|
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 |
4.48e-62 |
|
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: 196.02 E-value: 4.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 48 KLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78000194 208 MAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 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 |
8.47e-19 |
|
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: 80.43 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 7 KMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLlaadETAAKAEADVA 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKA----EESEKLKTNNE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78000194 87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-283 |
3.23e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAK 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 161 KYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 78000194 241 FAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 283
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-266 |
5.89e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 165 VARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|..
gi 78000194 245 SVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEE 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-282 |
3.32e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 12 KLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRR 91
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 92 IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVI 171
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 172 IESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 251
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|.
gi 78000194 252 SIDDLEEKVAHAKEENLSMHQMLDQTLLELN 282
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-266 |
4.56e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 37 KQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 117 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 196
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 197 LRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-261 |
2.30e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKA 81
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 82 EADVASLNRRIQLVEEELDRAQERL-------ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHI 154
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 155 AEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKE 234
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
250 260 270
....*....|....*....|....*....|....*
gi 78000194 235 --------AETRAEFAERSVTKLEKSIDDLEEKVA 261
Cdd:TIGR02168 948 eysltleeAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-244 |
2.05e-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: 54.38 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 22 AEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDR 101
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 102 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEA----KHIAEDADRKYEEVARKLVIIESDLE 177
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78000194 178 RAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-283 |
2.43e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 50 LRASEDERDRVL--EELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:COG1196 218 LKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 207
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78000194 208 MAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 283
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-282 |
3.54e-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: 54.29 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 27 ADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDRAQERL 106
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 107 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELS 186
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 187 EGQVRQLEEQLRIMDQTLKALMAAEDKysQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250
....*....|....*.
gi 78000194 267 NLSMHQMLDQTLLELN 282
Cdd:TIGR02168 470 LEEAEQALDAAERELA 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-266 |
1.91e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKA 81
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 82 EADVASLNrriqlveeeldraqERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:TIGR02168 809 RAELTLLN--------------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 162 YEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKE-AETRAE 240
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLE 954
|
250 260
....*....|....*....|....*.
gi 78000194 241 FAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENK 980
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-193 |
2.54e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDrvLEELHKAEDSLLAADETAAKAEAD 84
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*....
gi 78000194 165 VARKLviiESDLERAEERAELSEGQVRQL 193
Cdd:COG4913 767 LRENL---EERIDALRARLNRAEEELERA 792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-226 |
3.40e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 14 DKENALDRAEQA-EADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVlEELHKAEDSLLAADETAAKAEADVASLNRRI 92
Cdd:PTZ00121 1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVII 172
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 78000194 173 ESDLERAEERAELSEGQVRQlEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIK 226
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-267 |
8.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 5 KKKMQMLKLDKENALDRAEQ---AEADKKAAEDRSKQLEEDISAKEKLLRASE----DERDRVLEELHKAEDSLLAADET 77
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 78 AAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIES-RAQKDEEKMEIQEIQLKEAKHIAE 156
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 157 DADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAE 236
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
250 260 270
....*....|....*....|....*....|.
gi 78000194 237 TRAEFAERSVTKLEKSIDDLEEkVAHAKEEN 267
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEE-LKKAEEEN 1659
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-256 |
2.51e-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: 48.51 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 15 KENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQL 94
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 95 VEEELDRAQERLATALQKLEEAEKAADEsergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLviieS 174
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELRELESKR----S 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 175 DLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEdkysqkedkYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSID 254
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---------YSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
..
gi 78000194 255 DL 256
Cdd:TIGR02168 983 EL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-258 |
6.42e-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: 47.36 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 18 ALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEE 97
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLE 177
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 178 RAEERaeLSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYE----------EEIKVLSDKLKEAETRAEFAERSVT 247
Cdd:TIGR02168 940 NLQER--LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKE 1017
|
250
....*....|.
gi 78000194 248 KLEKSIDDLEE 258
Cdd:TIGR02168 1018 TLEEAIEEIDR 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-265 |
7.30e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLA-----ADE 76
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAeevrkAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 77 TAAKAEADVASLNRR---IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKH 153
Cdd:PTZ00121 1193 LRKAEDARKAEAARKaeeERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 154 IAEDAD-----RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYE---EEI 225
Cdd:PTZ00121 1273 KAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEA 1352
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 78000194 226 KVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 265
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-273 |
1.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 12 KLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASE----DERDRVLEELHKAEDSLLAADETAAKAE----A 83
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKKADEAKKAAEAKKKADeakkA 1518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYE 163
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 164 EVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQtLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAE 243
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270
....*....|....*....|....*....|
gi 78000194 244 RSVTKLEKSIDDLEEKVAHAKEENLSMHQM 273
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-246 |
1.08e-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: 46.60 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 39 LEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 118
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 119 AADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLR 198
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 78000194 199 IMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 246
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
22-241 |
1.29e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 22 AEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDErdrvLEELhKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDR 101
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAA----LEEF-RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 102 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEI---------QLKEAKH-IAEDADRKYEEVARKLVI 171
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpDVIALRAqIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 172 IESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEeikvLSDKLKEAETRAEF 241
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-220 |
1.42e-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: 46.37 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 16 ENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRAS---------EDERDRVLEELHKAEDSLLAA----DETAAKAE 82
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTdqnaletngQAQRDAILEESRAVTKELTTLaqglDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 83 ADVASLNR-RIQLVEEELDRAQERLATALQ----KLEEAEKAADESERGMK--VIESRA--QKDEEKMEIQEIQLKEAKh 153
Cdd:NF012221 1638 YAGESGDQwRNPFAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVKdaVAKSEAgvAQGEQNQANAEQDIDDAK- 1716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78000194 154 iaEDADRKYEEVARKlviiESDLERAEERAELSEGQVRQLEEQlRIMDQTLKALMAAEDKYSQKEDK 220
Cdd:NF012221 1717 --ADAEKRKDDALAK----QNEAQQAESDANAAANDAQSRGEQ-DASAAENKANQAQADAKGAKQDE 1776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-266 |
1.55e-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: 46.21 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 20 DRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLlaadetaAKAEADVASLNRRIQLVEEEL 99
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-------SDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 100 DRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKmeIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERA 179
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED--LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 180 EERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEK 259
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
....*..
gi 78000194 260 VAHAKEE 266
Cdd:TIGR02169 891 RDELEAQ 897
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-265 |
2.05e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKA 81
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 162 YEEVARKlviiesdlERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEF 241
Cdd:PTZ00121 1387 AEEKKKA--------DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
250 260
....*....|....*....|....*.
gi 78000194 242 AERSVTKLE--KSIDDLEEKVAHAKE 265
Cdd:PTZ00121 1459 AEEAKKKAEeaKKADEAKKKAEEAKK 1484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-176 |
2.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 6 KKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDI-SAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEAD 84
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiQEIQLKEAKH--IAEDADRKY 162
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnIPARLLALR 446
|
170
....*....|....
gi 78000194 163 EEVARKLVIIESDL 176
Cdd:COG4913 447 DALAEALGLDEAEL 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-284 |
2.98e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 170 VIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKL 249
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190
....*....|....*....|....*....|....*
gi 78000194 250 EKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNNM 284
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-274 |
3.37e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 23 EQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLE------ELHKAEDSLLAADETAakAEADVASLNRRIQLVE 96
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkEKREYEGYELLKEKEA--LERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 97 EELDRAQERLATALQKLEEAEKAADE-SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESD 175
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 176 LERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDD 255
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250
....*....|....*....
gi 78000194 256 LEEKVAHAKEENLSMHQML 274
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAI 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-258 |
3.92e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 7 KMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 87 SLNRRIQLVEEEL------------DRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHI 154
Cdd:TIGR02169 762 ELEARIEELEEDLhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 155 AEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKE 234
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260
....*....|....*....|....
gi 78000194 235 AETRAEFAERSVTKLEKSIDDLEE 258
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEE 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-266 |
4.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 82 -EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHI--AEDA 158
Cdd:PTZ00121 1587 kKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 159 DRKYEEVARKLVII----------ESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVL 228
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270
....*....|....*....|....*....|....*...
gi 78000194 229 SDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-280 |
6.99e-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: 44.28 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 62 EELHKAEDSLLAADETAAKAEADvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKM 141
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELE--ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 142 EIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKY 221
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 78000194 222 EEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLE 280
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-194 |
7.44e-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: 44.28 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAK 80
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGmkviESRAQKDEEKMEIQEIQLKEAKHIA--EDA 158
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----ELQAELEELEEELEELQEELERLEEalEEL 466
|
170 180 190
....*....|....*....|....*....|....*.
gi 78000194 159 DRKYEEVARKLVIIESDLERAEERAELSEGQVRQLE 194
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-260 |
7.64e-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: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAK 80
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 81 AEADVAslNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:TIGR02169 784 LEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 161 KYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAEtRAE 240
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPK 940
|
250 260
....*....|....*....|
gi 78000194 241 FAERSVTKLEKSIDDLEEKV 260
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAEL 960
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-266 |
1.02e-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: 43.52 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 15 KENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHK-AEDSLLAADETAAKAEADVASLNRRIQ 93
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 173
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 174 SDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEF-------AERSV 246
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskYEQEL 471
|
250 260
....*....|....*....|
gi 78000194 247 TKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4-265 |
1.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 4 IKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDErdrvlEELHKAEDsLLAADETAAKAEA 83
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA-----EEAKKAEE-ERNNEEIRKFEEA 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 84 DVASLNRRIQLVEEEldraQERLATALQKLEEAEKA--ADESERGMKVIESRaQKDEEKMEIQEIQLK--EAKHIAEDAD 159
Cdd:PTZ00121 1261 RMAHFARRQAAIKAE----EARKADELKKAEEKKKAdeAKKAEEKKKADEAK-KKAEEAKKADEAKKKaeEAKKKADAAK 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 160 RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL--MAAEDKYSQKEDKYEEEIKVLSDKLKEAET 237
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
250 260 270
....*....|....*....|....*....|
gi 78000194 238 RAEFAERSVTKLE--KSIDDLEEKVAHAKE 265
Cdd:PTZ00121 1416 AKKKADEAKKKAEekKKADEAKKKAEEAKK 1445
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2-152 |
2.22e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKekllrasederdrvlEELHKAEDSLLAADETAAKA 81
Cdd:COG1566 65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAE---------------AEIAAAEAQLAAAQAQLDLA 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78000194 82 EADvasLNRRIQLVE------EELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEiQLKEAK 152
Cdd:COG1566 130 QRE---LERYQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAE 202
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-258 |
2.51e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQ 147
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 148 LKEAKHIAEDADRKYEEvARKLVIIESDLERAEERAELSEGQVRQLEEqlRIMDQTLKALMAAEDKysqkeDKYEEEIKV 227
Cdd:PRK02224 484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRE--TIEEKRERAEELRERA-----AELEAEAEE 555
|
250 260 270
....*....|....*....|....*....|.
gi 78000194 228 LSDKLKEAETRAEFAERSVTKLEKSIDDLEE 258
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-271 |
2.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKE--KLLRASEDERDRVLEELHKAEDSLLAadETAAKAE 82
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 83 ADVASLNRRIQLVE--EELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:PTZ00121 1574 EDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 161 KYEEVARklvIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:PTZ00121 1654 KAEEENK---IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
250 260 270
....*....|....*....|....*....|.
gi 78000194 241 FAERSVTKLEKSIDDLEEKVAHAKEENLSMH 271
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-257 |
2.69e-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: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 28 DKKAAEDRSKQLEEDISAKEKLLRASEDERDRV--LEELHKAEDSLLAADETAAKAEADVASLN-----RRIQLVEEELD 100
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 101 RAQERLATALQKLEEAEKAADESERgmkviesraqkdeekmeiQEIQLKEAkhIAEDADRKYEEVARKLVIIESDLERAE 180
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78000194 181 ERAELSEGQVRQLEEQLrimDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 257
Cdd:COG4913 359 RRRARLEALLAALGLPL---PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
18-276 |
3.37e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 18 ALDRAEQAEADKKAAEDRSKQLEEDISAKEKLlraSEDERDRVLEElhkaEDSLLAADETAAKAEADVASLNRRIQLVEE 97
Cdd:PRK10929 49 ALQSALNWLEERKGSLERAKQYQQVIDNFPKL---SAELRQQLNNE----RDEPRSVPPNMSTDALEQEILQVSSQLLEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 98 ------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIESRAQKDEEkmeiqeiqlkeakhiAEDADRKYEEVARK 168
Cdd:PRK10929 122 srqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 169 LVIIESDLER--AEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEdkyeeeikvlsdklkeaetrAEFAERSV 246
Cdd:PRK10929 187 ALVDELELAQlsANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQRE--------------------AERALEST 246
|
250 260 270
....*....|....*....|....*....|
gi 78000194 247 TKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 276
Cdd:PRK10929 247 ELLAEQSGDLPKSIVAQFKINRELSQALNQ 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-238 |
5.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 13 LDKENALDRAEQAEA---DKKAAEDRSKQLEEDISAKEKLlRASEDERDRVLEELHKAEDSLLAADetAAKAEADVASLN 89
Cdd:COG4913 218 LEEPDTFEAADALVEhfdDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALR--LWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkviesraqkdeEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEA-------------QIRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78000194 170 VIIESDLERAEERAELSEG----QVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:COG4913 362 ARLEALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
83-283 |
7.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 83 ADVASLNRRIQLVEEELDRAQERlatalqkLEEAEKAADESERGMKVIESRAQKDEE----KMEIQEIQLKEAKHIAEDA 158
Cdd:COG1196 165 AGISKYKERKEEAERKLEATEEN-------LERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 159 DRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 78000194 239 AEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 283
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
5-259 |
9.14e-04 |
|
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: 40.73 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEAD 84
Cdd:pfam02463 201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:pfam02463 281 KKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 165 VARKLVIIESDLERAE----ERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:pfam02463 361 LEKLQEKLEQLEEELLakkkLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIE 440
|
250
....*....|....*....
gi 78000194 241 FAERSVTKLEKSIDDLEEK 259
Cdd:pfam02463 441 LKQGKLTEEKEELEKQELK 459
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-268 |
1.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAK 80
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQ--LKEAKHIAEDA 158
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 159 DRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270
....*....|....*....|....*....|
gi 78000194 239 AEFAERSVTKLEKSIDDLEEKVAHAKEENL 268
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
12-276 |
1.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 12 KLDKENALDRAEQAEADkkAAEDRSKQLEEDI-SAKEKLLRASEDER-----DRVLEELHKAEDSLLAADETAAKAEADV 85
Cdd:PRK04863 301 QLAAEQYRLVEMARELA--ELNEAESDLEQDYqAASDHLNLVQTALRqqekiERYQADLEELEERLEEQNEVVEEADEQQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 86 ASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEK---AADESERGMKVIESRAQKDEEKMEIQE 145
Cdd:PRK04863 379 EENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 146 IQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEgQVRQLEEQlRIMDQTLKAL---MAAEDKYSQKEDKYE 222
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQ-RHLAEQLQQLrmrLSELEQRLRQQQRAE 536
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 78000194 223 EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 276
Cdd:PRK04863 537 RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-185 |
2.18e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 5 KKKMQMLKLDK-ENALDRAEQ---AEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADEtAAK 80
Cdd:PTZ00121 1604 EKKMKAEEAKKaEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKK 1682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA-ADESERGMKVIESRAQKDEEKMEIQEIQLKEAK-----HI 154
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiaHL 1762
|
170 180 190
....*....|....*....|....*....|..
gi 78000194 155 AEDADRKYEEVAR-KLVIIESDLERAEERAEL 185
Cdd:PTZ00121 1763 KKEEEKKAEEIRKeKEAVIEEELDEEDEKRRM 1794
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
70-266 |
3.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 70 SLLAADETAAKAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLK 149
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 150 EAKHIAEDADRKYEEVARKLVIIESDLErAEERAELSeGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLS 229
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDVLLG-SESFSDFL-DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 78000194 230 DKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-268 |
3.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRAseDERDRVLEELHKAEDSLLAADETAAKA 81
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLK--------EAKH 153
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeekkkadEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 154 IAEDAdRKYEEVARKlviieSDLERAEERAELSEGQVRQLEEQLRIMDQTLKA----LMAAEDKYSQKEDKYEEEIKVLS 229
Cdd:PTZ00121 1439 KAEEA-KKADEAKKK-----AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeakKKAEEAKKKADEAKKAAEAKKKA 1512
|
250 260 270
....*....|....*....|....*....|....*....
gi 78000194 230 DKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENL 268
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-257 |
3.75e-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: 38.80 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAK 80
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER---LSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 161 KYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
250
....*....|....*..
gi 78000194 241 FAERSVTKLEKSIDDLE 257
Cdd:pfam02463 497 ERSQKESKARSGLKVLL 513
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
18-166 |
4.21e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 38.31 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 18 ALDRAEQAEADKKAAEDRSKqleeDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADvaslnRRIQLVEE 97
Cdd:PRK12472 199 AEDAARAADEAKTAAAAAAR----EAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAE-----ERQQKAAQ 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78000194 98 ELDRAQERLATALQKLEEAEKAADESERGMKVIESRAqkdeekmeiqeiqlKEAKHIAEDADRKYEEVA 166
Cdd:PRK12472 270 QAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKK--------------AETAKAATDAKLALEPVS 324
|
|
| DUF5930 |
pfam19353 |
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ... |
31-133 |
4.32e-03 |
|
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.
Pssm-ID: 466052 [Multi-domain] Cd Length: 320 Bit Score: 38.24 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 31 AAEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLlaaDETAAKAEADVASLNRRIQLVEEELDR-AQERLAtA 109
Cdd:pfam19353 123 ASEERRRELETGIEVIQSTLRRTMKERDAARAELAALQAEL---EGGGAAAAARAADADATLDFLTAALAEtAAERDQ-I 198
|
90 100
....*....|....*....|....
gi 78000194 110 LQKLEEAEKAADESERGMKVIESR 133
Cdd:pfam19353 199 AADAQDALAEADELALEIRLMEER 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
32-240 |
4.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 32 AEDRSKQLEEDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETAAKAEADVASLNRRIQLVEEELDRAQERLATALQ 111
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 112 KLEEAEKAADESE------------RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERA 179
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78000194 180 EERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-266 |
4.98e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 15 KENALDRAEQAEADKKAAEDR---SKQLEEDISAKEKLLRASEDERdrvLEELHKAEDSLLAadETAAKAEADVASLNRR 91
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKkteTGKAEEARKAEEAKKKAEDARK---AEEARKAEDARKA--EEARKAEDAKRVEIAR 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 92 iqLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAdRKYEEVARKLVI 171
Cdd:PTZ00121 1159 --KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA-KKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000194 172 IESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 251
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250
....*....|....*
gi 78000194 252 SIDDLEEKVAHAKEE 266
Cdd:PTZ00121 1316 KADEAKKKAEEAKKK 1330
|
|
| |
