|
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 |
2.03e-66 |
|
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: 206.80 E-value: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 48 KLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669250879 208 EAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
7-152 |
5.06e-18 |
|
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: 78.50 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 7 KMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLlaaeEAAAKAEADVA 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKA----EESEKLKTNNE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669250879 87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-264 |
2.50e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAK 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....
gi 669250879 241 FAERSVTKLEKSIDDLEDELYAQK 264
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-279 |
8.68e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 165 VARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*
gi 669250879 245 SVTKLEKSIDDLEDELYAQKLKYKAISEELDHALN 279
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-284 |
7.42e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 37 KQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 117 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 196
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 197 LKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDH 276
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*...
gi 669250879 277 ALNDMTSI 284
Cdd:TIGR02168 927 LELRLEGL 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-283 |
3.38e-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: 57.37 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 11 LKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNR 90
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 91 RIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLv 170
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 171 iiesdleraeeraelsegkcAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAefAERSVTKLE 250
Cdd:TIGR02168 389 --------------------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELE 446
|
250 260 270
....*....|....*....|....*....|...
gi 669250879 251 KSIDDLEDELYAQKLKYKAISEELDHALNDMTS 283
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDA 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-235 |
4.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKA 81
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669250879 162 YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEA 235
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-270 |
6.87e-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: 56.60 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKA 81
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 82 EADVASLNRRIQLVEEELDRAQERL-------ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHI 154
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 155 AEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKE 234
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
250 260 270
....*....|....*....|....*....|....*..
gi 669250879 235 -AETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAI 270
Cdd:TIGR02168 948 eYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-266 |
4.72e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 24 QAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRAQ 103
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 104 ERLATALQKLEEaekaadesergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERA 183
Cdd:TIGR02168 288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 184 ELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQ 263
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
...
gi 669250879 264 KLK 266
Cdd:TIGR02168 434 ELK 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-239 |
1.66e-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: 51.69 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 22 AEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDR 101
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 102 AQERLATALQKLEEAEKAA------------------DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYE 163
Cdd:COG4942 95 LRAELEAQKEELAELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669250879 164 EVARKLViiesdlERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRA 239
Cdd:COG4942 175 ELEALLA------ELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-260 |
4.65e-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: 50.83 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 23 EQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRA 102
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 103 QERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER 182
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 183 AELSEGK---------------------CAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEF 241
Cdd:TIGR02168 840 LEDLEEQieelsedieslaaeieeleelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250
....*....|....*....
gi 669250879 242 AERSVTKLEKSIDDLEDEL 260
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRI 938
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-260 |
6.07e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDrvLEELHKAEDSLLAAEEAAAKAEAD 84
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 165 VARKLviiESDLERAEERAELSEGKCAELEEELKTV-TNNLKSLEAQAEKYSQKEDRY----EEEIKVLSDKLKEAETRA 239
Cdd:COG4913 767 LRENL---EERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLALLdrleEDGLPEYEERFKELLNEN 843
|
250 260
....*....|....*....|...
gi 669250879 240 EFAERS--VTKLEKSIDDLEDEL 260
Cdd:COG4913 844 SIEFVAdlLSKLRRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-275 |
7.90e-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: 50.07 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 20 DRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEEL 99
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 100 DRAQERLATALQKLEEAEKAADESERgmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERA 179
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEA--RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 180 EERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDE 259
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250
....*....|....*.
gi 669250879 260 LYAQKLKYKAISEELD 275
Cdd:TIGR02169 898 LRELERKIEELEAQIE 913
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-246 |
8.88e-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: 50.07 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 39 LEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 118
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 119 AADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELK 198
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 669250879 199 TVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSV 246
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-284 |
2.01e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALD-RAEQAEADKKAAEDRSKQLEEDIAAKEKLLRvsedERDRVLEELHKAEDSLLAAEEAAAK 80
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERyQALLKEKREYEGYELLKEKEALERQKEAIER----QLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 81 AEADVASLNRRIQ-LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLkeakhiaEDAD 159
Cdd:TIGR02169 270 IEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI-------EELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 160 RKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRA 239
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 669250879 240 EFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-284 |
3.59e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVII 172
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 173 ESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKS 252
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190
....*....|....*....|....*....|..
gi 669250879 253 IDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-281 |
7.15e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 170 VIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKL 249
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190
....*....|....*....|....*....|..
gi 669250879 250 EKSIDDLEDELYAQKLKYKAISEELDHALNDM 281
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-260 |
9.09e-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: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 7 KMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 87 SLNRRIQLVEEELdrAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA 166
Cdd:TIGR02169 762 ELEARIEELEEDL--HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 167 RKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSV 246
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250
....*....|....
gi 669250879 247 TKLEKSIDDLEDEL 260
Cdd:TIGR02169 920 SELKAKLEALEEEL 933
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-226 |
9.62e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 14 DKENALDRAEQA-EADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVlEELHKAEDSLLAAEEAAAKAEADVASLNRRI 92
Cdd:PTZ00121 1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVII 172
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 669250879 173 ESDLERAEERAELSEGKCAElEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIK 226
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-277 |
1.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAK 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELeeELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 669250879 241 FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-259 |
1.49e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 15 KENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQL 94
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 95 VEEELDRAQERLATALQKLEEAEKAADESERG-------MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVAR 167
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 168 KLVIIESDLERAE-ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLS-------DKLKEAETRA 239
Cdd:TIGR02168 923 KLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERY 1002
|
250 260
....*....|....*....|....*..
gi 669250879 240 EF-------AERSVTKLEKSIDDLEDE 259
Cdd:TIGR02168 1003 DFltaqkedLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
18-259 |
3.75e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 18 ALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLnrRIQLVEE 97
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL--EEALNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLE 177
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 178 RAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 257
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
..
gi 669250879 258 DE 259
Cdd:TIGR02169 945 EI 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-260 |
5.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 23 EQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLE------ELHKAEDSLLaaEEAAAKAEADVASLNRRIQLVE 96
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkEKREYEGYEL--LKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 97 EELDRAQERLATALQKLEEAEKAADE-SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESD 175
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 176 LERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDD 255
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
....*
gi 669250879 256 LEDEL 260
Cdd:TIGR02169 411 LQEEL 415
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
28-261 |
8.79e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 28 DKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRAQERLA 107
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 108 TALQKLEEAEKAAD--------ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA---RKLVIIESDL 176
Cdd:PRK05771 118 ELEQEIERLEPWGNfdldlsllLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEVEEEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 177 ERAE-ERAELSEGKC-----AELEEELKTVTNNLKSLEAQAEKYSQKedrYEEEIKVLSDKL----KEAETRAEFA---- 242
Cdd:PRK05771 198 KKLGfERLELEEEGTpseliREIKEELEEIEKERESLLEELKELAKK---YLEELLALYEYLeielERAEALSKFLktdk 274
|
250 260
....*....|....*....|....*...
gi 669250879 243 ---------ERSVTKLEKSIDDLEDELY 261
Cdd:PRK05771 275 tfaiegwvpEDRVKKLKELIDKATGGSA 302
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-258 |
8.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 5 KKKMQMLKLDKENALDRAEQ---AEADKKAAEDRSKQLEEDIAAKEKLLRVSE----DERDRVLEELHKAEDSLLAAEEA 77
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 78 AAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIES-RAQKDEEKMEIQEIQLKEAKHIAE 156
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 157 DADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAE 236
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
250 260
....*....|....*....|..
gi 669250879 237 TRAEFAERSVTKLEKSIDDLED 258
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEE 1651
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-219 |
9.85e-05 |
|
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: 43.67 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 16 ENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVS---------EDERDRVLEELHKAEDSLLAAEEAAAKAEADVA 86
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTdqnaletngQAQRDAILEESRAVTKELTTLAQGLDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 87 SLNR-----RIQLVEEELDRAQERLATALQ----KLEEAEKAADESERGMK--VIESRA--QKDEEKMEIQEIQLKEAKh 153
Cdd:NF012221 1638 YAGEsgdqwRNPFAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVKdaVAKSEAgvAQGEQNQANAEQDIDDAK- 1716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669250879 154 iaEDADRKYEEVARKlviiESDLERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKED 219
Cdd:NF012221 1717 --ADAEKRKDDALAK----QNEAQQAESDANAAAND-AQSRGEQDASAAENKANQAQADAKGAKQD 1775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-258 |
1.76e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQ 147
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 148 LKEAKHIAEDADRKYEEvARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKV 227
Cdd:PRK02224 484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
250 260 270
....*....|....*....|....*....|.
gi 669250879 228 LSDKLKEAETRAEFAERSVTKLEKSIDDLED 258
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-269 |
1.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKA 81
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 162 YEEVaRKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEF 241
Cdd:PTZ00121 1387 AEEK-KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
250 260
....*....|....*....|....*...
gi 669250879 242 AERSvTKLEKSIDDLEDELYAQKLKYKA 269
Cdd:PTZ00121 1466 AEEA-KKADEAKKKAEEAKKADEAKKKA 1492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-176 |
2.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 6 KKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDI-AAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEAD 84
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiQEIQLKEAKH--IAEDADRKY 162
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnIPARLLALR 446
|
170
....*....|....
gi 669250879 163 EEVARKLVIIESDL 176
Cdd:COG4913 447 DALAEALGLDEAEL 460
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-275 |
3.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 14 DKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRIQ 93
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 173
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 174 SDLERAEERAE-----LSEGKCAELEEELKTVTN---------NLKSLEAQAEKYSQKEDRYEEEIKVLSDkLKEAETRA 239
Cdd:PRK02224 433 ATLRTARERVEeaealLEAGKCPECGQPVEGSPHvetieedreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRI 511
|
250 260 270
....*....|....*....|....*....|....*.
gi 669250879 240 EFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
84-260 |
5.48e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI-ESRAQKDEEKMEIQEI--QLKEAKHIAEDADR 160
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIeDLRETIAETEREREELaeEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 240
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
170 180
....*....|....*....|
gi 669250879 241 FAERSVTKLEKSIDDLEDEL 260
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEI 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-251 |
7.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKE--KLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAE 82
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 83 ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRaQKDEEKMEIQEIQLKEAKHIAEDADRKY 162
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 163 EEVARKLVIIESDLERAEERAELSEGKCAelEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFA 242
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
....*....
gi 669250879 243 ERSVTKLEK 251
Cdd:PTZ00121 1733 EEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-244 |
8.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 5 KKKMQMLKLDKENAlDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEAD 84
Cdd:PTZ00121 1469 AKKADEAKKKAEEA-KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 85 VASLNRRIQLVE-------EELDRAQERLATALQKLEEAEKAAD----------ESERGMKVIESRAQKDEEKMEIQEIQ 147
Cdd:PTZ00121 1548 ADELKKAEELKKaeekkkaEEAKKAEEDKNMALRKAEEAKKAEEarieevmklyEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 148 LKEAKHIAEDADRKYEEVARKlviiESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKV 227
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
250
....*....|....*..
gi 669250879 228 LSDKLKEAETRAEFAER 244
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEE 1720
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
18-233 |
8.45e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 18 ALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLlrvSEDERDRVLEELHKAEDsllaaeeaaAKAEADVASLNRRI----- 92
Cdd:PRK10929 49 ALQSALNWLEERKGSLERAKQYQQVIDNFPKL---SAELRQQLNNERDEPRS---------VPPNMSTDALEQEIlqvss 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 93 QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIESRAQKDEEkmeiqeiqlkeakhiAEDADRKYE 163
Cdd:PRK10929 117 QLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 164 EVARKLVIIESDL---------ERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDRYEEEI----KVLS 229
Cdd:PRK10929 182 SAALKALVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdlpKSIV 261
|
....
gi 669250879 230 DKLK 233
Cdd:PRK10929 262 AQFK 265
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-269 |
1.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDI--AAKEKLLRVSEDERD----------RVLEELHKAED 69
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAedARKAEEARKAEDAKKaeaarkaeevRKAEELRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 70 SllaaeeaaakAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLK 149
Cdd:PTZ00121 1199 A----------RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 150 EAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG--------KCAELEEELKTVTNNLKSLEAQAEKYSQKEDRY 221
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 669250879 222 EEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL----EDELYAQKLKYKA 269
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-277 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 85 VASLNRRIQLVEEELDRAQERlatalqkLEEAEKAADESERGMKVIESRAQKDEE----KMEIQEIQLKEAKHIAEDADR 160
Cdd:COG1196 167 ISKYKERKEEAERKLEATEEN-------LERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 240
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190
....*....|....*....|....*....|....*..
gi 669250879 241 FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-251 |
1.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQ---LEEDIAAKEKLLRVSEDERDRvlEELHKAEDSLLAAEEAA 78
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEearKAEDAKKAEAVKKAEEAKKDA--EEAKKAEEERNNEEIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 79 AKAEADVASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADesergMKVIESRAQKDEEKMEIQEIQLK--EAKHIA 155
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEAKKAEE-----KKKADEAKKKAEEAKKADEAKKKaeEAKKKA 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 156 EDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKED--RYEEEIKVLSDKLK 233
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELK 1411
|
250
....*....|....*...
gi 669250879 234 EAETRAEFAERSVTKLEK 251
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEE 1429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-238 |
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 669250879 13 LDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAKAEADVASLNRRI 92
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 93 QLVEEELDRAQERLATALQKLEEAEKAADESERgmkviesraqkdeEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVII 172
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEA-------------QIRGNGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 173 ESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKY----SQKEDRYEEEIKVLSDKLKEAETR 238
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-258 |
2.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEE-DIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAK 80
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 81 AEADvASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIESR-AQKDEEKMEIQEIQLKEAKHIAEDA 158
Cdd:PTZ00121 1629 EEEK-KKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKkAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 159 DRKYEEVARKlviiESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQ---KEDRYEEEIKVLSDKLKEA 235
Cdd:PTZ00121 1708 KKKEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlkkEEEKKAEEIRKEKEAVIEE 1783
|
250 260
....*....|....*....|...
gi 669250879 236 ETRAEfAERSVTKLEKSIDDLED 258
Cdd:PTZ00121 1784 ELDEE-DEKRRMEVDKKIKDIFD 1805
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-275 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 97 EELDRAQERLATALQKLE----------EAEKAADESERGMKVIE-SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEV 165
Cdd:COG4913 235 DDLERAHEALEDAREQIEllepirelaeRYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 166 ARKLVIIESDLERAEERAELSEG-KCAELEEELKTVTNNLKSLEAQAEKYSQKEDR----YEEEIKVLSDKLKEAETRAE 240
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*
gi 669250879 241 FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 275
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-234 |
2.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 38 QLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLlaaeeAAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 117
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAAL-----EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 118 KAADESERGMKVIESRAQKDEEKMEIQEIQLKEAkhiaeDADRKYEEVARKL-----VIIESDLERAEERAELSEgkcaE 192
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYtpnhpDVIALRAQIAALRAQLQQ----E 310
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 669250879 193 LEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKE 234
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
107-266 |
3.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 107 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELS 186
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 187 EGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLK 266
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-242 |
3.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 30 KAAEDRSKQLEEDIAAKEKLLRVSEDERDRvlEELHKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 110 -LQKLEEAEKAADESERGMKVIESRAQKDEEKmeIQEIQLkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 188
Cdd:COG4913 336 gGDRLEQLEREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 669250879 189 KCAELEEELKTVTNNLKSLEAQAEKYSQkedRYEEEIKVLSDKLKEAETRAEFA 242
Cdd:COG4913 413 ALRDLRRELRELEAEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
22-241 |
5.57e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.07 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 22 AEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDErdrvLEELhKAEDSLLAAEEAAAKAEADVASLNRRIQLVEEELDR 101
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAA----LEEF-RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 102 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEI---------QLKEAKH-IAEDADRKYEEVARKLVI 171
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpDVIALRAqIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 172 IESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEeikvLSDKLKEAETRAEF 241
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-269 |
5.72e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.82 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 179 AEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 258
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|.
gi 669250879 259 ELYAQKLKYKA 269
Cdd:COG4942 98 ELEAQKEELAE 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-257 |
6.98e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 37.99 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 18 ALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHkAEDSLLAAEEAAAKAEADVASLNRRIQLVEE 97
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL-ARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADrkyEEVARKLVIIESDLE 177
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA---ERLAEEELELEEALL 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 178 RAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 257
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
18-240 |
7.96e-03 |
|
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: 37.62 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 18 ALDRAEQA-EADKKAAEDRSKQLEEDIAAKEKLLRVSEDerdrvLEELhkaEDSLLAAEEAAAKAEADVASLNRRIQLVE 96
Cdd:COG3096 317 ELSARESDlEQDYQAASDHLNLVQTALRQQEKIERYQED-----LEEL---TERLEEQEEVVEEAAEQLAEAEARLEAAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 97 EELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKH---IAE 156
Cdd:COG3096 389 EEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVAD 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 157 DADRKYEEVARKLVIIESDLERAE-------------------ERAELSEGKCAELEEELktvtNNLKSLEAQAEKYSQK 217
Cdd:COG3096 469 AARRQFEKAYELVCKIAGEVERSQawqtarellrryrsqqalaQRLQQLRAQLAELEQRL----RQQQNAERLLEEFCQR 544
|
250 260
....*....|....*....|...
gi 669250879 218 EDRYEEEIKVLSDKLKEAETRAE 240
Cdd:COG3096 545 IGQQLDAAEELEELLAELEAQLE 567
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
90-260 |
8.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALR------EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 170 VIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEkysqkEDRYEeeikvlsdklkeaetraefAERSVTKL 249
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE-----EALAE-------------------AEAALRDL 417
|
170
....*....|.
gi 669250879 250 EKSIDDLEDEL 260
Cdd:COG4913 418 RRELRELEAEI 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-262 |
8.36e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.81 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAE-DSLLAAEEAAAK 80
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEeDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIA----- 155
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaee 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 156 ---EDADRKYEEVARKLVIIESDLERAEERAELSEGKCAEL---EEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLS 229
Cdd:PTZ00121 1667 akkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270
....*....|....*....|....*....|...
gi 669250879 230 DKLKEAETRAEFAERSVTKLEKSIDDLEDELYA 262
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-257 |
8.64e-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: 37.64 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAK 80
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER---LSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 240
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
250
....*....|....*..
gi 669250879 241 FAERSVTKLEKSIDDLE 257
Cdd:pfam02463 497 ERSQKESKARSGLKVLL 513
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
90-237 |
9.55e-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: 37.29 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDE---------EKMEIQEIQLKEAKHIAEDADR 160
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkEDKQVAENQKREIEKAQIEIKK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669250879 161 KYEEVARKLVIIESDLER-AEERAELSEGKCAELEEELKTVTNNLKSL--EAQAEKYSQKEDRYEEEIKVLSDKLKEAET 237
Cdd:pfam05262 293 NDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSLNEDAIDSSNPVYGLKVVDPIT 372
|
|
| |
