|
Name |
Accession |
Description |
Interval |
E-value |
| Paralemmin |
pfam03285 |
Paralemmin; |
19-350 |
3.79e-110 |
|
Paralemmin;
Pssm-ID: 460875 Cd Length: 301 Bit Score: 324.78 E-value: 3.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 19 AEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEGTPSSASEGDEDMRRQMQEDEQKARHLEESISRLEQEIEEL 98
Cdd:pfam03285 1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 99 ENTDALPTAtargsvaapspapgpalrpapedqraeavpnsqqtpvgtpkeKQISNTPLRtvdgstmmkaamysvEITVE 178
Cdd:pfam03285 81 EEESSISAK------------------------------------------KENLAEKLL---------------EITVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 179 KDKVTGETRVLSSTTVLPRELLPQGIKVYEDETKVVHAM---DGTAENGIHPLSSSEVDELIHKADEVTLNEAGSVVGAV 255
Cdd:pfam03285 104 KDKVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTAAPE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 256 ET----RGPSEEAVRTTPSRR------------EITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETQKVL 319
Cdd:pfam03285 184 VRgtadGGDVSPKEEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVL 263
|
330 340 350
....*....|....*....|....*....|....*...
gi 1387278134 320 GLQDTITAELVVIEDAAEPKEPA-------PPNGSAAE 350
Cdd:pfam03285 264 GLETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
12-112 |
1.69e-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: 46.30 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEGTPSSASEGDEDMRRQMQEDEQKARHLEESISRL 91
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
90 100
....*....|....*....|.
gi 1387278134 92 EQEIEELENTDALPTATARGS 112
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAA 246
|
|
| DDRRRQL_YjdP |
NF041443 |
DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a ... |
22-80 |
2.57e-04 |
|
DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a signal peptide and with a highly charged C-terminal region of typically five tandem 7-mer repeats approximated by DDRRRQL. The family is named for founding member YjdP from Escherichia coli K-12.
Pssm-ID: 469333 [Multi-domain] Cd Length: 102 Bit Score: 39.97 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387278134 22 RRRQaeIENRRRQLEDDRRQLQHlkskalRERWLlegtpssasegDEDmRRQMQEDEQK 80
Cdd:NF041443 63 RRRQ--YDDRRRQLEDRRRQLDD------RQRQL-----------DQE-RRQLEDEERR 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-101 |
3.73e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 9 PSQQERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKS--KALRER-WLLEGTPSSASEGDEDMRRQMQEDEQKARHLE 85
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEekEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
90
....*....|....*.
gi 1387278134 86 ESISRLEQEIEELENT 101
Cdd:TIGR02169 483 KELSKLQRELAEAEAQ 498
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
12-100 |
8.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQA--EIENRRRQLEDD----RRQLQHLKSKaLRERwllEGTPSSASEGDEDMRRQMQEDEQKARHLE 85
Cdd:PRK12704 48 KKEAEAIKKEALLEAkeEIHKLRNEFEKElrerRNELQKLEKR-LLQK---EENLDRKLELLEKREEELEKKEKELEQKQ 123
|
90
....*....|....*
gi 1387278134 86 ESISRLEQEIEELEN 100
Cdd:PRK12704 124 QELEKKEEELEELIE 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Paralemmin |
pfam03285 |
Paralemmin; |
19-350 |
3.79e-110 |
|
Paralemmin;
Pssm-ID: 460875 Cd Length: 301 Bit Score: 324.78 E-value: 3.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 19 AEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEGTPSSASEGDEDMRRQMQEDEQKARHLEESISRLEQEIEEL 98
Cdd:pfam03285 1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 99 ENTDALPTAtargsvaapspapgpalrpapedqraeavpnsqqtpvgtpkeKQISNTPLRtvdgstmmkaamysvEITVE 178
Cdd:pfam03285 81 EEESSISAK------------------------------------------KENLAEKLL---------------EITVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 179 KDKVTGETRVLSSTTVLPRELLPQGIKVYEDETKVVHAM---DGTAENGIHPLSSSEVDELIHKADEVTLNEAGSVVGAV 255
Cdd:pfam03285 104 KDKVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTAAPE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 256 ET----RGPSEEAVRTTPSRR------------EITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETQKVL 319
Cdd:pfam03285 184 VRgtadGGDVSPKEEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVL 263
|
330 340 350
....*....|....*....|....*....|....*...
gi 1387278134 320 GLQDTITAELVVIEDAAEPKEPA-------PPNGSAAE 350
Cdd:pfam03285 264 GLETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
12-112 |
1.69e-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: 46.30 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEGTPSSASEGDEDMRRQMQEDEQKARHLEESISRL 91
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
90 100
....*....|....*....|.
gi 1387278134 92 EQEIEELENTDALPTATARGS 112
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-101 |
5.38e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWllegtpSSASEGDEDMRRQMQEDEQKARHLEESISRL 91
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL------QDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
90
....*....|
gi 1387278134 92 EQEIEELENT 101
Cdd:COG4717 226 EEELEQLENE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
13-110 |
2.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 13 ERLQAIAEKRRRQAEIENRRRQLEDDRRQLqhlksKALRERWLLEGTPSSASEGDEDMRRQMQEDEQKARHLEESISRLE 92
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEEL-----LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
|
90
....*....|....*...
gi 1387278134 93 QEIEELENTDALPTATAR 110
Cdd:COG4717 460 AELEQLEEDGELAELLQE 477
|
|
| DDRRRQL_YjdP |
NF041443 |
DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a ... |
22-80 |
2.57e-04 |
|
DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a signal peptide and with a highly charged C-terminal region of typically five tandem 7-mer repeats approximated by DDRRRQL. The family is named for founding member YjdP from Escherichia coli K-12.
Pssm-ID: 469333 [Multi-domain] Cd Length: 102 Bit Score: 39.97 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387278134 22 RRRQaeIENRRRQLEDDRRQLQHlkskalRERWLlegtpssasegDEDmRRQMQEDEQK 80
Cdd:NF041443 63 RRRQ--YDDRRRQLEDRRRQLDD------RQRQL-----------DQE-RRQLEDEERR 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-100 |
3.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQAEIENRRRQLEDDRRQLQhlksKALRErwLLEGTPSSASEGDEDMRRQMQEDEQKARHLEESISRL 91
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQ----EELEE--LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
....*....
gi 1387278134 92 EQEIEELEN 100
Cdd:COG4717 219 QEELEELEE 227
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
12-85 |
9.31e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 9.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387278134 12 QERLQAIAE-KRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEgtpssASEGDEDMRRQMQEDEQKARHLE 85
Cdd:pfam17380 523 EERQKAIYEeERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-----AMEREREMMRQIVESEKARAEYE 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-104 |
1.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 11 QQERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRerwllegtpssASEGDEDMRRQMQEDEQKARHLEESISR 90
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE-----------LLAELARLEQDIARLEERRRELEERLEE 320
|
90
....*....|....
gi 1387278134 91 LEQEIEELENTDAL 104
Cdd:COG1196 321 LEEELAELEEELEE 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-106 |
1.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKS--------KALRERwlLEGTPSSASEGDEDMRrQMQEDEQKARH 83
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqelEALEAE--LAELPERLEELEERLE-ELRELEEELEE 167
|
90 100
....*....|....*....|...
gi 1387278134 84 LEESISRLEQEIEELENTDALPT 106
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLAT 190
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-99 |
1.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 11 QQERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEgtpsSASEGDEDMRRQMQEDEQKARHLEESISR 90
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----EAQAEEYELLAELARLEQDIARLEERRRE 313
|
....*....
gi 1387278134 91 LEQEIEELE 99
Cdd:COG1196 314 LEERLEELE 322
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-99 |
2.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 11 QQERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEGTPSSASEGDEDMRRQMQEDEQKARhleesISR 90
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE-----LER 771
|
....*....
gi 1387278134 91 LEQEIEELE 99
Cdd:COG1196 772 LEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-101 |
3.73e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 9 PSQQERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKS--KALRER-WLLEGTPSSASEGDEDMRRQMQEDEQKARHLE 85
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEekEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
90
....*....|....*.
gi 1387278134 86 ESISRLEQEIEELENT 101
Cdd:TIGR02169 483 KELSKLQRELAEAEAQ 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-99 |
7.46e-03 |
|
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: 38.50 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 10 SQQERLQAIAEKRRRQAEIENRRRQLEDDRRQLQHLKS--KALRERWL-LEGTPSSASEGDEDMRRQMQEDEQKARHLEE 86
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAAnLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
90
....*....|...
gi 1387278134 87 SISRLEQEIEELE 99
Cdd:TIGR02168 853 DIESLAAEIEELE 865
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
12-100 |
8.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 12 QERLQAIAEKRRRQA--EIENRRRQLEDD----RRQLQHLKSKaLRERwllEGTPSSASEGDEDMRRQMQEDEQKARHLE 85
Cdd:PRK12704 48 KKEAEAIKKEALLEAkeEIHKLRNEFEKElrerRNELQKLEKR-LLQK---EENLDRKLELLEKREEELEKKEKELEQKQ 123
|
90
....*....|....*
gi 1387278134 86 ESISRLEQEIEELEN 100
Cdd:PRK12704 124 QELEKKEEELEELIE 138
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3-100 |
9.63e-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: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387278134 3 VLVAETPSQQErlqAIAEKRRRQAEIENRRRQLEDDRRQLQHLKSKALRERWLLEGTPSSAsegdedmRRQMQEDEQKAR 82
Cdd:COG4942 10 LLALAAAAQAD---AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------ARRIRALEQELA 79
|
90
....*....|....*...
gi 1387278134 83 HLEESISRLEQEIEELEN 100
Cdd:COG4942 80 ALEAELAELEKEIAELRA 97
|
|
| |
