|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-282 |
2.67e-60 |
|
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: 191.40 E-value: 2.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 48 KRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERAR 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 128 KCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700163 208 EVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 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 |
2.85e-21 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 87.36 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 7 KMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEgeva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700163 87 ALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-276 |
1.24e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 24 TLEQQNKEANIRA--EKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLER 101
Cdd:TIGR02168 672 ILERRREIEELEEkiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 102 SEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEE 181
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 182 RAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELV 261
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250
....*....|....*
gi 2068700163 262 NEKEKYKSITDELDQ 276
Cdd:TIGR02168 912 ELRRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-276 |
1.65e-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: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 5 KKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGE 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 85 VAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADEserarkclenranmeddrvgiLETQLAQAKHIAEEADKKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEE---------------------LEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 165 VARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAER 244
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270
....*....|....*....|....*....|..
gi 2068700163 245 SVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 276
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-270 |
3.72e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 2 DAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNA 81
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 82 EGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKK 161
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 162 YEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEF 241
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|....*....
gi 2068700163 242 AERSVQKLQKEVDRLEDELVNEKEKYKSI 270
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-263 |
1.93e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 23 DTLEQQNKEAN----IRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEED 98
Cdd:TIGR02168 203 KSLERQAEKAErykeLKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 99 LERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLER 178
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 179 AEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
....*
gi 2068700163 259 ELVNE 263
Cdd:TIGR02168 443 EELEE 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-281 |
3.67e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 47 QKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERA 126
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 127 RKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKS 206
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700163 207 LEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 281
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-270 |
8.05e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 1 MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSN 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADK 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 161 KYEEVARKLAMVEADLERAEERAETGESKIVELeeELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270
....*....|....*....|....*....|
gi 2068700163 241 FAERSVQKLQKEVDRLEDELVNEKEKYKSI 270
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-266 |
2.55e-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: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 1 MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSN 80
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADK 160
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 161 KYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAE 240
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260
....*....|....*....|....*.
gi 2068700163 241 FAERSVQKLQKEVDRLEDELVNEKEK 266
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-259 |
2.69e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 7 KMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 87 ALNRRIQLLEEDLERSEERLNTATTKLA-------EASQAADESERAR-----KCLENRANMEDDRVGILETQLAQAKHI 154
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLShsripeiQAELSKLEEEVSRiearlREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 155 AEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMRE 234
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260
....*....|....*....|....*
gi 2068700163 235 AEARAEFAERSVQKLQKEVDRLEDE 259
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-281 |
1.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 45 NLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESE 124
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 125 RARKCLENRANMEDDRVGILETQLAqakhiaeeadkkyeEVARKLAMVEADLERAEERAETGESKIVELEEELR------ 198
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELA--------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTllneea 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 199 -VVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQT 277
Cdd:TIGR02168 820 aNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
....
gi 2068700163 278 FSEL 281
Cdd:TIGR02168 900 SEEL 903
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-193 |
6.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 20 DRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLEN---------DLDQVQESLLKANTQLEEkdkaLSNAEGEVAALNR 90
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELER----LDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 91 RIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLa 170
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL- 771
|
170 180
....*....|....*....|...
gi 2068700163 171 mvEADLERAEERAETGESKIVEL 193
Cdd:COG4913 772 --EERIDALRARLNRAEEELERA 792
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
39-245 |
1.02e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 39 SEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQ 118
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 119 AADESERARKCLENRANMED-----DRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVEL 193
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068700163 194 EEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERS 245
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-269 |
1.49e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 32 ANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATT 111
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 112 KLAEASQAADESERARKCLENRANME----DDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGE 187
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 188 SKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELthrmreaearaefaERSVQKLQKEVDRLEDELVNEKEKY 267
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL--------------QQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 2068700163 268 KS 269
Cdd:COG4942 244 PA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
35-266 |
1.78e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 35 RAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLA 114
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 115 EASQAADESERARKclENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELE 194
Cdd:TIGR02169 748 SLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068700163 195 EELrvvgnnlKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEK 266
Cdd:TIGR02169 826 LEK-------EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-283 |
8.89e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 2 DAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNA 81
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 82 EGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKK 161
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 162 YEEVARKLA-MVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAaqrednfEEQIKELTHRMREAEARAE 240
Cdd:TIGR02168 938 IDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA-------IEEYEELKERYDFLTAQKE 1010
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2068700163 241 FAERSVQKLQKEVDRLEDELVNE-KEKYKSITDELDQTFSELSG 283
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEIDREARERfKDTFDQVNENFQRVFPKLFG 1054
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-260 |
1.20e-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: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 13 LEKDNAMDRADTLEQQNKEANiraeKSEEEVHNLQKRMQQLEnDLDQVQESLLKANTQLEEKDKALSNAEGEVAAlnRRI 92
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLE----RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQ--RRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 93 QLLEEDLERSEERLNTATTKLAEASQAADE-SERARKCLENRANMEDDRVGILETQLAQAKhiaeeadKKYEEVARKLAM 171
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDAlREELDELEAQIRGNGGDRLEQLEREIERLE-------RELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 172 VEADLERAEERAETGESKIVELEEElrvvgnnlkslevseekAAQREDNFEEQIKELthrmreaEARAEFAERSVQKLQK 251
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAE-----------------AAALLEALEEELEAL-------EEALAEAEAALRDLRR 419
|
....*....
gi 2068700163 252 EVDRLEDEL 260
Cdd:COG4913 420 ELRELEAEI 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-282 |
3.66e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 6 KKMQAMKLEKDNAMDR-ADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGE 84
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERlRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 85 VAALNRRIQLLEEDLER-SEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYE 163
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 164 EVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNF---------------------- 221
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELkreldrlqeelqrlseeladln 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700163 222 ------EEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 282
Cdd:TIGR02169 427 aaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
70-284 |
5.40e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 70 QLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATT---------KLAEASQAADESERARKCLENranmEDDR 140
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDA----SSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 141 VGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVgnnlKSLEVSEEKAAQREDN 220
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE----LRALLEERFAAALGDA 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700163 221 FEEQIKElthrmreaearaeFAERSVQKLQKEVDRLEDELVNE----KEKYKSITDELDQTFSELSGY 284
Cdd:COG4913 763 VERELRE-------------NLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLESLPEY 817
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-203 |
1.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 18 AMDRADTLEQQnkEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAAL-NRRIQLLE 96
Cdd:COG4913 267 ARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 97 EDLERSEERLNTATTKLAEASQAADESErarkcLENRANMEDdrvgiLETQLAQAKHIAEEADKKYEEVARKLAMVEADL 176
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALG-----LPLPASAEE-----FAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|....*..
gi 2068700163 177 ERAEERAEtgeskivELEEELRVVGNN 203
Cdd:COG4913 415 RDLRRELR-------ELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9-276 |
2.38e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 9 QAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAAL 88
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 89 NRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAK--------------HI 154
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 155 AEEADKKYEEVARKLAMVEADLERAEERAETGESkIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMRE 234
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2068700163 235 AEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 276
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3-284 |
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 2068700163 3 AIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAE 82
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 83 GEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQ-AKHIAEEADKK 161
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 162 YEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEF 241
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2068700163 242 AERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY 284
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
184-284 |
5.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 184 ETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQ---IKELTHRMREAEARAEFAERSVQKLQKEVDRLEDEL 260
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
90 100
....*....|....*....|....
gi 2068700163 261 VNEKEKYKSITDELDQTFSELSGY 284
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSEL 398
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
42-198 |
6.98e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 42 EVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASqaad 121
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700163 122 eSERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELR 198
Cdd:COG1579 87 -NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-282 |
1.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 122 ESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVG 201
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 202 NNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 281
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
.
gi 2068700163 282 S 282
Cdd:COG1196 368 L 368
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
9-198 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 9 QAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRmqqleNDLDQVQESLLKANTQLEEKDKALSNAEGEVAAL 88
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 89 NRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDD--RVGILETQLAQAKhiaeeaDKKYEEVA 166
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAALR------AQLQQEAQ 312
|
170 180 190
....*....|....*....|....*....|..
gi 2068700163 167 RKLAMVEADLERAEERAETGESKIVELEEELR 198
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
25-220 |
1.47e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 25 LEQQNKEANIRAEKSEEEVhNLQKRMQQLENDLDQVQESllkaNTQLEEKDKALSNAEG----------------EVAAL 88
Cdd:NF012221 1551 AKQDDAAQNALADKERAEA-DRQRLEQEKQQQLAAISGS----QSQLESTDQNALETNGqaqrdaileesravtkELTTL 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 89 NRRIQLLEEDLERSEER------------LNTATTKLAEASQAADES-ERARKCLENRANMEDDRVGILETQLAQAKHIA 155
Cdd:NF012221 1626 AQGLDALDSQATYAGESgdqwrnpfagglLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQ 1705
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700163 156 EEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSleVSEEKAAQREDN 220
Cdd:NF012221 1706 ANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDAS--AAENKANQAQAD 1768
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2-189 |
1.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 2 DAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNA 81
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 82 EGEVAALN------------RRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLA 149
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700163 150 QAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESK 189
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
77-199 |
2.20e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 77 ALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAE--ASQAADESERAR-----KCLENRANMEDDRVGILETQLA 149
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700163 150 QAKHIAEEADKKYE----EVA---RKLAMVEADLERAEERAETGESKIVELEEELRV 199
Cdd:PRK09039 127 SEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-276 |
2.38e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 4 IKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEG 83
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 84 EVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYE 163
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 164 EVARKLAMVEADLERAEER--AETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEF 241
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
250 260 270
....*....|....*....|....*....|....*
gi 2068700163 242 AERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 276
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-196 |
2.94e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 1 MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEE------- 73
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 74 -----KDKALSNAEgEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQL 148
Cdd:COG4942 116 lgrqpPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068700163 149 AQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEE 196
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
20-187 |
3.55e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 20 DRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESllkantqLEEKDKALSNAEGEVAALNRRIQLLEEDL 99
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR-------LEECRVAAQAHNEEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 100 ERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERA 179
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
....*...
gi 2068700163 180 EERAETGE 187
Cdd:PRK02224 439 RERVEEAE 446
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
5-260 |
6.72e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 5 KKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKD--------- 75
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpve 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 76 -----KALSNAEGEVAALNRRIQLLEEDLERSEERLNTATtklaeasqAADESERARKCLENRANMEDDRVGILETQLAQ 150
Cdd:PRK02224 463 gsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEE 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 151 AKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNfEEQIKELTH 230
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA-EDEIERLRE 613
|
250 260 270
....*....|....*....|....*....|
gi 2068700163 231 RMREAEARAEFAERSVQKLQKEVDRLEDEL 260
Cdd:PRK02224 614 KREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
150-273 |
7.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 150 QAKHIAEEADKKYEEVaRKLAMVEADLERAEERAEtgeskiveLEEELRVVGNNLKSLEvseEKAAQREDNFEEQIKELT 229
Cdd:PRK12704 39 EAKRILEEAKKEAEAI-KKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQKEENLDRKLELLE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2068700163 230 HR---MREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDE 273
Cdd:PRK12704 107 KReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
22-277 |
9.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 22 ADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQvqeslLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLER 101
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 102 SEERLNTATTKLAEASQAADESerarkclenranMEDDRVGILETQLAQAKHIAEEADKKYEEvaRKLAMVEADLERAEE 181
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEL------------LQSPVIQQLRAQLAELEAELAELSARYTP--NHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 182 RAetgeskivELEEELRVVgnnLKSLEVSEEKAAQREDNFEEQIKELTHRMreaearaefaeRSVQKLQKEVDRLEDELV 261
Cdd:COG3206 304 RA--------QLQQEAQRI---LASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREVE 361
|
250
....*....|....*.
gi 2068700163 262 NEKEKYKSITDELDQT 277
Cdd:COG3206 362 VARELYESLLQRLEEA 377
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
57-275 |
1.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 57 LDQVQESLLKANTQLEEKD-----KALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERA----R 127
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 128 KCLENRANMEDDRVGILEtQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL 207
Cdd:PRK02224 262 DLRETIAETEREREELAE-EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700163 208 EVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELD 275
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-246 |
1.80e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 2 DAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEK-SEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSN 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AEGEVAALNRRIQLLEEDLER--------------SEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILET 146
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEerkrrdklteeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 147 QLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIK 226
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
250 260
....*....|....*....|
gi 2068700163 227 ELTHRMREAEARAEFAERSV 246
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERV 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3-168 |
2.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 3 AIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEE--KDKALSN 80
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENR-----ANMEDDRVGILETQLAQAKHIA 155
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeelAELEAELEELEAEREELAAKIP 173
|
170
....*....|...
gi 2068700163 156 EEADKKYEEVARK 168
Cdd:COG1579 174 PELLALYERIRKR 186
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
33-282 |
2.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 33 NIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKAlsnaegEVAALNRRIQLLEEDLERSEERLNTATTK 112
Cdd:PRK05771 35 DLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKV------SVKSLEELIKDVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 113 LAE--ASQAADESERAR-KCLENrANMEDDRVGILETQLAQAKHIAEEADKKYEEvarklamvEADLERAEERAETGESK 189
Cdd:PRK05771 109 ISEleNEIKELEQEIERlEPWGN-FDLDLSLLLGFKYVSVFVGTVPEDKLEELKL--------ESDVENVEYISTDKGYV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 190 IV----------ELEEELRVVGnnLKSLEVSEEKAAQrednfeEQIKELTHRmreaearaefaersVQKLQKEVDRLEDE 259
Cdd:PRK05771 180 YVvvvvlkelsdEVEEELKKLG--FERLELEEEGTPS------ELIREIKEE--------------LEEIEKERESLLEE 237
|
250 260
....*....|....*....|...
gi 2068700163 260 LVNEKEKYksiTDELDQTFSELS 282
Cdd:PRK05771 238 LKELAKKY---LEELLALYEYLE 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-181 |
2.39e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 4 IKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEG 83
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 84 EVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEaDKKYE 163
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLE 954
|
170
....*....|....*...
gi 2068700163 164 EVARKLAMVEADLERAEE 181
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEP 972
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
6-231 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 6 KKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDL-----------------DQVQESLLKAN 68
Cdd:COG3096 347 EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqaldvqqtraiqyQQAVQALEKAR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 69 TQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQA-------ADESERARKCLENRANMED--- 138
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAyelvckiAGEVERSQAWQTARELLRRyrs 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 139 -----DRVGILETQLAQAKHIAE---EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEvs 210
Cdd:COG3096 507 qqalaQRLQQLRAQLAELEQRLRqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR-- 584
|
250 260
....*....|....*....|.
gi 2068700163 211 eekaaQREDNFEEQIKELTHR 231
Cdd:COG3096 585 -----QQLEQLRARIKELAAR 600
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
38-227 |
2.64e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 38.90 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 38 KSEEEVHNLQKRMQQLENDLD----QVQEsLLKAN------TQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLN 107
Cdd:COG0497 169 ALKKELEELRADEAERARELDllrfQLEE-LEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEALSGGEGGALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 108 TATTKLAEASQAADESERARKCLEN---------------RANMEDD--RVGILETQLAQAKHIAeeadKKY----EEVA 166
Cdd:COG0497 248 QALRALERLAEYDPSLAELAERLESalieleeaaselrryLDSLEFDpeRLEEVEERLALLRRLA----RKYgvtvEELL 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700163 167 RKLAMVEADLER---AEERAETGESKIVELEEELRVVGNNLkslevSE--EKAAQRednFEEQIKE 227
Cdd:COG0497 324 AYAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL-----SAarKKAAKK---LEKAVTA 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
47-276 |
2.80e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 47 QKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQaadESERA 126
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 127 RKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKS 206
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 207 LEVSEEKAAQREDNFEEQIKELthrmreaearaefaersvqklQKEVDRLEDELVNEKEKYKSITDELDQ 276
Cdd:COG4942 176 LEALLAELEEERAALEALKAER---------------------QKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
5-204 |
3.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 5 KKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKAntQLEEKDKALSNAEGE 84
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE--AEKEAQQAIKEAKKE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 85 VAALNRRIQLLE--EDLERSEERLNTATTKLAEASQAADESERARKcLENRANMEDDRVGILetQLAQAKHIAEEADKKY 162
Cdd:PRK00409 586 ADEIIKELRQLQkgGYASVKAHELIEARKRLNKANEKKEKKKKKQK-EKQEELKVGDEVKYL--SLGQKGEVLSIPDDKE 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700163 163 EEV---ARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNL 204
Cdd:PRK00409 663 AIVqagIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLEL 707
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-259 |
3.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 9 QAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAAL 88
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 89 NRRIQLLEEDLERSEERLNTAT---TKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEV 165
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEaeeKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 166 ARKLAMVEADLERAEERAEtgesKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERS 245
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
250
....*....|....
gi 2068700163 246 VQKLQKEVDRLEDE 259
Cdd:PTZ00121 1777 KEAVIEEELDEEDE 1790
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
35-183 |
3.63e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.17 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 35 RAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAA----LNRRIQLLEEDLeRSEERLNTAT 110
Cdd:pfam00529 69 KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQaqidLARRRVLAPIGG-ISRESLVTAG 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700163 111 TKLAEASQAADESERArkclenRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERA 183
Cdd:pfam00529 148 ALVAQAQANLLATVAQ------LDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRA 214
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
7-216 |
3.66e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.74 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 7 KMQAMKLEKDNAMDRADTLEQQNKEANIR----AEKSEEEVHNLQKRMQQLENDLDQVQESL--LKANTQlEEKDKALSN 80
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTLAlldkIDRQKEETEQLKQQLAQAPAKLRQAQAELeaLKDDND-EETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AegEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAadeSERARKCL-ENRANMEDDRVGILETQLAQAKHIAEEAD 159
Cdd:PRK11281 121 L--SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ---PERAQAALyANSQRLQQIRNLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068700163 160 KKYEEvarkLAMVEA--DLERAE-------------ERAETGEsKIVELEEELRVVGN--NLKSLEVSEEKAAQ 216
Cdd:PRK11281 196 LLQAE----QALLNAqnDLQRKSlegntqlqdllqkQRDYLTA-RIQRLEHQLQLLQEaiNSKRLTLSEKTVQE 264
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-284 |
4.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 1 MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEKSEEEVHNLQKRMQQLEnDLDQVQESLLKANTQLEEKDKALSN 80
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AEGEVAALNRRIQLLEEDLERSEERLNtattKLAEASQAADESERARKCLENRANmEDDRVGILETQLAQAKhiAEEADK 160
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK--KRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 161 KYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEK-----AAQREDNFEEQIKELTHRMREA 235
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRI 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2068700163 236 EARAEFAERSVQKLQKEVDRLEDELVNEKE--KYKSITDELDQTFSELSGY 284
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKY 515
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
36-122 |
6.02e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 37.78 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 36 AEKSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAAL--------NRRIQLLEEDLERSEERLN 107
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAqaqalqtaQNNLATAQAALANAEARLA 335
|
90
....*....|....*
gi 2068700163 108 TATTKLAEASQAADE 122
Cdd:TIGR04320 336 KAKEALANLNADLAK 350
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
164-282 |
7.76e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 37.81 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 164 EVARKLAMVEADLERAEERAETGESK----IVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARA 239
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2068700163 240 EFAERS-VQKLQKEVDRLEDELVN---EKEKYKSITDELDQTFSELS 282
Cdd:COG1193 570 REEAEEiLREARKEAEELIRELREaqaEEEELKEARKKLEELKQELE 616
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3-227 |
8.71e-03 |
|
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: 37.41 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 3 AIKKKMQAMKLEKDNAMDRADTLEQQNKEANIRAEK------SEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDK 76
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEERKRELERIRQEEiameisRMRELERLQMERQQKNERVRQELEAARKVKILEEERQR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 77 ALSNAEGEVA--------ALNRRIQLLEEDLERSEERLNTATTKLAEASQA--ADESERARKCLE------NRANMEDDR 140
Cdd:pfam17380 414 KIQQQKVEMEqiraeqeeARQREVRRLEEERAREMERVRLEEQERQQQVERlrQQEEERKRKKLElekekrDRKRAEEQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 141 VGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEER--AETGESKIVELEEELRVVGNNLK-SLEVSEEKAAQR 217
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRreAEEERRKQQEMEERRRIQEQMRKaTEERSRLEAMER 573
|
250
....*....|
gi 2068700163 218 EDNFEEQIKE 227
Cdd:pfam17380 574 EREMMRQIVE 583
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-170 |
8.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.45 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 1 MDAIKKKMQAMKLEKdnamdradTLEQQNKEANIRAEkSEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSN 80
Cdd:PRK12704 44 LEEAKKEAEAIKKEA--------LLEAKEEIHKLRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700163 81 AEGEVAALNRRIQLLEEDLERSEERLNTAttklaeasqaadeserarkcLENRANM--EDDRVGILETQLAQAKHIAEEA 158
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQE--------------------LERISGLtaEEAKEILLEKVEEEARHEAAVL 174
|
170
....*....|..
gi 2068700163 159 DKKYEEVARKLA 170
Cdd:PRK12704 175 IKEIEEEAKEEA 186
|
|
| |
