|
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 |
1.12e-71 |
|
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: 220.29 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 48 KKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVR 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 128 KVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559676 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 |
1.88e-20 |
|
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: 85.05 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 7 KMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEaeva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559676 87 ALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQ 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-281 |
2.31e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 25 AEEKARQQQERV---EKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:COG1196 220 EELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 102 AEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEE 181
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 182 RAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELV 261
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260
....*....|....*....|
gi 42559676 262 HEKEKYKAISEELDQTFQEL 281
Cdd:COG1196 460 ALLELLAELLEEAALLEAAL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-283 |
5.66e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 7 KMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVA 86
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 87 ALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVA 166
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSV 246
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 42559676 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 |
8.48e-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: 77.40 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 25 AEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEE 104
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 105 RLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAE 184
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 185 AGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEK 264
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250
....*....|....*..
gi 42559676 265 EKYKAISEELDQTFQEL 281
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-281 |
2.07e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 82 EAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 162 YDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559676 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 |
2.77e-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: 67.00 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 35 RVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEKLG 114
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 115 EASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELE 194
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 195 EELRVVGNNLKSLEV-----SEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKA 269
Cdd:TIGR02168 393 LQIASLNNEIERLEArlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|..
gi 42559676 270 ISEELDQTFQEL 281
Cdd:TIGR02168 473 AEQALDAAEREL 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-281 |
1.30e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 27 EKARQQQERVEKLEEELRDTQKKMMQveNELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERL 106
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 107 IIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQL----KEAQLLAEEAdrkyDEVARKLAMVEADLERAEER 182
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleEELEELEEEL----EELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 183 AEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVH 262
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250
....*....|....*....
gi 42559676 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 |
9.76e-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: 62.00 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 84 EVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYD 163
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 164 EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKE-AETRAEFA 242
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEA 956
|
250 260
....*....|....*....|....*...
gi 42559676 243 ERSVQKLQKEVDRLEDELVHEKEKYKAI 270
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-284 |
1.73e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 6 KKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEE--------ELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKK 77
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 78 VQEAEAEVAALNRRIQlleedfERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEE 157
Cdd:TIGR02169 267 LEEIEQLLEELNKKIK------DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 158 ADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAET 237
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 42559676 238 RAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-260 |
2.57e-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: 60.84 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 82 EAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEAdrk 161
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL--- 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 162 ydevarklamvEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:TIGR02168 858 -----------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250
....*....|....*....
gi 42559676 242 AERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-279 |
3.06e-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: 60.84 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELeeELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270
....*....|....*....|....*....|....*....
gi 42559676 241 FAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQ 279
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-244 |
3.33e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 22 ADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 102 AEERLIIATEKLGE---ASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQL-LAEEADRKYDEVARKLAMVEADLE 177
Cdd:COG4942 95 LRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559676 178 RAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAER 244
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-281 |
2.53e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 27 EKARQQQERVEKLEEELRDTQK-----KMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 102 AEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEE 181
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 182 RAEAGENKIVELEEELRVVGNNLKSLevseekalqredsyEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELv 261
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQL--------------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL- 430
|
250 260
....*....|....*....|
gi 42559676 262 hEKEKYKAISEELDQTFQEL 281
Cdd:TIGR02168 431 -EEAELKELQAELEELEEEL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-239 |
4.96e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 18 AMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 98 DFERAEERL---IIATEKLGEA--------SQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVA 166
Cdd:COG4942 98 ELEAQKEELaelLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559676 167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEvseekalQREDSYEEQIRLLTQRLKEAETRA 239
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ-------QEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-273 |
3.14e-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: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 7 KMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 87 ALNRRIQLLEEDFERAEERLIIATEKLGEaSQTADESERVRKVMENRSLQdEERVYQLEAQLKEAQLLAEEADRKYDEVA 166
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLSH-SRIPEIQAELSKLEEEVSRI-EARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSV 246
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250 260
....*....|....*....|....*..
gi 42559676 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 |
3.70e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTG-ANAQLEEKEKKVQEAEAEVAALNRRI 92
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 93 QLLEEDFERAEERLIIATEKLGEASQTADE-SERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAM 171
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 172 VEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQK 251
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260
....*....|....*....|...
gi 42559676 252 EVDRLEDELVHEKEKYKAISEEL 274
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAI 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-284 |
8.01e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 94 LLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVE 173
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 174 ADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEV 253
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
250 260 270
....*....|....*....|....*....|.
gi 42559676 254 DRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
15-247 |
1.40e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 15 KDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKM--MQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRI 92
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 93 QLLEEDFERAEERL--IIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEadrkydEVARKLA 170
Cdd:COG3206 243 AALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ------EAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42559676 171 MVEADLERAEERAEAGENKIVELEEELRvvgnNLKSLEVsEEKALQRE-DSYEEQIRLLTQRLKEAETRAEFAERSVQ 247
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA----ELPELEA-ELRRLEREvEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-193 |
2.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 20 DRADAAEEKARQQQERVEKLEEELRDTQKKMMQVEN--ELDKAQEELTGANAQLEEKEKKVQEAEA---EVAALNRRIQL 94
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 95 LEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLamvEA 174
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EE 773
|
170
....*....|....*....
gi 42559676 175 DLERAEERAEAGENKIVEL 193
Cdd:COG4913 774 RIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-276 |
4.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 67 ANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQ--- 143
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 144 -----------LEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEE 212
Cdd:TIGR02168 748 riaqlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42559676 213 KALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-233 |
8.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559676 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLK 233
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-282 |
8.87e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 133 RSLQDEERVYQLEA---QLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEV 209
Cdd:COG1196 216 RELKEELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559676 210 SEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELS 282
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-280 |
9.64e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERvrkvmENRSLQDEERVYQLEAQLKEAQLLAEEADR 160
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-----ELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAE 240
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42559676 241 FAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQE 280
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-276 |
1.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 22 ADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFER 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 102 AEERliiateklgEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLL--AEEADRKYDEVARKLAMVEADLERA 179
Cdd:PRK02224 424 LRER---------EAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 180 EERAEAGEnKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDE 259
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
250
....*....|....*..
gi 42559676 260 LVHEKEKYKAISEELDQ 276
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-231 |
1.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 19 MDRADAAEEKARQQQERVEKLEEeLRDTQKKMMQVENELDKAQEELTGAnaQLEEKEKKVQEAEAEVAALNRRIQLLEED 98
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 99 FERAEERLIIATEKLGEASQTADEServrkvmenrslqDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVE----A 174
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 42559676 175 DLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQR 231
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
40-245 |
6.34e-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: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 40 EEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQT 119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 120 ADESERVRK----VMENRSLQDE-ERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELE 194
Cdd:COG3883 95 LYRSGGSVSyldvLLGSESFSDFlDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42559676 195 EELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERS 245
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-284 |
6.36e-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: 47.37 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 24 AAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEK--------EKKVQEAEAEVAALNRRIQLL 95
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 96 EEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEAD 175
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 176 LERAEERAEAGENKI-------VELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQK 248
Cdd:TIGR02169 394 LEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270
....*....|....*....|....*....|....*.
gi 42559676 249 LQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-258 |
9.34e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVA-----ALNRRIQLLEEDFERAEERLIIATEKLGEASQTAD--ESERVRKVMENRSLQD-----EERVYQLEAQL 148
Cdd:TIGR02169 784 LEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKEqiksiEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 149 KEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLL 228
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
250 260 270
....*....|....*....|....*....|
gi 42559676 229 tQRLKEAETRAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02169 944 -EEIPEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
19-275 |
1.04e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 19 MDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQ-LEEKEKKVQEAEAevaaLNRRIQLLEE 97
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQaLEDLEKILTEKEA----LQGKINILEM 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 98 DFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLeaqLKEAQLLAEEADRKYDEVarklAMVEADLE 177
Cdd:PLN02939 178 RLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSL---SKELDVLKEENMLLKDDI----QFLKAELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 178 RAEERaeagENKIVELEEELRVVGNNLKSLE----VSEEKALQ----REDSYEEQIRLLTQRLKEAETRAEFAERSVQK- 248
Cdd:PLN02939 251 EVAET----EERVFKLEKERSLLDASLRELEskfiVAQEDVSKlsplQYDCWWEKVENLQDLLDRATNQVEKAALVLDQn 326
|
250 260
....*....|....*....|....*....
gi 42559676 249 --LQKEVDRLEDELvHEKEKYKAISEELD 275
Cdd:PLN02939 327 qdLRDKVDKLEASL-KEANVSKFSSYKVE 354
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
26-142 |
1.07e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 26 EEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEK-EKKVQEAEAEVAALNRRIQLLE--EDFERA 102
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQkgGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 42559676 103 EERLIIATEKLGEASQTADESERVRKVmENRSLQDEERVY 142
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKE-KQEELKVGDEVK 644
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
69-284 |
1.26e-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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 69 AQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRS-----LQDEERVYQ 143
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAelerlDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 144 LEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVvgnnlkslevseekalQREDSYEE 223
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL----------------ELRALLEE 753
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559676 224 QIRLLTQRLKEAETRAEFAERsVQKLQKEVDRLEDELV----HEKEKYKAISEELDQTFQELSGY 284
Cdd:COG4913 754 RFAAALGDAVERELRENLEER-IDALRARLNRAEEELEramrAFNREWPAETADLDADLESLPEY 817
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-274 |
1.41e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 52 QVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEE----RLIIATEKLGEASQTADESERVR 127
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 128 KVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559676 208 EVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEEL 274
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
10-273 |
1.52e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 10 AMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALN 89
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 90 RRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLkeAQLLAEEADRKYDEVARKL 169
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL--AALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 170 AMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKL 249
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260
....*....|....*....|....
gi 42559676 250 QKEVDRLEDELVHEKEKYKAISEE 273
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALE 289
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-284 |
1.75e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDeervyQLEAQLKEAQLLAEEADR 160
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAE 240
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 42559676 241 FAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY 284
Cdd:COG4372 282 ALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
164-282 |
2.45e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 45.52 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 164 EVARKLAMVEADLERAEERAEAGENK----IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRA 239
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 42559676 240 EF-AERSVQKLQKEVDRLEDEL---VHEKEKYKAISEELDQTFQELS 282
Cdd:COG1193 570 REeAEEILREARKEAEELIRELreaQAEEEELKEARKKLEELKQELE 616
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
22-276 |
2.75e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 22 ADAAEEKARQQQERVEkLEEELRDTQKKMMQVENELDKAQEELTGANA------------------QLEEKEKKVQEAEA 83
Cdd:COG3096 832 PDPEAELAALRQRRSE-LERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 84 EVAALNRRIQLLE----------EDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEER--------VYQLE 145
Cdd:COG3096 911 FIQQHGKALAQLEplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGllgensdlNEKLR 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 146 AQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGnnLKSLEVSEEKALQREDSYEEQI 225
Cdd:COG3096 991 ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG--VQADAEAEERARIRRDELHEEL 1068
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 42559676 226 RLLTQRLKEAETRAEFAERSVQKLQKEVDRLEdelvhekEKYKAISEELDQ 276
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE-------RDYKQEREQVVQ 1112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-259 |
2.85e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 84 EVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESErvrkvmENRSLQDEErvyQLEAQLKEAQLLAEEADRKYD 163
Cdd:TIGR02169 780 ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK------LNRLTLEKE---YLEKEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 164 EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAE 243
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
250
....*....|....*.
gi 42559676 244 RSVQKLQKEVDRLEDE 259
Cdd:TIGR02169 931 EELSEIEDPKGEDEEI 946
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
33-282 |
3.94e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 33 QERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEK 112
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 113 LGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVE 192
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 193 LEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISE 272
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250
....*....|
gi 42559676 273 ELDQTFQELS 282
Cdd:COG4372 270 EKDTEEEELE 279
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
25-224 |
4.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 25 AEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERA-- 102
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 103 ----EERLIIATEKLGEASQTADESERVRkVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLER 178
Cdd:COG3883 94 alyrSGGSVSYLDVLLGSESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 42559676 179 AEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQ 224
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
36-284 |
4.31e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 36 VEKLEEELRDTQKKMMQVENELDKAQeeltganaQLEEKEKKVQE--AEAEVAALNRRIQLLEEDFERAEERLIIATEKL 113
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLR--------SYLPKLNPLREekKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 114 GEasqtadeservrkvmenrsLQDEERvyQLEAQLKEAQLLA-----EEADRKYDEVARKLAMVEADLERAEERAEAGEN 188
Cdd:PRK05771 110 SE-------------------LENEIK--ELEQEIERLEPWGnfdldLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 189 KIV--------------------ELEEELRVVGnnLKSLEVSEEKALQRE-DSYEEQIRLLTQRLKEAETRaefAERSVQ 247
Cdd:PRK05771 169 VEYistdkgyvyvvvvvlkelsdEVEEELKKLG--FERLELEEEGTPSELiREIKEELEEIEKERESLLEE---LKELAK 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 42559676 248 KLQKEVDRLEDELVHEKEKYKAISEEL--DQTFQeLSGY 284
Cdd:PRK05771 244 KYLEELLALYEYLEIELERAEALSKFLktDKTFA-IEGW 281
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-281 |
4.51e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 97 EDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYqleAQLKEAQLLAEEADRKYDEVARKLAMVEADL 176
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 177 ERAEERAEAGENKIVELEEELRVVGNN--------LKSLEVSEEKALQREDSYEEQIRLLtqRLKEAETRAEFAE----- 243
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGGDrleqlereIERLERELEERERRRARLEALLAAL--GLPLPASAEEFAAlraea 389
|
170 180 190
....*....|....*....|....*....|....*....
gi 42559676 244 -RSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:COG4913 390 aALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-268 |
8.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKarQQQERVEKLEEELRDTQKKMMQvenELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEKKKADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 82 EAEVAALNRRIQLlEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:PTZ00121 1582 KAEEAKKAEEARI-EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 162 YdEVARKLAMVEADLERAEERAEAgenkivelEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:PTZ00121 1661 I-KAAEEAKKAEEDKKKAEEAKKA--------EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
250 260
....*....|....*....|....*..
gi 42559676 242 AERSVQKLQKEVDRLEDELVHEKEKYK 268
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-280 |
1.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANA--QLEEKEKKVQ 79
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 80 EAEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEAd 159
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 160 RKYDEVARKLAMVEAD-LERAEERAEAGENKivELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETR 238
Cdd:PTZ00121 1278 RKADELKKAEEKKKADeAKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 42559676 239 AEFAERSVQK-----LQKEVDRLEDELVHEKEKYKAISEELDQTFQE 280
Cdd:PTZ00121 1356 ADEAEAAEEKaeaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-250 |
1.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 82 EAEVAalnrriqLLEEDFERAEERLiiateklgeaSQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:PRK02224 299 LAEAG-------LDDADAEAVEARR----------EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 162 YDEVARklamVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:PRK02224 362 REEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
....*....
gi 42559676 242 AERSVQKLQ 250
Cdd:PRK02224 438 ARERVEEAE 446
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
14-216 |
1.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 14 EKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 94 ------------LLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRK 161
Cdd:COG3883 97 rsggsvsyldvlLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 42559676 162 YDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQ 216
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
28-273 |
1.30e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 28 KARQQQERVEKLEEELRDTQKKMMQVENELDkaqeeltganaqleEKEKKVQEAEAEVAALNRRIQLLE--EDFE----- 100
Cdd:PRK05771 73 REEKKKVSVKSLEELIKDVEEELEKIEKEIK--------------ELEEEISELENEIKELEQEIERLEpwGNFDldlsl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 101 -RAEERLIIATEKLGEASQTADESERVRKVMENRSlQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLamveADLERA 179
Cdd:PRK05771 139 lLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIS-TDKGYVYVVVVVLKELSDEVEEELKKLGFERLEL----EEEGTP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 180 EERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQredSYEEqirLLTQRLKEAETRAEFA-------------ERSV 246
Cdd:PRK05771 214 SELIREIKEELEEIEKERESLLEELKELAKKYLEELL---ALYE---YLEIELERAEALSKFLktdktfaiegwvpEDRV 287
|
250 260
....*....|....*....|....*...
gi 42559676 247 QKLQKEVDRLEDELVH-EKEKYKAISEE 273
Cdd:PRK05771 288 KKLKELIDKATGGSAYvEFVEPDEEEEE 315
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
52-277 |
1.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 52 QVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALnrriqlleedfeRAEERLIIATEKLGEASQTADESERVRKVME 131
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEF------------RQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 132 NRSLQDEERVYQLEAQLKEAQLLAEE--ADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEV 209
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559676 210 SEEKALQRE-DSYEEQIRLLTQRLKEAETRAefaeRSVQKLQKEVDRLEDELVHEKEKYKAISEELDQT 277
Cdd:COG3206 313 RILASLEAElEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2-228 |
1.38e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKiekdnamDRADAAEEKARQQQERVEKLEEE-------------LRDTQKKMMQVENELDKAQEELTGAN 68
Cdd:PRK11281 76 DRQKEETEQLK-------QQLAQAPAKLRQAQAELEALKDDndeetretlstlsLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 69 AQLEEKEKKVQEAEAEVAALNRRIQLLEE--DFERAEERLIIATEK-LGEASQTADE--SERVRKVMENRS-LQD----- 137
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLQQIRNllKGGKVGGKALRPSQRvLLQAEQALLNaqNDLQRKSLEGNTqLQDllqkq 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 138 ----EERVYQLEAQLkeaQLLAEEADRKYDEVARKLAmveADLERAEERAEAGENKIV--ELEEELRVV---------GN 202
Cdd:PRK11281 229 rdylTARIQRLEHQL---QLLQEAINSKRLTLSEKTV---QEAQSQDEAARIQANPLVaqELEINLQLSqrllkatekLN 302
|
250 260 270
....*....|....*....|....*....|
gi 42559676 203 NL--KSLEVSE--EKALQREDSYEEQIRLL 228
Cdd:PRK11281 303 TLtqQNLRVKNwlDRLTQSERNIKEQISVL 332
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-275 |
1.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 38 KLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKK-----VQEAEAEVAALNRRIQLLEEDFERAEERLIIATEK 112
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 113 LGEASQTADESERVRKVMENRSLQDEERVYQLEA---QLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENK 189
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 190 IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKA 269
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
....*.
gi 42559676 270 ISEELD 275
Cdd:PRK02224 403 APVDLG 408
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-281 |
1.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 5 KKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVE--NELDKAQEELTGANAQLEEKEKKVQEAE 82
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 83 aEVAALNRRIQLLEEDFERAEERLiiATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEA-QLKEAQLLAEEADRK 161
Cdd:PTZ00121 1422 -EAKKKAEEKKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 162 YDEVARKLAMVEA--DLERAEERAEAGENKIVELE---EELRVVGNNLKSLEVSEEKALQR--EDSYEEQIRLLTQRLKE 234
Cdd:PTZ00121 1499 ADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKNM 1578
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 42559676 235 AETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-276 |
2.08e-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: 42.75 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 62 EELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLIIATEKlgeasQTADESERVRKVMENrslqdEERV 141
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEK-----REYEGYELLKEKEAL-----ERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 142 YQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEA-GENKIVELEEELRVVGNNLKSLEVSEEKALQREDS 220
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 42559676 221 YEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
44-183 |
3.33e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 44 RDTQKKMMQVENELDKAQEELTGANAQLEEKEKkVQEAEAEVAALNRRIQLLEEDFERAEErliIATEKLGeASQTADES 123
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAE-IAAAEAQLAAAQAQLDLAQRELERYQA---LYKKGAV-SQQELDEA 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 124 ERVRKVMENRSLQDEERVYQLEAQLKEAQLLAeEADRKYDEVARKLAMVEADLERAEERA 183
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLREEEELA-AAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-259 |
3.78e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERvekLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 82 EAEVAALNRRIQLLEEDFERAEERLIIATE---KLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEA 158
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 159 DRKYDEVARKLAMVEADLERAEERAEagenKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETR 238
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
250 260
....*....|....*....|.
gi 42559676 239 AEFAERSVQKLQKEVDRLEDE 259
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDE 1790
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
17-281 |
4.97e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 17 NAMDRADAAEEKARQQQERVE---KLEEELRDtqkkmmQVENELDKAQEelTGANAQLEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:PRK10929 55 NWLEERKGSLERAKQYQQVIDnfpKLSAELRQ------QLNNERDEPRS--VPPNMSTDALEQEILQVSSQLLEKSRQAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 94 lleEDFERAEErliIAtEKLGEASQTADEServrkvmeNRSLQDEERvyQLEAQ------LKEAQLLAEEAdrkydEVAR 167
Cdd:PRK10929 127 ---QEQDRARE---IS-DSLSQLPQQQTEA--------RRQLNEIER--RLQTLgtpntpLAQAQLTALQA-----ESAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 168 KLAMVEaDLERAEERAeageNKIVELEEeLRVvgnnlkslEVSEEKAlQREDSYEEQIR--LLTQRLKEAETRAEfaerS 245
Cdd:PRK10929 185 LKALVD-ELELAQLSA----NNRQELAR-LRS--------ELAKKRS-QQLDAYLQALRnqLNSQRQREAERALE----S 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 42559676 246 VQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PRK10929 246 TELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM 281
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-176 |
5.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 6 KKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVE-NELDKAQEELTGANAQLEEKEKKVQEAEAE 84
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 85 VAALNRRIQLLEEDFER----AEERLIIATEKLGEASQTADESERVRKvmenrslQDEERVYQLEAQLKEAQ----LLAE 156
Cdd:COG4913 368 LAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALR-------DLRRELRELEAEIASLErrksNIPA 440
|
170 180
....*....|....*....|
gi 42559676 157 EADRKYDEVARKLAMVEADL 176
Cdd:COG4913 441 RLLALRDALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-282 |
5.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 147 QLKEAQLLAEEADRKYDEVARKLAMVEA-DLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQI 225
Cdd:COG4913 253 LLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559676 226 R--------LLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELS 282
Cdd:COG4913 333 RgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
30-276 |
5.48e-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: 41.26 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 30 RQQQERVEKLEEE-LRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDfERAEERLII 108
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE-ERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 109 ATEKLGEASQTADESERVRkvMENRslQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERaeagEN 188
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQ--MERQ--QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR----EV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 189 KIVELEEELRVVGNNLKSLEVSEEKALQREDSyEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYK 268
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQE-EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK 516
|
....*...
gi 42559676 269 AISEELDQ 276
Cdd:pfam17380 517 LLEKEMEE 524
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
51-282 |
1.04e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 51 MQVENELD-------KAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERL------IIATEKLGEAS 117
Cdd:PRK04863 275 MRHANERRvhleealELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 118 QTADE-SERVRKVMENRSLQDEervyqleaQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEE 196
Cdd:PRK04863 355 ADLEElEERLEEQNEVVEEADE--------QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 197 LRVVGNN---LKSLEVSEEKALQREDSYEEQIRLLTQRL---KEAETRAEFAERSVQKLQKEVDRLE-----DELVHEKE 265
Cdd:PRK04863 427 KQLCGLPdltADNAEDWLEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVSRSEawdvaRELLRRLR 506
|
250
....*....|....*..
gi 42559676 266 KYKAISEELDQTFQELS 282
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLS 523
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-284 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVEnELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKvmenrSLQDEERVYQLEAQLKeaQLLAEEADR 160
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELE--RLKKRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 161 KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEK-----ALQREDSYEEQIRLLTQRLKEA 235
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRI 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 42559676 236 ETRAEFAERSVQKLQKEVDRLEDELVHEKE--KYKAISEELDQTFQELSGY 284
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKY 515
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-93 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDnamdraDAAEEKARQQQERVEKLEEELRDTQKKM----------MQVENELDKAQEELTGANAQ 70
Cdd:COG0542 413 LDELERRLEQLEIEKE------ALKKEQDEASFERLAELRDELAELEEELealkarweaeKELIEEIQELKEELEQRYGK 486
|
90 100
....*....|....*....|...
gi 42559676 71 LEEKEKKVQEAEAEVAALNRRIQ 93
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR 509
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
140-273 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 140 RVYQLEAQLKEAQLLAE---EADRKYDEVARKLAMVEADLERAEERAEagenkiveLEEELRVVGNNLKSLEvseEKALQ 216
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQ 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 217 REDSYEEQIRLLTQR---LKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEE 273
Cdd:PRK12704 94 KEENLDRKLELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-281 |
1.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKiEKDNAMDRADAAEEKARQQQERVE--KLEEELRDTQKKmmQVENELDKAQEELTGANAQLEEKEKKVQ 79
Cdd:PTZ00121 1473 DEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 80 EAEAEVAALNRRIQLLEEDFERAEERLIIATEKLGEASQT--ADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEE 157
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 158 ADRKYDEVARKLAmvEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEvSEEKALQREDSYEEQIRLLTQRLKEAET 237
Cdd:PTZ00121 1630 EEKKKVEQLKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 42559676 238 RAEFAERSVQKLQkEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PTZ00121 1707 LKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
51-284 |
1.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 51 MQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERA-------EERLIIATEKLGEASQTADES 123
Cdd:PRK04863 344 LRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyQQALDVQQTRAIQYQQAVQAL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 124 ERVRKVMENRSLQDEervyQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAE-------------ERAEAGENKI 190
Cdd:PRK04863 424 ERAKQLCGLPDLTAD----NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayqlvrkiagevSRSEAWDVAR 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 191 VELE--EELRVVGNNLKSLE--VSE-EKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKE 265
Cdd:PRK04863 500 ELLRrlREQRHLAEQLQQLRmrLSElEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
250
....*....|....*....
gi 42559676 266 KYKAISEELDQTFQELSGY 284
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRL 598
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-131 |
1.65e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 16 DNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAevAALNRRIQLL 95
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAA 758
|
90 100 110
....*....|....*....|....*....|....*.
gi 42559676 96 EEDFERAEERLIIATEKLGEASQTADESERVRKVME 131
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
29-276 |
1.93e-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: 39.55 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 29 ARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEE---DFERAEER 105
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 106 LIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKeaqlLAEEADRKYDEVARKLAMVEADLERAEERAEA 185
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS----VADAARRQFEKAYELVCKIAGEVERSQAWQTA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 186 GEnkIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLT---QRLKEAETRAEFAERSVQKLQKEVDRLEDELVH 262
Cdd:COG3096 498 RE--LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEELEEQAAE 575
|
250
....*....|....
gi 42559676 263 EKEKYKAISEELDQ 276
Cdd:COG3096 576 AVEQRSELRQQLEQ 589
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
121-238 |
2.02e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 121 DESERVRKVMEnrSLQDEERvyQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIV-ELEEELRV 199
Cdd:PRK00409 513 EDKEKLNELIA--SLEELER--ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIkEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 42559676 200 VGNNLKSLEVSEEKALQREDSyEEQIRLLTQRLKEAETR 238
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHEL-IEARKRLNKANEKKEKK 626
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-275 |
2.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 2 DAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEA 81
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 82 EAEVAALN---------------------RRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQdEER 140
Cdd:PRK02224 446 EALLEAGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL-EEL 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 141 VYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQRED- 219
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADa 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559676 220 -----------------SYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELD 275
Cdd:PRK02224 605 edeierlrekrealaelNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERD 677
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-276 |
2.44e-03 |
|
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: 39.23 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 84 EVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYD 163
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 164 EVARKLAMVEADLERAEER--AEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEF 241
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
250 260 270
....*....|....*....|....*....|....*
gi 42559676 242 AERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
10-186 |
2.60e-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: 38.59 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 10 AMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKkmmQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALN 89
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA---QQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 90 RRIQLLEEDFERAEERLIiateklGEASQTADESERVRKVMENRSLQD------EERVYQLEAQLKEAQLLAEEADRKYD 163
Cdd:pfam09787 121 EELRYLEEELRRSKATLQ------SRIKDREAEIEKLRNQLTSKSQSSssqselENRLHQLTETLIQKQTMLEALSTEKN 194
|
170 180
....*....|....*....|...
gi 42559676 164 EVARKLAMVEADLERAEERAEAG 186
Cdd:pfam09787 195 SLVLQLERMEQQIKELQGEGSNG 217
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
16-281 |
3.44e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.74 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 16 DNAMDRADA-AEEKARQQQ--------ERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKK------VQE 80
Cdd:PRK11281 46 DALNKQKLLeAEDKLVQQDleqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstlsLRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIiateklgeASQTAdeSERVRKVMENRSlqdeERVYQLEAQLKEAQllAEEADR 160
Cdd:PRK11281 126 LESRLAQTLDQLQNAQNDLAEYNSQLV--------SLQTQ--PERAQAALYANS----QRLQQIRNLLKGGK--VGGKAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 161 KYDEVAR---KLAMVEA--DLERAEeraEAGENKIVELEEELRvvgnNLKSLEVseekalqreDSYEEQIRLL-----TQ 230
Cdd:PRK11281 190 RPSQRVLlqaEQALLNAqnDLQRKS---LEGNTQLQDLLQKQR----DYLTARI---------QRLEHQLQLLqeainSK 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 42559676 231 RLKEAETRAEFAersvQKLQKEVDRLEDELVH-EKEKYKAISEELDQTFQEL 281
Cdd:PRK11281 254 RLTLSEKTVQEA----QSQDEAARIQANPLVAqELEINLQLSQRLLKATEKL 301
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-190 |
4.20e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.50 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 1 MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQE 80
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 81 AEAEVAALNRRIQLLEEDFERAEERLIIATEKL-GEASQTADESERVRKVMENRSLQDEERVYQLEAQLKE---AQLLAE 156
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpVNLAAI 992
|
170 180 190
....*....|....*....|....*....|....
gi 42559676 157 EADRKYDEVARKLAMVEADLERAEERAEAGENKI 190
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
23-281 |
4.69e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 23 DAAEEKARQQQERVEKLEEELRDTQKKM-------MQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLL 95
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 96 EEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEAD 175
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 176 LERAEERAEAGE----------------------------NKIVELEEELRVVGNNLKSLEVSEEKALQ------REDSY 221
Cdd:PRK02224 435 LRTARERVEEAEalleagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERL 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 222 EEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQEL 281
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
59-243 |
4.70e-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: 38.39 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 59 KAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLiiatEKLGEASQTADESERVRKVMENRSLQDE 138
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHL----NLVQTALRQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 139 ERVYQLEA---QLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNlkslEVSEEKAL 215
Cdd:COG3096 365 EQEEVVEEaaeQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLP----DLTPENAE 440
|
170 180
....*....|....*....|....*...
gi 42559676 216 QREDSYEEQIRLLTQRLKEAETRAEFAE 243
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLSVAD 468
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
24-276 |
5.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 24 AAEEKARQQQERVEKLEEELRDTQKKMMQV----ENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEED- 98
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLnllaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDp 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 99 --FERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEER--------VYQLEAQLKEAQLLAEEADRKYDEVARK 168
Cdd:PRK04863 935 eqFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEmlaknsdlNEKLRQRLEQAEQERTRAREQLRQAQAQ 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 169 LAMVEADLERAEERAEAGENKIVELEEELRVVGnnLKSLEVSEEKALQREDSyeeqirlLTQRLKEAETRAEFAERSVQK 248
Cdd:PRK04863 1015 LAQYNQVLASLKSSYDAKRQMLQELKQELQDLG--VPADSGAEERARARRDE-------LHARLSANRSRRNQLEKQLTF 1085
|
250 260
....*....|....*....|....*...
gi 42559676 249 LQKEVDRLEDELVHEKEKYKAISEELDQ 276
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
26-276 |
5.50e-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: 38.10 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 26 EEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEER 105
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 106 L--IIATEKLGEASQTadeSERVRKVMENRSLQDEERVYQLEAQLKEAQLL---------AEEADRKYDEVARKLAMVEA 174
Cdd:TIGR00606 774 LgtIMPEEESAKVCLT---DVTIMERFQMELKDVERKIAQQAAKLQGSDLDrtvqqvnqeKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 175 DLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVD 254
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260
....*....|....*....|..
gi 42559676 255 RLEDELVHEKEKYKAISEELDQ 276
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKN 952
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
33-156 |
7.00e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 37.70 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 33 QERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKV----------QEAEAEVAALNRRIQLLEEDFERA 102
Cdd:pfam05667 348 ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaeeniAKLQALVDASAQRLVELAGQWEKH 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 42559676 103 EERLIIATEKLGEAsQTADESERVRKVMENRSLQDEERVYQLEAQLKE---AQLLAE 156
Cdd:pfam05667 428 RVPLIEEYRALKEA-KSNKEDESQRKLEEIKELREKIKEVAEEAKQKEelyKQLVAE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-226 |
7.76e-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: 37.74 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 4 IKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEA 83
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559676 84 EVAALNRRIQLLEEDFERAEERLIIATEKLGEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEaDRKYD 163
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLE 954
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559676 164 EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIR 226
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| |
