|
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 |
1.08e-72 |
|
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: 222.98 E-value: 1.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 48 KKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 128 KVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 551509811 208 EAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 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 |
6.02e-25 |
|
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: 96.99 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 7 KMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEgdva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 551509811 87 ALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-264 |
9.05e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 1 MEAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAAD 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 161 KYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....
gi 551509811 241 FAERTVAKLEKSIDDLEDELYAQK 264
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-279 |
2.38e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADA 81
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 161
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 162 YEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEF 241
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270
....*....|....*....|....*....|....*...
gi 551509811 242 AERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHALN 279
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-284 |
1.88e-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: 70.47 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 32 AEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQ 111
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 112 KLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKAS 191
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 192 DLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAIS 271
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250
....*....|...
gi 551509811 272 EELDHALNDMTSL 284
Cdd:TIGR02168 922 EKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-278 |
3.45e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 48 KKLKQTEDELDKFSEGLKD--AQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1196 216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 126 GMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLK 205
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 551509811 206 SLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHAL 278
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
31-266 |
6.89e-10 |
|
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: 59.01 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 31 AAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATAL 110
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 111 QKLEEAEKAADESERGMKVIENRamkDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKA 190
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 551509811 191 SDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDELYAQKLK 266
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-284 |
1.59e-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: 58.53 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 4 IKKKMQMLKLDKENAID----RAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELS----- 74
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevs 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 75 --EKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienRAMKDEEKMEIQEMQLKEAK 152
Cdd:TIGR02168 278 elEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-------KLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 153 HIAEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKL 232
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 551509811 233 KEAETRAefAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSL 284
Cdd:TIGR02168 431 EEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-239 |
2.66e-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: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 18 AIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 98 ELDRAQERLATALQKLEEAEKAADE----SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILE 173
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 551509811 174 GDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-256 |
9.96e-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: 56.22 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADA 81
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 161
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 162 YEEVARKLVILEGDLERAEEradlaecKASDLEEELKNVTNNLKSLeaqAEKYSEKEDKYEEEIKVLTDKLKEAETRaef 241
Cdd:TIGR02168 903 LRELESKRSELRRELEELRE-------KLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEE--- 969
|
250
....*....|....*
gi 551509811 242 AERTVAKLEKSIDDL 256
Cdd:TIGR02168 970 ARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-277 |
1.12e-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: 55.83 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 1 MEAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAAD 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 161 KYEEVARKLVILEGDLERAEERADLAECKASdlEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 551509811 241 FAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-274 |
1.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 22 AEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDR 101
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 102 AQERLA---TALQKLE-----------EAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVAR 167
Cdd:COG1196 286 AQAEEYellAELARLEqdiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 168 KLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVA 247
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260
....*....|....*....|....*..
gi 551509811 248 KLEKSIDDLEDELYAQKLKYKAISEEL 274
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-259 |
4.31e-08 |
|
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: 54.30 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 7 KMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 87 ALNRRIQLVEEEL------------DRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHI 154
Cdd:TIGR02169 762 ELEARIEELEEDLhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 155 AEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKE 234
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260
....*....|....*....|....*
gi 551509811 235 AETRAEFAERTVAKLEKSIDDLEDE 259
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-270 |
4.94e-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: 53.91 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 5 KKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFseglkdaqeklelsEKKAADAEGD 84
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL--------------EAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 85 VAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEE 164
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 165 VARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKE-AETRAEFAE 243
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAE 957
|
250 260
....*....|....*....|....*..
gi 551509811 244 RTVAKLEKSIDDLEDELYAQKLKYKAI 270
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-275 |
8.65e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAadesergmkVIENRAMKDEEKMEIQEMQLKEAKHI--AEEAD 159
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 160 RKYEEVARKLVILEGDLERAEERADLAEcKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
250 260 270
....*....|....*....|....*....|....*.
gi 551509811 240 EFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-277 |
4.10e-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: 51.22 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 37 KQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 117 EKAADESERGMKviENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEE 196
Cdd:TIGR02169 750 EQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 197 LKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDH 276
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
.
gi 551509811 277 A 277
Cdd:TIGR02169 908 L 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-246 |
4.61e-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: 50.84 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 16 ENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKL-----ELSEKKA--ADAEGDVAAL 88
Cdd:TIGR02169 269 EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLakleaEIDKLLAeiEELEREIEEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 89 NRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARK 168
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 551509811 169 LVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTV 246
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-240 |
1.40e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 24 QAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRA- 102
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 103 -----QERLATALQKLEEAEKAADESERgMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLE 177
Cdd:COG3883 93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 551509811 178 RAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-284 |
1.49e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 97 EELDRAQERLAtaLQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDL 176
Cdd:COG1196 220 EELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 177 ERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDL 256
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180
....*....|....*....|....*...
gi 551509811 257 EDELYAQKLKYKAISEELDHALNDMTSL 284
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEEL 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-260 |
2.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 66 DAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENramkdeekmEIQE 145
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAER---------EIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 146 mqLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEi 225
Cdd:COG4913 673 --LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190
....*....|....*....|....*....|....*
gi 551509811 226 kvLTDKLKEAETRAEFAERTVAKLEKSIDDLEDEL 260
Cdd:COG4913 750 --LLEERFAAALGDAVERELRENLEERIDALRARL 782
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
22-257 |
4.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 22 AEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEglkdaqeklelsEKKAADAEGDVAALNRRIQLVEEELDR 101
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 102 AQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAkhiaeEADRKYEEVARKLVILEgdleraEE 181
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA-----ELSARYTPNHPDVIALR------AQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551509811 182 RADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDK---LKEAETRAEFAERTVAKLEKSIDDLE 257
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELeaeLRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
23-233 |
7.56e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 23 EQAETDKKAAEDKCKQ--------LED--ELLDLQKKLKQTEDELDKFSEGLKdaQEKLELSEK-KAADAEGDVAALNRR 91
Cdd:PRK10929 33 EQAKAAKTPAQAEIVEalqsalnwLEErkGSLERAKQYQQVIDNFPKLSAELR--QQLNNERDEpRSVPPNMSTDALEQE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 92 I-----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIENRAMKDEEkmeiqemqlkeakhiAEE 157
Cdd:PRK10929 111 IlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 158 ADRKYEEVARKLVILEGDL---------ERAEERADLAECKASDLEEELKNVTNNLKSLEAQ-AEKYSEKEDKYEEEI-- 225
Cdd:PRK10929 176 TALQAESAALKALVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgd 255
|
250
....*....|
gi 551509811 226 --KVLTDKLK 233
Cdd:PRK10929 256 lpKSIVAQFK 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-179 |
8.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQL---------EDELLDLQKKLKQTEDELDKFSEG---LKDAQE 69
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASsddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 70 KLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienramKDEEKMEIQEMQLK 149
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR----------ALLEERFAAALGDA 762
|
170 180 190
....*....|....*....|....*....|
gi 551509811 150 EAKHIAEEADRKYEEVARKLVILEGDLERA 179
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-213 |
9.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 32 AEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEK--KAADAEGDVAALNRRIQLVEEELDRAQE---RL 106
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 107 ATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLviLEGDLERAEERADLA 186
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGDAVER 765
|
170 180
....*....|....*....|....*..
gi 551509811 187 EcKASDLEEELKNVTNNLKSLEAQAEK 213
Cdd:COG4913 766 E-LRENLEERIDALRARLNRAEEELER 791
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-273 |
9.94e-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: 46.98 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 9 QMLKLDKENAIDRAEQAETDKKAAE--DKCKQLEDELLDLQKKLKQ-TEDELDKFSEGLKDAQEKLELSEKKAADAEGDV 85
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISEleKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 86 AALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEV 165
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 166 ARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERT 245
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260
....*....|....*....|....*...
gi 551509811 246 VAKLEKSIDDLEDELYAQKLKYKAISEE 273
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
21-260 |
1.76e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 21 RAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAalnrRIQLVEEELD 100
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 101 RAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAE 180
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 181 ERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDEL 260
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-242 |
2.19e-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: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 19 IDRAEQAETDKKAAEDKCKQLEdELLDLQKKLKQTEDELDKFSEGLK-----DAQEKLELSEKKAADAEGDVAALNRRIQ 93
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 94 LVEEELDRAQERLATA--------LQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAkhiAEEADRKYEEV 165
Cdd:COG4913 313 RLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEA 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 551509811 166 ARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKvltDKLKEAETRAEFA 242
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---EALGLDEAELPFV 463
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-258 |
2.22e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 14 DKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKL---KQTEDELDKFSEGLKDAQE-KLELSEKKAADAEGDVAALN 89
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEEA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKL 169
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 170 VILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKL 249
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
....*....
gi 551509811 250 EKSIDDLED 258
Cdd:PTZ00121 1643 AEEKKKAEE 1651
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
40-248 |
2.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 40 EDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKA 119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 120 ADESERGMKVIENRAMKDEEKMEIQEMQLkeAKHIAEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKN 199
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLSA--LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 551509811 200 VTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAK 248
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1-261 |
6.21e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 1 MEAIKKKMQMLKLDKE-NAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEK-KA 78
Cdd:PRK05771 52 LTKLSEALDKLRSYLPkLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwGN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 79 ADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIenramkdeekmeiqeMQLKEAKHIAEEA 158
Cdd:PRK05771 132 FDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVV---------------VVLKELSDEVEEE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 159 DRKYEevARKLVILEGdlERAEERAdlaeckaSDLEEELKNVTNNLKSLEAQAEKYSEkedKYEEEIKVLTDKL----KE 234
Cdd:PRK05771 197 LKKLG--FERLELEEE--GTPSELI-------REIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielER 262
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 551509811 235 AETRAEFA--ERTVA-----------KLEKSIDDLEDELY 261
Cdd:PRK05771 263 AEALSKFLktDKTFAiegwvpedrvkKLKELIDKATGGSA 302
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-269 |
6.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 6 KKMQMLKLDKENA--IDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKfSEGLKDAQEKLELSEKKAADAEG 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 84 DVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 164 EVaRKLVILEGDLERAEERADLAECKASDLE--EELKNVTNNLKSLEAQAEKYSEKedKYEEEIKVLTDKLKEAETRAEF 241
Cdd:PTZ00121 1389 EK-KKADEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKAEEAKKK 1465
|
250 260
....*....|....*....|....*...
gi 551509811 242 AERTvAKLEKSIDDLEDELYAQKLKYKA 269
Cdd:PTZ00121 1466 AEEA-KKADEAKKKAEEAKKADEAKKKA 1492
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
40-277 |
8.28e-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: 44.17 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 40 EDELLDLQKKLKQTEdELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLA------------ 107
Cdd:COG3096 333 SDHLNLVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 108 -----TALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKH---IAEEADRKYEEVARKLVILEGDLERA 179
Cdd:COG3096 412 aiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 180 E--ERADLAECKASDLEEELKNVtNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLE 257
Cdd:COG3096 492 QawQTARELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
250 260
....*....|....*....|
gi 551509811 258 DELYAQKLKYKAISEELDHA 277
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQL 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-273 |
8.70e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSE-KKAAD 80
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 81 AEGDVAALNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAd 159
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 160 RKYEEVarklvilegdlERAEERADLAECKASdleeELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:PTZ00121 1278 RKADEL-----------KKAEEKKKADEAKKA----EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
250 260 270
....*....|....*....|....*....|....
gi 551509811 240 EFAERTVAKLEKSIDDLEDELYAQKLKYKAISEE 273
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-251 |
1.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKE--NAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAA 79
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 80 DAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD 159
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 160 RKYEEVARklvILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:PTZ00121 1653 KKAEEENK---IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
250
....*....|..
gi 551509811 240 EFAERTVAKLEK 251
Cdd:PTZ00121 1730 IKAEEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-277 |
1.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQleDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADA 81
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLK-EAKHIAEEADR 160
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 161 KYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEE-----EIKVLTDKLKEA 235
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaaEAKKKADEAKKA 1518
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 551509811 236 ETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-284 |
1.54e-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: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 97 EELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKmeiQEMQLKEAKHIAEEADRKYEEVARKLVILEGDL 176
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLR---AALRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 177 ERAEERADLAECKASDLEEELKNVTNN--------LKSLEAQAEKYSEKEDKYEEEIKVLtdKLKEAETRAEFAE----- 243
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGGDrleqlereIERLERELEERERRRARLEALLAAL--GLPLPASAEEFAAlraea 389
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 551509811 244 -RTVAKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSL 284
Cdd:COG4913 390 aALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-246 |
1.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 14 DKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551509811 174 GDLERAEERADLAECKASdlEEELKNVTNNLKSLEAQAEKY-SEKEDKYEEEIKvltdklKEAETRAEFAERTV 246
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEIrKEKEAVIEEELD------EEDEKRRMEVDKKI 1800
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-220 |
1.88e-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: 42.90 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 16 ENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQT----------------EDELDKFSEGLKDAQEKLELSEKKAA 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTdqnaletngqaqrdaiLEESRAVTKELTTLAQGLDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 80 DAE--GDvaalNRRIQLVEEELDRAQERLATALQKLEEA-EKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAK---- 152
Cdd:NF012221 1638 YAGesGD----QWRNPFAGGLLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEqdid 1713
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551509811 153 HIAEEADRKYEEVARKlvilEGDLERAEERADLAECKA-SDLEEELKNVTNnlKSLEAQAEKYSEKEDK 220
Cdd:NF012221 1714 DAKADAEKRKDDALAK----QNEAQQAESDANAAANDAqSRGEQDASAAEN--KANQAQADAKGAKQDE 1776
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-260 |
2.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 16 ENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSE--------KKAADAEGdVAA 87
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVET-IEE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 88 LNRRIQLVEEELDRAQERLATALQKLEEAEkAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVAR 167
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 168 KLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDkYEEEIKVLTDKLKEAETRAEFAERTVA 247
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLA 630
|
250
....*....|...
gi 551509811 248 KLEKSIDDLEDEL 260
Cdd:PRK02224 631 EKRERKRELEAEF 643
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-269 |
2.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSE------ 75
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkaee 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 76 -KKAADAEGDVAALNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKH 153
Cdd:PTZ00121 1193 lRKAEDARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 154 IAEEADRKYEEVARKLVILEGDLERAEERADLAEC--------KASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEI 225
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 551509811 226 KVLTDKLKEAETRAEFAERTVAKLEKSIDDL----EDELYAQKLKYKA 269
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
23-259 |
3.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 23 EQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRA 102
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 103 QERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQL--KEAKHIAEEADRKYEEVARKLVILEGDLERAE 180
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551509811 181 ERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDE 259
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
12-129 |
4.00e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 12 KLDKENAIDRAEQAETDKKAA--EDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKlelsEKKAADAEGDVAALN 89
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRrlEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE----ERREIRKDREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 551509811 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-172 |
4.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 1 MEAIKKKMQMLKldKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKaad 80
Cdd:PRK12704 44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 81 aegdvaaLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMkVIENraMKDEEKMEIQEMQLKEAKHIAEEADR 160
Cdd:PRK12704 119 -------LEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI-LLEK--VEEEARHEAAVLIKEIEEEAKEEADK 188
|
170
....*....|..
gi 551509811 161 KyeevARKLVIL 172
Cdd:PRK12704 189 K----AKEILAQ 196
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-259 |
5.38e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 2 EAIKKKMQMLKLDKENAIDRAEQAEtDKKAAEDKCKQLEDELLDLQK--KLKQTEDELDKFSEGLKDAQEKLELSEKKAA 79
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 80 DAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAadESERGMKVIENRAMKDEEKMEIQEM-QLKEAKHIAEEA 158
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 159 DRKYEEVARKLVILEGDLERAEERADlaecKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAETR 238
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
250 260
....*....|....*....|.
gi 551509811 239 AEFAERTVAKLEKSIDDLEDE 259
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDE 1790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-284 |
6.70e-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: 40.52 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 74 SEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKh 153
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 154 iaEEADRKYEEVARKLVILEGDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLK 233
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 551509811 234 EAETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSL 284
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
22-239 |
7.90e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 22 AEQAETDKKAAEdkckqledELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEE---E 98
Cdd:PRK04863 365 EEQNEVVEEADE--------QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLpdlT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 99 LDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEI-----QEMQLKEAKHIAEEADRKYEE--------- 164
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLvrkiaGEVSRSEAWDVARELLRRLREqrhlaeqlq 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 165 -VARKLVILEGDLE----------RAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLK 233
Cdd:PRK04863 517 qLRMRLSELEQRLRqqqraerllaEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
....*.
gi 551509811 234 EAETRA 239
Cdd:PRK04863 597 RLAARA 602
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
5-283 |
1.28e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 5 KKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLEDELLDLQKKLKQTEDElDKFSEGLKDAQEKL--ELSEKKAADAE 82
Cdd:PLN02939 141 EKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE-KIHVEILEEQLEKLrnELLIRGATEGL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 83 GdVAALNRRIQLVEEE---LDRAQERLATALQKLEEAEkaadesERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD 159
Cdd:PLN02939 220 C-VHSLSKELDVLKEEnmlLKDDIQFLKAELIEVAETE------ERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 160 RKYEEVARKLVILEGDLERAEERADLAEC---KASDLEEELKNVTNNLKslEAQAEKYSekedkyEEEIKVLTDKLKEAE 236
Cdd:PLN02939 293 LQYDCWWEKVENLQDLLDRATNQVEKAALvldQNQDLRDKVDKLEASLK--EANVSKFS------SYKVELLQQKLKLLE 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 551509811 237 TRAEFAERT----VAKLEKSIDDLEDELyaQKLKYKAISEELDHALNDMTS 283
Cdd:PLN02939 365 ERLQASDHEihsyIQLYQESIKEFQDTL--SKLKEESKKRSLEHPADDMPS 413
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-237 |
1.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 39 LEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEK 118
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 119 AADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLERAEERADlaeckasDLEEELK 198
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG-------DAPVDLG 408
|
170 180 190
....*....|....*....|....*....|....*....
gi 551509811 199 NVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAET 237
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
78-277 |
1.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 78 AADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEE 157
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 158 ADRKYEEVARKLVILEGDLErAEERADLAEcKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKLKEAET 237
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLG-SESFSDFLD-RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 551509811 238 RAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
30-256 |
2.10e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.29 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 30 KAAEDKCKQLEDELLDLQKKLKQTEDELDKFSEGLK---------DAQEKLELSEKKAADAEGDVAALNRRIQLVEEELD 100
Cdd:COG0497 161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEeleaaalqpGEEEELEEERRRLSNAEKLREALQEALEALSGGEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 101 RAQERLATALQKLEEAEKAadesergmkvienramkDEEKMEIQEMqLKEAKHIAEEADRKYEEVARKLVILEGDLERAE 180
Cdd:COG0497 241 GALDLLGQALRALERLAEY-----------------DPSLAELAER-LESALIELEEAASELRRYLDSLEFDPERLEEVE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 181 ER---------------ADLAEcKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLTDKlkeaetRAEFAERT 245
Cdd:COG0497 303 ERlallrrlarkygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA------RKKAAKKL 375
|
250
....*....|.
gi 551509811 246 VAKLEKSIDDL 256
Cdd:COG0497 376 EKAVTAELADL 386
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
14-234 |
2.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 14 DKENAIDRAEQAETDKKAAEDkckQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELSEKkaadaegdvaalnrriq 93
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIE---ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK----------------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 94 lvEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEiqemQLKEAKHIAEEADRKYEEVARKLVILE 173
Cdd:PHA02562 277 --VIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAID----ELEEIMDEFNEQSKKLLELKNKISTNK 350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551509811 174 GDLERAEERADLAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEI---KVLTDKLKE 234
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKyhrGIVTDLLKD 414
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
54-197 |
2.25e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 54 EDELDKFSEGLKDAQEKLELSEKKAADAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienr 133
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ-------- 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 551509811 134 amkdeekmeiqemQLKEAKHIAEEADRKYE----EVA---RKLVILEGDLERAEERADLAECKASDLEEEL 197
Cdd:PRK09039 124 -------------ELDSEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-133 |
2.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 1 MEAIKKKMQMLKLDKENAIDRAEQAETDKKAAEDKCKQLE--------DELLDLQKKLKQTEDELDKFSEGLKDAQEKLE 72
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 551509811 73 LSEKKAADAEGDVAALNRRIQL----VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAAlleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
15-260 |
4.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 15 KENAIDRAEQA-ETDKKAAEDKCkQLEDELLDLQKKLKQTEDELDKFSEGLKDAQEKLELsekkaadAEGDVAALNRRIQ 93
Cdd:PRK04863 315 ELAELNEAESDlEQDYQAASDHL-NLVQTALRQQEKIERYQADLEELEERLEEQNEVVEE-------ADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 94 LVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENR--AMKDEEKMEIQEM-QLKEAKH 153
Cdd:PRK04863 387 AAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQLCGLPDLTADNAEDWleEFQAKEQEATEELlSLEQKLS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 154 IAEEADRKYEEVARKLVILEGDLERAEeradlAECKASDLE---EELKNVTNNLKSLEAQ---AEKYSEKEDKYEEEIKV 227
Cdd:PRK04863 467 VAQAAHSQFEQAYQLVRKIAGEVSRSE-----AWDVARELLrrlREQRHLAEQLQQLRMRlseLEQRLRQQQRAERLLAE 541
|
250 260 270
....*....|....*....|....*....|...
gi 551509811 228 LTDKLKEAETRAEFAERTVAKLEKSIDDLEDEL 260
Cdd:PRK04863 542 FCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
133-279 |
4.00e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.37 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 133 RAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGDLEraeeradlaecKASDLEEELKNVTnnLKSLEAQAE 212
Cdd:PRK05771 23 EALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLP-----------KLNPLREEKKKVS--VKSLEELIK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 551509811 213 KYSEKEDKYEEEIKVLTDKLKEAETRaefaertVAKLEKSIDDLEdelyaqklKYKAISEELDHALN 279
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEISELENE-------IKELEQEIERLE--------PWGNFDLDLSLLLG 141
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
90-237 |
7.72e-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: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDE---------EKMEIQEMQLKEAKHIAEEADR 160
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkEDKQVAENQKREIEKAQIEIKK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 161 KYEEVARKLVILEGDLER-AEERADLAECKASDLEEELKNVTNNLKSL--EAQAEKYSEKEDKYEEEIKVLTDKLKEAET 237
Cdd:pfam05262 293 NDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSLNEDAIDSSNPVYGLKVVDPIT 372
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
11-152 |
8.90e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 36.95 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551509811 11 LKLDKENAIDRAEQAETDKKAAEDKCKQLEDELldlqkklkQTEDELDKFSEGLKDAQEKLELSEKKaadaegdvaaLNR 90
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAEL--------GAEAEIAAAEAQLAAAQAQLDLAQRE----------LER 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 551509811 91 RIQLVE------EELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEmQLKEAK 152
Cdd:COG1566 136 YQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAE 202
|
|
| |
