|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
38-272 |
4.99e-63 |
|
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: 197.94 E-value: 4.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 38 KRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMR 117
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 118 KVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNLKSL 197
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3080761 198 EVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 272
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1-142 |
4.61e-22 |
|
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: 88.90 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 1 MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEgevaALNR 80
Cdd:pfam12718 5 LKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3080761 81 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR 142
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-266 |
5.51e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 25 RAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLA 104
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 105 EASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELE 184
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 185 EELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDEL 264
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
..
gi 3080761 265 DQ 266
Cdd:COG1196 473 AL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-256 |
4.35e-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: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 3 LEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRI 82
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 83 QLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMV 162
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 163 EADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKE 242
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|....
gi 3080761 243 VDRLEDELVNEKEK 256
Cdd:COG1196 472 AALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-267 |
2.01e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 13 DTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERS 92
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 93 EERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEER 172
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 173 AETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVN 252
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250
....*....|....*
gi 3080761 253 EKEKYKSITDELDQT 267
Cdd:TIGR02168 920 LREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-260 |
2.77e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 2 KLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRR 81
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 82 IQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAM 161
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 162 VEADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQK 241
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
250
....*....|....*....
gi 3080761 242 EVDRLEDELVNEKEKYKSI 260
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGV 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-271 |
7.24e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 26 AEKAEEeVHNLQKRMQQLE-----NDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTAT 100
Cdd:COG1196 209 AEKAER-YRELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 101 TKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKF 180
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 181 VELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSI 260
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|.
gi 3080761 261 TDELDQTFSEL 271
Cdd:COG1196 448 AEEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-253 |
8.69e-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: 65.08 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 13 DTLEQQNKEAN----IRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEED 88
Cdd:TIGR02168 203 KSLERQAEKAErykeLKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 89 LERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLER 168
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 169 AEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLED 248
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
....*
gi 3080761 249 ELVNE 253
Cdd:TIGR02168 443 EELEE 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-260 |
2.06e-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: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 1 MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNR 80
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 81 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLA 160
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 161 MVEADLERAEERAETGESKFVELeeELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQ 240
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250 260
....*....|....*....|
gi 3080761 241 KEVDRLEDELVNEKEKYKSI 260
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-266 |
3.14e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 1 MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNR 80
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 81 RIQLLEEDLERSEERLNTATTKLAEaSQAADESERMRKVLENRSlSDEERMDALENQLKEARFLAEEADRKYDEVARKLA 160
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSH-SRIPEIQAELSKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 161 MVEADLERAEERAETGESKFVELEEElrvvgnnLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQ 240
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260
....*....|....*....|....*.
gi 3080761 241 KEVDRLEDELVNEKEKYKSITDELDQ 266
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-223 |
4.53e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 22 ANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATT 101
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 102 KLAE----------ASQAADESERMRKVLENRSLSDEERMDALENQLKEARF-LAEEADRKYDEVARKLAMVEADLERAE 170
Cdd:COG4942 98 ELEAqkeelaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3080761 171 ERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLK 223
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10-183 |
1.13e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 10 DRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLEN---------DLDQVQESLLKANTQLEEkdkaLSNAEGEVAALNR 80
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELER----LDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 81 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLa 160
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL- 771
|
170 180
....*....|....*....|...
gi 3080761 161 mvEADLERAEERAETGESKFVEL 183
Cdd:COG4913 772 --EERIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-247 |
1.49e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 3 LEKDNAMDRADTLEQQNKEANiraeKAEEEVHNLQKRMQQLEnDLDQVQESLLKANTQLEEKDKALSNAEGEVAAlnRRI 82
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLE----RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQ--RRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 83 QLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDE-ERMDALENQLKEARflaeeadRKYDEVARKLAM 161
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLE-------RELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 162 VEADLERAEERAETGESKFVELEEELRvvgnnlkslevseekanQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQK 241
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAA-----------------ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*.
gi 3080761 242 EVDRLE 247
Cdd:COG4913 427 EIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-250 |
1.72e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 1 MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNR 80
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 81 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEA------------ 148
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieeleelie 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 149 ---------DRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLT 219
Cdd:TIGR02168 870 eleselealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
250 260 270
....*....|....*....|....*....|..
gi 3080761 220 N-KLKAAEARAEFAERSVQKLQKEVDRLEDEL 250
Cdd:TIGR02168 950 SlTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-272 |
6.60e-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: 53.52 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 35 NLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESE 114
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 115 RMRKVLENRSLSDEERMDALENQLKEARflaeeadrkydevaRKLAMVEADLERAEERAETGESKFVELEEELRVVGNNL 194
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAE--------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3080761 195 KSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 272
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-216 |
3.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 10 DRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDL 89
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 90 ERSEERLNTATTKLAEASQAADESERMRKVLENRSLsdEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERA 169
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIE--ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3080761 170 EERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIK 216
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
29-216 |
5.22e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 29 AEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQ 108
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 109 AADESERMRK----VLENRSLSDE-ERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVEL 183
Cdd:COG3883 94 ALYRSGGSVSyldvLLGSESFSDFlDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|...
gi 3080761 184 EEELRVVGNNLKSLEVSEEKANQREEAYKEQIK 216
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-257 |
1.24e-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: 49.30 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 27 EKAEEEVHNLQKRMQQLENDLDQVQESL--------LKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNT 98
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 99 ATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGES 178
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3080761 179 KFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKY 257
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-193 |
2.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 16 EQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLE-EDLERSEE 94
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 95 RLNTATTKLAEASQAADESERMRKVLEnrsLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAE 174
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|....*....
gi 3080761 175 tgeskfvELEEELRVVGNN 193
Cdd:COG4913 423 -------ELEAEIASLERR 434
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
57-274 |
3.06e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 57 ANTQLEEKDKALSNAEGEVAALNRRIQLLEE-DLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALe 135
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 136 NQLKEARFLAEEadrKYDEVARKLAMVE---------ADLERAEERAETGESKFVELEEELRvvgnnlkSLEVSEEKANQ 206
Cdd:PHA02562 258 NKLNTAAAKIKS---KIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLE-------KLDTAIDELEE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3080761 207 REEAYKEQIKT---LTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY 274
Cdd:PHA02562 328 IMDEFNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
35-267 |
3.23e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 35 NLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSN--AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE 112
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 113 SERM--RKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEvaRKLAMVEADLERAEERAetgeskfvELEEELRVV 190
Cdd:COG3206 245 LRAQlgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDVIALRAQIAALRA--------QLQQEAQRI 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3080761 191 gnnLKSLEVSEEKANQREEAYKEQIKTLTNKLKaaearaefaerSVQKLQKEVDRLEDELVNEKEKYKSITDELDQT 267
Cdd:COG3206 315 ---LASLEAELEALQAREASLQAQLAQLEARLA-----------ELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-272 |
7.49e-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: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 27 EKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNA--------EGEVAALNRRIQLLEEDLERSE--ERL 96
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLErsIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 97 NTATTKLAEASQAADESERMRKVLENRSLSDE-----ERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEE 171
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREieeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 172 RAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELV 251
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
250 260
....*....|....*....|.
gi 3080761 252 NEKEKYKSITDELDQTFSELS 272
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELA 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1-219 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 1 MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRmqqleNDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNR 80
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 81 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDE---------ERMDALENQLK-EARFLAEEADR 150
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialrAQIAALRAQLQqEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3080761 151 KYDEVARKLAMVEADLERAEERAET---GESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLT 219
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
11-266 |
2.08e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 11 RADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLE 90
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 91 RSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAE 170
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 171 ERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDEL 250
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250
....*....|....*.
gi 3080761 251 VNEKEKYKSITDELDQ 266
Cdd:COG4372 272 DTEEEELEIAALELEA 287
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
28-194 |
2.17e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 28 KAEEEVHNLQKRMQQLENDLD----QVQEsLLKAN------TQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLN 97
Cdd:COG0497 169 ALKKELEELRADEAERARELDllrfQLEE-LEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEALSGGEGGALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 98 TATTKLAEASQAADESERMRKVLEN---------RSLS--------DEERMDALENQLKEARFLAeeadRKY----DEVA 156
Cdd:COG0497 248 QALRALERLAEYDPSLAELAERLESalieleeaaSELRryldslefDPERLEEVEERLALLRRLA----RKYgvtvEELL 323
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 3080761 157 RKLAMVEADLER---AEERAETGESKFVELEEELRVVGNNL 194
Cdd:COG0497 324 AYAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-266 |
2.74e-05 |
|
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: 44.75 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 37 QKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEAsqaadeserm 116
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 117 rkvlenrslsdEERMDALENQLKEARFLAEEADRKYDEVAR----KLAMVEADLERAEERAETGESKFVELEEELRVVGN 192
Cdd:COG4942 89 -----------EKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3080761 193 NLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 266
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-249 |
5.60e-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: 44.29 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 11 RADTLEQQNKEANiraEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLE 90
Cdd:TIGR02169 270 IEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 91 RSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAE 170
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3080761 171 ERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDE 249
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
60-274 |
1.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 60 QLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNtATTKLAEAS-------QAADESERMRKVLENRSLSDEErMD 132
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSwdeidvaSAEREIAELEAELERLDASSDD-LA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 133 ALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYK 212
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3080761 213 EQIktltnklkaaearaefaERSVQKLQKEVDRLEDELVNE----KEKYKSITDELDQTFSELSGY 274
Cdd:COG4913 769 ENL-----------------EERIDALRARLNRAEEELERAmrafNREWPAETADLDADLESLPEY 817
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
32-188 |
1.42e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 32 EVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASqaad 111
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3080761 112 eSERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELR 188
Cdd:COG1579 87 -NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
16-221 |
4.41e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 16 EQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERS--- 92
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 93 ---EERLNTATTKLAEASQAADESERMRkVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERA 169
Cdd:COG3883 95 lyrSGGSVSYLDVLLGSESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3080761 170 EERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNK 221
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10-177 |
4.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 10 DRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLlkantqlEEKDKALSNAEGEVAALNRRIQLLEEDL 89
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL-------EECRVAAQAHNEEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 90 ERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERA 169
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
....*...
gi 3080761 170 EERAETGE 177
Cdd:PRK02224 439 RERVEEAE 446
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1-179 |
5.23e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 1 MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALN- 79
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 80 -----------RRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEA 148
Cdd:COG3883 108 llgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|.
gi 3080761 149 DRKYDEVARKLAMVEADLERAEERAETGESK 179
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
4-257 |
6.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 4 EKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQ 83
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 84 LLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARF---------LAEEADRKYDE 154
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEaeaeqaldeLLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 155 VARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAER 234
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260
....*....|....*....|...
gi 3080761 235 SVQKLQKEVDRLEDELVNEKEKY 257
Cdd:COG4372 279 EIAALELEALEEAALELKLLALL 301
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
11-142 |
6.05e-04 |
|
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: 40.29 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 11 RADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEE--KDKALSNAEGEVAALNRRIQLLEED 88
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 3080761 89 LERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR 142
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2-267 |
8.71e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 2 KLEKDNAMDRADTLEQQNKEANIR----AEKAEEEVHNLQKRMQQLENDLDQVQESL--LKANTQlEEKDKALSNAegEV 75
Cdd:PRK11281 47 ALNKQKLLEAEDKLVQQDLEQTLAlldkIDRQKEETEQLKQQLAQAPAKLRQAQAELeaLKDDND-EETRETLSTL--SL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 76 AALNRRIQLLEEDLERSEERLNTATTKLAEASQAadeSERMRKVLENRSlsdeERMDALENQLKEARflAEEADRKYDEV 155
Cdd:PRK11281 124 RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ---PERAQAALYANS----QRLQQIRNLLKGGK--VGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 156 AR---KLAMVEA--DLERAE-------------ERAETGEsKFVELEEELRVVGN--NLKSLEVSEEKANQREEAYKEQi 215
Cdd:PRK11281 195 VLlqaEQALLNAqnDLQRKSlegntqlqdllqkQRDYLTA-RIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQDEAA- 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 3080761 216 KTLTNKLKAAEARAEFAERsvQKLQKEVDRLeDELVNEKEKYKSITDELDQT 267
Cdd:PRK11281 273 RIQANPLVAQELEINLQLS--QRLLKATEKL-NTLTQQNLRVKNWLDRLTQS 321
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-198 |
9.64e-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: 40.44 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 2 KLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQesllKANTQLEEkdkALSNAEGEVAALNRR 81
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER----KRRDKLTE---EYAELKEELEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 82 IQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAM 161
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
170 180 190
....*....|....*....|....*....|....*..
gi 3080761 162 VEADLERAEERAETGESKFVELEEELRVVGNNLKSLE 198
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
23-258 |
9.74e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 23 NIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKAlsnaegEVAALNRRIQLLEEDLERSEERLNTATTK 102
Cdd:PRK05771 35 DLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKV------SVKSLEELIKDVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 103 LAEAsqaadesermrkvlenrslsdEERMDALENQLKEARFLA-----EEADRKYDEVARKLAMVEADLER--------- 168
Cdd:PRK05771 109 ISEL---------------------ENEIKELEQEIERLEPWGnfdldLSLLLGFKYVSVFVGTVPEDKLEelklesdve 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 169 -AEERAETGESKFV----------ELEEELRVVGnnLKSLEVSEEK-ANQREEAYKEQIKTLTNKLKAAEARAEFAErsv 236
Cdd:PRK05771 168 nVEYISTDKGYVYVvvvvlkelsdEVEEELKKLG--FERLELEEEGtPSELIREIKEELEEIEKERESLLEELKELA--- 242
|
250 260
....*....|....*....|..
gi 3080761 237 QKLQKEVDRLEDELVNEKEKYK 258
Cdd:PRK05771 243 KKYLEELLALYEYLEIELERAE 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-222 |
1.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 36 LQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAAD--ES 113
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 114 ERMRKVLENRSLSDEERMDALENQLKEARflaeEADRKYDEVARKLAMVEADLERAEER-AETGESKFVELEEELRVVGN 192
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|
gi 3080761 193 NLKSLEVSEEKANQREEAYKEQIKTLTNKL 222
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
29-272 |
1.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 29 AEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQ 108
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 109 AADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELR 188
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 189 VVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTF 268
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
....
gi 3080761 269 SELS 272
Cdd:COG4372 269 VEKD 272
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3-271 |
2.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 3 LEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQEsllkantQLEEKDKALSNAEGEVAALNRRI 82
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-------EAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 83 QLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMV 162
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPH 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 163 EADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAyKEQIKTLTNKLKAAEARAEFAERSVQKLQKE 242
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEELRER 545
|
250 260
....*....|....*....|....*....
gi 3080761 243 VDRLEDELVNEKEKYKSITDELDQTFSEL 271
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
26-112 |
2.14e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.94 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 26 AEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAAL--------NRRIQLLEEDLERSEERLN 97
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAqaqalqtaQNNLATAQAALANAEARLA 335
|
90
....*....|....*
gi 3080761 98 TATTKLAEASQAADE 112
Cdd:TIGR04320 336 KAKEALANLNADLAK 350
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
135-263 |
2.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 135 ENQLKEARFLAE---EADRKYDEVARKLAMVEADLERAEERAEtgeskfveLEEELRVVGNNLKSLEvseEKANQREEAY 211
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQKEENL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 3080761 212 KEQIKTLT---NKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDE 263
Cdd:PRK12704 99 DRKLELLEkreEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
15-221 |
2.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 15 LEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLD----------QVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQL 84
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQ 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 85 LEEDLERSEERLNTAT-------------TKLAEASQAADESERMRKVLEN---------------RSLSDEERmdaLEN 136
Cdd:COG3096 453 ATEEVLELEQKLSVADaarrqfekayelvCKIAGEVERSQAWQTARELLRRyrsqqalaqrlqqlrAQLAELEQ---RLR 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 137 QLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAEtgeskfvELEEELRVVGNNLKSLEvseekanQREEAYKEQIK 216
Cdd:COG3096 530 QQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE-------ELEEQAAEAVEQRSELR-------QQLEQLRARIK 595
|
....*
gi 3080761 217 TLTNK 221
Cdd:COG3096 596 ELAAR 600
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
154-272 |
3.20e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 38.97 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 154 EVARKLAMVEADLERAEERAETGESKF----VELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTN-KLKAAEAR 228
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDVekliEELERERRELEEEREEAERLREELEKLREELEEKLEELEEeKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 3080761 229 AEFAERSVQKLQKEVDRLEDELVN---EKEKYKSITDELDQTFSELS 272
Cdd:COG1193 570 REEAEEILREARKEAEELIRELREaqaEEEELKEARKKLEELKQELE 616
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-179 |
3.57e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.90 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 3 LEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRI 82
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 83 QLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSD-------------EERMDALENQLKEARFLAEEAD 149
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaelqrvEEEIRALEPVNMLAIQEYEEVL 985
|
170 180 190
....*....|....*....|....*....|
gi 3080761 150 RKYDEVARKLAMVEADLERAEERAETGESK 179
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-141 |
3.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 4 EKDNAMDRADTLEQQNKEANIRAEKAEEEVHN--------LQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEV 75
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 76 AALNRRIQL----LEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEA 141
Cdd:COG4913 383 AALRAEAAAlleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
25-182 |
3.99e-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: 37.60 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 25 RAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIqlleedlERSEERLNTATT--K 102
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-------KKYEEQLGNVRNnkE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 103 LAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVE 182
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
47-265 |
4.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 47 LDQVQESLLKANTQLEEKD-----KALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLE 121
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 122 NRSLS---DEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNLKSLE 198
Cdd:PRK02224 262 DLRETiaeTEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3080761 199 VSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELD 265
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-265 |
4.65e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 39 RMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERS-EERLNTATTKLAEASQAADESERMR 117
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 118 KVLENRSLSDEERMDALENQLKEARFLAEEADRKYDE----VARKLAMVEADLERAEERAETGESKFVELEEELRVVGNN 193
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3080761 194 LKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELD 265
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10-174 |
4.81e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.82 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 10 DRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESL---LKANTQLEEKD--KALSNAEgEVAALNRRIQL 84
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRALYRLGRQPplALLLSPE-DFLDAVRRLQY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 85 LEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEA 164
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
170
....*....|
gi 3080761 165 DLERAEERAE 174
Cdd:COG4942 221 EAEELEALIA 230
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
15-266 |
4.83e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.08 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 15 LEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEE 94
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 95 RLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAE 174
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 175 TGESKFV--ELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVN 252
Cdd:TIGR04523 556 KENLEKEidEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
250
....*....|....
gi 3080761 253 EKEKYKSITDELDQ 266
Cdd:TIGR04523 636 IKSKKNKLKQEVKQ 649
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
25-173 |
5.62e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 37.79 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 25 RAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAA----LNRRIQLLEEDLeRSEERLNTAT 100
Cdd:pfam00529 69 KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQaqidLARRRVLAPIGG-ISRESLVTAG 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3080761 101 TKLAEASQAADESE-RMRKVLENRSLSDEERMDALENQLKEARFLAEEADrkydevaRKLAMVEADLERAEERA 173
Cdd:pfam00529 148 ALVAQAQANLLATVaQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAE-------AELKLAKLDLERTEIRA 214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-271 |
7.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.97 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 87 EDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERmdalenqlkeARFLAEEADRKYDEVARKLAMVEADL 166
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLR----------AALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 167 ERAEERAETGESKFVELEEELRVVGNNLKSLEvseekaNQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRL 246
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180
....*....|....*....|....*
gi 3080761 247 EDELVNEKEKYKSITDELDQTFSEL 271
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEAL 403
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
54-222 |
9.65e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 37.24 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 54 LLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNtattKLAEASQAADESERMRKVLENRSLSDEERMDA 133
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN----LVQTALRQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3080761 134 LEN---QLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNlkslEVSEEKANQREEA 210
Cdd:COG3096 370 VEEaaeQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLP----DLTPENAEDYLAA 445
|
170
....*....|..
gi 3080761 211 YKEQIKTLTNKL 222
Cdd:COG3096 446 FRAKEQQATEEV 457
|
|
| |
