|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
49-283 |
2.37e-68 |
|
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: 211.81 E-value: 2.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 49 KKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 128
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 129 KVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 208
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669633260 209 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDGLDHVLNDMT 283
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
8-153 |
5.81e-23 |
|
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: 91.60 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 8 KMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEaeva 87
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669633260 88 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAK 153
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-265 |
1.99e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 2 MEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADR 161
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 162 KYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....
gi 669633260 242 FAERSVAKLEKTIDDLEDELYAQK 265
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-267 |
4.03e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 25 QAEAEQKQAEERS---KQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELD 101
Cdd:COG1196 219 KEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 102 RAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTE 181
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 182 ERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 261
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
....*.
gi 669633260 262 YAQKLK 267
Cdd:COG1196 459 EALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-261 |
5.08e-13 |
|
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: 68.93 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 27 EAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQER 106
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 107 LATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAEL 186
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669633260 187 AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 261
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-227 |
1.31e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRK 162
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669633260 163 YEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIK 227
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
21-248 |
3.08e-09 |
|
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: 57.08 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 21 DRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEEL 100
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 101 DRAQERLATALQKleeAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERT 180
Cdd:COG4942 100 EAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669633260 181 EERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 248
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-267 |
5.06e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 25 QAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQ 104
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 105 ERLATALQKLEEaekaadesergmkvIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERA 184
Cdd:TIGR02168 288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 185 ELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQ 264
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
...
gi 669633260 265 KLK 267
Cdd:TIGR02168 434 ELK 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-261 |
2.20e-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: 55.06 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 22 RAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELD 101
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 102 RAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEL-------QEIQLKEAKRIAEEADRKYEEVARKLVIIE 174
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 175 GDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKIL-TDKLKEAETRAEFAERSVAKLEKT 253
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRR 973
|
....*...
gi 669633260 254 IDDLEDEL 261
Cdd:TIGR02168 974 LKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-261 |
4.19e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 49 KKLKGTEDELDKYSEALKD--AQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 126
Cdd:COG1196 216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 127 GMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLK 206
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 669633260 207 SLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 261
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-260 |
1.22e-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: 52.76 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 20 LDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLnrRIQLVEEE 99
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL--EEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 100 LDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLER 179
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 180 TEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLED 259
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
.
gi 669633260 260 E 260
Cdd:TIGR02169 946 I 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-247 |
1.35e-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: 52.76 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 27 EAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQER 106
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 107 LATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAEL 186
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 669633260 187 AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSV 247
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-259 |
2.60e-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: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 2 MEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKD-------AQEKLEL 74
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 75 AEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKR 154
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 155 IAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELeeELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLK 234
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260
....*....|....*....|....*
gi 669633260 235 EAETRAEFAERSVAKLEKTIDDLED 259
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLER 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-276 |
3.25e-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: 51.61 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 22 RAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELaekkaadaeaevasLNRRIQLVEEELD 101
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 102 RAQERLATALQKLEEAEKAADESERGMKviENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTE 181
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 182 ERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 261
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250
....*....|....*
gi 669633260 262 YAQKLKYKAISDGLD 276
Cdd:TIGR02169 892 DELEAQLRELERKIE 906
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
33-267 |
3.57e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 33 AEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQ 112
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 113 KLEEAEkaaDESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCS 192
Cdd:COG4942 98 ELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669633260 193 ELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLK 267
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-250 |
6.98e-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: 50.44 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 16 KENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQL 95
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 96 VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRalkdeekMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEG 175
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE-------RASLEEALALLRSELEELSEELRELESKRSELRR 915
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669633260 176 DLERTEERAELAESKCSELEEELKNVtnnlksLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKL 250
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNL------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
23-261 |
1.63e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 23 AEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDR 102
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 103 AQERLATALQKLEEAEKAADESERGMKV--------------IENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEvAR 168
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 169 KLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIkiltdklKEAETRAEFAERSVA 248
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA-------AEAEEEAEEAREEVA 575
|
250
....*....|...
gi 669633260 249 KLEKTIDDLEDEL 261
Cdd:PRK02224 576 ELNSKLAELKERI 588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
23-244 |
3.03e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 23 AEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEalkdaQEKLELAEKKAADAEAEVASLNRRIQLVEEELDR 102
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 103 AQERLATALQKLEEAEKAADEsergmkVIENRALKD-EEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDL-ERT 180
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPE------LLQSPVIQQlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633260 181 EERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEE---EIKILTDKLKEAETRAEFAE 244
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEAR 378
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
23-261 |
8.18e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 23 AEQAEAEQKQAEERSKQLEDELATMQKKLKGTEdELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDR 102
Cdd:PRK04863 316 LAELNEAESDLEQDYQAASDHLNLVQTALRQQE-KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 103 AQERLA-----------------TALQKLEEAEK---AADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRK 162
Cdd:PRK04863 395 LKSQLAdyqqaldvqqtraiqyqQAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 163 YEEVARKLVIIEGDLERtEERAELAESKCSELEEElKNVTNNLKSLEAQ---AEKYSQKEDKYEEEIKILTDKLKEAETR 239
Cdd:PRK04863 475 FEQAYQLVRKIAGEVSR-SEAWDVARELLRRLREQ-RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDD 552
|
250 260
....*....|....*....|..
gi 669633260 240 AEFAERSVAKLEKTIDDLEDEL 261
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESV 574
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
21-261 |
9.63e-06 |
|
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: 46.87 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 21 DRAEQAEAEQKQAEERSKQLE-------DELATMQKKLKGTEdELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRI 93
Cdd:COG3096 306 YRLVEMARELEELSARESDLEqdyqaasDHLNLVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 94 QLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAK--- 153
Cdd:COG3096 385 EAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEqkl 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 154 RIAEEADRKYEEVARKLVIIEGDLERTEeraelAESKCSELEE---ELKNVTNNLKSLEAQ---AEKYSQKEDKYEEEIK 227
Cdd:COG3096 465 SVADAARRQFEKAYELVCKIAGEVERSQ-----AWQTARELLRryrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLE 539
|
250 260 270
....*....|....*....|....*....|....
gi 669633260 228 ILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 261
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-245 |
4.60e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 6 KKKMQMLKLDKENVLDRAEQ---AEAEQKQAEERSKQLEDELATMQKKLKGteDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKA--EEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGmkvieNRALKDEEKMELQEIQLKEAKRIAEEAdRK 162
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-----DEAKKAEEAKKADEAKKAEEAKKADEA-KK 1541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 163 YEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEF 242
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
...
gi 669633260 243 AER 245
Cdd:PTZ00121 1622 AEE 1624
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-273 |
1.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQE--KLELAEKKAA 80
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 81 DAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEAd 160
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 161 RKYEEVARKLVIIEGDLERTEERAELAES---------KCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTD 231
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEakkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 669633260 232 KLKEAETRAEFAERSVAKLEKTIDDL----EDELYAQKLKYKAISD 273
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKAEED 1403
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
12-154 |
1.19e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 12 LKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATmQKKLKGTEDELDKYSEALKDAQEKLElaekkaadaeaevaslnR 91
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELE-----------------R 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633260 92 RIQLVE------EELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEiQLKEAKR 154
Cdd:COG1566 136 YQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAEL 203
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-270 |
1.63e-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: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 67 DAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENRALkdeekmelqe 146
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREIA---------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 147 iQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKY---- 222
Cdd:COG4913 672 -ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElral 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 669633260 223 -EEEIKILTDKLKEAETRAEFAERsVAKLEKTIDDLEDELYAQKLKYKA 270
Cdd:COG4913 751 lEERFAAALGDAVERELRENLEER-IDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
94-272 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 94 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVII 173
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 174 EGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKT 253
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170
....*....|....*....
gi 669633260 254 IDDLEDELYAQKLKYKAIS 272
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLN 399
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-225 |
1.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 15 DKENVLDRAEQA-EAEQKQAEERSKQLEDELATMQKKLKGTEDELDKySEALKDAQEKLELAEKKAADAEAEVASLNRRI 93
Cdd:PTZ00121 1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 94 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVII 173
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 669633260 174 EGDLERTEERAELAESKCSelEEELKNVTNNLKSLEAQAEKYSQKEDKYEEE 225
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3-130 |
2.11e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQ-AEAEQKQAEERSKQLEDELATMQ---KKLKGTEDELDKYSEALKDAQEKLELAEKK 78
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEhEERELTEEEEEIRRLEEQVERLEaevEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 669633260 79 AADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 130
Cdd:COG2433 460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-270 |
2.20e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRK 162
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 163 YEEVaRKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEF 242
Cdd:PTZ00121 1387 AEEK-KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
250 260
....*....|....*....|....*...
gi 669633260 243 AERSvAKLEKTIDDLEDELYAQKLKYKA 270
Cdd:PTZ00121 1466 AEEA-KKADEAKKKAEEAKKADEAKKKA 1492
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
21-221 |
2.97e-04 |
|
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: 42.13 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 21 DRAEQ-AEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSE-AL-KDAQEKLELAEKKAADAEAEVASLNRRIQLVE 97
Cdd:NF012221 1554 DDAAQnALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQnALeTNGQAQRDAILEESRAVTKELTTLAQGLDALD 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 98 EE-------------------LDRAQERLATALQKLEEA-EKAADESERGMKVIENRALKDEEKMELQEIQLKEA-KRIA 156
Cdd:NF012221 1634 SQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAeQDID 1713
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633260 157 E---EADRKYEEVARKlviiEGDLERTEERAELAESKC-SELEEELKNVTNnlKSLEAQAEKYSQKEDK 221
Cdd:NF012221 1714 DakaDAEKRKDDALAK----QNEAQQAESDANAAANDAqSRGEQDASAAEN--KANQAQADAKGAKQDE 1776
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
25-248 |
4.82e-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: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 25 QAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRA- 103
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 104 -----QERLATALQKLEEAEKAADESERgMKVIENRALKDEEKMElqeiQLKEAKRIAEEADrkyEEVARKLVIIEGDLE 178
Cdd:COG3883 93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLE----ELKADKAELEAKK---AELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 179 RTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 248
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
16-230 |
5.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 16 KENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLK---------GTEDELDKYSEALKDAQEKLELAEKKAADAEAEV 86
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 87 ASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKAADESERGMKVIENRALKDEEKMELQEiqlkEAKRIAEEA 159
Cdd:COG3206 243 AALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELSARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669633260 160 DRKYEEVARKLVIIEGDLERTEERAEL---AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILT 230
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-188 |
5.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRK 162
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
170 180
....*....|....*....|....*.
gi 669633260 163 YEEVARKLVIIEGDLERTEERAELAE 188
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2-241 |
6.25e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 2 MEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADR 161
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 162 KYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
14-243 |
7.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 14 LDKENVLDRAEQ----------AEAEQKQAEERSKQLED--ELATMQKKLKGTEDELDKYSEALKD--AQEKLELAEKKA 79
Cdd:COG4913 218 LEEPDTFEAADAlvehfddlerAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 80 ADAEAEVASLNRRIQLVEEELDRAQERLATA--------LQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKE 151
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 152 AkriAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKiltD 231
Cdd:COG4913 378 S---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---E 451
|
250
....*....|..
gi 669633260 232 KLKEAETRAEFA 243
Cdd:COG4913 452 ALGLDEAELPFV 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-117 |
7.97e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 21 DRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEEL 100
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
90
....*....|....*..
gi 669633260 101 DRAQERLATALQKLEEA 117
Cdd:COG4913 772 EERIDALRARLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-273 |
8.87e-04 |
|
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: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 98 EELDRAQERLATALQKLE----------EAEKAADESERGMKVIE-NRALKDEEKMELQEIQLKEAKRIAEEADRKYEEV 166
Cdd:COG4913 235 DDLERAHEALEDAREQIEllepirelaeRYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 167 ARKLVIIEGDLERTEE--------RAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDkyeEEIKILTDKLKEAET 238
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLP---ASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*
gi 669633260 239 RAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISD 273
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-249 |
9.15e-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: 40.13 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 2 MEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLelaekkaad 81
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 82 aeaevaslnrriqlvEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADR 161
Cdd:COG4942 107 ---------------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 162 KYEEVARKLViiegdlERTEERAELAESKcSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG4942 172 ERAELEALLA------ELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*...
gi 669633260 242 FAERSVAK 249
Cdd:COG4942 245 AAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-180 |
9.52e-04 |
|
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: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQL---------EDELATMQKKLKGTEDELDKYSEA---LKDAQE 70
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASsddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 71 KLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienralKDEEKMELQEIQLK 150
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR----------ALLEERFAAALGDA 762
|
170 180 190
....*....|....*....|....*....|
gi 669633260 151 EAKRIAEEADRKYEEVARKLVIIEGDLERT 180
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
20-210 |
1.03e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 20 LDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVA-------SLNRR 92
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 93 IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVI 172
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 669633260 173 IEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEA 210
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-172 |
1.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 1 MMEAIKKKMQMLKldKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLElaekkaa 80
Cdd:PRK12704 43 ILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELE------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 81 daeAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMkVIENraLKDEEKMELQEIqlkeAKRIAEEAD 160
Cdd:PRK12704 114 ---KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI-LLEK--VEEEARHEAAVL----IKEIEEEAK 183
|
170
....*....|..
gi 669633260 161 RKYEEVARKLVI 172
Cdd:PRK12704 184 EEADKKAKEILA 195
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
4-263 |
1.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 4 AIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAE 83
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 84 AEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKY 163
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 164 EEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFA 243
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260
....*....|....*....|
gi 669633260 244 ERSVAKLEKTIDDLEDELYA 263
Cdd:COG4372 268 LVEKDTEEEELEIAALELEA 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-241 |
1.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 48 QKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 127
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 128 MKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESkcSELEEELKNvtnnlks 207
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757
|
170 180 190
....*....|....*....|....*....|....
gi 669633260 208 lEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG4913 758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-271 |
1.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 141 KMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKED 220
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 669633260 221 KYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAI 271
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
108-267 |
1.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 108 ATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELA 187
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 188 ESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLK 267
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-282 |
1.83e-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: 39.67 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 140 EKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKE 219
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669633260 220 DKYEEEIKILTDKL-----KEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDGLDHVLNDM 282
Cdd:TIGR02169 775 HKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
5-234 |
2.37e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.27 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 5 IKKKMQMLKLDKEnvLDRAEQAEA---------EQKQAEERSKQLE---DELATMQKKLKgteDELDKYSEALKDAQEKL 72
Cdd:PRK10929 28 ITQELEQAKAAKT--PAQAEIVEAlqsalnwleERKGSLERAKQYQqviDNFPKLSAELR---QQLNNERDEPRSVPPNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 73 elaekkaadaeaEVASLNRRI-----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIENralkd 138
Cdd:PRK10929 103 ------------STDALEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGT----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 139 eekmelQEIQLKEAKRIAEEAdrkyEEVARKLVIIEGDLE------RTE---ERAELAESKCSELEEELKNVTNNLKSLE 209
Cdd:PRK10929 166 ------PNTPLAQAQLTALQA----ESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQALRNQLNSQR 235
|
250 260 270
....*....|....*....|....*....|
gi 669633260 210 AQ-AEKYSQKEDKYEEEI----KILTDKLK 234
Cdd:PRK10929 236 QReAERALESTELLAEQSgdlpKSIVAQFK 265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3-190 |
2.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 83 EAEVASLN------------RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLK 150
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 669633260 151 EAKRIAEEADRKYEEVARKLVIIEGDLERTEERAELAESK 190
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
21-262 |
2.61e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.14 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 21 DRAEQAEAEQKQAEERSKQLEDeLATMQKKLKGTEDELDKYS--EALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEE 98
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRS-YLPKLNPLREEKKKVSVKSleELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 99 ELDRAQerlatALQKLEEAEKAADESERgMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKY-------------EE 165
Cdd:PRK05771 122 EIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsdevEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 166 VARKLVIIEGDLERTEERAELAeskcSELEEELKNVTNNLKSLEAQAEKYSQKEDK----YEEEIKILTDK----LKEAE 237
Cdd:PRK05771 196 ELKKLGFERLELEEEGTPSELI----REIKEELEEIEKERESLLEELKELAKKYLEellaLYEYLEIELERaealSKFLK 271
|
250 260 270
....*....|....*....|....*....|.
gi 669633260 238 TRAEFA------ERSVAKLEKTIDDLEDELY 262
Cdd:PRK05771 272 TDKTFAiegwvpEDRVKKLKELIDKATGGSA 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-261 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 24 EQAEAEQKQAEERSKQLE---DELATMQKKLKGTEDELDKYSEALKDAQE-KLELAEKKAADAEAEVASLNRRIQLVEEE 99
Cdd:TIGR02169 173 EKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 100 LDRAQERLATALQKLEEAEKAADE-SERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLE 178
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 179 RTEERAElaeskcseleeelknvtnnlkSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLE 258
Cdd:TIGR02169 333 KLLAEIE---------------------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
...
gi 669633260 259 DEL 261
Cdd:TIGR02169 392 EKL 394
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-227 |
4.28e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 5 IKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKqlEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEA 84
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 85 EVASLNRRIQLVEEELDRAQErlatALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRKYE 164
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAE----ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669633260 165 EVARKlviiEGDLERTEERAELAESKCSELEEELKNVTNnlKSLEAQAEKYSQKEDKYEEEIK 227
Cdd:PTZ00121 1748 EAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIF 1804
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-270 |
4.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKK---LKGTEDELDKYSEALKDAQEKLELAEKKA 79
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 80 ADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGmkviENRALKDEEKMELQEIQLK--------E 151
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAEEAKKADEAKKKaeeakkadE 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 152 AKRIAEEADRKYEEVARKlviiegdLERTEERAELAESKCSELEEELKNVTNNLKSLEAQA--EKYSQKEDKYEEEIKIL 229
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKA-------AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKA 1560
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 669633260 230 TDKLKEAETRAEFAERSVA--------KLEKTIDDLEDELYAQKLKYKA 270
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMAlrkaeeakKAEEARIEEVMKLYEEEKKMKA 1609
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-272 |
4.62e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.41 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 3 EAIKKKMQMLKLDKENVLDRAEQaEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQ-EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADRK 162
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 163 YEEVARKLVIIEGDLERTEERAELaESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEF 242
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDEL-ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
250 260 270
....*....|....*....|....*....|
gi 669633260 243 AERSVAKLEKTIDDLEDELYAQKLKYKAIS 272
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-134 |
4.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 2 MEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEE---------------RSKQLEDELATMQKKLKGTEDELDKYSEALK 66
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREeldeleaqirgnggdRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669633260 67 DAQEKLELAEKKAADAEAEVAslnRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 134
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
91-226 |
6.75e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 37.67 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 91 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDE---------EKMELQEIQLKEAKRIAEEADR 161
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkEDKQVAENQKREIEKAQIEIKK 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669633260 162 KYEEVARKLVIIEGDLER-TEERAELAESKCSELEEELKNVTNNLKSL--EAQAEKYSQKEDKYEEEI 226
Cdd:pfam05262 293 NDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSLNEDAIDSSN 360
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
105-265 |
6.76e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.11 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 105 ERLATALQKLEEAEKAADESERGMKVIEN-----RALKDEEKMELQEIQLKEAKRIAEEADRKYEEVARKLVIIEGDLER 179
Cdd:PRK10929 48 EALQSALNWLEERKGSLERAKQYQQVIDNfpklsAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 180 TEERA-ELAES------KCSELEEELKNVTNNLKSLE-------------AQAEKYSQKEDKYEEEIKILTDKLKE--AE 237
Cdd:PRK10929 128 EQDRArEISDSlsqlpqQQTEARRQLNEIERRLQTLGtpntplaqaqltaLQAESAALKALVDELELAQLSANNRQelAR 207
|
170 180
....*....|....*....|....*...
gi 669633260 238 TRAEFAERSVAKLEKTIDDLEDELYAQK 265
Cdd:PRK10929 208 LRSELAKKRSQQLDAYLQALRNQLNSQR 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-258 |
8.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 37.61 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 91 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKRIAEEADrkyEEVARKL 170
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA---ERLAEEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633260 171 VIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKL 250
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
....*...
gi 669633260 251 EKTIDDLE 258
Cdd:COG1196 773 EREIEALG 780
|
|
| |
