|
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 |
2.09e-61 |
|
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: 194.09 E-value: 2.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 48 KKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 128 KVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785335257 208 EAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQTLLELN 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 |
2.65e-23 |
|
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: 92.75 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 7 KMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEaeva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785335257 87 SLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-284 |
1.80e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 5 KKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAE 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 85 VASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 165 VARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEK 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1785335257 245 SVVKLEKTIDDLEENLSAAKEESIELNQTLDQTLLELNNM 284
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-282 |
3.09e-14 |
|
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: 72.78 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 23 EQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRA 102
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 103 QERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEER 182
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 183 AEVAESKCGDLEEELKNVTNNLKSLEAQadkyaskEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSA 262
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260
....*....|....*....|
gi 1785335257 263 AKEESIELNQTLDQTLLELN 282
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-266 |
8.23e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 1 MDAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATD 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 81 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 161 KYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....*.
gi 1785335257 241 FAEKSVVKLEKTIDDLEENLSAAKEE 266
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-251 |
9.13e-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: 59.30 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 11 LKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNR 90
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 91 RIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARK-- 168
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKva 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 169 ------------LVVLEGDLERSEERAEVAESKCGDLEEELKNvtNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETD 236
Cdd:TIGR02168 390 qlelqiaslnneIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250
....*....|....*
gi 1785335257 237 GRVEFAEKSVVKLEK 251
Cdd:TIGR02168 468 EELEEAEQALDAAER 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-233 |
1.01e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDA 81
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 82 EAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRK 161
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785335257 162 YEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLK 233
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-282 |
2.23e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 51 KSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVI 130
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 131 ENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQ 210
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 211 ADKYASKEDKYEDEI-------------------KLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELN 271
Cdd:TIGR02168 395 IASLNNEIERLEARLerledrrerlqqeieellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250
....*....|.
gi 1785335257 272 QTLDQTLLELN 282
Cdd:TIGR02168 475 QALDAAERELA 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-276 |
6.21e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 30 KQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 110 LQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQL-----REAKNIAEESDRKYEEVARKLVVLEGDLERSEERAE 184
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 185 VAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAK 264
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250
....*....|..
gi 1785335257 265 EESIELNQTLDQ 276
Cdd:TIGR02169 903 RKIEELEAQIEK 914
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-258 |
7.32e-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: 56.60 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 18 AIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEE 97
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 98 ELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLE 177
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 178 RSEER--------AEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKL 249
Cdd:TIGR02168 940 NLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
....*....
gi 1785335257 250 EKTIDDLEE 258
Cdd:TIGR02168 1020 EEAIEEIDR 1028
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-239 |
1.00e-08 |
|
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: 55.54 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 18 AIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 98 ELDRAQERLATALQKLEETEK----AVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLE 173
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785335257 174 GDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRV 239
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-258 |
1.68e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQI-EEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATD 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 81 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDR 160
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 161 KYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVE 240
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
250
....*....|....*...
gi 1785335257 241 FAEKSVVKLEKTIDDLEE 258
Cdd:TIGR02169 487 KLQRELAEAEAQARASEE 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-257 |
2.42e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 22 AEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDR 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 102 AQERLATALQKLEETEKAVDESERGMKV--------------IENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEvAR 167
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 168 KLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVV 247
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250
....*....|
gi 1785335257 248 KLEKTIDDLE 257
Cdd:PRK02224 583 ELKERIESLE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-262 |
2.55e-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: 54.68 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDA 81
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 82 EAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEEsdrk 161
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES---- 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 162 yeevarklvvLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEF 241
Cdd:TIGR02168 857 ----------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250 260
....*....|....*....|.
gi 1785335257 242 AEKSVVKLEKTIDDLEENLSA 262
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-284 |
7.83e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 65 KEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQ 144
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 145 EQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELK-------NVTNNLKSLEAQADKYASK 217
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLRERLESLERRIAATERR 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785335257 218 EDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQTLLELNNM 284
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
57-276 |
9.00e-08 |
|
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: 53.03 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 57 VEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEETEKA 119
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARAL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 120 VDESERGMKVIENRATKDEEKMVDQEQQLREAK---NIAEESDRKYEEVARKLVVLEGDLERSEErAEVAESKCGDLeEE 196
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEEVLELEqklSVADAARRQFEKAYELVCKIAGEVERSQA-WQTARELLRRY-RS 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 197 LKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFA---EKSVVKLEKTIDDLEENLSAAKEESIELNQT 273
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
...
gi 1785335257 274 LDQ 276
Cdd:COG3096 587 LEQ 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-258 |
1.27e-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: 52.76 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 7 KMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 87 SLNRRIQLVEEELDRAQERLAT---------------ALQKLEETEKAVDESERGMKVIENRATKDEEKMvdqEQQLREA 151
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDlearlshsripeiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL---EKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 152 KNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEK 231
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260
....*....|....*....|....*..
gi 1785335257 232 LKETDGRVEFAEKSVVKLEKTIDDLEE 258
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-266 |
3.09e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 67 AQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLAtALQKLEEtekaVDESERGMKVIENRAtkdeekmvdqeQ 146
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREI-----------A 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 147 QLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEik 226
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-- 749
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1785335257 227 LLSEKLKETDGRvEFAEKSVVKLEKTIDDLEENLSAAKEE 266
Cdd:COG4913 750 LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEE 788
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
31-236 |
3.54e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 31 QAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATAL 110
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 111 QKLEETEKAVDESE------------RGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLER 178
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785335257 179 SEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETD 236
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
23-276 |
1.01e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 23 EQAEGDKKQAEdrckqiEEEVMALQ------KKTKSTEDEVEKYSESV-------KEAQEKL--EMAEKKATDAEAEVAS 87
Cdd:PRK10929 33 EQAKAAKTPAQ------AEIVEALQsalnwlEERKGSLERAKQYQQVIdnfpklsAELRQQLnnERDEPRSVPPNMSTDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 88 LNRRI-----QLVEE------ELDRAQE---RLATALQKLEETEKAVDESERGMKVIENRATKdeekmvdqeqqLREAKN 153
Cdd:PRK10929 107 LEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTP-----------LAQAQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 154 IAeesdRKYEEVARKLVVLEGDL---------ERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQAdkyaskedkyede 224
Cdd:PRK10929 176 TA----LQAESAALKALVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQRE------------- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1785335257 225 ikllseklketdgrVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQ 276
Cdd:PRK10929 239 --------------AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQ 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-267 |
1.48e-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: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 22 AEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDR 101
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 102 AQERLATALQKLEETekavdesergMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEE 181
Cdd:COG4942 95 LRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 182 RAEvaeskcgDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLS 261
Cdd:COG4942 165 LRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*.
gi 1785335257 262 AAKEES 267
Cdd:COG4942 238 AAAERT 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-281 |
1.90e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 70 KLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKD-------EEKMV 142
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 143 DQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYE 222
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785335257 223 DEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQTLLEL 281
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-208 |
2.38e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 1 MDAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATD 80
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 81 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESErgMKVIENRATKDEEKMVDQEQQLREAKNIAEESDR 160
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELRE 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1785335257 161 KYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLE 208
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-282 |
5.67e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 57 VEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAqERLATALQKLEETEKAV-----DESERGMKVIE 131
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKA-ERYKELKAELRELELALlvlrlEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 132 NRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQA 211
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785335257 212 DKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQTLLELN 282
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
57-276 |
6.31e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 57 VEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEETEK- 118
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 119 ------AVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARklvvLEGDLERSEErAEVAESKCGD 192
Cdd:PRK04863 430 cglpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRK----IAGEVSRSEA-WDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 193 LEEElKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSE---KLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIE 269
Cdd:PRK04863 505 LREQ-RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEfckRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA 583
|
....*..
gi 1785335257 270 LNQTLDQ 276
Cdd:PRK04863 584 LRQQLEQ 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-233 |
8.10e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 1 MDAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATD 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 81 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDR 160
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785335257 161 KYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLK 233
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2-150 |
8.87e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAED-RCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMA---EKK 77
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEeEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785335257 78 ATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERG----MKVIENrATKDEEKMVDQEQQLRE 150
Cdd:COG2433 460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGelvpVKVVEK-FTKEAIRRLEEEYGLKE 535
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-178 |
1.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDR---CKQIEE------EVMALQKKTKSTEDEVEKYSES---VKEAQE 69
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEyswdeiDVASAEREIAELEAELERLDASsddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 70 KLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERgmkvienratKDEEKMVDQEQQLR 149
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR----------ALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*....
gi 1785335257 150 EAKNIAEESDRKYEEVARKLVVLEGDLER 178
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELER 791
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-220 |
1.76e-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: 45.98 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 16 ENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTE------------DEVEKYSESV----KEAQEKLEMAEKKAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAVtkelTTLAQGLDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 80 DAEAE--------VASLNRRIQ--------LVEEELDRAQERLATALQKLeetEKAVDESERGMKvienratKDEEKMVD 143
Cdd:NF012221 1638 YAGESgdqwrnpfAGGLLDRVQeqlddakkISGKQLADAKQRHVDNQQKV---KDAVAKSEAGVA-------QGEQNQAN 1707
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785335257 144 QEQQLREAKNIAEEsdRKYEEVARKlvvleGDLERSEERAEVAESKCGDL-EEELKNVTNnlKSLEAQADKYASKEDK 220
Cdd:NF012221 1708 AEQDIDDAKADAEK--RKDDALAKQ-----NEAQQAESDANAAANDAQSRgEQDASAAEN--KANQAQADAKGAKQDE 1776
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-234 |
1.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 38 QIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLE--MAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 116 TEKAVDESERGMKVIENRATKDE--EKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAevaeskcgdl 193
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---------- 314
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1785335257 194 eeeLKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKE 234
Cdd:COG3206 315 ---LASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
37-274 |
2.36e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 37 KQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVAslnrRIQLVEEELDRAQERLATALQKLEET 116
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 117 EKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEE 196
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785335257 197 LKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTL 274
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
22-236 |
2.96e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 22 AEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKY---------SESVKEAQEKLEMAEKKATDAEAEVASLNRRI 92
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 93 QLVEEELDRAQERLATALQK--LEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNiaeesdRKYEEVARKLV 170
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA------QLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785335257 171 VLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDeiklLSEKLKETD 236
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES----LLQRLEEAR 378
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
41-259 |
3.54e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 41 EEVMALQKKTKSTEDEVEKYS--ESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQerlatALQKLEETEK 118
Cdd:PRK05771 63 RSYLPKLNPLREEKKKVSVKSleELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----PWGNFDLDLS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 119 AVDESERgMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKY-------------EEVARKLVVLEGDLERSEERAEV 185
Cdd:PRK05771 138 LLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsdevEEELKKLGFERLELEEEGTPSEL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 186 AESkcgdLEEELKNVTNNLKSLEAQADKYAskeDKYEDEIKLLSEKL----KETDGRVEFA-------------EKSVVK 248
Cdd:PRK05771 217 IRE----IKEELEEIEKERESLLEELKELA---KKYLEELLALYEYLeielERAEALSKFLktdktfaiegwvpEDRVKK 289
|
250
....*....|.
gi 1785335257 249 LEKTIDDLEEN 259
Cdd:PRK05771 290 LKELIDKATGG 300
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-184 |
8.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 30 KQAEDRCKQIEEEVMAL-----QKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVE-EELDRAQ 103
Cdd:COG4913 265 AAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 104 ERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERA 183
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
.
gi 1785335257 184 E 184
Cdd:COG4913 425 E 425
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-272 |
1.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 5 KKKMQMLKLDKENAIDRAEQ---AEGDKKQAEDRCKQIEEEVMALQKKTKSTE----DEVEKYSESVKEAQEKLEMAE-K 76
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEeA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 77 KATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAE 156
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 157 ESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETD 236
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
250 260 270
....*....|....*....|....*....|....*.
gi 1785335257 237 GRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQ 272
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-259 |
1.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 55 DEVEKYSESVKEAQEKLEMAEKKATDAEaEVASLNRRIQLVEEELDRAqeRLATALQKLEETEKAVDESERGMKVIENRA 134
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 135 TKDEEKMVDQEQQLREAKN-IAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEElknVTNNLKSLEAQADK 213
Cdd:COG4913 312 ERLEARLDALREELDELEAqIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP---LPASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1785335257 214 YASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEEN 259
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-281 |
3.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 13 LDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRI 92
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 93 QLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVL 172
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPH 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 173 EGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEaQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKT 252
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
250 260
....*....|....*....|....*....
gi 1785335257 253 IDDLEENLSAAKEESIELNQTLDQTLLEL 281
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-276 |
6.29e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 115 ETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLE 194
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 195 EELKNvtnnlksLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTL 274
Cdd:TIGR02168 754 KELTE-------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
..
gi 1785335257 275 DQ 276
Cdd:TIGR02168 827 ES 828
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
23-283 |
6.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 23 EQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRA 102
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 103 QERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEER 182
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 183 AEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSA 262
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
250 260
....*....|....*....|.
gi 1785335257 263 AKEESIELNQTLDQTLLELNN 283
Cdd:COG4372 295 LKLLALLLNLAALSLIGALED 315
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-252 |
6.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAE-KKATD 80
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 81 A-EAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESd 159
Cdd:PTZ00121 1199 ArKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 160 RKYEEVARKLVVLEGD-LERSEERAEVAESKCGDLE----EELKNVTNNLKSlEAQADKYASKEDKYEDEIKLLSEKLKE 234
Cdd:PTZ00121 1278 RKADELKKAEEKKKADeAKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
250
....*....|....*...
gi 1785335257 235 TDGRVEFAEKSVVKLEKT 252
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKE 1374
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-266 |
7.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 82 -EAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNI--AEES 158
Cdd:PTZ00121 1587 kKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 159 DRKYEEVARKLVVL----------EGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLL 228
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785335257 229 SEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEE 266
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-272 |
1.10e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 14 DKENAIDRAEQAEGDKKQAEDRCKQIEEEVMA--LQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRR 91
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 92 IQLVE-EELDRAQERLATALQKLEETEKAvdesERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLV 170
Cdd:PTZ00121 1561 EEKKKaEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 171 VLEGDLERSEERAEVAESKcgdlEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAEKSVVKLE 250
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKA----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
250 260
....*....|....*....|..
gi 1785335257 251 KTIDDLEENLSAAKEESIELNQ 272
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEE 1734
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-266 |
1.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 5 KKKMQMLKLDKENAIDRAEQ---AEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDA 81
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEakkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 82 EAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRK 161
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 162 YEEVARKlvvlEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEF 241
Cdd:PTZ00121 1642 EAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
250 260
....*....|....*....|....*
gi 1785335257 242 AEKSVVKLEKTIDDLEENLSAAKEE 266
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
61-276 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 61 SESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEK 140
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 141 MVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDK 220
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785335257 221 YEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQ 276
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-246 |
1.36e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 5 KKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKT---KSTEDEVEKYSESVKEAQEKLEMAE------ 75
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEedkkka 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 76 ---KKATDAEAEVASLNRRIQLVE--EELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLRE 150
Cdd:PTZ00121 1408 delKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 151 AKNIAEESDRKYEEVARKlvvlEGDLERSEERAEVAESKCGDleeELKNVTNNLKSLEAQA--DKYASKEDKYEDEIKLL 228
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKKAD---EAKKAEEAKKADEAKKaeEKKKADELKKAEELKKA 1560
|
250
....*....|....*...
gi 1785335257 229 SEKLKETDGRVEFAEKSV 246
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNM 1578
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
82-282 |
1.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 82 EAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKavdesERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRK 161
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 162 YEEVARKLVVLEGDLERSEERAEVAEskcgdLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLK-ETDGRVE 240
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILA 316
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785335257 241 FAEKSVVKLEKTIDDLEENLSAAKEESIELNQTLDQtLLELN 282
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLE 357
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2-152 |
1.47e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.65 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVmalqkktkSTEDEVEKYSESVKEAQEKLEMAEKkatda 81
Cdd:COG1566 65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAEL--------GAEAEIAAAEAQLAAAQAQLDLAQR----- 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785335257 82 eaevaSLNRRIQLVE------EELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKdEEKMVDQEQQLREAK 152
Cdd:COG1566 132 -----ELERYQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAA-QAQVAQAEAALAQAE 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-245 |
1.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 6 KKMQMLKLDKENA--IDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKySESVKEAQEKLEMAEKKATDAEA 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 84 EVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 164 EVaRKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFAE 243
Cdd:PTZ00121 1389 EK-KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
..
gi 1785335257 244 KS 245
Cdd:PTZ00121 1468 EA 1469
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3-158 |
1.70e-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: 39.14 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 3 AIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMA--EKKATD 80
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785335257 81 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEES 158
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
29-266 |
2.05e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 39.61 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 29 KKQAEDRCKQIEEEVMALQKKTKSTEDEVEKyseSVKEAQEKLEMAEKKATDAEAE---------VASLNRRIQLVEEEL 99
Cdd:NF033838 109 EKSEAELTSKTKKELDAAFEQFKKDTLEPGK---KVAEATKKVEEAEKKAKDQKEEdrrnyptntYKTLELEIAESDVEV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 100 DRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEV-------------A 166
Cdd:NF033838 186 KKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKnvatseqdkpkrrA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 167 RKLVVLEGDLE-RSEERAEVAESKCGD-------LEEELKNVTNNLKSLEAQADKYASKEDKYED----EIKLLSEKLKE 234
Cdd:NF033838 266 KRGVLGEPATPdKKENDAKSSDSSVGEetlpspsLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyptnTYKTLELEIAE 345
|
250 260 270
....*....|....*....|....*....|..
gi 1785335257 235 TDGRVEFAEKSVVKLEKTIDDLEENLSAAKEE 266
Cdd:NF033838 346 SDVKVKEAELELVKEEAKEPRNEEKIKQAKAK 377
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3-266 |
2.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 3 AIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAE 82
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 83 AEVASLNRRIQLVEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKY 162
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 163 EEVARKLVVLEGDLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADKYASKEDKYEDEIKLLSEKLKETDGRVEFA 242
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260
....*....|....*....|....
gi 1785335257 243 EKSVVKLEKTIDDLEENLSAAKEE 266
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEA 291
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
54-284 |
2.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 54 EDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLnRRIQLVEEELDRAQERLATalQKLEETEKAVDESERGMKVIENR 133
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAE--LEYLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 134 ATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLvvlegdLERSEERAEVAESKCGDLEEELKNVTNNLKSLEAQADK 213
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785335257 214 YASKEDKYEDEIKLLSEKLKETDGRVEFAEksvvklektiDDLEENLSAAKEESIELNQTLDQTLLELNNM 284
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEEL----------EALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-265 |
3.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 2 DAIKKKMQMLKLDKENAIDRAEQAEGDKKQAEDRCKQIEE-EVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKkATD 80
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-LKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 81 AEAEVASLNRRIQLVEEELDRAQE-RLATALQKLEETEKAVDESERGMKVIENR-ATKDEEKMVDQEQQLREAKNIAEES 158
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKkAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 159 DRKYEEVARKLVVLEGDLERSEERAEVAESKcgdlEEELKNVTNNLKSLEAQADKYA---SKEDKYEDEIKLLSEKLKEt 235
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAhlkKEEEKKAEEIRKEKEAVIE- 1782
|
250 260 270
....*....|....*....|....*....|
gi 1785335257 236 DGRVEFAEKSVVKLEKTIDDLEENLSAAKE 265
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
14-187 |
3.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 14 DKENAIDRAEQAEGDKKQAEDRCKQIEEEVMALQKKTKSTEDEVEKYsesvkEAQEKLEMAEKKATDAEAEVASLNRRIQ 93
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 94 LVE---EELDRAQERLATALQKLEETEKAVDESERGMKV-IENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKL 169
Cdd:COG4717 150 ELEerlEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....*...
gi 1785335257 170 VVLEGDLERSEERAEVAE 187
Cdd:COG4717 230 EQLENELEAAALEERLKE 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-238 |
6.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.20 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 14 DKENAIDRAEQAEGDKKQAEDRCKQIEEEvmalQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRiq 93
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 94 lvEEELDRAQERLATALQKLEETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLE 173
Cdd:PTZ00121 1387 --AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785335257 174 GDLERSEERAEVAESKCGDLEEELKNVTNNLKSlEAQADKYASKEDKYEDEIKLLSEKLKETDGR 238
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
55-198 |
6.29e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 37.75 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 55 DEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLAtALQKLeeTEK---AVDEsergmkVIE 131
Cdd:COG0497 254 ERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLA-LLRRL--ARKygvTVEE------LLA 324
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785335257 132 NRATKDEE--KMVDQEQQLREAKNIAEESDRKYEEVARKLvvlegdlerSEERAEVAESKCGDLEEELK 198
Cdd:COG0497 325 YAEELRAElaELENSDERLEELEAELAEAEAELLEAAEKL---------SAARKKAAKKLEKAVTAELA 384
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-283 |
9.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 37.35 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 34 DRCKQIEEEVMALQKKTKSTEDEVEKYSESVKEAQEKLEMAEKKATDAEAEVASLNRRIQLVEEELDRAQERLatalQKL 113
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 114 EETEKAVDESERGMKVIENRATKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKLVVLEGDLERSEERAEVAESKcGDL 193
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 194 EEELKNVTNNLKSLEAQADKYASKedkyEDEIKLLSEKLKETDGRVEFAEKSVVKLEKTIDDLEENLSAAKEESIELNQT 273
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388
|
250
....*....|
gi 1785335257 274 LDQTLLELNN 283
Cdd:PRK03918 389 LEKELEELEK 398
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
90-236 |
9.46e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 37.50 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785335257 90 RRIQLVEEELDRAQERLATALQKLEEtekavdesergmkVIEnratKDEEKMVDQEQQLREAKNIAEESDRKYEEVARKL 169
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNE-------------LIA----SLEELERELEQKAEEAEALLKEAEKLKEELEEKK 557
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785335257 170 VVLEGDLERSEERAEV-AESKCGDLEEELKNVTNNLKSLEaQADKYASKEDKYEDEIKLLSEKLKETD 236
Cdd:PRK00409 558 EKLQEEEDKLLEEAEKeAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKE 624
|
|
| |
