|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-282 |
3.00e-60 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 191.01 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 48 KKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 128 KVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672052482 208 IASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDIT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
7-152 |
5.43e-26 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 99.69 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 7 KMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEadva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672052482 87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-264 |
3.88e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....
gi 672052482 241 FAERSVAKLEKTIDDLEDEVYAQK 264
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-264 |
8.46e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 165 VARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAER 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|
gi 672052482 245 SVAKLEKTIDDLEDEVYAQK 264
Cdd:COG1196 464 LLAELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-274 |
3.25e-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: 63.54 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 110 LQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESR 189
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 190 ARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
....*
gi 672052482 270 ISEEL 274
Cdd:TIGR02168 920 LREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
21-278 |
1.01e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 21 RAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELD 100
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 101 RAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSE 180
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 181 ERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEV 260
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250
....*....|....*...
gi 672052482 261 YAQKMKYKAISEELDNAL 278
Cdd:COG1196 466 AELLEEAALLEAALAELL 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-284 |
5.15e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 29 KKQAED--RCKQLEEEQQALQKKLKGTEDevEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERL 106
Cdd:COG1196 206 ERQAEKaeRYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 107 ATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVA 186
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 187 ESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMK 266
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250
....*....|....*...
gi 672052482 267 YKAISEELDNALNDITSL 284
Cdd:COG1196 444 LEEAAEEEAELEEEEEAL 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-213 |
1.78e-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: 54.77 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 18 AIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 98 ELDRAQERLATALQKLEEAEKA-----------ADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVA 166
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 672052482 167 RKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEE 213
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-284 |
7.55e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 102 AQERLATALQKLEEAEKAadesergmkVIENRAMKDEEKMELQEMQLKEAKHI--AEDSDRKYEEVARKLVILEGELERS 179
Cdd:PRK02224 424 LREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 180 EERAEVAESrARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDE 259
Cdd:PRK02224 495 EERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
250 260
....*....|....*....|....*
gi 672052482 260 VYAQKMKYKAISEELDnALNDITSL 284
Cdd:PRK02224 574 VAELNSKLAELKERIE-SLERIRTL 597
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-277 |
9.72e-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: 53.14 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 161 KYEEVARKLVILEGELERseERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 672052482 241 FAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNA 277
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-275 |
2.97e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 4 IKKKMQMLKLDKENAID----RAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEK--- 76
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevs 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 77 ------------------KATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDE 138
Cdd:TIGR02168 278 eleeeieelqkelyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 139 EKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEysTKE 218
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AEL 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 672052482 219 DKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELD 275
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-221 |
9.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 38 QLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLE--QAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 116 AEKAADESERGMKVIENRAMKDEEKMELQEMQLKEA--------KH---------IAEDSDRKYEEVARKLVILEGELER 178
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAelsarytpNHpdvialraqIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 672052482 179 SEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKY 221
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-260 |
1.26e-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: 49.67 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 18 AIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEE 97
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 178 RSEERA---------------EVAESRARQLEEELRTMDQALKSL----IASEEEYSTKEDKYEEEIKLLeeklkeaetr 238
Cdd:TIGR02168 940 NLQERLseeysltleeaealeNKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYDFLTAQK---------- 1009
|
250 260
....*....|....*....|..
gi 672052482 239 aEFAERSVAKLEKTIDDLEDEV 260
Cdd:TIGR02168 1010 -EDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-270 |
2.18e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADEsergmkvienramkdeekmelQEMQLKEAKHIAEDSDRK 161
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE---------------------LSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 162 YEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETR--- 238
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlse 947
|
250 260 270
....*....|....*....|....*....|....*..
gi 672052482 239 -----AEFAERSVAKLEKTIDDLEDEVYAQKMKYKAI 270
Cdd:TIGR02168 948 eysltLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-260 |
2.23e-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: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQL-EEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
250 260
....*....|....*....|
gi 672052482 241 FAERSVAKLEKTIDDLEDEV 260
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERV 506
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
7-220 |
4.62e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.91 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 7 KMQMLKLDKENAIDRAEQ-AEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESvkdAQEKLEQAEKKATDAEA-- 83
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQnALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQN---ALETNGQAQRDAILEESra 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 84 ---DVASLNRRIQLVEEE-------------------LDRAQERLATALQKLEEA-EKAADESERGMKVIENRAMKDEEK 140
Cdd:NF012221 1618 vtkELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 141 MELQEMQLKEAKHIAED----SDRKYEEVARKlvilEGELERSEERAEVAESRARQLEEElrtmDQALKSLIASEEEYST 216
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDakadAEKRKDDALAK----QNEAQQAESDANAAANDAQSRGEQ----DASAAENKANQAQADA 1769
|
....
gi 672052482 217 KEDK 220
Cdd:NF012221 1770 KGAK 1773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-277 |
6.08e-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: 47.37 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 110 LQKLEEAEKAADESERGMKviENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESR 189
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 190 ARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
....*...
gi 672052482 270 ISEELDNA 277
Cdd:TIGR02169 901 LERKIEEL 908
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-142 |
1.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 6 KKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTE-DEVEKYSESVKDAQEKLEQAEKKATDAEAD 84
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 672052482 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKME 142
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-199 |
2.27e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEAD-VASLNR 90
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 91 RIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHiaeDSDRKYEEVARKLV 170
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELR 422
|
170 180
....*....|....*....|....*....
gi 672052482 171 ILEGELERSEERAEVAESRARQLEEELRT 199
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-198 |
3.13e-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: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDR---CKQLEEEQ------QALQKKLKGTEDEVEKYSES---VKDAQE 69
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEYSwdeidvASAEREIAELEAELERLDASsddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 70 KLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienramkdeekmelqemQLK 149
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR---------------------ALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 672052482 150 EAKHIAEDSDRKYEEVARKLvilegelersEERAEVAESRARQLEEELR 198
Cdd:COG4913 752 EERFAAALGDAVERELRENL----------EERIDALRARLNRAEEELE 790
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-284 |
4.77e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 65 KDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQ 144
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 145 EMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEE 224
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 225 IKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-218 |
5.80e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEqqalqkkLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 672052482 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLiasEEEYSTKE 218
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL---QRELAEAE 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
9-284 |
5.91e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 9 QMLKLDKENAIDRAEQAEADKKQAE--DRCKQLEEEQQALQKKLKGTED-------------EVEKYSESVKDAQEKLEQ 73
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEmaRELEELSARESDLEQDYQAASDhlnlvqtalrqqeKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRAMK 136
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 137 DEEKMELQEMQLKEAKH---IAEDSDRKYEEVARKLVILEGELERSEeraevAESRARQLEEELRTMDQALKSLIASEEE 213
Cdd:COG3096 446 FRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQ-----AWQTARELLRRYRSQQALAQRLQQLRAQ 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672052482 214 YSTKEDKYEEEIKLLEEKLK------EAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-269 |
9.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 6 KKMQMLKLDKENA--IDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKySESVKDAQEKLEQAEKKATDAEA 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 164 EV-----ARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETR 238
Cdd:PTZ00121 1389 EKkkadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
250 260 270
....*....|....*....|....*....|.
gi 672052482 239 AEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-269 |
9.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 66 DAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENRAmkdeekmelqe 145
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREI----------- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 146 MQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEI 225
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 672052482 226 KLLEEKLKEAETR----AEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:COG4913 751 LEERFAAALGDAVerelRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
12-129 |
1.04e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 12 KLDKENAIDRAEQAEADK--KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKatdaEADVASLN 89
Cdd:COG2433 396 EAEREKEHEERELTEEEEeiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 672052482 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
11-212 |
1.11e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 11 LKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQK------KLKGTEDEVEKY---SESVKDAQEKLEQAEKKATDA 81
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQaqaeleALKDDNDEETREtlsTLSLRQLESRLAQTLDQLQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkvIENRAMKDEEKMELQ-EMQLKEAKHiaeDSDR 160
Cdd:PRK11281 141 QNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGK-----VGGKALRPSQRVLLQaEQALLNAQN---DLQR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 672052482 161 KYEEVARKLVILeGELERSEERAEVAesrarQLEEELRTMDQAL--KSLIASEE 212
Cdd:PRK11281 213 KSLEGNTQLQDL-LQKQRDYLTARIQ-----RLEHQLQLLQEAInsKRLTLSEK 260
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-260 |
1.45e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 5 KKKMQMLKLDKENAIDRAEQ---AEADKKQAEDRCKQLEEEQQAlqKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 162 YEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEF 241
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250
....*....|....*....
gi 672052482 242 AERSVAKLEKTIDDLEDEV 260
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEK 1646
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-213 |
1.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 14 DKENAIDRAEQA-EADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKySESVKDAQEKLEQAEKKATDAEADVASLNRRI 92
Cdd:PTZ00121 1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVIL 172
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 672052482 173 EGELERSEERAEVAEsrARQLEEELRTMDQALKSLIASEEE 213
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEE--AKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-216 |
2.09e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEkysesvkDAQEKLEQAEKKATDA 81
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-------EALRAAAELAAQLEEL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 672052482 162 YEEVARKLVILEGELERSEERAEVAesRARQLEEELRTMDQALKSLIASEEEYST 216
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-273 |
2.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKL---KGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM---KVIENRAMKDEEKMELQEMQLK--------E 150
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKaeeakkadE 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 151 AKHIAEDSDRKYEEVARKLVILEG--ELERSEERAEVAESRA---RQLEEELRTMDQALKS--LIASEEEYSTKEDKYEE 223
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKaeeAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAE 1567
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 672052482 224 EIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEE 273
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
15-284 |
3.07e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 15 KENAIDRAEQA-EADKKQAEDRCkQLEEEQQALQKKLKGTEDEVEKYSES-------VKDAQEKLEQAEKKATDAEADVA 86
Cdd:PRK04863 315 ELAELNEAESDlEQDYQAASDHL-NLVQTALRQQEKIERYQADLEELEERleeqnevVEEADEQQEENEARAEAAEEEVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 87 SLNRRIQLVEEELDRAQERLAT---ALQKLEEAEK---AADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:PRK04863 394 ELKSQLADYQQALDVQQTRAIQyqqAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 161 KYEEVARKLVILEGELERSEeraevAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLK------E 234
Cdd:PRK04863 474 QFEQAYQLVRKIAGEVSRSE-----AWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEfckrlgK 548
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 672052482 235 AETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2-125 |
3.85e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDR-------------CKQLEEEQQALQKKLKGTEDEVEKYSESVKD-- 66
Cdd:COG1566 65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQlarleaelgaeaeIAAAEAQLAAAQAQLDLAQRELERYQALYKKga 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 67 -AQEKLEQAEKKATDAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1566 145 vSQQELDEARAALDAAQAQLEAAQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAEL 203
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-247 |
4.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 24 QAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRA- 102
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 103 -----QERLATALQKLEEAEKAADESERgMKVIENRAMKDEEKMElqemQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:COG3883 93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 178 RSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVA 247
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-213 |
4.91e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVAslNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169 784 LEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 672052482 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEE 213
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-240 |
4.96e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-255 |
8.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTE----DEVEKYSESVKDAQEKLEQAEKKATDAE----A 83
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKKADEAKKAAEAKKKADeakkA 1518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYE 163
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 164 EVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKsliaSEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAE 243
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK----KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
250
....*....|..
gi 672052482 244 RSVAKLEKTIDD 255
Cdd:PTZ00121 1675 KKAEEAKKAEED 1686
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-276 |
1.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 48 KKLKGTEDEVEKYSESVK------DAQEKLEQAEKKATDAEADVASLN-----RRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4913 235 DDLERAHEALEDAREQIEllepirELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 117 EKAADESERgmkvienramkdeekmelQEMQLKEAkhIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEE 196
Cdd:COG4913 315 EARLDALRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 197 LRTMDQALKSLIAseeeystkedkyeeeiklleeklkEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDN 276
Cdd:COG4913 375 LPASAEEFAALRA------------------------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
55-198 |
1.24e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 55 DEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLAT--ALQK---------LEEAEKAADES 123
Cdd:COG0497 254 ERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALlrRLARkygvtveelLAYAEELRAEL 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672052482 124 ERgmkvIENramkDEEKMELQEMQLKEAKhiaedsdRKYEEVARKLvilegelerSEERAEVAESRARQLEEELR 198
Cdd:COG0497 334 AE----LEN----SDERLEELEAELAEAE-------AELLEAAEKL---------SAARKKAAKKLEKAVTAELA 384
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-251 |
1.98e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIE--NRAMKDEEKMELQEMQLKEAKHIAEDS 158
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqeLQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 159 DRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETR 238
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250
....*....|...
gi 672052482 239 AEFAERSVAKLEK 251
Cdd:COG4372 280 IAALELEALEEAA 292
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
48-273 |
2.19e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 48 KKLKGTEDEVEKYS--ESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQerlatALQKLEEAEKAADESER 125
Cdd:PRK05771 70 NPLREEKKKVSVKSleELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----PWGNFDLDLSLLLGFKY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 126 gMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKY----------EEVARKLVILEGELERSEERAEVAEsRARQLEE 195
Cdd:PRK05771 145 -VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsDEVEEELKKLGFERLELEEEGTPSE-LIREIKE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 196 ELRTMDQALKSLIASEEEYSTKEDKYEEEIKLL-EEKLKEAETRAEFA-------------ERSVAKLEKTIDDL-EDEV 260
Cdd:PRK05771 223 ELEEIEKERESLLEELKELAKKYLEELLALYEYlEIELERAEALSKFLktdktfaiegwvpEDRVKKLKELIDKAtGGSA 302
|
250
....*....|...
gi 672052482 261 YAQKMKYKAISEE 273
Cdd:PRK05771 303 YVEFVEPDEEEEE 315
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
27-128 |
2.30e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 27 ADKKQAEDRCKQLEEEQQALQK-KLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVAslnrRIQLVEEELDRAQER 105
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKeQDEASFERLAELRDELAELEEELEALKARWEAEKELIE----EIQELKEELEQRYGK 486
|
90 100
....*....|....*....|...
gi 672052482 106 LATALQKLEEAEKAADESERGMK 128
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR 509
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
54-156 |
3.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 38.65 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 54 EDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMKVIEN 132
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELRQLQK 598
|
90 100
....*....|....*....|....*.
gi 672052482 133 RAMKDEEKMELQEMQ--LKEAKHIAE 156
Cdd:PRK00409 599 GGYASVKAHELIEARkrLNKANEKKE 624
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-177 |
4.38e-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: 38.50 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 81 AEADVASLNRRIQLVEEELDRAQERLATALQKL-EEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSD 159
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
170
....*....|....*...
gi 672052482 160 RKYEEVARKLVILEGELE 177
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKE 1010
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
21-278 |
4.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 21 RAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELD 100
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 101 RAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSE 180
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 181 ERaEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEV 260
Cdd:COG4372 192 AN-RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250
....*....|....*...
gi 672052482 261 YAQKMKYKAISEELDNAL 278
Cdd:COG4372 271 KDTEEEELEIAALELEAL 288
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
22-101 |
5.18e-03 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 463000 [Multi-domain] Cd Length: 187 Bit Score: 37.17 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKgteDEVEKYSESVKDAQEKLEQAEKKATDaeaDVASLNRRIQLVEEELDR 101
Cdd:pfam10211 114 ALQAEQGKAELEKKIADLEEEKEELEKQVA---ELKAKCEAIEKREEERRQAEEKKHAE---EIAFLKKTNQQLKAQLER 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
37-263 |
5.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 37 KQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 117 EKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEE 196
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672052482 197 LRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQ 263
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-245 |
6.21e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.20 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 82 EADvaslnrriQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:PTZ00121 1367 EAA--------EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 162 YEEVARKlvilEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEF 241
Cdd:PTZ00121 1439 KAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
....
gi 672052482 242 AERS 245
Cdd:PTZ00121 1515 AKKA 1518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-259 |
6.43e-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: 37.82 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 32 AEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQ 111
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 112 KLEEAEKAADESERGMKVIENRamkDEEKMELqemqlkeakhiaedSDRKYEEVARKLVILEGELERSEERAEvaesrar 191
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQ---PPLALLL--------------SPEDFLDAVRRLQYLKYLAPARREQAE------- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672052482 192 QLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDE 259
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-273 |
6.60e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.20 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQE--------KLEQ 73
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarkaeevrKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKH 153
Cdd:PTZ00121 1193 LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 154 IAEDSDRKYEEVARKLVILEGELERSEERAEVAEsrARQLEEELRTMDQALKsliaSEEEYSTKEDKYEEEIKLLEEKLK 233
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAKK----KAEEAKKKADAAKKKAEEAKKAAE 1346
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672052482 234 EAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEE 273
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-284 |
6.66e-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: 37.44 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKh 153
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 154 iaEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLK 233
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 672052482 234 EAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-133 |
7.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 11 LKLDKENAIDRAEQAEADKKQAE-DRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKkatDAEADVASLN 89
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAA 390
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 672052482 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
12-259 |
7.97e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 37.71 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRR 91
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 92 IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVI 171
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 172 LEGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEK 251
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
....*...
gi 672052482 252 TIDDLEDE 259
Cdd:COG3064 260 LGAALAAA 267
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-277 |
9.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.43 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 5 KKKMQMLKLDKENAIDRAEQAEaDKKQAEDRCKQLEEEQQALQKKLKGtedevEKYSESVKDAQEKLEQAEKKATDAEAD 84
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKA-----EEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmKVIENRAMKDEEKMELQEMQLK-EAKHIAEDSDRKYE 163
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKKKADELKKAaAAKKKADEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672052482 164 EVARKlvileGELERSEERAEVAESRARQLEEELRTMDQALKSLIASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAe 243
Cdd:PTZ00121 1429 EKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA- 1502
|
250 260 270
....*....|....*....|....*....|....
gi 672052482 244 RSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNA 277
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
|
| |
