|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
151-464 |
9.76e-130 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 381.19 E-value: 9.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 151 EEREQIKTLNNRFASFIDKVQFLEQQNKVLDTKWALLQEQGTKTVKPeVETLFEDYINILSRRLGFTVAEKGHLDAELRR 230
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 231 SQGVLEDYKYKYEDEISKRTAAENEFLTLKKDADAAFMIENELTAKVHSLIDEINFLRTLFDAEMSQMQTPLSDTSVIIS 310
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 311 MDNNHSLDMESIIAEVKTQYENIAKKSQAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51092301 391 CANLQAAIADAEQRGEMALKDARGKLEGLKDAPQKAKQDRTRLQKEYQELLSVNIYLDVEITTYRKLLEGEENR 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
15-148 |
6.93e-27 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 106.28 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 15 GSSASSARVPGLNHSGFSCVSLCQSRGISGSGPMCRVASFGSRSLYSEGSSKRISIGGSSCGNREFYGRHY--------- 85
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFgggggggfg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51092301 86 -------------GGDLGIGRGACGCFGFGAGAGFGDGYGGAGFPGYPSGGIQEVTISQSLLIPLNLQIDPTIQRV 148
Cdd:pfam16208 81 ggfgggggggfggGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-468 |
2.91e-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: 50.44 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 320 ESIIAEVKTQYENIAKKSQAEAESWYQTKYE--ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAA 397
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51092301 398 IADAEQRGEMA---LKDARGKLEGLKDAPQKAKQDRTRLQKEYQELLSVNIYLDVEITTYRK---LLEGEENRFNGE 468
Cdd:TIGR02168 325 LEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-441 |
2.12e-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: 47.07 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 362 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDARGKLEGLKDAPQKAKQDRTRLQKEYQ 438
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
...
gi 51092301 439 ELL 441
Cdd:COG4942 108 ELL 110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
141-462 |
8.01e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 141 IDPT-IQRVRTEEREQIKTLNNRFASFIDKVQFLEQQNKVLDTKWALLQEQ------GTKTVKPEVETLFEDYINILSR- 212
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 213 --RLGFTVAEKGHLDAElRRSQGVLEDYKYKyeDEISKRTAAENEFLTLKKDADAAFMIENELTAKVHSLIDEINFLRTL 290
Cdd:PRK01156 482 eeKIREIEIEVKDIDEK-IVDLKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 291 FDAEMSQMQTPLSDTSVIISmdnnhSLDMESIIA---EVKTQYENIAKKSQaEAESWYQTKYEELQVTAGRHGDD---LR 364
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 365 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDARGKLEGLKDAPQKAKQDRTRLQKEYQELLSVN 444
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 51092301 445 IYLDVEITTYRKLLEGEE 462
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
151-464 |
9.76e-130 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 381.19 E-value: 9.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 151 EEREQIKTLNNRFASFIDKVQFLEQQNKVLDTKWALLQEQGTKTVKPeVETLFEDYINILSRRLGFTVAEKGHLDAELRR 230
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 231 SQGVLEDYKYKYEDEISKRTAAENEFLTLKKDADAAFMIENELTAKVHSLIDEINFLRTLFDAEMSQMQTPLSDTSVIIS 310
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 311 MDNNHSLDMESIIAEVKTQYENIAKKSQAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51092301 391 CANLQAAIADAEQRGEMALKDARGKLEGLKDAPQKAKQDRTRLQKEYQELLSVNIYLDVEITTYRKLLEGEENR 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
15-148 |
6.93e-27 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 106.28 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 15 GSSASSARVPGLNHSGFSCVSLCQSRGISGSGPMCRVASFGSRSLYSEGSSKRISIGGSSCGNREFYGRHY--------- 85
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFgggggggfg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51092301 86 -------------GGDLGIGRGACGCFGFGAGAGFGDGYGGAGFPGYPSGGIQEVTISQSLLIPLNLQIDPTIQRV 148
Cdd:pfam16208 81 ggfgggggggfggGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-468 |
2.91e-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: 50.44 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 320 ESIIAEVKTQYENIAKKSQAEAESWYQTKYE--ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAA 397
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51092301 398 IADAEQRGEMA---LKDARGKLEGLKDAPQKAKQDRTRLQKEYQELLSVNIYLDVEITTYRK---LLEGEENRFNGE 468
Cdd:TIGR02168 325 LEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-440 |
3.39e-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: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 140 QIDPTIQRVRtEEREQIKTLNNRFASFIDKVqfLEQQNKVLDTKWALLQEQGTKTVKPEVEtlfedyINILSRRLGFTVA 219
Cdd:TIGR02169 167 EFDRKKEKAL-EELEEVEENIERLDLIIDEK--RQQLERLRREREKAERYQALLKEKREYE------GYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 220 EKGHLDAELRRSQGVLEDYKYKYeDEISKRTAAENEFL-TLKKDADAafMIENE---LTAKVHSLIDEINFLRTLFDAEM 295
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEI-SELEKRLEEIEQLLeELNKKIKD--LGEEEqlrVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 296 SQMQTPLSDTSVIISMDNNHSLDMESIIAEV------KTQYENIAKKSQAEAESWYQtKYEELQVTAGRHGDD------- 362
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIeeerkrRDKLTEEYAELKEELEDLRA-ELEEVDKEFAETRDElkdyrek 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 363 LRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR----------GEMALKDARGKLEGLKDAPQKAKQDRTR 432
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
....*...
gi 51092301 433 LQKEYQEL 440
Cdd:TIGR02169 474 LKEEYDRV 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-441 |
2.12e-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: 47.07 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 362 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDARGKLEGLKDAPQKAKQDRTRLQKEYQ 438
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
...
gi 51092301 439 ELL 441
Cdd:COG4942 108 ELL 110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
141-462 |
8.01e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 141 IDPT-IQRVRTEEREQIKTLNNRFASFIDKVQFLEQQNKVLDTKWALLQEQ------GTKTVKPEVETLFEDYINILSR- 212
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 213 --RLGFTVAEKGHLDAElRRSQGVLEDYKYKyeDEISKRTAAENEFLTLKKDADAAFMIENELTAKVHSLIDEINFLRTL 290
Cdd:PRK01156 482 eeKIREIEIEVKDIDEK-IVDLKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 291 FDAEMSQMQTPLSDTSVIISmdnnhSLDMESIIA---EVKTQYENIAKKSQaEAESWYQTKYEELQVTAGRHGDD---LR 364
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 365 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDARGKLEGLKDAPQKAKQDRTRLQKEYQELLSVN 444
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 51092301 445 IYLDVEITTYRKLLEGEE 462
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
199-442 |
8.60e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 199 VETLFEDYINILSRRLGFTVAEKGHLDAELRRSQGVLEDYKykyedeiskrtaAENEFLTLKKDADAAFMIENELTAKVH 278
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 279 SLIDEINFLRtlfdAEMSQMQTPLSDTSVIISMDNNHSldmesIIAEVKTQYENIakksqaeaeswyQTKYEELQVTAGR 358
Cdd:COG3206 230 EARAELAEAE----ARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAEL------------EAELAELSARYTP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 359 HGDDLRNTKQEIAEINRMIQR--------LRSEIDHVKKQCANLQAAIADAEQRGEmALKDARGKLEGLkdapqkaKQDR 430
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQeaqrilasLEAELEALQAREASLQAQLAQLEARLA-ELPELEAELRRL-------EREV 360
|
250
....*....|..
gi 51092301 431 TRLQKEYQELLS 442
Cdd:COG3206 361 EVARELYESLLQ 372
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
204-517 |
8.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 204 EDYINILSRRLGFTVAEKGHLDAELRRSQGVLEDYKYKYEDEISKRTAAENEFLTLKKDADAAFMIENELTAKVHSLI-- 281
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAra 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 282 -----DEINFLRTLFDAEM-SQMQTPLSDTSVIISMDNNhsldmesIIAEVKTQYENIAKKsQAEAESwyqtKYEELQVT 355
Cdd:COG3883 95 lyrsgGSVSYLDVLLGSESfSDFLDRLSALSKIADADAD-------LLEELKADKAELEAK-KAELEA----KLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 356 AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKLEGLKDAPQKAKQDRTRLQK 435
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 436 EYQELLSVNIYLDVEITTYRklLEGEENRFNGEGIGPVNISVVPSTGSSGYDSAGGANRNHGLGGGSSHSYGRNHGLGGG 515
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSA--GAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAG 320
|
..
gi 51092301 516 FS 517
Cdd:COG3883 321 AV 322
|
|
| DUF1351 |
pfam07083 |
Protein of unknown function (DUF1351); This family consists of several bacterial and phage ... |
324-441 |
2.43e-04 |
|
Protein of unknown function (DUF1351); This family consists of several bacterial and phage proteins of around 230 residues in length. The function of this family is unknown.
Pssm-ID: 429283 [Multi-domain] Cd Length: 210 Bit Score: 42.37 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 324 AEVKTQYENIAKKSQAEAEswyqtKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCAnlqAAIADAEQ 403
Cdd:pfam07083 9 AAISFNFEELETYVDGIVA-----KYEGLVVTE----DTVKEAKKERAELNKIAKALDDKRKEVKKQYS---EPYDEFEA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 51092301 404 RG---EMALKDARGKL-EGLKDAPQKAKQDRTRLQKE-YQELL 441
Cdd:pfam07083 77 KIkelVAKIKEAIDPIdEQIKAFEEKEKDAKRQLVKAlISELA 119
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-475 |
2.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 148 VRTEEREQIKTLNNRFASFIDKVQFLEQQNKVLDTKWALLQEQGTKTVKPEVETlfEDYINILSRRLGFTVAEKGHLDAE 227
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--SRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 228 LRRSQGVLEDYKYKYEDEISKRTAAENEFLTLKKDAdaafmieNELTAKVHSLIDEINFLRTLFDAEmsqmQTPLSDTSV 307
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-------EELEAQIEQLKEELKALREALDEL----RAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 308 IISMDNNHSLDMESIIAEVKTQYENIAKKSQAEAEswyqtkyeelqvtagrhgdDLRNTKQEIAEINRMIQRLRSEIDHV 387
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 388 KKQCANLQAAIADAE----------QRGEMALKDARGKLEGLKDA-------PQKAKQDRTRLQK----EYQELLSVNIY 446
Cdd:TIGR02168 879 LNERASLEEALALLRseleelseelRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQErlseEYSLTLEEAEA 958
|
330 340 350
....*....|....*....|....*....|.
gi 51092301 447 LDVEITTYRKLLEGEENRFNGE--GIGPVNI 475
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKikELGPVNL 989
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
320-465 |
3.96e-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: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 320 ESIIAEVKTQYENIAKKSQA----EAESWY-------QTKYEELQ-----VTAGrhGDDLRNTKQEIAEINRMIQRLRSE 383
Cdd:COG4913 630 EERLEALEAELDALQERREAlqrlAEYSWDeidvasaEREIAELEaelerLDAS--SDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 384 IDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLKDAPQKAkqDRTRLQKEYQELLSVNIYLDV------EITTYRKL 457
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLE--LRALLEERFAAALGDAVERELrenleeRIDALRAR 781
|
....*...
gi 51092301 458 LEGEENRF 465
Cdd:COG4913 782 LNRAEEEL 789
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
292-419 |
5.14e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 292 DAEMSQMQTPLSDTSVIISMDNNHSLDMESIIAEVKtqyeniAKKSQAEAE-----SWYQTKYEELQVTAGRHGD---DL 363
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR------ASLSAAEAErsrlqALLAELAGAGAAAEGRAGElaqEL 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 51092301 364 RNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGemalKDARGKLEGL 419
Cdd:PRK09039 126 DSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADL 177
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-440 |
7.78e-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: 42.36 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 210 LSRRLGFTVAEKGHLDAELRRSQGVLEDYKYKYEDEISKRTAAENEFLTLKKDADAAFMIENELTAKVHSLIDEINFLRT 289
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 290 LFD---AEMSQMQTPLSDTSVIISmDNNHSLDMeSIIAEVKTQYENIaKKSQAEAESwyqtKYEELQVTAGRHGDDLRNT 366
Cdd:TIGR02169 759 ELKeleARIEELEEDLHKLEEALN-DLEARLSH-SRIPEIQAELSKL-EEEVSRIEA----RLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51092301 367 KQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQ---RGEMALKDARGKLEGLKDAPQKAKQDRTRLQKEYQEL 440
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEeleELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
224-436 |
1.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 224 LDAELRRSQGVLEDYKyKYEDEISKRTAA-----ENEFLTLKKDADAAFMIENELTAKVHSLI-------DEINFLRTLF 291
Cdd:PHA02562 186 LDMKIDHIQQQIKTYN-KNIEEQRKKNGEniarkQNKYDELVEEAKTIKAEIEELTDELLNLVmdiedpsAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 292 DAEMSQMQTplsdTSVIISMDNNHSL---------DMESIIAEVKTQYENIAKKSQAEaeswyQTKYEELQVTAGRHgDD 362
Cdd:PHA02562 265 AKIKSKIEQ----FQKVIKMYEKGGVcptctqqisEGPDRITKIKDKLKELQHSLEKL-----DTAIDELEEIMDEF-NE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51092301 363 LRNTKQE----IAEINRMIQRLRSEIDHVKKQCANLQAAIADAEqrgemalkdarGKLEGLKDAPQKAKQDRTRLQKE 436
Cdd:PHA02562 335 QSKKLLElknkISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA-----------EELAKLQDELDKIVKTKSELVKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
347-464 |
4.90e-03 |
|
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: 38.75 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 347 TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLKDApqka 426
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGNVRNN---- 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 51092301 427 kqdrtrlqKEYQELLSvniyldvEITTYRKLLEGEENR 464
Cdd:COG1579 89 --------KEYEALQK-------EIESLKRRISDLEDE 111
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-451 |
4.94e-03 |
|
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: 39.62 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 156 IKTLNNRFASFIDKVQFLEQQNKVLDTKWALLQE--QGTKTVKPEVETLFEDYINilsrrlgftvaEKGHLDAELRRSQG 233
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeiNEKTTEISNTQTQLNQLKD-----------EQNKIKKQLSEKQK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 234 VLEDYKYK---YEDEISKrtaAENEFLTLKKDAdaafmiENELTAKVHSLIDEInflrtlfDAEMSQMQTPLSDTsviis 310
Cdd:TIGR04523 275 ELEQNNKKikeLEKQLNQ---LKSEISDLNNQK------EQDWNKELKSELKNQ-------EKKLEEIQNQISQN----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 311 mdnnhsldmESIIAEVKTQYENIaKKSQAEAESWYQTKyeelqvtagrhgddlrntKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:TIGR04523 334 ---------NKIISQLNEQISQL-KKELTNSESENSEK------------------QRELEEKQNEIEKLKKENQSYKQE 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51092301 391 CANLQAAIADAEQRGEMALKDARGKLEGLKdapqKAKQDRTRLQKEYQELLSVNIYLDVEI 451
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIK----KLQQEKELLEKEIERLKETIIKNNSEI 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-440 |
5.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 330 YENIAKKSQAEAE-SWYQTKYEELqvtagrhgddlrntKQEIAEinrmIQRLRSEIDHVKKQCANLQAAIADAEQRG--- 405
Cdd:COG4717 128 LPLYQELEALEAElAELPERLEEL--------------EERLEE----LRELEEELEELEAELAELQEELEELLEQLsla 189
|
90 100 110
....*....|....*....|....*....|....*.
gi 51092301 406 -EMALKDARGKLEGLKDAPQKAKQDRTRLQKEYQEL 440
Cdd:COG4717 190 tEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
302-440 |
5.12e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 302 LSDTSVIISMD------------NNHSLDME--SIIAEVKTQYENI--AKKSQAEAESWYQTKYEELQVTAGRHGDDLRN 365
Cdd:PHA02562 159 LLDISVLSEMDklnkdkirelnqQIQTLDMKidHIQQQIKTYNKNIeeQRKKNGENIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 366 TKQEIAEINRMIQ--------------RLRSEIDHVKKQ---------CANLQAAIADAEQR---GEMALKDARGKLEGL 419
Cdd:PHA02562 239 LTDELLNLVMDIEdpsaalnklntaaaKIKSKIEQFQKVikmyekggvCPTCTQQISEGPDRitkIKDKLKELQHSLEKL 318
|
170 180
....*....|....*....|....
gi 51092301 420 KDAPQKAKQ---DRTRLQKEYQEL 440
Cdd:PHA02562 319 DTAIDELEEimdEFNEQSKKLLEL 342
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-440 |
5.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 346 QTKYEELQVTAGRHGDDlrntkqEIAEINRMIQRLRSEIDHVKKQCANLQAAIAD------------AEQRGEMA--LKD 411
Cdd:COG4913 322 REELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAAlglplpasaeefAALRAEAAalLEA 395
|
90 100
....*....|....*....|....*....
gi 51092301 412 ARGKLEGLKDAPQKAKQDRTRLQKEYQEL 440
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
206-413 |
7.29e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.14 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 206 YINILSRRLGF--TVAEKGHLDAELRRSqgvledYKYKYEDEISKRtaAENEFLTLKKDADAafMIE--NELTAKVHSLI 281
Cdd:PRK05771 51 LLTKLSEALDKlrSYLPKLNPLREEKKK------VSVKSLEELIKD--VEEELEKIEKEIKE--LEEeiSELENEIKELE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 282 DEINFLRTL--FDAEMSQMQTpLSDTSVII-SMDNNHSLDMESIIAEVKTQYENIAK---------KSQAEAESWYQTK- 348
Cdd:PRK05771 121 QEIERLEPWgnFDLDLSLLLG-FKYVSVFVgTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvvLKELSDEVEEELKk 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51092301 349 --YEELQVTAGRHGDD-LRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADA----EQRGEMALKDAR 413
Cdd:PRK05771 200 lgFERLELEEEGTPSElIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLK 271
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-466 |
9.45e-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: 38.88 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 320 ESIIAEVKTQYENI--------------AKKSQAEAESW------YQTKYEELQVTAGR-------HGDDLRNTKQEIAE 372
Cdd:TIGR02168 192 EDILNELERQLKSLerqaekaerykelkAELRELELALLvlrleeLREELEELQEELKEaeeeleeLTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092301 373 INRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMA---LKDARGKLEGLKDAPQKAKQDRTRLQKEYQEllsvniyLDV 449
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEELAE-------LEE 344
|
170
....*....|....*..
gi 51092301 450 EITTYRKLLEGEENRFN 466
Cdd:TIGR02168 345 KLEELKEELESLEAELE 361
|
|
| |
