|
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 |
9.87e-73 |
|
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: 9.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 48 KKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1C1G_B 208 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 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 |
1.00e-26 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 101.61 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 7 KMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEadva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1C1G_B 87 SLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-275 |
4.73e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 5 KKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 85 VASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 165 VA-------RKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAET 237
Cdd:COG1196 384 LAeellealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*...
1C1G_B 238 RAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 275
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-264 |
9.99e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERgmkviesRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-------ALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 162 YEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEF 241
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|...
1C1G_B 242 AERSVTKLEKSIDDLEDELYAQK 264
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-284 |
1.45e-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: 70.86 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 37 KQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 117 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 196
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 197 IKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDH 276
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*...
1C1G_B 277 ALNDMTSI 284
Cdd:TIGR02168 927 LELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-278 |
7.29e-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: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 27 ADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERL 106
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 107 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELS 186
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 187 EGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLK 266
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|..
1C1G_B 267 YKAISEELDHAL 278
Cdd:COG1196 472 AALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-283 |
1.70e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 4 IKKKMQMLKLDKENALD----RADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKAT 79
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 80 DAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD 159
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 160 RKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRA 239
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280
....*....|....*....|....*....|....*....|....
1C1G_B 240 efAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTS 283
Cdd:TIGR02168 438 --LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-239 |
1.88e-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: 60.55 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 18 ALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 98 ELDRAQERLATALQKLEEAEKA-----------ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA 166
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1C1G_B 167 RKLViiesdlERAEERAELSEGKcAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRA 239
Cdd:COG4942 178 ALLA------ELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-275 |
2.18e-10 |
|
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: 61.24 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 34 DRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKL 113
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 114 EEAEKAADESErgmkviesrAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAEL 193
Cdd:TIGR02169 761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 194 EEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEE 273
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
..
1C1G_B 274 LD 275
Cdd:TIGR02169 912 IE 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-278 |
1.69e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 48 KKLKATEDELDKYSEALKD--AQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1196 216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 126 GMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLK 205
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1C1G_B 206 SLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHAL 278
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-251 |
3.72e-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: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 162 YEEVARKLviiesdlerAEERAELSEGkcAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEF 241
Cdd:COG1196 437 EEEEEEAL---------EEAAEEEAEL--EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
250
....*....|
1C1G_B 242 AERSVTKLEK 251
Cdd:COG1196 506 FLEGVKAALL 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-258 |
7.58e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQ 147
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 148 LKEAKHIAEDADRKYEEvARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKV 227
Cdd:PRK02224 484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
250 260 270
....*....|....*....|....*....|.
1C1G_B 228 LSDKLKEAETRAEFAERSVTKLEKSIDDLED 258
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-260 |
8.01e-09 |
|
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: 56.23 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 7 KMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 87 SLNRRIQLFEEELdrAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA 166
Cdd:TIGR02169 762 ELEARIEELEEDL--HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 167 RKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 246
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250
....*....|....
1C1G_B 247 TKLEKSIDDLEDEL 260
Cdd:TIGR02169 920 SELKAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-260 |
1.79e-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: 55.45 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 1 MDAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 81 AEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMeiqeiqlkeakhiaEDADR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL--------------ETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKslEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALE 464
|
250 260
....*....|....*....|
1C1G_B 241 FAERSVTKLEKSIDDLEDEL 260
Cdd:TIGR02168 465 ELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-256 |
4.85e-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: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 162 YEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQ-AEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250
....*....|....*.
1C1G_B 241 FAERSVTKLEKSIDDL 256
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-284 |
7.76e-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: 53.52 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 47 QKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEAdvaSLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERG 126
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAER---YKELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 127 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKS 206
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C1G_B 207 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
23-261 |
1.21e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 52.62 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 23 DEAEADKKAAEDRSK--QLEDELVSLQKKLKATEDELDKYS-----EALKDAQEKLELAEKKATDAEADVASLNRRIQLF 95
Cdd:PRK05771 40 LSNERLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 96 EEELDRAQerlatALQKLEEAEKAADESERgMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA---RKLVII 172
Cdd:PRK05771 120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 173 ESDLERAE-ERAELSEGKC-----AELEEEIKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKL----KEAETRAEFA 242
Cdd:PRK05771 194 EEELKKLGfERLELEEEGTpseliREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFL 270
|
250 260 270
....*....|....*....|....*....|..
1C1G_B 243 -------------ERSVTKLEKSIDDLEDELY 261
Cdd:PRK05771 271 ktdktfaiegwvpEDRVKKLKELIDKATGGSA 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-246 |
1.51e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 39 LEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEK 118
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 119 AADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIK 198
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1C1G_B 199 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 246
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-260 |
3.84e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 5 KKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDkySEALKDAQEKLELAEKKATDAEAD 84
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 85 VASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 165 VARKLviiESDLERAEERAELSEGKCAELEEEIKTV-TNNLKSLEAQAEKYSQKEDKY----EEEIKVLSDKLKEAETRA 239
Cdd:COG4913 767 LRENL---EERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLALLdrleEDGLPEYEERFKELLNEN 843
|
250 260
....*....|....*....|...
1C1G_B 240 EFAERS--VTKLEKSIDDLEDEL 260
Cdd:COG4913 844 SIEFVAdlLSKLRRAIREIKERI 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-271 |
5.57e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 43 LVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADE 122
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 123 SERGMK----VIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIK 198
Cdd:COG4942 95 LRAELEaqkeELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1C1G_B 199 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAIS 271
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-215 |
1.27e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 1 MDAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 81 AEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGmkviESRAQKDEEKMEIQEIQLKEAKHIAEdadr 160
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----ELQAELEELEEELEELQEELERLEEA---- 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1C1G_B 161 kyeevarklviiesdLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYS 215
Cdd:TIGR02168 463 ---------------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
45-234 |
1.56e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 45 SLQKKLKATEDELDKYSEALKDAQEKLELAEKKATD--AEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADE 122
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 123 SERGMKVIESRAQKDEEKMEIQEIQLKEAkhiaeDADRKYEEVARKL-----VIIESDLERAEERAELSEgkcaELEEEI 197
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYtpnhpDVIALRAQIAALRAQLQQ----EAQRIL 315
|
170 180 190
....*....|....*....|....*....|....*..
1C1G_B 198 KTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKE 234
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-281 |
2.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 90 RRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 170 VIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKL 249
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190
....*....|....*....|....*....|..
1C1G_B 250 EKSIDDLEDELYAQKLKYKAISEELDHALNDM 281
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-258 |
2.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 5 KKKMQMLKLDKENALDRADE---AEADKKAAEDRSKQLEDELVSLQKKLKATE----DELDKYSEALKDAQEKLELAEKK 77
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 78 ATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIES-RAQKDEEKMEIQEIQLKEAKHIAE 156
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 157 DADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAE 236
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
250 260
....*....|....*....|..
1C1G_B 237 TRAEFAERSVTKLEKSIDDLED 258
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEE 1651
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
25-240 |
2.46e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 25 AEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRA-- 102
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 103 ----QERLATALQKLEEAEKAADESERgMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLER 178
Cdd:COG3883 94 alyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
1C1G_B 179 AEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-260 |
3.13e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 66 DAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLAtALQKLEEaekaADESERGMKVIESRAQkdeekmeiqe 145
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREIA---------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 146 iQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEi 225
Cdd:COG4913 672 -ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190
....*....|....*....|....*....|....*
1C1G_B 226 kvLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 260
Cdd:COG4913 750 --LLEERFAAALGDAVERELRENLEERIDALRARL 782
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-220 |
3.50e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 48.29 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 16 ENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATE------------DELDKYSEA----LKDAQEKLELAEKKAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 80 DAEAdvASLNRRIQLFEEELDRAQERLATALQ----KLEEAEKAADESERGMK--VIESRA--QKDEEKMEIQEIQLKEA 151
Cdd:NF012221 1638 YAGE--SGDQWRNPFAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVKdaVAKSEAgvAQGEQNQANAEQDIDDA 1715
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1C1G_B 152 KhiaEDADRKYEEVARKlviiESDLERAEERAELSEGKcAELEEEIKTVTNNLKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1716 K---ADAEKRKDDALAK----QNEAQQAESDANAAAND-AQSRGEQDASAAENKANQAQADAKGAKQDE 1776
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
15-229 |
1.27e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 15 KENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKA---------TEDELDKYSEALKDAQEKLELAEKKATDAEADV 85
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 86 ASLNRRIQLFEEEL-----DRAQERLATALQKLE--EAEKAADESERGMKVIESRAQKDEEKMEIQEiqlkEAKHIAEDA 158
Cdd:COG3206 243 AALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELSARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1C1G_B 159 DRKYEEVARKLVIIESDLERAEERAEL---SEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLS 229
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-242 |
1.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 13 LDKENALDRADEAEAD-------KKAAEDRSKQLE--DELVSLQKKLKATEDELDKYSE-----ALKDAQEKLELAEKKA 78
Cdd:COG4913 218 LEEPDTFEAADALVEHfddleraHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 79 TDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAE-KAADESERGMKVIESRAQKDEEKMEIQEIQLK----EAKH 153
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAalglPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 154 IAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKLK 233
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA---RLLALRDALAEALG 454
|
....*....
1C1G_B 234 EAETRAEFA 242
Cdd:COG4913 455 LDEAELPFV 463
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-260 |
2.01e-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: 45.83 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 15 KENALDRADEAEADKKAAEDRSKQLEDELVSLQKKlKATEDELDKYSEALKDAQEKLELAEKKATDA-----EADVASLN 89
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKEKEALERqkeaiERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 90 RRIQLFEEELDRAQERLATALQKLEE-AEKAADESERGMKVIesraqkdEEKMEIQEIQLKEAKHIAEDADRKYEEVARK 168
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRV-------KEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 169 LVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTK 248
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250
....*....|..
1C1G_B 249 LEKSIDDLEDEL 260
Cdd:TIGR02169 404 LKRELDRLQEEL 415
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
52-260 |
3.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 52 ATEDELDKYSEALKDAQEKLELAEKKA-----TDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERG 126
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 127 MKVI-ESRAQKDEEKMEIQEI--QLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNN 203
Cdd:PRK02224 257 EAEIeDLRETIAETEREREELaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1C1G_B 204 LKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 260
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-176 |
3.74e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 12 KLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEA---------------LKDAQEKLELAEK 76
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlereIERLERELEERER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 77 KATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiQEIQLKEAKH--I 154
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnI 438
|
170 180
....*....|....*....|..
1C1G_B 155 AEDADRKYEEVARKLVIIESDL 176
Cdd:COG4913 439 PARLLALRDALAEALGLDEAEL 460
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-269 |
7.97e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 6 KKMQMLKLDKENA--LDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKySEALKDAQEKLELAEKKATDAEA 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 84 DVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 164 EVaRKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAE 243
Cdd:PTZ00121 1389 EK-KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
250 260
....*....|....*....|....*.
1C1G_B 244 RSvTKLEKSIDDLEDELYAQKLKYKA 269
Cdd:PTZ00121 1468 EA-KKADEAKKKAEEAKKADEAKKKA 1492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-226 |
9.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 14 DKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 94 LFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1C1G_B 174 SDLERAEERAELSEGKCAElEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIK 226
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-251 |
1.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 -EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEakhiaEDADR 160
Cdd:PTZ00121 1587 kKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE-----EENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 161 KYEEVARKLviiESDLERAEEraelsegkCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:PTZ00121 1662 KAAEEAKKA---EEDKKKAEE--------AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
250
....*....|.
1C1G_B 241 FAERSVTKLEK 251
Cdd:PTZ00121 1731 KAEEAKKEAEE 1741
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
40-271 |
2.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 40 EDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKA 119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 120 ADESERGMKVIEsraqkdeekmeiqeiQLKEAKHIAEDADRkyeeVARKLVIIESD---LERAEERAELSEGKCAELEEE 196
Cdd:COG3883 95 LYRSGGSVSYLD---------------VLLGSESFSDFLDR----LSALSKIADADadlLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1C1G_B 197 IKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAIS 271
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-258 |
2.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 14 DKENALDRADEAEADKKAAEDRSKQLEDELVSLqkklkatedeldkysealkdaQEKLELAEKKATDAEADVASLNRRIQ 93
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEEL---------------------RDRLEECRVAAQAHNEEAESLREDAD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 94 LFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 173
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 174 SDLERAEERAE-----LSEGKCAELEEEIK--TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEfAERSV 246
Cdd:PRK02224 433 ATLRTARERVEeaealLEAGKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRI 511
|
250
....*....|..
1C1G_B 247 TKLEKSIDDLED 258
Cdd:PRK02224 512 ERLEERREDLEE 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-258 |
2.92e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 5 KKKMQMLKLDKENALDRADEAeadKKAAEDRSKQleDELVSLQKKLKAteDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEA---KKAAEAKKKA--DEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 85 VASLNRRIQLFEEELDRAQERLATALQKLEEAEKAadesERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 165 VARKLVIIESDLERAEERAElsegKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
250
....*....|....
1C1G_B 245 SVTKLEKSIDDLED 258
Cdd:PTZ00121 1707 LKKKEAEEKKKAEE 1720
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
20-240 |
2.94e-04 |
|
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: 42.25 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 20 DRADEAEADKKAAEDRskqledeLVSLQKKLKATEdELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEEL 99
Cdd:COG3096 320 ARESDLEQDYQAASDH-------LNLVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 100 DRAQERLA-----------------TALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKH---IAEDAD 159
Cdd:COG3096 392 DSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAAR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 160 RKYEEVARKLVIIESDLERAE-------------------ERAELSEGKCAELEEEIktvtNNLKSLEAQAEKYSQKEDK 220
Cdd:COG3096 472 RQFEKAYELVCKIAGEVERSQawqtarellrryrsqqalaQRLQQLRAQLAELEQRL----RQQQNAERLLEEFCQRIGQ 547
|
250 260
....*....|....*....|
1C1G_B 221 YEEEIKVLSDKLKEAETRAE 240
Cdd:COG3096 548 QLDAAEELEELLAELEAQLE 567
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-277 |
3.45e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 76 KKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIA 155
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 156 EDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEA 235
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200
....*....|....*....|....*....|....*....|..
1C1G_B 236 ETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-231 |
3.61e-04 |
|
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: 41.86 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 16 ENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLkateDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLF 95
Cdd:COG3096 371 EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL----DVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAF 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 96 EEELDRAQERLATALQKLEEAEKAADESERGMKVIE------SRAQKDEEKMEIQEiQLKEAKHIAEDAdrkyEEVARKL 169
Cdd:COG3096 447 RAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiagevERSQAWQTARELLR-RYRSQQALAQRL----QQLRAQL 521
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1C1G_B 170 VIIESDLERAEERAELSEGKC-----------------AELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDK 231
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCqrigqqldaaeeleellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-213 |
3.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 15 KENALDRADEAEADKKAAEDRSKQLED---ELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA-------EAD 84
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeagldDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 85 VASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDA------ 158
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRreeiee 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1C1G_B 159 -DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEK 213
Cdd:PRK02224 389 lEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2-186 |
4.47e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDE---LVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKA 78
Cdd:pfam00529 40 DRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAEldrLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 79 TDAEADvasLNRRIQLFEEELdRAQERLATALQKLEEAEKAADESergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDA 158
Cdd:pfam00529 120 AQAQID---LARRRVLAPIGG-ISRESLVTAGALVAQAQANLLAT------VAQLDQIYVQITQSAAENQAEVRSELSGA 189
|
170 180
....*....|....*....|....*...
1C1G_B 159 DRKYEEVARKLVIIESDLERAEERAELS 186
Cdd:pfam00529 190 QLQIAEAEAELKLAKLDLERTEIRAPVD 217
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
18-233 |
5.68e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 18 ALDRADEAEADKKAAEDRSKQLE---DELVSLQKKLKAtedELDKYSEALKDAQEKLELA--EKKATDAEADVASLNRRI 92
Cdd:PRK10929 49 ALQSALNWLEERKGSLERAKQYQqviDNFPKLSAELRQ---QLNNERDEPRSVPPNMSTDalEQEILQVSSQLLEKSRQA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 93 QlfeEELDRAQE---RLATALQKLEEAEKAADESERGMKVIESRAQKDEEkmeiqeiqlkeakhiAEDADRKYEEVARKL 169
Cdd:PRK10929 126 Q---QEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C1G_B 170 VIIESDL---------ERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQ-AEKYSQKEDKYEEEI----KVLSDKLK 233
Cdd:PRK10929 188 LVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdlpKSIVAQFK 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-275 |
6.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 97 EELDRAQERLATALQKLE----------EAEKAADESERGMKVIE-SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEV 165
Cdd:COG4913 235 DDLERAHEALEDAREQIEllepirelaeRYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 166 ARKLVIIESDLERAEERAELSEG-KCAELEEEIKTVTNNLKSLEAQAEKYSQK----EDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*
1C1G_B 241 FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 275
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-251 |
6.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 1 MDAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 81 AEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQ--LKEAKHIAEDA 158
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 159 DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250
....*....|...
1C1G_B 239 AEFAERSVTKLEK 251
Cdd:COG4372 280 IAALELEALEEAA 292
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
25-274 |
7.22e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 25 AEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQE 104
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 105 RLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAE 184
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 185 LSEGKC-AELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQ 263
Cdd:COG4372 189 LKEANRnAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250
....*....|.
1C1G_B 264 KLKYKAISEEL 274
Cdd:COG4372 269 VEKDTEEEELE 279
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
33-129 |
8.52e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 33 EDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKatdaEADVASLNRRIQLFEEELDRAQERLATALQK 112
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISRLDREIERLERELEEERERIEELKRK 494
|
90
....*....|....*..
1C1G_B 113 LEEAEKAADESERGMKV 129
Cdd:COG2433 495 LERLKELWKLEHSGELV 511
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2-89 |
1.14e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSE-ALKDAQEKLELAEKKATD 80
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQAALANAEARLAK 336
|
....*....
1C1G_B 81 AEADVASLN 89
Cdd:TIGR04320 337 AKEALANLN 345
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-277 |
1.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQleDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLK-EAKHIAEDADR 160
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLE-----AQAEKYSQKEDKYEEEIKVLSDKLKEA 235
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeakkkAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
250 260 270 280
....*....|....*....|....*....|....*....|..
1C1G_B 236 ETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
54-256 |
1.22e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 54 EDELDKYSEALKDAQEklelAEKKATDAEADVASLNRRIQLFE---EELDRA------QERLATALQKLEEAEK------ 118
Cdd:COG0497 154 EELLEEYREAYRAWRA----LKKELEELRADEAERARELDLLRfqlEELEAAalqpgeEEELEEERRRLSNAEKlrealq 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 119 ----AADESERG--------MKVIESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER---- 182
Cdd:COG0497 230 ealeALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlall 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 183 -----------AELSEgKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKlkeaetRAEFAERSVTKLEK 251
Cdd:COG0497 309 rrlarkygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA------RKKAAKKLEKAVTA 381
|
....*
1C1G_B 252 SIDDL 256
Cdd:COG0497 382 ELADL 386
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3-284 |
1.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 3 AIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAE 82
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 83 ADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKY 162
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 163 EEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFA 242
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
1C1G_B 243 ERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-165 |
1.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 1 MDAIKKKMQMLKldKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKatd 80
Cdd:PRK12704 44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 81 aeadvasLNRRIQLFEEELDRAQERLATALQKLEE-AEKAADES-ERGMKVIESRAQKDEEKMeIQEIQlKEAKhiaEDA 158
Cdd:PRK12704 119 -------LEQKQQELEKKEEELEELIEEQLQELERiSGLTAEEAkEILLEKVEEEARHEAAVL-IKEIE-EEAK---EEA 186
|
....*..
1C1G_B 159 DRKYEEV 165
Cdd:PRK12704 187 DKKAKEI 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-275 |
1.93e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 74 AEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKh 153
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 154 iaEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLK 233
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
1C1G_B 234 EAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 275
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-259 |
2.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 2 DAIKKKMQMLKLDKENALDRADEAEaDKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 82 EADVASLNRRIQLFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEI-QLKEAKHIAEDADR 160
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALK 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 161 KYEEVARKLVIIESDLERAEERAElsegKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
250
....*....|....*....
1C1G_B 241 FAERSVTKLEKSIDDLEDE 259
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-272 |
2.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 15 KENALDRADEAEADKKAAEDRSKqleDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRiql 94
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--- 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 95 fEEELDRAQE-RLATALQKLEEAEKAAD--ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVI 171
Cdd:PTZ00121 1524 -ADEAKKAEEaKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 172 IESDLERAEERAELSEGKCAE---LEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTK 248
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
250 260
....*....|....*....|....
1C1G_B 249 LEKSIDDLEDELYAQKLKYKAISE 272
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEE 1706
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
4-234 |
2.41e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 39.23 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 4 IKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEdelVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEA 83
Cdd:NF033838 183 VEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAE---ATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 84 DVASLNRRIQLFEeeldraqerLATALQKlEEAEKAADeSERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD---- 159
Cdd:NF033838 260 KPKRRAKRGVLGE---------PATPDKK-ENDAKSSD-SSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKeedr 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 160 RKYEEVARK---LVIIESDLERAEERAEL--SEGKCAELEEEIKTVTNNLKSLEAQA---EKYSQKEDKYEEEIK---VL 228
Cdd:NF033838 329 RNYPTNTYKtleLEIAESDVKVKEAELELvkEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKrkaAE 408
|
....*.
1C1G_B 229 SDKLKE 234
Cdd:NF033838 409 EDKVKE 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-257 |
2.72e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 18 ALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEA----DVASLNRRIQ 93
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAsdlrEADARYYVLG 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 94 LFEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADrkyEEVARKLVIIE 173
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA---ERLAEEELELE 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 174 SDLERAEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSI 253
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
....
1C1G_B 254 DDLE 257
Cdd:COG1196 777 EALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-277 |
2.72e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 5 KKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKlkATEDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 85 vaslnrriqlfEEELDRAQERLATALQKLEEAEKAADE----SERGMKVIESRAQKDEEKMEIQEIQLK-EAKHIAEDAD 159
Cdd:PTZ00121 1356 -----------ADEAEAAEEKAEAAEKKKEEAKKKADAakkkAEEKKKADEAKKKAEEDKKKADELKKAaAAKKKADEAK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 160 RKYEEVARKlviiESDLERAEERAELSEGKcaeLEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEeikvlSDKLKEAETRA 239
Cdd:PTZ00121 1425 KKAEEKKKA----DEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKA 1492
|
250 260 270
....*....|....*....|....*....|....*...
1C1G_B 240 EFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
22-260 |
2.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 22 ADEAEADKKAAEDRSKQLEDELVSLQKKLKATEdELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDR 101
Cdd:PRK04863 316 LAELNEAESDLEQDYQAASDHLNLVQTALRQQE-KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 102 AQERLA-----------------TALQKLEEAEK---AADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:PRK04863 395 LKSQLAdyqqaldvqqtraiqyqQAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 162 YEEVARKLVIIESDLERAEERAELSEgKCAELEEEiKTVTNNLKSLEAQ---AEKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:PRK04863 475 FEQAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQ-RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDD 552
|
250 260
....*....|....*....|..
1C1G_B 239 AEFAERSVTKLEKSIDDLEDEL 260
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESV 574
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
12-121 |
3.16e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.55 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 12 KLDKENALDRADEAEADKKA---AEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATD-AEADVAS 87
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKlatAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQtAQNNLAT 322
|
90 100 110
....*....|....*....|....*....|....
1C1G_B 88 LNRRIQLFEEELDRAQERLATALQKLEEAEKAAD 121
Cdd:TIGR04320 323 AQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| outer_NodT |
TIGR01845 |
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ... |
16-112 |
3.41e-03 |
|
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins]
Pssm-ID: 273830 [Multi-domain] Cd Length: 460 Bit Score: 38.55 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 16 ENALDRADEAEADKKAAEdrsKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKK----------ATDAEADV 85
Cdd:TIGR01845 147 ESALAQLEAAEADSQAAR---LTLSASIANAYVQLAALRAQLDVYHAALASRRKTLELTQKRyaagvaaasdVRQAEAAV 223
|
90 100
....*....|....*....|....*..
1C1G_B 86 ASLNRRIQLFEEELDRAQERLATALQK 112
Cdd:TIGR01845 224 ASAEAELPSLDVQIAQARNALAALLGK 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-284 |
4.45e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.49 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 33 EDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEELDRAQERLATALQK 112
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 113 LEEAE-------------KAADESERGMKVIESRAQKDEEKMEIQEIQLKEakhiaEDADRKYEEVARKLVIIESDLERA 179
Cdd:TIGR00606 781 EESAKvcltdvtimerfqMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK-----QEKQHELDTVVSKIELNRKLIQDQ 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 180 EERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDE 259
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS 935
|
250 260
....*....|....*....|....*
1C1G_B 260 LYAQKLKYKAISEELDHALNDMTSI 284
Cdd:TIGR00606 936 NKKAQDKVNDIKEKVKNIHGYMKDI 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-199 |
4.54e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.50 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 1 MDAIKKKMQMLKLDKENALDRADEAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 81 AEADVASLNRRIQLFEEELDRAQERLATALQKL-EEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD 159
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
170 180 190 200
....*....|....*....|....*....|....*....|
1C1G_B 160 RKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEIKT 199
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
23-234 |
8.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 37.30 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 23 DEAEADKKAAEDRSKQLEDELVSLQKKLKA----TEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLFEEe 98
Cdd:PHA02562 205 EEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEK- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 99 ldraQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiqeiQLKEAKHIAEDADRKYEEVARKLVIIESDLER 178
Cdd:PHA02562 284 ----GGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAID----ELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1C1G_B 179 AEERAELSEGKCAELEEEIKTVTNNLKSLEAQAEKYSQKEDKYEEEI---KVLSDKLKE 234
Cdd:PHA02562 356 LVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKyhrGIVTDLLKD 414
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
90-238 |
9.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 37.50 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 90 RRIQLFEEELDRAQERLATALQKLEEaekaadesergmkVIESRaqkdEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNE-------------LIASL----EELERELEQKAEEAEALLKEAEKLKEELEEKK 557
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C1G_B 170 VIIESDLERAEERAELS-EGKCAELEEEIKTVTNNLKSLEaQAEKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:PRK00409 558 EKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| |
