|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-282 |
1.03e-72 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 222.98 E-value: 1.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 48 KKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVR 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 128 KVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559665 208 EVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELS 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 |
1.34e-21 |
|
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: 88.13 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 7 KMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAeva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559665 87 aLNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQ 152
Cdd:pfam12718 78 -LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-281 |
1.76e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 25 AEEKARQQQERV---EKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:COG1196 220 EELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 102 AEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEE 181
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 182 RAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELV 261
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260
....*....|....*....|
gi 42559665 262 HEKEKYKAISEELDQTFQEL 281
Cdd:COG1196 460 ALLELLAELLEEAALLEAAL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-283 |
3.27e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 7 KMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVA 86
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 87 ALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVA 166
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSV 246
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 42559665 247 QKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSG 283
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-281 |
6.01e-16 |
|
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: 77.79 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 25 AEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEE 104
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 105 RLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAE 184
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 185 AGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEK 264
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250
....*....|....*..
gi 42559665 265 EKYKAISEELDQTFQEL 281
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-281 |
7.93e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 82 EAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 162 YDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559665 242 AERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-281 |
1.25e-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: 67.77 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 35 RVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLE 114
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 115 EASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELE 194
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 195 EELRVVGNNLKSLEV-----SEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKA 269
Cdd:TIGR02168 393 LQIASLNNEIERLEArlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|..
gi 42559665 270 ISEELDQTFQEL 281
Cdd:TIGR02168 473 AEQALDAAEREL 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-281 |
5.43e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 27 EKARQQQERVEKLEEELRDTQKKMMQveNELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERL 106
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 107 KIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQL----KEAQLLAEEAdrkyDEVARKLAMVEADLERAEER 182
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleEELEELEEEL----EELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 183 AEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVH 262
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250
....*....|....*....
gi 42559665 263 EKEKYKAISEELDQTFQEL 281
Cdd:COG1196 440 EEEALEEAAEEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-270 |
6.29e-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: 62.77 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 84 EVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYD 163
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 164 EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKE-AETRAEFA 242
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEA 956
|
250 260
....*....|....*....|....*...
gi 42559665 243 ERSVQKLQKEVDRLEDELVHEKEKYKAI 270
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-279 |
7.76e-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: 62.38 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 94 LLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVE 173
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 174 ADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSE------------EKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleeleeelEELQEELERLEEALEELREELEEAEQALDA 479
|
250 260 270
....*....|....*....|....*....|....*...
gi 42559665 242 AERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQ 279
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-260 |
1.63e-10 |
|
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: 61.61 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 82 EAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEAdrk 161
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL--- 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 162 ydevarklamvEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:TIGR02168 858 -----------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250
....*....|....*....
gi 42559665 242 AERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERL 945
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-244 |
2.08e-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: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 22 ADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 102 AEERLKIATEKLEE---ASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQL-LAEEADRKYDEVARKLAMVEADLE 177
Cdd:COG4942 95 LRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559665 178 RAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAER 244
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-284 |
6.63e-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: 59.70 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 6 KKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEE--------ELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKK 77
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 78 VQEAEAEVAALNRRIQLLEEDFERAeerlkiATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEE 157
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLR------VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 158 ADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAET 237
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 42559665 238 RAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-281 |
1.03e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 27 EKARQQQERVEKLEEELRDTQK-----KMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 102 AEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEE 181
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 182 RAEAGENKIVELEEELRVVGNNLKSLevseekalqredsyEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELv 261
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQL--------------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL- 430
|
250 260
....*....|....*....|
gi 42559665 262 hEKEKYKAISEELDQTFQEL 281
Cdd:TIGR02168 431 -EEAELKELQAELEELEEEL 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-240 |
1.79e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 161 KYDEVARKL-----AMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEA 235
Cdd:TIGR02168 415 RRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
....*
gi 42559665 236 ETRAE 240
Cdd:TIGR02168 495 ERLQE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-273 |
1.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 7 KMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 87 ALNRRIQLLEEDFerAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVA 166
Cdd:TIGR02169 762 ELEARIEELEEDL--HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSV 246
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250 260
....*....|....*....|....*..
gi 42559665 247 QKLQKEVDRLEDELVHEKEKYKAISEE 273
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-274 |
2.53e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTG-ANAQLEEKEKKVQEAEAEVAALNRRI 92
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 93 QLLEEDFERAEERLKIATEKLEEASQTADE-SERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAM 171
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 172 VEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQK 251
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260
....*....|....*....|...
gi 42559665 252 EVDRLEDELVHEKEKYKAISEEL 274
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAI 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-284 |
4.88e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 94 LLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVE 173
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 174 ADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEV 253
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
250 260 270
....*....|....*....|....*....|.
gi 42559665 254 DRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-231 |
1.72e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 19 MDRADAAEEKARQQQERVEKLEEeLRDTQKKMMQVENELDKAQEELTGAnaQLEEKEKKVQEAEAEVAALNRRIQLLEED 98
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 99 FERAEERLKIATEKLEEASQTADEServrkvmenrslqDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVE----A 174
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 42559665 175 DLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQR 231
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-276 |
1.75e-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: 52.37 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 67 ANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQ--- 143
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 144 -----------LEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEE 212
Cdd:TIGR02168 748 riaqlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42559665 213 KALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-280 |
2.01e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERvrkvmENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-----ELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAE 240
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559665 241 FAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQE 280
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
54-282 |
2.59e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 54 ENELDKAQEELTGANAQLEEKEKKVQ--EAEAEVA---------ALNRRIQLLEEDFERAEERLKIATEKLEEASQTADE 122
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEplERQAEKAeryrelkeeLKELEAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 123 SERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGN 202
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 203 NLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELS 282
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
15-247 |
3.26e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 15 KDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKM--MQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRI 92
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 93 QLLEEDFERAEERLK--IATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEadrkydEVARKLA 170
Cdd:COG3206 243 AALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ------EAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42559665 171 MVEADLERAEERAEAGENKIVELEEELRvvgnNLKSLEVsEEKALQRE-DSYEEQIRLLTQRLKEAETRAEFAERSVQ 247
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA----ELPELEA-ELRRLEREvEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-226 |
3.92e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMmqveNELDKAQEELTGANAQLEEkekKVQE 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRDKLTE---EYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559665 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIR 226
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-276 |
1.20e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 22 ADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 102 AEERLKIATEKLEEASQTadeservrkVMENRSLQDEERVYQLEAQLKEAQLL--AEEADRKYDEVARKLAMVEADLERA 179
Cdd:PRK02224 424 LREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 180 EERAEAGEnKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDE 259
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
250
....*....|....*..
gi 42559665 260 LVHEKEKYKAISEELDQ 276
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-274 |
1.66e-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: 49.28 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 52 QVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEE----RLKIATEKLEEASQTADESERVR 127
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 128 KVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559665 208 EVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEEL 274
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-284 |
2.12e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDeervyQLEAQLKEAQLLAEEADR 160
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAE 240
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 42559665 241 FAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:COG4372 282 ALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-170 |
2.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLE--EELRDTQKKMMQVENELDKAQEE----------LTGANA 69
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAElerldassddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 70 QLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLK 149
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
170 180
....*....|....*....|..
gi 42559665 150 EAQ-LLAEEADRKYDEVARKLA 170
Cdd:COG4913 773 ERIdALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-257 |
2.87e-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: 48.53 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKL-EEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRae 240
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE-- 484
|
250
....*....|....*..
gi 42559665 241 faersVQKLQKEVDRLE 257
Cdd:TIGR02169 485 -----LSKLQRELAEAE 496
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
19-275 |
3.37e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 19 MDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQ-LEEKEKKVQEAEAevaaLNRRIQLLEE 97
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQaLEDLEKILTEKEA----LQGKINILEM 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 98 DFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLeaqLKEAQLLAEEADRKYDEVarklAMVEADLE 177
Cdd:PLN02939 178 RLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSL---SKELDVLKEENMLLKDDI----QFLKAELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 178 RAEERaeagENKIVELEEELRVVGNNLKSLE----VSEEKALQ----REDSYEEQIRLLTQRLKEAETRAEFAERSVQK- 248
Cdd:PLN02939 251 EVAET----EERVFKLEKERSLLDASLRELEskfiVAQEDVSKlsplQYDCWWEKVENLQDLLDRATNQVEKAALVLDQn 326
|
250 260
....*....|....*....|....*....
gi 42559665 249 --LQKEVDRLEDELvHEKEKYKAISEELD 275
Cdd:PLN02939 327 qdLRDKVDKLEASL-KEANVSKFSSYKVE 354
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-260 |
4.07e-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: 48.14 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAalNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:TIGR02169 784 LEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAE 240
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
250 260
....*....|....*....|....*.
gi 42559665 241 ------FAERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02169 942 edeeipEEELSLEDVQAELQRVEEEI 967
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
36-284 |
4.24e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 36 VEKLEEELRDTQKKMMQVENELDKAQeeltganaQLEEKEKKVQE--AEAEVAALNRRIQLLEEDFERAEERLKIATEKL 113
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLR--------SYLPKLNPLREekKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 114 EEasqtadeservrkvmenrsLQDEERvyQLEAQLKEAQLLA-----EEADRKYDEVARKLAMVEADLERAEERAEAGEN 188
Cdd:PRK05771 110 SE-------------------LENEIK--ELEQEIERLEPWGnfdldLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 189 KIV--------------------ELEEELRVVGnnLKSLEVSEEKALQRE-DSYEEQIRLLTQRLKEAETRaefAERSVQ 247
Cdd:PRK05771 169 VEYistdkgyvyvvvvvlkelsdEVEEELKKLG--FERLELEEEGTPSELiREIKEELEEIEKERESLLEE---LKELAK 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 42559665 248 KLQKEVDRLEDELVHEKEKYKAISEEL--DQTFQeLSGY 284
Cdd:PRK05771 244 KYLEELLALYEYLEIELERAEALSKFLktDKTFA-IEGW 281
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
40-245 |
5.25e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 40 EEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQT 119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 120 ADESERVRK----VMENRSLQDE-ERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELE 194
Cdd:COG3883 95 LYRSGGSVSyldvLLGSESFSDFlDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42559665 195 EELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERS 245
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
69-284 |
7.13e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 69 AQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRS-----LQDEERVYQ 143
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAelerlDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 144 LEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVvgnnlkslevseekalQREDSYEE 223
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL----------------ELRALLEE 753
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559665 224 QIRLLTQRLKEAETRAEFAERsVQKLQKEVDRLEDELV----HEKEKYKAISEELDQTFQELSGY 284
Cdd:COG4913 754 RFAAALGDAVERELRENLEER-IDALRARLNRAEEELEramrAFNREWPAETADLDADLESLPEY 817
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
33-282 |
7.72e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 33 QERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEK 112
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 113 LEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVE 192
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 193 LEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISE 272
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250
....*....|
gi 42559665 273 ELDQTFQELS 282
Cdd:COG4372 270 EKDTEEEELE 279
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
22-265 |
8.49e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 22 ADAAEEKARQQQERVEkLEEELRDTQKKMMQVENELDKAQEELTGANA------------------QLEEKEKKVQEAEA 83
Cdd:COG3096 832 PDPEAELAALRQRRSE-LERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 84 EVAALNRRIQLLE----------EDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEER--------VYQLE 145
Cdd:COG3096 911 FIQQHGKALAQLEplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGllgensdlNEKLR 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 146 AQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGnnLKSLEVSEEKALQREDSYEEQI 225
Cdd:COG3096 991 ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG--VQADAEAEERARIRRDELHEEL 1068
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559665 226 RLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKE 265
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
26-142 |
1.06e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 26 EEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEK-EKKVQEAEAEVAALNRRIQLLE--EDFERA 102
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQkgGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 42559665 103 EERLKIATEKLEEASQTADESERVRKVmENRSLQDEERVY 142
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKE-KQEELKVGDEVK 644
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-281 |
1.40e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 97 EDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYqleAQLKEAQLLAEEADRKYDEVARKLAMVEADL 176
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 177 ERAEERAEAGENKIVELEEELRVVGNN--------LKSLEVSEEKALQREDSYEEQIRLLtqRLKEAETRAEFAE----- 243
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGGDrleqlereIERLERELEERERRRARLEALLAAL--GLPLPASAEEFAAlraea 389
|
170 180 190
....*....|....*....|....*....|....*....
gi 42559665 244 -RSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:COG4913 390 aALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
164-282 |
2.70e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 45.52 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 164 EVARKLAMVEADLERAEERAEAGENK----IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRA 239
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 42559665 240 EF-AERSVQKLQKEVDRLEDEL---VHEKEKYKAISEELDQTFQELS 282
Cdd:COG1193 570 REeAEEILREARKEAEELIRELreaQAEEEELKEARKKLEELKQELE 616
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-275 |
3.99e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 38 KLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKK-----VQEAEAEVAALNRRIQLLEEDFERAEERLKIATEK 112
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 113 LEEASQTADESERVRKVMENRSLQDEERVYQLEA---QLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENK 189
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 190 IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKA 269
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
....*.
gi 42559665 270 ISEELD 275
Cdd:PRK02224 403 APVDLG 408
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
52-281 |
4.49e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 52 QVENELDKAQ-----------EELTGANAQLEEKE------KKVQEAEAEVAALNR--RIQLLEEDFERA---------- 102
Cdd:PRK10929 27 QITQELEQAKaaktpaqaeivEALQSALNWLEERKgsleraKQYQQVIDNFPKLSAelRQQLNNERDEPRsvppnmstda 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 103 --EERLKIATEKLEEASQTADESERVRKVME------------NRSLQDEERvyQLEAQ------LKEAQLLAEEAdrky 162
Cdd:PRK10929 107 leQEILQVSSQLLEKSRQAQQEQDRAREISDslsqlpqqqteaRRQLNEIER--RLQTLgtpntpLAQAQLTALQA---- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 163 dEVARKLAMVEaDLERAEERAEaGENKIVELEEELRvvgnnlkslevseEKALQREDSYEEQIR--LLTQRLKEAETRAE 240
Cdd:PRK10929 181 -ESAALKALVD-ELELAQLSAN-NRQELARLRSELA-------------KKRSQQLDAYLQALRnqLNSQRQREAERALE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 42559665 241 faerSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PRK10929 245 ----STELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM 281
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-268 |
5.07e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKarQQQERVEKLEEELRDTQKKMMQvenELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEKKKADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 82 EAEVAALNRRIQLlEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:PTZ00121 1582 KAEEAKKAEEARI-EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 162 YdEVARKLAMVEADLERAEERAEAgenkivelEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:PTZ00121 1661 I-KAAEEAKKAEEDKKKAEEAKKA--------EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
250 260
....*....|....*....|....*..
gi 42559665 242 AERSVQKLQKEVDRLEDELVHEKEKYK 268
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
25-224 |
5.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 25 AEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEE 104
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 105 RLKIA------TEKLEEASQTADESERVRkVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLER 178
Cdd:COG3883 94 ALYRSggsvsyLDVLLGSESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 42559665 179 AEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQ 224
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
52-277 |
5.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 52 QVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEedferAEERLKIATEKLEEASQTADESERVRKvme 131
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELA--- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 132 nrslQDEERVYQLEAQLKEAQLLAEE--ADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEV 209
Cdd:COG3206 237 ----EAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559665 210 SEEKALQRE-DSYEEQIRLLTQRLKEAETRAefaeRSVQKLQKEVDRLEDELVHEKEKYKAISEELDQT 277
Cdd:COG3206 313 RILASLEAElEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-281 |
6.05e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 5 KKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVE--NELDKAQEELTGANAQLEEKEKKVQEAE 82
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 83 aEVAALNRRIQLLEEDFERAEERLKiATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKY 162
Cdd:PTZ00121 1422 -EAKKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 163 DEVARKLAMVEA--DLERAEERAEAGENKIVELE---EELRVVGNNLKSLEVSEEKALQR--EDSYEEQIRLLTQRLKEA 235
Cdd:PTZ00121 1500 DEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKNMA 1579
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 42559665 236 ETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
28-273 |
6.49e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 28 KARQQQERVEKLEEELRDTQKKMMQVENELDkaqeeltganaqleEKEKKVQEAEAEVAALNRRIQLLE--EDFE----- 100
Cdd:PRK05771 73 REEKKKVSVKSLEELIKDVEEELEKIEKEIK--------------ELEEEISELENEIKELEQEIERLEpwGNFDldlsl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 101 -RAEERLKIATEKLEEASQTADESERVRKVMENRSlQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLamveADLERA 179
Cdd:PRK05771 139 lLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIS-TDKGYVYVVVVVLKELSDEVEEELKKLGFERLEL----EEEGTP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 180 EERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQredSYEEqirLLTQRLKEAETRAEFA-------------ERSV 246
Cdd:PRK05771 214 SELIREIKEELEEIEKERESLLEELKELAKKYLEELL---ALYE---YLEIELERAEALSKFLktdktfaiegwvpEDRV 287
|
250 260
....*....|....*....|....*...
gi 42559665 247 QKLQKEVDRLEDELVH-EKEKYKAISEE 273
Cdd:PRK05771 288 KKLKELIDKATGGSAYvEFVEPDEEEEE 315
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
14-216 |
6.90e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 94 ------------LLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:COG3883 97 rsggsvsyldvlLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 42559665 162 YDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQ 216
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
29-282 |
7.38e-05 |
|
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: 43.60 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 29 ARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKI 108
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 109 ATEKLEEasQTADESERVRKVmenrslqdeervYQLEAQLKEAQLLAEEAdrkYDEVARKLAMVEADLERAEERAEAGEN 188
Cdd:COG4942 95 LRAELEA--QKEELAELLRAL------------YRLGRQPPLALLLSPED---FLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 189 KIVELEEelrvvgnnlksLEVSEEKALQREDSYEEQIRLLTQRLKEAETRaefAERSVQKLQKEVDRLEDELVHEKEKYK 268
Cdd:COG4942 158 DLAELAA-----------LRAELEAERAELEALLAELEEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....
gi 42559665 269 AISEELDQTFQELS 282
Cdd:COG4942 224 ELEALIARLEAEAA 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-250 |
7.44e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 82 EAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERvrkvmenrslqdeervyQLEAQLKEAQLLAEEADRK 161
Cdd:PRK02224 299 LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE-----------------EAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 162 YDEVARklamVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:PRK02224 362 REEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
....*....
gi 42559665 242 AERSVQKLQ 250
Cdd:PRK02224 438 ARERVEEAE 446
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2-228 |
1.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKiekdnamDRADAAEEKARQQQERVEKLEEE-------------LRDTQKKMMQVENELDKAQEELTGAN 68
Cdd:PRK11281 76 DRQKEETEQLK-------QQLAQAPAKLRQAQAELEALKDDndeetretlstlsLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 69 AQLEEKEKKVQEAEAEVAALNRRIQLL---------EEDFERAEERLKIATE-KLEEASqtadeSERVRKVMENRS-LQD 137
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLQQIrnllkggkvGGKALRPSQRVLLQAEqALLNAQ-----NDLQRKSLEGNTqLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 138 ---------EERVYQLEAQLkeaQLLAEEADRKYDEVARKLAmveADLERAEERAEAGENKIV--ELEEELRVV------ 200
Cdd:PRK11281 224 llqkqrdylTARIQRLEHQL---QLLQEAINSKRLTLSEKTV---QEAQSQDEAARIQANPLVaqELEINLQLSqrllka 297
|
250 260 270
....*....|....*....|....*....|....*
gi 42559665 201 ---GNNL--KSLEVSE--EKALQREDSYEEQIRLL 228
Cdd:PRK11281 298 tekLNTLtqQNLRVKNwlDRLTQSERNIKEQISVL 332
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
44-183 |
1.62e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 44 RDTQKKMMQVENELDKAQEELTGANAQLEEKEKkVQEAEAEVAALNRRIQLLEEDFERAEERLK---IATEKLEEASQTA 120
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAE-IAAAEAQLAAAQAQLDLAQRELERYQALYKkgaVSQQELDEARAAL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559665 121 DESERVRKvmenrslQDEERVYQLEAQLKEAQLLAeEADRKYDEVARKLAMVEADLERAEERA 183
Cdd:COG1566 158 DAAQAQLE-------AAQAQLAQAQAGLREEEELA-AAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-280 |
1.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANA--QLEEKEKKVQ 79
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 80 EAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEAd 159
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 160 RKYDEVARKLAMVEAD-LERAEERAEAGENKivELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETR 238
Cdd:PTZ00121 1278 RKADELKKAEEKKKADeAKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 42559665 239 AEFAERSVQK-----LQKEVDRLEDELVHEKEKYKAISEELDQTFQE 280
Cdd:PTZ00121 1356 ADEAEAAEEKaeaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-176 |
1.95e-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: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 6 KKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVE-NELDKAQEELTGANAQLEEKEKKVQEAEAE 84
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 85 VAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVmenRSLQDEERVYQLEAQLKEAQ----LLAEEADR 160
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELRELEAEIASLErrksNIPARLLA 444
|
170
....*....|....*.
gi 42559665 161 KYDEVARKLAMVEADL 176
Cdd:COG4913 445 LRDALAEALGLDEAEL 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-276 |
2.51e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 84 EVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYD 163
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 164 EVARKLAMVEADLERAEER--AEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
250 260 270
....*....|....*....|....*....|....*
gi 42559665 242 AERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-276 |
3.33e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 62 EELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEeasqtADESERVRKVMENrslqdEERV 141
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE-----YEGYELLKEKEAL-----ERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 142 YQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEA-GENKIVELEEELRVVGNNLKSLEVSEEKALQREDS 220
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 42559665 221 YEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-259 |
3.43e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERvekLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 82 EAEVAALNRRIQLLEEDFERAEERLKIATE---KLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEA 158
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 159 DRKYDEVARKLAMVEADLERAEERAEagenKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETR 238
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
250 260
....*....|....*....|.
gi 42559665 239 AEFAERSVQKLQKEVDRLEDE 259
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDE 1790
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
21-259 |
4.46e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 21 RADAAEEKARQQQERVEKLEEElrdtqkkMMQVENELDKAQEELTGANAQLEEKE--------KKVQEAEAEVAALNRRI 92
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQ-------LVQANGELEKASREETFARTALKNARldlrrlfdEKQSEKDKKNKALAERK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 93 QLLEEDFERAEERLKIATEKLEEASQTADESERvrkvmENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMV 172
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR-----EARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 173 EADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKeaeTRAEFAERSVQKLQKE 252
Cdd:pfam12128 753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA---TQLSNIERAISELQQQ 829
|
....*..
gi 42559665 253 VDRLEDE 259
Cdd:pfam12128 830 LARLIAD 836
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
30-276 |
4.88e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 30 RQQQERVEKLEEELRDTQKKMMQVENELDKaqeeltganaQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIA 109
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRR----------KLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 110 TEKLE----EASQTADESERVRKV--MENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERa 183
Cdd:pfam17380 357 ERKREleriRQEEIAMEISRMRELerLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 184 eagENKIVELEEELRVVGNNLKSLEVSEEKALQREDSyEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHE 263
Cdd:pfam17380 436 ---EVRRLEEERAREMERVRLEEQERQQQVERLRQQE-EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE 511
|
250
....*....|...
gi 42559665 264 KEKYKAISEELDQ 276
Cdd:pfam17380 512 ERKRKLLEKEMEE 524
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-281 |
5.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 6 KKMQAMKIEKDNAMDRADAAEEKARQQQERVE--KLEEELRDTQKKmmQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 84 EVAALNRRIQLLEEDFERAEERLKIATEKLEEASQT--ADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 162 YDEVARKLAmvEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEvSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:PTZ00121 1634 KVEQLKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559665 242 AERSVQKLQkEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PTZ00121 1711 EAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
21-260 |
5.88e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 21 RADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQeaeaEVAALNRRIQLLEEDFE 100
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 101 RAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAE 180
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 181 ERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDEL 260
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
99-238 |
7.96e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 99 FERAEeRLKIATEKLEEA-SQTADESERVRKVMEnrSLQDEERvyQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLE 177
Cdd:PRK00409 491 FEIAK-RLGLPENIIEEAkKLIGEDKEKLNELIA--SLEELER--ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED 565
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559665 178 RAEERAEAGENKIV-ELEEELRVVGNNLKSLEVSEEKALQREDSyEEQIRLLTQRLKEAETR 238
Cdd:PRK00409 566 KLLEEAEKEAQQAIkEAKKEADEIIKELRQLQKGGYASVKAHEL-IEARKRLNKANEKKEKK 626
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
51-282 |
9.10e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 51 MQVENELD-------KAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLK------IATEKLEEAS 117
Cdd:PRK04863 275 MRHANERRvhleealELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 118 QTADE-SERVRKVMENRSLQDEervyqleaQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEE 196
Cdd:PRK04863 355 ADLEElEERLEEQNEVVEEADE--------QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 197 LRVVGNN---LKSLEVSEEKALQREDSYEEQIRLLTQRL---KEAETRAEFAERSVQKLQKEVDRLE-----DELVHEKE 265
Cdd:PRK04863 427 KQLCGLPdltADNAEDWLEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVSRSEawdvaRELLRRLR 506
|
250
....*....|....*..
gi 42559665 266 KYKAISEELDQTFQELS 282
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLS 523
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-284 |
9.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVEnELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKvmenrSLQDEERVYQLEAQLKeaQLLAEEADR 160
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELE--RLKKRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEK-----ALQREDSYEEQIRLLTQRLKEA 235
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRI 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 42559665 236 ETRAEFAERSVQKLQKEVDRLEDELVHEKE--KYKAISEELDQTFQELSGY 284
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKY 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
23-281 |
1.00e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 23 DAAEEKARQQQERVEKLEEELRDTQKKM-------MQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLL 95
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 96 EEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEAD 175
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 176 LERAEERAEAGE----------------------------NKIVELEEELRVVGNNLKSLEVSEEKALQ------REDSY 221
Cdd:PRK02224 435 LRTARERVEEAEalleagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERL 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 222 EEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
29-276 |
1.06e-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: 40.71 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 29 ARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEE---DFERAEER 105
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 106 LKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKeaqlLAEEADRKYDEVARKLAMVEADLERAEERAEA 185
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS----VADAARRQFEKAYELVCKIAGEVERSQAWQTA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 186 GEnkIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLT---QRLKEAETRAEFAERSVQKLQKEVDRLEDELVH 262
Cdd:COG3096 498 RE--LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEELEEQAAE 575
|
250
....*....|....
gi 42559665 263 EKEKYKAISEELDQ 276
Cdd:COG3096 576 AVEQRSELRQQLEQ 589
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-93 |
1.25e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDnamdraDAAEEKARQQQERVEKLEEELRDTQKKM----------MQVENELDKAQEELTGANAQ 70
Cdd:COG0542 413 LDELERRLEQLEIEKE------ALKKEQDEASFERLAELRDELAELEEELealkarweaeKELIEEIQELKEELEQRYGK 486
|
90 100
....*....|....*....|...
gi 42559665 71 LEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR 509
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
24-276 |
1.27e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 24 AAEEKARQQQERVEKLEEELRDTQKKMMQV----ENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEED- 98
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLnllaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDp 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 99 --FERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEER--------VYQLEAQLKEAQLLAEEADRKYDEVARK 168
Cdd:PRK04863 935 eqFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEmlaknsdlNEKLRQRLEQAEQERTRAREQLRQAQAQ 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 169 LAMVEADLERAEERAEAGENKIVELEEELRVVGnnLKSLEVSEEKALQREDSyeeqirlLTQRLKEAETRAEFAERSVQK 248
Cdd:PRK04863 1015 LAQYNQVLASLKSSYDAKRQMLQELKQELQDLG--VPADSGAEERARARRDE-------LHARLSANRSRRNQLEKQLTF 1085
|
250 260
....*....|....*....|....*...
gi 42559665 249 LQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
140-273 |
1.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 140 RVYQLEAQLKEAQLLAE---EADRKYDEVARKLAMVEADLERAEERAEagenkiveLEEELRVVGNNLKSLEvseEKALQ 216
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQ 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 217 REDSYEEQIRLLTQR---LKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEE 273
Cdd:PRK12704 94 KEENLDRKLELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-150 |
1.71e-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: 39.65 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKL-EEASQTADESERVRKVMENRSLQDEERVYQLEAQLKE 150
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-275 |
2.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQ-------EELTGANAQLEE 73
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 74 KEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIAT--EKLEEASQTADES-ERVRKVMENRSLQDE---ERVYQLEAQ 147
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELiAERRETIEEKRERAEelrERAAELEAE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 148 LKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAgENKIVELEEELRVVGNNLKSLEVSEEKALQREDsyEEQIRL 227
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAEDEIERLREKREALAELND--ERRERL 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 42559665 228 LTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELD 275
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERD 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-226 |
2.70e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 84 EVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEaDRKYD 163
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLE 954
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559665 164 EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIR 226
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
59-243 |
2.79e-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: 39.17 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 59 KAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKiateKLEEASQTADESERVRKVMENRSLQDE 138
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN----LVQTALRQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 139 ERVYQLEA---QLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNlkslEVSEEKAL 215
Cdd:COG3096 365 EQEEVVEEaaeQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLP----DLTPENAE 440
|
170 180
....*....|....*....|....*...
gi 42559665 216 QREDSYEEQIRLLTQRLKEAETRAEFAE 243
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLSVAD 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
83-260 |
2.95e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 83 AEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVR-KVMENRSLQDEERVYQLEAQLKEaqllAEEADRK 161
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREReKAERYQALLKEKREYEGYELLKE----KEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 162 YDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQRE-DSYEEQIRLLTQRLKEAETRAE 240
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELE 318
|
170 180
....*....|....*....|
gi 42559665 241 FAERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEI 338
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
42-198 |
3.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 42 ELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASqtad 121
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559665 122 eSERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELR 198
Cdd:COG1579 87 -NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
26-276 |
3.70e-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: 38.87 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 26 EEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEER 105
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 106 LKIATEKLEEASQTADESERVRKVMENRSlQDEERVYQLEAQLKEAQLL---------AEEADRKYDEVARKLAMVEADL 176
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDVTIMERFQMELK-DVERKIAQQAAKLQGSDLDrtvqqvnqeKQEKQHELDTVVSKIELNRKLI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 177 ERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRL 256
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK 932
|
250 260
....*....|....*....|
gi 42559665 257 EDELVHEKEKYKAISEELDQ 276
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKN 952
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
10-186 |
3.76e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.20 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 10 AMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKkmmQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALN 89
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA---QQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 90 RRIQLLEEDFERAEERLKiateklEEASQTADESERVRKVMENRSLQD------EERVYQLEAQLKEAQLLAEEADRKYD 163
Cdd:pfam09787 121 EELRYLEEELRRSKATLQ------SRIKDREAEIEKLRNQLTSKSQSSssqselENRLHQLTETLIQKQTMLEALSTEKN 194
|
170 180
....*....|....*....|...
gi 42559665 164 EVARKLAMVEADLERAEERAEAG 186
Cdd:pfam09787 195 SLVLQLERMEQQIKELQGEGSNG 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-269 |
4.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKaRQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEK-KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 81 AEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADE----SERVRKVMENRSLQDEERVYQLEAQLK-EAQLLA 155
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkAEEKKKADEAKKKAEEDKKKADELKKAaAAKKKA 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 156 EEADRKYDEVARklamVEADLERAEERAEAGENKIVELE----EELRVVGNNLKSLEVSEEKA--LQREDSYEEQIRLLT 229
Cdd:PTZ00121 1421 DEAKKKAEEKKK----ADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAeeAKKADEAKKKAEEAK 1496
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559665 230 QRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKA 269
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-275 |
4.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.38 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 60 AQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEE 139
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 140 RVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQRED 219
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559665 220 SYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRL-------EDELVHEKEKYKAISEELD 275
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQRE 805
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
16-281 |
5.17e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.35 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 16 DNAMDRADA-AEEKARQQQ--------ERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKvQEAEAEVA 86
Cdd:PRK11281 46 DALNKQKLLeAEDKLVQQDleqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-TLSTLSLR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 87 ALNRRIQLLEEDFERAEERLKIATEKLeEASQTAdeSERVRKVMENRSlqdeERVYQLEAQLKEAQllAEEADRKYDEVA 166
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQL-VSLQTQ--PERAQAALYANS----QRLQQIRNLLKGGK--VGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 167 R---KLAMVEA--DLERAEeraEAGENKIVELEEELRvvgnNLKSLEVseekalqreDSYEEQIRLL-----TQRLKEAE 236
Cdd:PRK11281 196 LlqaEQALLNAqnDLQRKS---LEGNTQLQDLLQKQR----DYLTARI---------QRLEHQLQLLqeainSKRLTLSE 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 42559665 237 TRAEFAersvQKLQKEVDRLEDELVH-EKEKYKAISEELDQTFQEL 281
Cdd:PRK11281 260 KTVQEA----QSQDEAARIQANPLVAqELEINLQLSQRLLKATEKL 301
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
38-204 |
5.27e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 38.13 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 38 KLEEELRDTQKKMMQVENELDKAQ---EELTGAN------AQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKI 108
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRfqlEELEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 109 ATEKLEEASQTADESERVRKVMEN---------RSLQ--------DEERVYQLEAQLKEAQLLAeeadRKY----DEVAR 167
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESalieleeaaSELRryldslefDPERLEEVEERLALLRRLA----RKYgvtvEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 42559665 168 KLAMVEADLER---AEERAEAGENKIVELEEELRVVGNNL 204
Cdd:COG0497 325 YAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
88-284 |
5.41e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.07 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 88 LNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVAR 167
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 168 KLAMVEADLERAEERA--------------------EAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQ--- 224
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFqkvikmyekggvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskk 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 225 IRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
41-199 |
5.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 41 EELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLE--EDFERAEERLKIATEKLEEASQ 118
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 119 TADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEE----ADRKYDEVARKLAMVEADLERAEERAEAGENKIVELE 194
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
....*
gi 42559665 195 EELRV 199
Cdd:COG4717 234 NELEA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-282 |
6.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.97 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 147 QLKEAQLLAEEADRKYDEVARKLAMVEA-DLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQI 225
Cdd:COG4913 253 LLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559665 226 RLL-TQRLKEAETRAEFAERSVQKLQKEVDRLED-------ELVHEKEKYKAISEELDQTFQELS 282
Cdd:COG4913 333 RGNgGDRLEQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAALRAEAAALLEALE 397
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
37-122 |
7.94e-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: 37.40 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 37 EKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAAL--------NRRIQLLEEDFERAEERLKI 108
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAqaqalqtaQNNLATAQAALANAEARLAK 336
|
90
....*....|....
gi 42559665 109 ATEKLEEASQTADE 122
Cdd:TIGR04320 337 AKEALANLNADLAK 350
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-280 |
8.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.81 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 2 DAIKKKMQAMKiEKDNAMDRADAAEEKARQ--QQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQ 79
Cdd:PTZ00121 1381 DAAKKKAEEKK-KADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 80 EAEAEVAALNRRIQLLE---EDFERAEERLKIATE---KLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQL 153
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKkkaEEAKKADEAKKKAEEakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 154 LAEEADRKYDEVARKLAMVEAD-------LERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIR 226
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEekkkaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 42559665 227 LLTQRLKEAETRAEFAERSVQKLQKEVDRLEdELVHEKEKYKAISEELDQTFQE 280
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEE 1672
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
30-151 |
8.91e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 37.62 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559665 30 RQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAalnrriQLLEEDFERAEERLKIA 109
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE------QLQEKAAETSQERKQKR 218
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 42559665 110 TEKLEEASQTADESERvrkvmENRSLQDEervyqleaQLKEA 151
Cdd:PRK11448 219 KEITDQAAKRLELSEE-----ETRILIDQ--------QLRKA 247
|
|
| |
