 330
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS----LSAAEAERSRL-QALLAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89357932 331 QLHQEIQR-------LQSQTENLKKQNASLQAAITDAEQRGelalKDAQAKVD----ELEAALRMAKQNLAR 391
Cdd:PRK09039 127 SEKQVSARalaqvelLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-412 |
7.54e-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: 48.91 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 169 LRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvvlkkdvdgvflsKMELEGKLEALREYLYFLK- 247
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------------IEELEEDLHKLEEALNDLEa 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 248 HLNEEELGQLQTQASDtsvvlsmdnnryldfssiITEVRARYEEIARSSKAEAEALYQTKyqelqvsaQLHGDRMQETKV 327
Cdd:TIGR02169 787 RLSHSRIPEIQAELSK------------------LEEEVSRIEARLREIEQKLNRLTLEK--------EYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 328 QISQLHQEIQRLQSQTENLKKQNASLQAAItdAEQRGELA-----LKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 402
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEEL--EELEAALRdlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250
....*....|
gi 89357932 403 KLSLDVEIAT 412
Cdd:TIGR02169 919 LSELKAKLEA 928
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-417 |
9.62e-06 |
|
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: 47.84 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 311 LQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLA 390
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....*..
gi 89357932 391 RLLceyQELTSTKLSLDVEIATYRRLL 417
Cdd:COG4942 87 ELE---KEIAELRAELEAQKEELAELL 110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
232-418 |
1.54e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 232 LEGKLEALREYLYFLkhlnEEELGQLQTQASDTSVVLS--MDNNRYLDFSSIITEVRARYEEI------ARSSKAEAEAL 303
Cdd:COG3206 166 LELRREEARKALEFL----EEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELesqlaeARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 304 YQTKYQEL----QVSAQLHGD--------RMQETKVQISQL-------HQEIQRLQSQTENLKKQnasLQAAITDAEQRG 364
Cdd:COG3206 242 LAALRAQLgsgpDALPELLQSpviqqlraQLAELEAELAELsarytpnHPDVIALRAQIAALRAQ---LQQEAQRILASL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89357932 365 ELALKDAQAKVDELEAALRMAKQNLARL---LCEYQELTStklslDVEIA--TYRRLLE 418
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELpelEAELRRLER-----EVEVAreLYESLLQ 372
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-398 |
2.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvvlkKDVDGVFLSKMELEGKLEALREYLYF 245
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 246 LKHLNEE------ELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAqlHG 319
Cdd:COG4913 687 LAALEEQleeleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA--VE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 320 DRMQEtkvqisQLHQEIQRLQSQTENLKKQnasLQAAITDAEQRGELALKDAQAKVDELEAALRMakqnLARL----LCE 395
Cdd:COG4913 765 RELRE------NLEERIDALRARLNRAEEE---LERAMRAFNREWPAETADLDADLESLPEYLAL----LDRLeedgLPE 831
|
...
gi 89357932 396 YQE 398
Cdd:COG4913 832 YEE 834
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
167-403 |
4.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 167 DQLRKQLEQLQGERGALDAELKACRDQEEEykskyeeeaHRRatlENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFL 246
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEE---------FRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 247 khlnEEELGQLQTQASDTSVVLSMDNNryldfSSIITEVRARYEEiARSSKAEAEALYQTKYQELQvSAQlhgDRMQETK 326
Cdd:COG3206 239 ----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAE-LEAELAELSARYTPNHPDVI-ALR---AQIAALR 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89357932 327 VQISQLHQEI-QRLQSQTENLKKQNASLQAAITDAEQRGeLALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 403
Cdd:COG3206 305 AQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-393 |
8.56e-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: 44.75 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 305 QTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRM 384
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEA 101
|
....*....
gi 89357932 385 AKQNLARLL 393
Cdd:COG4942 102 QKEELAELL 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
290-418 |
8.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 290 EEIARSSKAEAEAlyQTKYQELQVS-AQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASL--------------Q 354
Cdd:COG4913 309 AELERLEARLDAL--REELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefaalR 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89357932 355 AAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLE 418
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
166-422 |
2.35e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQ------------LQGERGALDAELKACRDQEEEYKSKYEE-----EAHRR-----ATLENDFVVLKKDVD 223
Cdd:PRK02224 189 LDQLKAQIEEkeekdlherlngLESELAELDEEIERYEEQREQARETRDEadevlEEHEErreelETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 224 GVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQ-TQASDTSVVLSMDnnrylDFSSIITEVRARYEEIARSSKA---E 299
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARRE-----ELEDRDEELRDRLEECRVAAQAhneE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 300 AEALYQtkyqelqvSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELE 379
Cdd:PRK02224 344 AESLRE--------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER----FGDAPVDLGNAE 411
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 89357932 380 AALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEEC 422
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
305-409 |
2.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 305 QTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAALRM 384
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLES 161
|
90 100
....*....|....*....|....*
gi 89357932 385 AKQNLARLLCEYQELTSTKLSLDVE 409
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALD 186
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
236-418 |
2.92e-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: 43.56 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 236 LEALREYLYFLKHLNEEELGQLQTQASDTSVVLSmDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQ---------- 305
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK-ENNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnnie 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 306 ---TKYQELQVSAQlhgDRMQETKVQISQLHQEIQRL----QSQTENLKKQNASLQAAITDAEQRGE---LALKDAQAKV 375
Cdd:pfam05483 194 kmiLAFEELRVQAE---NARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKdltFLLEESRDKA 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 89357932 376 DELEAALRMAKQNLARLLCEYQELTS----TKLSLDVEIATYRRLLE 418
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKeledIKMSLQRSMSTQKALEE 317
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
163-390 |
2.94e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREY 242
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 243 LyflkhlnEEELGQLQTQASDTSVVLSMDNNRylDFSSIITEVRARyEEIARSSKAEAEALYQTK--YQELQVSAQLHGD 320
Cdd:COG3883 88 L-------GERARALYRSGGSVSYLDVLLGSE--SFSDFLDRLSAL-SKIADADADLLEELKADKaeLEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 321 RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLA 390
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
322-388 |
5.23e-04 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 40.52 E-value: 5.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89357932 322 MQETKVQISQLHQEIQRLQSQTENLKKQnaslqaaitdAEQRGELALKDAQAKV--------DELEAALRMAKQN 388
Cdd:COG0576 1 MEELEAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLaedllpvlDNLERALAAAEED 65
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
282-392 |
5.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 282 ITEVRARYEEI-ARSSKAEAEALYQTKYQEL-QVSAQLHG--DRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAI 357
Cdd:COG4717 104 LEELEAELEELrEELEKLEKLLQLLPLYQELeALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110
....*....|....*....|....*....|....*
gi 89357932 358 TDAEQRGELALKDAQAKVDELEAALRMAKQNLARL 392
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-385 |
9.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEeykskyeeeAHRRATLENDFVVLKkdvdgvflskmELEGKLEALREy 242
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELD---------ELEAQIRGNGGDRLE-----------QLEREIERLER- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 243 lyflkHLNE--EELGQLQTQASDtsVVLSMDNNRyLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHgd 320
Cdd:COG4913 353 -----ELEEreRRRARLEALLAA--LGLPLPASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-- 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89357932 321 rmqetkvqisQLHQEIQRLQSQTENLKKQNASLQAAITDAeqrgeLALKDAQAK-------VDELEAALRMA 385
Cdd:COG4913 423 ----------ELEAEIASLERRKSNIPARLLALRDALAEA-----LGLDEAELPfvgelieVRPEEERWRGA 479
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
267-390 |
1.15e-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: 41.25 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 267 VLSMDNNRYLDFSSI-ITEVRARYEEIARSSKAEAEAlyQTKYQELQvsaqlhgDRMQETKVQISQLHQEIQRLQSQTEN 345
Cdd:TIGR04320 230 FVNFNDSYIADGNKFdKTPIPNPPNSLAALQAKLATA--QADLAAAQ-------TALNTAQAALTSAQTAYAAAQAALAT 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 89357932 346 LKKQNASLQAAitdAEQRGELALKDAQAKVDELEAALRMAKQNLA 390
Cdd:TIGR04320 301 AQKELANAQAQ---ALQTAQNNLATAQAALANAEARLAKAKEALA 342
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-389 |
1.49e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 112 TQEIRTLNNQFASFIDKVRFLEQQNKVLETKWHLLQQQGLSGsqqglepvfEACLDQLRKQLEQLQGERGALDAELKACR 191
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL---------AEELAELEEKLEELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 192 DQEEEYKSkyeeeahRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQTQASdtsvvlSMD 271
Cdd:TIGR02168 365 AELEELES-------RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK------KLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 272 NNRYLDFSSIITEVRARYEEiARSSKAEAEALYQTKYQELQVSAQlhgdRMQETKVQISQLHQEIQRLQSQTENLKKQNA 351
Cdd:TIGR02168 432 EAELKELQAELEELEEELEE-LQEELERLEEALEELREELEEAEQ----ALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 89357932 352 SLQAAITDAEQR-GELALKDAQAKVDE-----LEAALRMAKQNL 389
Cdd:TIGR02168 507 GVKALLKNQSGLsGILGVLSELISVDEgyeaaIEAALGGRLQAV 550
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-419 |
1.51e-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: 40.90 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREYLyf 245
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-------ELRAELEAQKEEL-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 246 lkhlnEEELGQLQTqasdtsvvlsMDNNRYLDFssiitevraryeeiarsskaeaeALYQTKYQELQVSAQLHGDRMQET 325
Cdd:COG4942 107 -----AELLRALYR----------LGRQPPLAL-----------------------LLSPEDFLDAVRRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 326 KVQISQLHQEIQRLQSQTENLKKQNASLQAAitdaeqrgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLS 405
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
250
....*....|....
gi 89357932 406 LDVEIATYRRLLEG 419
Cdd:COG4942 218 LQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
163-409 |
1.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVflskMELEGKLEALREY 242
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIADA 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 243 LYFLKHLNE--EELGQLQTQASDTsvvLSMDNNRYLDFSSIITEvrARYEEiARSSKAEAEalyqtKYQElQVSAQLHGD 320
Cdd:PRK02224 605 EDEIERLREkrEALAELNDERRER---LAEKRERKRELEAEFDE--ARIEE-AREDKERAE-----EYLE-QVEEKLDEL 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 321 RMQETKVQ--ISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELalkdaQAKVDELEAALRmaKQN---LARLLCE 395
Cdd:PRK02224 673 REERDDLQaeIGAVENELEELEELRERREALENRVEALEALYDEAEEL-----ESMYGDLRAELR--QRNvetLERMLNE 745
|
250
....*....|....*....
gi 89357932 396 -----YQELTSTKLSLDVE 409
Cdd:PRK02224 746 tfdlvYQNDAYSHIELDGE 764
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
328-392 |
2.17e-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: 38.84 E-value: 2.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89357932 328 QISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARL 392
Cdd:pfam11559 60 TIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
279-392 |
2.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 279 SSIITEVRARYEEIARSSKAEA-----EALYQTKYQELQVSAQLHGD---RMQETKVQISQLHQEIQRLQSQTENLKKQN 350
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAeaikkEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 89357932 351 ASLQAAITDAEQRgELALKDAQAKVDELEAALRMAKQNLARL 392
Cdd:PRK12704 110 EELEKKEKELEQK-QQELEKKEEELEELIEEQLQELERISGL 150
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
303-391 |
2.32e-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: 40.31 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 303 LYQTKYQELQVSAQLhgdRMQETKVQISQLHQEIQRLQSqtenLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAAL 382
Cdd:COG0845 54 LDPPDLQAALAQAQA---QLAAAQAQLELAKAELERYKA----LLKKGAVSQQELDQAKA----ALDQAQAALAAAQAAL 122
|
....*....
gi 89357932 383 RMAKQNLAR 391
Cdd:COG0845 123 EQARANLAY 131
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
276-393 |
4.56e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 38.27 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 276 LDFSSIITEVRAryeeiARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQA 355
Cdd:pfam02321 69 FDGGKRRARVKA-----AKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLI 143
|
90 100 110
....*....|....*....|....*....|....*...
gi 89357932 356 AITDAEQrGELALKDAQAKVDELEAALRMAKQNLARLL 393
Cdd:pfam02321 144 SLLDVLQ-AEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
229-355 |
5.33e-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: 39.28 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 229 KMELEGKLEALREYLYFLKH---LNEEELGQLQTQasdtsvvlsmdNNRYLdfsSIITEVRARYEEIArsskAEAEALYQ 305
Cdd:pfam15070 199 KKELAKKLGQLQEELGELKEtleLKSQEAQSLQEQ-----------RDQYL---AHLQQYVAAYQQLA----SEKEELHK 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 89357932 306 TKYQELQVSAQLHGDRMQeTKVQISQLHQEIQRLQSQTENLKKQNASLQA 355
Cdd:pfam15070 261 QYLLQTQLMDRLQHEEVQ-GKVAAEMARQELQETQERLEALTQQNQQLQA 309
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
160-392 |
6.00e-03 |
|
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: 38.94 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 160 PVFEACLDQLRKQLEQLQGERGALDAELKacrdqeeeykskyeeeahRRATLENDFVVLKKDVDGvflSKMELEGKLEAL 239
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELD------------------RLQALESELAISRQDYDG---ATAQLRAAQAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 240 REYlyflkhlnEEELGQLQTQASDTsvvlsmdnnryldfssiitEVRARYEEIARSSKAEAEALYQtkyqelQVSAQLhg 319
Cdd:pfam00529 113 KAA--------QAQLAQAQIDLARR-------------------RVLAPIGGISRESLVTAGALVA------QAQANL-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89357932 320 drmQETKVQISQLHQEIqrLQSQTENLkkqnaslqaaitdAEQRGELAlkDAQAKVDELEAALRMAKQNLARL 392
Cdd:pfam00529 158 ---LATVAQLDQIYVQI--TQSAAENQ-------------AEVRSELS--GAQLQIAEAEAELKLAKLDLERT 210
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
294-393 |
6.56e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 38.87 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 294 RSSKAEAEALYQTKYQELQvsaqlhgDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRG--------- 364
Cdd:COG1538 50 RARIEAAKAQAEAAEADLR-------AARLDLAAEVAQAYFDLLAAQEQLALAEENLALAEELLELARARYeaglasrld 122
|
90 100 110
....*....|....*....|....*....|...
gi 89357932 365 ----ELALKDAQAKVDELEAALRMAKQNLARLL 393
Cdd:COG1538 123 vlqaEAQLAQARAQLAQAEAQLAQARNALALLL 155
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
231-398 |
7.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 231 ELEGKLEALREYLyfLKHLNEEELGQLQTQASDTS----VVLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEALY-- 304
Cdd:COG4717 351 ELLREAEELEEEL--QLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDee 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89357932 305 --QTKYQELQvsaqlhgDRMQETKVQISQLHQEIQRLQSQTENLKKQNaslqaAITDAEQRGELALKDAQAKVDELeAAL 382
Cdd:COG4717 429 elEEELEELE-------EELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEW-AAL 495
|
170
....*....|....*.
gi 89357932 383 RMAKQNLARLLCEYQE 398
Cdd:COG4717 496 KLALELLEEAREEYRE 511
|
|
| |
