|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-280 |
1.60e-68 |
|
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: 212.20 E-value: 1.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 128 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040681749 208 EAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMALNE 280
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAE 233
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
7-152 |
1.43e-25 |
|
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: 98.53 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 7 KMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEgdva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040681749 87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-265 |
5.44e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 81 AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 161 KYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....*
gi 1040681749 241 FAERSVAKLEKTIDDLEDRLYQQLE 265
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-280 |
1.30e-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: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 37 KQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 117 EKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEE 196
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR---LYQQLEKNRLLSNE 273
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrseLRRELEELREKLAQ 926
|
....*..
gi 1040681749 274 LRMALNE 280
Cdd:TIGR02168 927 LELRLEG 933
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-275 |
1.10e-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: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 30 KAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATA 109
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 110 LQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESK 189
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 190 CSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRL 269
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
....*.
gi 1040681749 270 LSNELR 275
Cdd:COG1196 475 LEAALA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-260 |
2.47e-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: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienRALKDEEKMEIQEIQLKEAKHIAEEADRK 161
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-------EAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 162 YEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEF 241
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250
....*....|....*....
gi 1040681749 242 AERSVAKLEKTIDDLEDRL 260
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERL 945
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-247 |
4.38e-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: 56.70 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 18 ALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 98 ELDRAQERLATALQKleeAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELE 177
Cdd:COG4942 98 ELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 178 RTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVA 247
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-280 |
8.77e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 24 QAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQ 103
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 104 ERLATALQKLEEaekaadesergmkvIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERA 183
Cdd:TIGR02168 288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 184 ELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLY-Q 262
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeA 433
|
250
....*....|....*...
gi 1040681749 263 QLEKNRLLSNELRMALNE 280
Cdd:TIGR02168 434 ELKELQAELEELEEELEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-275 |
1.09e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 48 KKLKGTEDELDKYSEALKD--AQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1196 216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 126 GMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLK 205
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 206 SLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 275
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-274 |
7.10e-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: 53.53 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 34 DRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKL 113
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 114 EEAEKAADESERGmkvienralKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSEL 193
Cdd:TIGR02169 761 KELEARIEELEED---------LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 194 EEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNE 273
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
.
gi 1040681749 274 L 274
Cdd:TIGR02169 912 I 912
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
23-278 |
1.10e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 23 EQAEGDKKAAE-DRSKQLEDDLLALQKKlKGTEDELDKYSEALKD--------AQEKLELAEKKATDAEG-DVASLNRRI 92
Cdd:PRK10929 33 EQAKAAKTPAQaEIVEALQSALNWLEER-KGSLERAKQYQQVIDNfpklsaelRQQLNNERDEPRSVPPNmSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 93 -----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIENRALKDEEkmeiqeiqlkeakhiAEEA 158
Cdd:PRK10929 112 lqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 159 DRKYEEVARKLVIVEGELE------RTE---ERAELNESKCSELEEELKTVTNNLKSLEaqaekysQKEdkyeeeikvlt 229
Cdd:PRK10929 177 ALQAESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQALRNQLNSQR-------QRE----------- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1040681749 230 dklkeaetrAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNEL-----RMAL 278
Cdd:PRK10929 239 ---------AERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqaqRMDL 283
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-260 |
1.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 81 AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 161 KYEEVARKLVIVEGELERTEERAELNESKCSELeeELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260
....*....|....*....|
gi 1040681749 241 FAERSVAKLEKTIDDLEDRL 260
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQ 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-260 |
1.35e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV--------------IENRALKDEEKMEIQEIQ 147
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 148 LKEAKHIAEEADRKYEEvARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAekysqkeDKYEEEIKV 227
Cdd:PRK02224 484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA-------AELEAEAEE 555
|
250 260 270
....*....|....*....|....*....|...
gi 1040681749 228 LTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 260
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-260 |
3.44e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 20 DRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAE-------KKATDAEGDVASLNRRI 92
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeidkllAEIEELEREIEEERKRR 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIV 172
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 173 EGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKT 252
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
....*...
gi 1040681749 253 IDDLEDRL 260
Cdd:TIGR02169 513 EEVLKASI 520
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-262 |
4.57e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 38 QLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLE--LAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 116 AEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAkhiaeEADRKYEEVARKLVIVEgelertEERAELNESKCSELEE 195
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA-----ELSARYTPNHPDVIALR------AQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040681749 196 ELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKvltdKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQ 262
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-260 |
5.45e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 47 QKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEG-----------DVASLNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 116 AEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEE 195
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040681749 196 ELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 260
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-259 |
7.88e-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: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 18 ALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEE 97
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELE 177
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 178 RTEER--------AELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKL 249
Cdd:TIGR02168 940 NLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
250
....*....|
gi 1040681749 250 EKTIDDLEDR 259
Cdd:TIGR02168 1020 EEAIEEIDRE 1029
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-266 |
1.38e-06 |
|
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: 48.99 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 43 LLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 122
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 123 SERGMK----VIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELK 198
Cdd:COG4942 95 LRAELEaqkeELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040681749 199 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 266
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
23-261 |
1.92e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 23 EQAEGDKKAAEDRSK--QLEDDLLALQKKLKGTEDELDKYS-----EALKDAQEKLELAEKKATDAEGDVASLNRRIQLV 95
Cdd:PRK05771 40 LSNERLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 96 EEELDRAQerlatALQKLEEAEKAADESERgMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVA---RKLVIV 172
Cdd:PRK05771 120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 173 EGELERTE-ERAELNESKC-----SELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLTDKL----KEAETRAEFA 242
Cdd:PRK05771 194 EEELKKLGfERLELEEEGTpseliREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFL 270
|
250 260 270
....*....|....*....|....*....|..
gi 1040681749 243 -------------ERSVAKLEKTIDDLEDRLY 261
Cdd:PRK05771 271 ktdktfaiegwvpEDRVKKLKELIDKATGGSA 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
18-257 |
1.93e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 18 ALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLnrRIQLVEE 97
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL--EEALNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELE 177
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 178 RTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLE 257
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-125 |
7.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQL---------EDDLLALQKKLKGTEDELDKYSEA---LKDAQE 69
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASsddLAALEE 692
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040681749 70 KLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-269 |
1.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 66 DAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLAT--ALQKLEEAEKAADESERGMKVIEN---RALKDEEK 140
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAeleRLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 141 MEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTN----NLKSLEAQAEKYSQ 216
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleERFAAALGDAVERE 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040681749 217 KEDKYEEEIKVLTDKLKEAETR-----AEFAER---SVAKLEKTIDDLED--RLYQQLEKNRL 269
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEEleramRAFNREwpaETADLDADLESLPEylALLDRLEEDGL 829
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-240 |
1.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 24 QAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRA- 102
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 103 -----QERLATALQKLEEAEKAADESERgMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELE 177
Cdd:COG3883 93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040681749 178 RTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-281 |
2.51e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 5 KKKMQMLKLDKENALDRAEQ---AEGDKKAAEDRSKQLEDDLLALQKKLKGTE----DELDKYSEALKDAQEKLELAEKK 77
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 78 ATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM-KVIENRALKDEEKMEIQEIQLKEAKHIAE 156
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 157 EADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAE 236
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1040681749 237 TRAEFAERSVAKLEKTIDDLEDrLYQQLEKNRLLSNELRMALNED 281
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-275 |
3.06e-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: 45.43 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 59 KYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQE------------------RLATALQKLEEAEKAA 120
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelelallvlRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 121 DESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTV 200
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040681749 201 TNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 275
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-269 |
3.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 20 DRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEEL 99
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 100 DRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARklvIVEGELERT 179
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK---IKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 180 EERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR 259
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
250
....*....|
gi 1040681749 260 LYQQLEKNRL 269
Cdd:PTZ00121 1750 KKDEEEKKKI 1759
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-259 |
4.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAE-KKATD 80
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 81 A-EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEAD 159
Cdd:PTZ00121 1199 ArKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 160 RKYEEVARKLVIVEGELERTEERAELNES--------KCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDK 231
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
250 260
....*....|....*....|....*...
gi 1040681749 232 LKEAETRAEFAERSVAKLEKTIDDLEDR 259
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
33-275 |
4.82e-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: 44.56 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 33 EDRSKQLEDDLLA-------LQKKLKGTEdELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQER 105
Cdd:COG3096 319 SARESDLEQDYQAasdhlnlVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 106 LA-----------------TALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKH---IAEEADRKYEEV 165
Cdd:COG3096 398 LAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 166 ARKLVIVEGELERTE-------------------ERAELNESKCSELEEELktvtNNLKSLEAQAEKYSQKEDKYEEEIK 226
Cdd:COG3096 478 YELVCKIAGEVERSQawqtarellrryrsqqalaQRLQQLRAQLAELEQRL----RQQQNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1040681749 227 VLTDKLKEAETRAEFAERSVAklektiDDLEDR--LYQQLEKNRLLSNELR 275
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAA------EAVEQRseLRQQLEQLRARIKELA 598
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-220 |
7.49e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 16 ENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTE------------DELDKYSEA----LKDAQEKLELAEKKAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 80 DAE--GDvaslNRRIQLVEEELDRAQERLATALQKLEEA-EKAADESERGMKVIENRALKDEEKMEIQEIQLKEAK---- 152
Cdd:NF012221 1638 YAGesGD----QWRNPFAGGLLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEqdid 1713
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040681749 153 HIAEEADRKYEEVARKlvivEGELERTEERAELNESKC-SELEEELKTVTNnlKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1714 DAKADAEKRKDDALAK----QNEAQQAESDANAAANDAqSRGEQDASAAEN--KANQAQADAKGAKQDE 1776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-266 |
7.85e-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: 43.90 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 15 KENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELA-EKKATDAEGDVASLNRRIQ 93
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 94 LVEEELDRAQERLATALQKLEEAEKAADESER--GMKVIENRALKDEEKMEIQEIQLKEAKhiAEEADRKYEEVARKLVI 171
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEReiEEERKRRDKLTEEYAELKEELEDLRAE--LEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 172 VEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEK 251
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250
....*....|....*
gi 1040681749 252 TIDDLEDRlYQQLEK 266
Cdd:TIGR02169 470 ELYDLKEE-YDRVEK 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-259 |
1.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 6 KKMQMLKLDKENA--LDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKySEALKDAQEKLELAEKKATDAEG 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 164 EVARKlvivegelERTEERAELNESKCSELE--EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEF 241
Cdd:PTZ00121 1389 EKKKA--------DEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250
....*....|....*...
gi 1040681749 242 AERSVAKLEKTIDDLEDR 259
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKK 1478
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
52-260 |
2.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 52 GTEDELDKYSEALKDAQEklELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkviE 131
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------E 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 132 NRALKDEEKMEIQEIQ----------------LKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEE 195
Cdd:PRK02224 249 RREELETLEAEIEDLRetiaeterereelaeeVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040681749 196 ELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 260
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-273 |
2.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 82 -EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHI--AEEA 158
Cdd:PTZ00121 1587 kKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 159 DRKYEEVARKlviveGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVltdKLKEAETR 238
Cdd:PTZ00121 1667 AKKAEEDKKK-----AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI---KAEEAKKE 1738
|
250 260 270
....*....|....*....|....*....|....*
gi 1040681749 239 AEFAERSVAKLEKtiDDLEDRLYQQLEKNRLLSNE 273
Cdd:PTZ00121 1739 AEEDKKKAEEAKK--DEEEKKKIAHLKKEEEKKAE 1771
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-226 |
2.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 14 DKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1040681749 174 GELERTEERAELNESKCSElEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIK 226
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-242 |
3.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 13 LDKENALDRAEQA-------EGDKKAAEDRSKQLE--DDLLALQKKLKGTEDELDKYSE-----ALKDAQEKLELAEKKA 78
Cdd:COG4913 218 LEEPDTFEAADALvehfddlERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 79 TDAEGDVASLNRRIQLVEEELDRAQERLATA--------LQKLEEAEKAADESERGMKVIENRALKDEEKmeIQEIQLkE 150
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEAL--LAALGL-P 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 151 AKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKvltD 230
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---E 451
|
250
....*....|..
gi 1040681749 231 KLKEAETRAEFA 242
Cdd:COG4913 452 ALGLDEAELPFV 463
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-268 |
3.50e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 82 EGDVASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 161 KYEEVARKLVIVEGELERTEERAELNESKCSEL---EEELKTVTNNLKSLEAQAEKYSQ---KEDKYEEEIKVLTDKLKE 234
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAkkeAEEDKKKAEEAKKDEEEKKKIAHlkkEEEKKAEEIRKEKEAVIE 1782
|
250 260 270
....*....|....*....|....*....|....
gi 1040681749 235 AETRAEfAERSVAKLEKTIDDLEDRLYQQLEKNR 268
Cdd:PTZ00121 1783 EELDEE-DEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-247 |
3.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 5 KKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGD 84
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEE 164
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 165 VARKlvivegeLERTEERAELNESKCSELEEELKTVTNNLKSLEAQA--EKYSQKEDKYEEEIKVLTDKLKEAETRAEFA 242
Cdd:PTZ00121 1502 AKKA-------AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
....*
gi 1040681749 243 ERSVA 247
Cdd:PTZ00121 1575 DKNMA 1579
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2-152 |
3.70e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLlalqkklkGTEDELDKYSEALKDAQEKLELAEKkatda 81
Cdd:COG1566 65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAEL--------GAEAEIAAAEAQLAAAQAQLDLAQR----- 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040681749 82 egdvaSLNRRIQLVE------EELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEiQLKEAK 152
Cdd:COG1566 132 -----ELERYQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAE 202
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
40-253 |
5.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 40 EDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 120 ADESERGMKVIEnralkdeekmeiqeiQLKEAKHIAEEADRkYEEVARKLVIVEGELERTEERAELNESKCSELEEELKT 199
Cdd:COG3883 95 LYRSGGSVSYLD---------------VLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1040681749 200 VTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTI 253
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-275 |
6.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 23 EQAEGDKKAAEDRSKQLE---DDLLALQKKLKGTEDELDKYSEALKDAQE---KLELAEKKATDA-----EGDVASLNRR 91
Cdd:TIGR02169 173 EKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKREyegYELLKEKEALERqkeaiERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 92 IQLVEEELDRAQERLATALQKLEEaekaadESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVI 171
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 172 VEGELERTEERAELNESKCSELEEELKTVTNNLKSLEaqaekysqkedkyeEEIKVLTDKLKEAETRAEFAERSVAKLEK 251
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK--------------EELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260
....*....|....*....|....
gi 1040681749 252 TIDDLEDRLYQQLEKNRLLSNELR 275
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQ 416
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
52-235 |
9.22e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 52 GTEDELDKYSEALKDAQEklelAEKKATDAEGDVASLNRRIQLVE---EELDRA------QERLATALQKLEEAEK---- 118
Cdd:COG0497 152 GLEELLEEYREAYRAWRA----LKKELEELRADEAERARELDLLRfqlEELEAAalqpgeEEELEEERRRLSNAEKlrea 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 119 ------AADESERG--------MKVIENRALKDEEKMEIQEiQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEER-A 183
Cdd:COG0497 228 lqealeALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlA 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040681749 184 ELNE-------------SKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEA 235
Cdd:COG0497 307 LLRRlarkygvtveellAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
7-231 |
1.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 7 KMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVA 86
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIEN---RALKDEEKMEIQEIQLKEAKHIAEEADRKYE 163
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040681749 164 EVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDK 231
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-258 |
1.50e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 13 LDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRI 92
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEAdrKYEEVARKLV-- 170
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAG--KCPECGQPVEgs 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 171 -IVEGELERTEERAELnESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKyEEEIKVLTDKLKEAETRAEFAERSVAKL 249
Cdd:PRK02224 465 pHVETIEEDRERVEEL-EAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEEL 542
|
....*....
gi 1040681749 250 EKTIDDLED 258
Cdd:PRK02224 543 RERAAELEA 551
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-277 |
1.57e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 20 DRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTE---DELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVE 96
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 97 -------EELDRAQERLATALQKLEEAEKAadesERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARK- 168
Cdd:PTZ00121 1560 aeekkkaEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKv 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 169 --LVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSV 246
Cdd:PTZ00121 1636 eqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270
....*....|....*....|....*....|.
gi 1040681749 247 AKLEKTIDDLEDRLYQQLEKNRLLSNELRMA 277
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-275 |
1.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 97 EELDRAQERLATALQKLE----------EAEKAADESERGMKVIE-NRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEV 165
Cdd:COG4913 235 DDLERAHEALEDAREQIEllepirelaeRYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 166 ARKLVIVEGELERTEERAELN--------ESKCSELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLTDKLKEAET 237
Cdd:COG4913 315 EARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGL---PLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*...
gi 1040681749 238 RAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 275
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
20-224 |
1.92e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 39.59 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 20 DRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGdvaslnrriqlvEEEL 99
Cdd:TIGR00927 688 ERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEG------------KHEV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 100 DRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEkmeiQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERT 179
Cdd:TIGR00927 756 ETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDE----GAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE 831
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1040681749 180 EERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEE 224
Cdd:TIGR00927 832 TGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEE 876
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-251 |
2.17e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 6 KKMQMLKLDKENALDRAEQ---AEGDKKAAEDRSKQLEDDLLALQKKLKGteDELDKYSEALKDAQEKLELAEKKATD-- 80
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEakkADEAKKKAEEAKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAEEAKKADea 1527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 81 ---AEGDVASLNRRIQLVE--EELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHI 154
Cdd:PTZ00121 1528 kkaEEAKKADEAKKAEEKKkaDELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 155 AEEADRKYEEVARKlvivEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKE 234
Cdd:PTZ00121 1608 KAEEAKKAEEAKIK----AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
250
....*....|....*..
gi 1040681749 235 AETRAEFAERSVAKLEK 251
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEE 1700
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
57-266 |
2.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 57 LDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKA 119
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 120 ADESERGMKVIENR--ALKDEEKMEIQEI-QLKEAKHIAEEADRKYEEVARKLVIVEGELERtEERAELNESKCSELEEE 196
Cdd:PRK04863 430 CGLPDLTADNAEDWleEFQAKEQEATEELlSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLREQ 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040681749 197 lKTVTNNLKSLEAQ---AEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 266
Cdd:PRK04863 509 -RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-233 |
2.88e-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: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 81 AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040681749 161 KYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLK 233
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-260 |
3.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 16 ENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAE--------KKATDAEGdVAS 87
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVET-IEE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 88 LNRRIQLVEEELDRAQERLATALQKLEEAEKAAdESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVAR 167
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 168 KLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDkYEEEIKVLTDKLKEAETRAEFAERSVA 247
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLA 630
|
250
....*....|...
gi 1040681749 248 KLEKTIDDLEDRL 260
Cdd:PRK02224 631 EKRERKRELEAEF 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-176 |
3.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 12 KLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEA---------------LKDAQEKLELAEK 76
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlereIERLERELEERER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 77 KATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEiQEIQLKEAKH--I 154
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnI 438
|
170 180
....*....|....*....|..
gi 1040681749 155 AEEADRKYEEVARKLVIVEGEL 176
Cdd:COG4913 439 PARLLALRDALAEALGLDEAEL 460
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-260 |
3.89e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 39 LEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA-------EGDVASLNRRIQLVEEELDRAQERLATALQ 111
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeagldDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 112 KLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCS 191
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 192 ELEEELKTVTNNLKSLEAQAEKYSQKEDKYEE--------------EIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLE 257
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495
|
...
gi 1040681749 258 DRL 260
Cdd:PRK02224 496 ERL 498
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
149-266 |
4.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 149 KEAKHIAEEADRKYEEVARKLVivegeLERTEERAELNEskcsELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVL 228
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKLRN----EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 1040681749 229 TDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 266
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
107-263 |
4.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 107 ATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELN 186
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040681749 187 ESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQ 263
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-133 |
4.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLE--------DDLLALQKKLKGTEDELDKYSEALKDAQEKLE 72
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040681749 73 LAEKKATDAEGDVASLNRRIQL----VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAAlleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
3-156 |
5.12e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 38.10 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 3 AIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKlkgTEDELDKYSEALKDAQEKLELAekkaTDAE 82
Cdd:pfam10168 558 EIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDK---QEKLMRRCKKVLQRLNSQLPVL----SDAE 630
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040681749 83 GDVASLNRRIQLVEEELDRaqeRLATALQKLEEAEK--AADESERGMKVIEnraLKDEEKMEIQEIQLKEAKHIAE 156
Cdd:pfam10168 631 REMKKELETINEQLKHLAN---AIKQAKKKMNYQRYqiAKSQSIRKKSSLS---LSEKQRKTIKEILKQLGSEIDE 700
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
30-266 |
5.78e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 30 KAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATA 109
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 110 LQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEevarKLVIVEGELERTEERAELNESK 189
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA----ALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040681749 190 cSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 266
Cdd:COG4372 190 -KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3-277 |
6.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.57 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 3 AIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAE 82
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 83 GDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKY 162
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 163 EEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFA 242
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270
....*....|....*....|....*....|....*
gi 1040681749 243 ERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMA 277
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-275 |
9.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.05 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 74 AEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAlkDEEKMEIQEIQLKEAKH 153
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 154 IAEEADRKyEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLK 233
Cdd:COG4942 96 RAELEAQK-EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1040681749 234 EAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 275
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-257 |
9.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.43 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGteDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLK--------EAKH 153
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeekkkadEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 154 IAEEAdRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEiKVLTDKLK 233
Cdd:PTZ00121 1439 KAEEA-KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAK 1516
|
250 260
....*....|....*....|....
gi 1040681749 234 EAETRAEFAERSVAKLEKTIDDLE 257
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAK 1540
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-280 |
9.83e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 37.26 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 4 IKKKMQMLKLDKENALDRAEQAEGDkKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEG 83
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQD-KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYE 163
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040681749 164 EVARKLVIVEGELERTEERAElNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAE 243
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDE-LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
250 260 270
....*....|....*....|....*....|....*..
gi 1040681749 244 RSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMALNE 280
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEE 982
|
|
| |
