|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
133-446 |
5.05e-152 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 437.43 E-value: 5.05e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 133 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRG 212
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 213 MQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLS 292
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 293 MDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 372
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387918 373 CANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 446
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
59-130 |
3.00e-24 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 98.96 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 59 RSLYGLGGSKRISI---GGGSCAISG-------------------------------GYGSRAGGSYGFGGPGF------ 98
Cdd:pfam16208 43 RSLYNLGGSKSISIsvaGGGSRPGSGfgfgggggggfgggfgggggggfgggggfggGFGGGGYGGGGFGGGGFggrggf 122
|
90 100 110
....*....|....*....|....*....|....
gi 194387918 99 --PVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRV 130
Cdd:pfam16208 123 ggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-428 |
6.22e-11 |
|
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: 65.46 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 133 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSELRG 212
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 213 MQDLVEDFKNKYEDEINKRTAAENEFVTLKKdvdaaymNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTSV 289
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 290 VLSMDNNR-------NLDLDSIIAEVKAQYEEIAQ----------RSRAEAESWYQtKYEELQVTAGRHGDDLRNTKQEI 352
Cdd:TIGR02168 825 RLESLERRiaaterrLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLN-ERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 353 AEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-----------GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQE 421
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 194387918 422 LMNVKLA 428
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
274-414 |
3.02e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.66 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 274 DAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 350
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387918 351 EIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGemalKDAKNKLEG----LEDALQKAKQDLAR 414
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
123-444 |
4.41e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 123 IDPT-IQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQ------GTKTVRQNLEPLFEQYINNLRR- 194
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 195 --QLDSIVGERGRLDSELRGMQDLVEDFKNKyedEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL 272
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 273 YDAELSQMQTHISDTSVVLSmdnnrNLDLDSIIA---EVKAQYEEIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 346
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 347 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 426
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 194387918 427 LALDVEIATYRKLLEGEE 444
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-441 |
8.19e-07 |
|
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: 51.99 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 192 LRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRA 271
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 272 L---YDAELSQMQTHISdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 347
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 348 TKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKL 427
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 194387918 428 ALDVEIATYRKLLE 441
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-422 |
1.37e-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: 51.22 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 122 QIDPTIQRVRaEEREQIKTLNNKFASFIDKVRflEQQNKVLETKWTLLQEQGTKTVRQNLE-PLFEQYINNLRRQLDSIV 200
Cdd:TIGR02169 167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 201 GERGRLDSELRGMQDLVEDFKNKYE------DEINKRTAA--ENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFL--- 269
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeer 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 270 RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQR----------------SRAEAESWYQTKYEE 333
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkefaetrdelkDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 334 LQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQrgemalkdaknKLEGLEDALQKAKQDLA 413
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-----------KLEQLAADLSKYEQELY 472
|
....*....
gi 194387918 414 RLLKEYQEL 422
Cdd:TIGR02169 473 DLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-422 |
1.73e-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: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 162 LETKWTLLQEQGTKTVRqnleplFEQYINNLRR-QLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVT 240
Cdd:TIGR02168 198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 241 LKKDVDAAYMNKVELQAKADTLTDEINFL---RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQ 317
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 318 RSRA------EAESWYQ---TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-G 387
Cdd:TIGR02168 352 ELESleaeleELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlE 431
|
250 260 270
....*....|....*....|....*....|....*
gi 194387918 388 EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 422
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-444 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 177 VRQNLEPLFEQ------YiNNLRRQLDsivgergRLDSELRGMQDlvEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYM 250
Cdd:COG1196 198 LERQLEPLERQaekaerY-RELKEELK-------ELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 251 NKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESwyQTK 330
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 331 YEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQcanlQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQ 410
Cdd:COG1196 346 LEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270
....*....|....*....|....*....|....
gi 194387918 411 DLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 444
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-438 |
5.28e-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: 49.28 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 250 MNKVELQAKADT----LTDEINFL-RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIaQRSRAEAE 324
Cdd:TIGR02168 202 LKSLERQAEKAErykeLKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 325 SwyqtKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMA---LKDAKNKLEGL 401
Cdd:TIGR02168 281 E----EIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEEL 349
|
170 180 190
....*....|....*....|....*....|....*..
gi 194387918 402 EDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 438
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-444 |
6.04e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 136 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQgtktvRQNLEPLFEQyINNLRRQLDSIVGERGRLDSELRGMQD 215
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 216 LVEDFKNKYEdEINKRTAAENEfvtLKKDVDaAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDtsvvLSMDN 295
Cdd:PRK03918 267 RIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 296 NRNLDLDSIIAEVKAQYEEIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRSEIDHVK 370
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 371 KQCANLQAAIADAEQRGE------MALKDAKNKL---------EGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 435
Cdd:PRK03918 405 EEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
....*....
gi 194387918 436 YRKLLEGEE 444
Cdd:PRK03918 485 LEKVLKKES 493
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
128-415 |
1.85e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 128 QRVRAEEREQIKTLNNKFASFIDKVRFLEQQN-------KVLETKWTLLQEQGTKTVRQNLE-----PLFEQYINNLRRQ 195
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvSSLESQLQDTQELLQEETRQKLNlstrlRQLEDERNSLQEQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 196 LDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLtdeinflralyDA 275
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-----------EK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 276 ELSQMQTHISDTSVVLsmDNNRNL---------DLDSIIAEVK---AQYEEiaQRSRAEAESwyqTKYEELQVTAGRHGD 343
Cdd:pfam01576 574 TKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALSLARALE 646
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194387918 344 DLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCANLQAAIADAEQrgemALKDAKNKLEGLEDALQKAKQDLARL 415
Cdd:pfam01576 647 EALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-441 |
2.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 186 EQYIN-NLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDeinkrTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 264
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 265 EINFLRALYDAELSQMQTHISDTSVVLSmdnnrnldlDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQVTAGRHGDD 344
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAEL------------EAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 345 LRNTKQEIAEINRMIQRLRSEIDhvkkqcANLQAAIADAEQRgemalkdaKNKLEGLEDALQKAKQDLARLLKEYQELMN 424
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR--------EASLQAQLAQLEARLAELPELEAELRRLER 358
|
250
....*....|....*....
gi 194387918 425 vklalDVEIA--TYRKLLE 441
Cdd:COG3206 359 -----EVEVAreLYESLLQ 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
344-425 |
5.46e-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: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 344 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQ 420
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 194387918 421 ELMNV 425
Cdd:COG4942 108 ELLRA 112
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
150-418 |
6.21e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 150 DKVRFLEQQNKVLETKWTLLQEQgTKTvrqnleplFEQYINNLRRQLDSIVgergrldSELRGMQD-LVEDFKNkYEDEI 228
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-IKT--------YNKNIEEQRKKNGENI-------ARKQNKYDeLVEEAKT-IKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 229 NKRTAAENEFVTLKKDVDAAY----MNKVELQAKADTLTDEINFLRAlYDAELSQMQThISDTsvvlsmdnnrnldlDSI 304
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQQ-ISEG--------------PDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 305 IAEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAGRHgDDLRNTKQE----IAEINRMIQRLRSEIDHVKKQCANLQAAI 380
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL-----DTAIDELEEIMDEF-NEQSKKLLElknkISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
250 260 270
....*....|....*....|....*....|....*...
gi 194387918 381 adaeqrgemalKDAKNKLEGLEDALQKAKQDLARLLKE 418
Cdd:PHA02562 375 -----------VDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-422 |
9.15e-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: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 343 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 422
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-438 |
1.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 234 AENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTsvvlsmdnnrNLDLDSIIAEVKA 310
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 311 QYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmA 390
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLA-E 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 194387918 391 LKDAKNKLEGLEDALQKAKQD----LARLLKEYQELMNVKLALDVEIATYRK 438
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-438 |
1.55e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 300 DLDSIIAEVKAQYEEIAQRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQA 378
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 379 AIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 438
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-424 |
1.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 201 GERGRLDSELRGMQDLVEDFKNkyedeINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL-----YDA 275
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDN-----RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswDEI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 276 ELSQMQTHISDTSVVLsmdnnRNLDLDS-IIAEVKAQYEEiAQRSRAEAESwyqtKYEELQVTAGRHgddlrntKQEIAE 354
Cdd:COG4913 662 DVASAEREIAELEAEL-----ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKELEQ 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 355 INRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMN 424
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
300-441 |
2.09e-04 |
|
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: 42.99 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 300 DLDSIIAEVKAQYEEI-AQRSRAEAE-SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK--KQCAN 375
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194387918 376 LQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELmnvKLALDVEIATYRKLLE 441
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
189-408 |
4.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 189 INNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEI-N 267
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 268 FLRALYDAELSqmqthISDTSVVLSMDN-----NRNLDLDSIIAEVKAQYEEI--AQRSRAEAESWYQTKYEELQVTAGR 340
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387918 341 HGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKA 408
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
202-422 |
4.09e-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: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 202 ERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRalydAELSQMQ 281
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 282 THISDTSVVLSMDNNRNldldsiIAEVKAQYEEIAQRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEIAEINRMIQR 361
Cdd:COG4942 104 EELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194387918 362 LRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 422
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-434 |
4.58e-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: 43.12 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 120 NLQIDPTIQRVRaEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQgtktvRQNLEPLFEQY----------I 189
Cdd:TIGR02168 224 ELELALLVLRLE-ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-----VSELEEEIEELqkelyalaneI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 190 NNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNK---YEDEINKRTA----AENEFVTLKKDVDAAYMNKVELQAKADTL 262
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEkleeLKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 263 TDEINFLRALYDAELSQMQTHisdtsvvlsmdNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHG 342
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASL-----------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 343 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMaLKDAKNKLEGLED---ALQKAKQDLARLLKEY 419
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEgvkALLKNQSGLSGILGVL 525
|
330
....*....|....*..
gi 194387918 420 QELMNV--KLALDVEIA 434
Cdd:TIGR02168 526 SELISVdeGYEAAIEAA 542
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
107-286 |
5.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 107 QEVTVNQSLLTPLNLQIDptiQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLfE 186
Cdd:COG4913 269 ERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-E 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 187 QYINNLRRQLDSIVGERGRLDSELRGMQ----DLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTL 262
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
170 180
....*....|....*....|....*..
gi 194387918 263 TDEINFLRA---LYDAELSQMQTHISD 286
Cdd:COG4913 425 EAEIASLERrksNIPARLLALRDALAE 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
126-426 |
1.14e-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: 41.93 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 126 TIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKwtlLQEQgtktvrQNLEPLFEQYINNLRRQLDSIVGERGR 205
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQ------EKLNQQKDEQIKKLQQEKELLEKEIER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 206 LDSElrgmqdlVEDFKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEINFLRalydAELSQMQTHIS 285
Cdd:TIGR04523 431 LKET-------IIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIK----QNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 286 DTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSR------AEAESWYQTKYEELQvtagrhGDDLRNTKQ----EIAEI 355
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEklesekKEKESKISDLEDELN------KDDFELKKEnlekEIDEK 566
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194387918 356 NRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 426
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-449 |
1.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 300 DLDSIIAEVKAQYEEIAQRSRA----EAESWYQTKYEELQVTAGRHGD---DLRNTKQEIAEINRMIQRLRSEIDHVKKQ 372
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 373 CANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKA-----KQDLARLLKEYQELM------NVKLALDVEIATYRKLLE 441
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAedlarLELRALLEERFAAALgdaverELRENLEERIDALRARLN 783
|
....*...
gi 194387918 442 GEECRLYG 449
Cdd:COG4913 784 RAEEELER 791
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
127-426 |
1.52e-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: 41.25 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 127 IQRVRAEEREQIKTLNNKFASfidkvrfLEQQNKVLETKWTLLQE-----------QGTKTVRQNLEPLFEQYINNLRRQ 195
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKEQELIFLLQAREKEIHDLEIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 196 LDSIVGERGRLDSElrgmqdlVEDFKNKYEDEINKRTAaenefvtLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA 275
Cdd:pfam05483 459 LTAIKTSEEHYLKE-------VEDLKTELEKEKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 276 ELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLR--NTKQEIA 353
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIE 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194387918 354 EINRMIQRLRSEIDHVKKQcanlqaaiADAEQRGEMALKDAKNKLEgLEdaLQKAKQDLARLLKEYQELMNVK 426
Cdd:pfam05483 605 NKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLE-LE--LASAKQKFEEIIDNYQKEIEDK 666
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
343-448 |
1.56e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 343 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 422
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237
|
90 100 110
....*....|....*....|....*....|...
gi 194387918 423 -------MNVKLALDVEIATYRKLLegEECRLY 448
Cdd:smart00787 238 eskiedlTNKKSELNTEIAEAEKKL--EQCRGF 268
|
|
| DUF1351 |
pfam07083 |
Protein of unknown function (DUF1351); This family consists of several bacterial and phage ... |
298-433 |
2.02e-03 |
|
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: 39.67 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 298 NLDLDSIIAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCAnlq 377
Cdd:pfam07083 1 ELSVTQKPAAISFNFEELETYVDGIVA-----KYEGLVVTE----DTVKEAKKERAELNKIAKALDDKRKEVKKQYS--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387918 378 AAIADAEQRG---EMALKDAKNKL----EGLEDALQKAKQDLARLLK-EYQELMNVKLAlDVEI 433
Cdd:pfam07083 69 EPYDEFEAKIkelVAKIKEAIDPIdeqiKAFEEKEKDAKRQLVKALIsELAEEYGVPLE-EIEI 131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
305-438 |
2.22e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 305 IAEVKAQYEEIAQRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 384
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 194387918 385 QRGEmalkdaknkLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 438
Cdd:COG4717 467 EDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
189-418 |
2.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 189 INNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTaaenEFVTLKKDVDAAYMNKVELQAKADTLTDEINF 268
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 269 LRALYDaELSQMQTHISDTSVVLSMDNN----RNLDLDSIIAEVKAQYEEI---AQRSRAEAESW------YQTKYEELQ 335
Cdd:PRK02224 284 LRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 336 VTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALK---DAKNKLEGLEDALQKAKQDL 412
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARERV 442
|
....*....
gi 194387918 413 A---RLLKE 418
Cdd:PRK02224 443 EeaeALLEA 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-414 |
4.25e-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: 39.36 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 170 QEQGTKTVRQNLEPLFEQyINNLRRQLDSIVGERGRLDSELRgmqdlvedfknKYEDEINKRTAAENEfvtLKKDVDAAY 249
Cdd:COG4942 18 QADAAAEAEAELEQLQQE-IAELEKELAALKKEEKALLKQLA-----------ALERRIAALARRIRA---LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 250 MNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAevkaQYEEIAQRSRAEAESwYQT 329
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEE-LRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 330 KYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDAKNKLEGLEDALQKAK 409
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEA 236
|
....*
gi 194387918 410 QDLAR 414
Cdd:COG4942 237 AAAAE 241
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
305-416 |
4.82e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.47 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 305 IAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQ-EIAEINRMIQRLRSEIDHVKKQCANLQAAIADA 383
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
90 100 110
....*....|....*....|....*....|....*.
gi 194387918 384 EQRGEMALKDAKNKLEGLE---DALQKAKQDLARLL 416
Cdd:COG2268 326 EAEAEAIRAKGLAEAEGKRalaEAWNKLGDAAILLM 361
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
306-421 |
6.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 306 AEVKAQYEEIAQRSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAI 380
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 194387918 381 ADAEQRGE----MALKDAKNKLegLEDALQKAKQDLARLLKEYQE 421
Cdd:PRK12704 138 EEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
352-447 |
7.24e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 352 IAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDAKNKLEGLeDALQKAKQDLA--RLLKEYQELMNVKLAL 429
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-RLRREREKAERY-QALLKEKREYEgyELLKEKEALERQKEAI 242
|
90
....*....|....*...
gi 194387918 430 DVEIATYRKLLEGEECRL 447
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI 260
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
176-422 |
7.81e-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: 37.98 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 176 TVRQNLEPLFEqyINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvEL 255
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 256 QAKADTLTDEINFLRalydaelsqmqthisdtsvvlsmdNNRnlDLDSIIAEVkaqyeEIAQRSRAEAEswyqtkyeelq 335
Cdd:COG1579 72 EARIKKYEEQLGNVR------------------------NNK--EYEALQKEI-----ESLKRRISDLE----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 336 vtagrhgddlrntkQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDL-AR 414
Cdd:COG1579 110 --------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPE 175
|
....*...
gi 194387918 415 LLKEYQEL 422
Cdd:COG1579 176 LLALYERI 183
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
305-415 |
8.40e-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: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 305 IAEVKAQYEEIaQRSRAEAESWY-QTKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADA 383
Cdd:COG4913 264 YAAARERLAEL-EYLRAALRLWFaQRRLELLE-------AELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
90 100 110
....*....|....*....|....*....|..
gi 194387918 384 EQRgemALKDAKNKLEGLEDALQKAKQDLARL 415
Cdd:COG4913 336 GGD---RLEQLEREIERLERELEERERRRARL 364
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
192-441 |
9.92e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 38.67 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 192 LRRQLDSIVGERGRLDSELRGMQDLVE----------DFKN------KYEDEINKRTAAENEFVTLKKDVDAAYM----- 250
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEhwirdiqaiaGIMKirpeftKLQQEFNTLESAELRLSHLHFGYKSDETliasr 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 251 ------NKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAE 324
Cdd:pfam12128 278 qeerqeTSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387918 325 SwyqtKYEELQVTAGRHGDDLRNTKQEIAEI----NRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKD------- 393
Cdd:pfam12128 358 N----LEERLKALTGKHQDVTAKYNRRRSKIkeqnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREqleagkl 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 194387918 394 -AKNKLEGLEDALQKAKQDLARLLKEYQELMNVKlALDVEIATYRKLLE 441
Cdd:pfam12128 434 eFNEEEYRLKSRLGELKLRLNQATATPELLLQLE-NFDERIERAREEQE 481
|
|
| |
