|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
83-336 |
2.46e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 83 KEVRATLEKVRKKMYG-EYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDsfsEMNSSLTSASIDLQKTLVDVTL 161
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 162 ENTDIREQIRNLKHTHEQSME-KLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMTRKLYNQYEEKMREEEQKHKA 240
Cdd:COG1196 293 LLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 241 EKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQ 320
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250
....*....|....*.
gi 2024348544 321 HLEEVAASLRERIKHL 336
Cdd:COG1196 453 ELEEEEEALLELLAEL 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-397 |
5.76e-11 |
|
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: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 164 TDIREQI-RNLKHTHEQS--MEKLREKQKQLETAQIEnqLLKLKVESSQEANAEvmremtrklYNQYEEKMREEEQKHKA 240
Cdd:TIGR02168 192 EDILNELeRQLKSLERQAekAERYKELKAELRELELA--LLVLRLEELREELEE---------LQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 241 EKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQ 320
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 321 HLEEVAASLRERIKHLDDMVHCQQKKVKHMV-------EEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKLEYLM 393
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELEsrleeleEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
....
gi 2024348544 394 ENQP 397
Cdd:TIGR02168 421 QEIE 424
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-328 |
2.50e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 72 ADQLKEEMNYIKEVRATLEKVRKKMYGEYDEMKRKIQQLTNELKVTNAH-------QESLENHVRVQAAALDSFSEMNSS 144
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaeLARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 145 LTSASIDLQKTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMTRKLy 224
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 225 nQYEEKMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQ 304
Cdd:COG1196 400 -AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260
....*....|....*....|....
gi 2024348544 305 LSGAKSESNSDSERSQHLEEVAAS 328
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-391 |
4.91e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 152 LQKTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVeSSQEANAEVMREMTRKLYNQYEEKm 231
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLANLERQLEEL- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 232 REEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKD-------QRIGELDRLIERMEEERHQLQKQLELNEIQ 304
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaeleeleSRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 305 LSGAKSESNSDSERSQHLEEvaaslrERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKE 384
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQ------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
....*..
gi 2024348544 385 LQDKLEY 391
Cdd:TIGR02168 476 ALDAAER 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-406 |
6.60e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 96 MYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDLQKTLVDVTLENTDIREQIRNLKH 175
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 176 THEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMT--RKLYNQYEEKMREEEQKHKAEKEI---LLEETN 250
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEelEAQIEQLKEELKALREALDELRAEltlLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 251 RLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLR 330
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024348544 331 ERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKIsfleceNKELQDKLEYLMENQPKTNVETRDA 406
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLEEAEALENKIEDDEEEA 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-394 |
3.65e-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: 59.31 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 73 DQLKEEMNYIKEVRATLEKVRKKMYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDL 152
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 153 QKTLVDVTLENTDIREQIRNLKHthEQSMEKLREKQKQLEtaQIENQLLKLkVESSQEANAEVMREMTRKlynQYEEKMR 232
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELS--KLEEEVSRI-EARLREIEQKLNRLTLEK---EYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 233 EEEQKHKAEKEILLEEtnrLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSES 312
Cdd:TIGR02169 836 QELQEQRIDLKEQIKS---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 313 NSDSERSQHLEEVAASLRERIKHLDDMVHcQQKKVKHMVEEIEMLRKKVKEKELfIIQLLEKISFLECEN--------KE 384
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEEELSLEDVQAELQRVEE-EIRALEPVNMLAIQEyeevlkrlDE 990
|
330
....*....|
gi 2024348544 385 LQDKLEYLME 394
Cdd:TIGR02169 991 LKEKRAKLEE 1000
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-395 |
8.71e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 228 EEKMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSG 307
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 308 AKSESNSDSERSQHLEEVAASLRERIKHLDDMVhcQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKIS-------FLEC 380
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNrltlekeYLEK 833
|
170
....*....|....*
gi 2024348544 381 ENKELQDKLEYLMEN 395
Cdd:TIGR02169 834 EIQELQEQRIDLKEQ 848
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-390 |
1.38e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 164 TDIREQI-RNLKHTHEQSM--EKLREKQKQLETAQIENQLLKLK-VESSQEANAEVMREMTRKLynqyeEKMREEEQKHK 239
Cdd:COG1196 192 EDILGELeRQLEPLERQAEkaERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAEL-----EELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 240 AEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERS 319
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024348544 320 QHLEEVAASLRERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKLE 390
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-390 |
1.79e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 178 EQSMEKLREKQKQLE-----TAQIENQLLKLKVESSQeanAEvmremtrkLYNQYEEKMREEEQKHKA-EKEILLEETNR 251
Cdd:COG1196 175 EEAERKLEATEENLErlediLGELERQLEPLERQAEK---AE--------RYRELKEELKELEAELLLlKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 252 LLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLRE 331
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024348544 332 RIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKLE 390
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-405 |
3.16e-07 |
|
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: 52.07 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 229 EKMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLE--LNEIQLS 306
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAelLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 307 GA--------KSESNSDSERSQH-LEEVAASLRERIKHLddmvhcqQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISF 377
Cdd:COG4942 117 GRqpplalllSPEDFLDAVRRLQyLKYLAPARREQAEEL-------RADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180
....*....|....*....|....*...
gi 2024348544 378 LECENKELQDKLEYLMENQPKTNVETRD 405
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAE 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-407 |
4.06e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 182 EKLREKQKQL-ETAQIENQLLKLKVESSQeanAEVMREMTRKLYNQYEEKMREEEQKHKAEKEillEETNRLLKAIEESN 260
Cdd:TIGR02169 227 ELLKEKEALErQKEAIERQLASLEEELEK---LTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 261 KKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLRERIKHLDDMV 340
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024348544 341 HCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKLEYLMENQPKTNVETRDAG 407
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-336 |
5.32e-07 |
|
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: 51.69 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 101 DEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSfsemnssLTSASIDLQKTLVDVTLENTDIREQIRNLKHTHEQS 180
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-------LERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 181 MEKLREKQKQLE----TAQIENQLLKLKVESSQEANAEVMREMTrkLYNQYEEKMREEEQKHKAEKEILleetnrllkai 256
Cdd:COG4942 96 RAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQ--YLKYLAPARREQAEELRADLAEL----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 257 eesnkkmqitETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLRERIKHL 336
Cdd:COG4942 163 ----------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-409 |
7.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 104 KRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDLQKTLVDVTLENTDIREQIRNLKHTHEQSmek 183
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 184 lrEKQKQLETAQIENQllklkvESSQEANAEVMREMTRKLYNQYEEKMREEEQKHKAEKEI--LLEETNRLLKAIEESNK 261
Cdd:COG1196 301 --EQDIARLEERRREL------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 262 KMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLRERIKHLDDMVH 341
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024348544 342 CQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEkisflecenKELQDKLEYLMENQPKTNVETRDAGVG 409
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLE---------ELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
72-248 |
3.21e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 72 ADQLKEEMNYIKEVRATLEKVRKKMYGEYDEMKRKIQQLTNELKVTNA------------------HQESLENHVRVQAA 133
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAeidklqaeiaeaeaeieeRREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 134 ALDSFSEMNSSLTSAS----IDLQKTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQ 209
Cdd:COG3883 98 SGGSVSYLDVLLGSESfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024348544 210 EANAEVMREMTRKLYNQYEEKMREEEQKHKAEKEILLEE 248
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-402 |
3.38e-06 |
|
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: 49.63 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 140 EMNSSLTSASIDLQKTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETA-----QIENQLLKLKVESS---QEA 211
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikELEKQLNQLKSEISdlnNQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 212 NAEVMREMTRKLYNQYE--------------------------EKMREEEQKHKAEKEILLEETNRLLKAIEESN--KKM 263
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKkleeiqnqisqnnkiisqlneqisqlKKELTNSESENSEKQRELEEKQNEIEKLKKENqsYKQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 264 QIT--ETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLRERIKHLDDMVH 341
Cdd:TIGR04523 385 EIKnlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024348544 342 CQQKKVKHMVEEI-------EMLRKKVKEKELFIIQLLEKISFLECENKELQDKLEYLMENQPKTNVE 402
Cdd:TIGR04523 465 SLETQLKVLSRSInkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
73-314 |
4.77e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 73 DQLKEEMNYIKEVRATLEKVRKKMYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSfsemnsslTSASIDL 152
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE--------LRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 153 QKtlvdvtlenTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKlKVESSQEANAEVMREMTRKLyNQYEEKMR 232
Cdd:COG4942 102 QK---------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAEL-AALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 233 EEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSES 312
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 2024348544 313 NS 314
Cdd:COG4942 251 LK 252
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
222-379 |
4.99e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 222 KLYNQYEEKMREEEQKHKAE----------------KEILLEETNRLLKAIEESNKKM-QITETSIKEKDQRIGELDRLI 284
Cdd:COG2433 343 KAYDAYKNKFERVEKKVPPDvdrdevkarvirglsiEEALEELIEKELPEEEPEAEREkEHEERELTEEEEEIRRLEEQV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 285 ERMEEERHQLQKQLElneiqlsgAKSESNSDSERSqhLEEvaASLRERIKHLDDmvhcqqKKVKHMVEEIEMLRKKVKEK 364
Cdd:COG2433 423 ERLEAEVEELEAELE--------EKDERIERLERE--LSE--ARSEERREIRKD------REISRLDREIERLERELEEE 484
|
170
....*....|....*
gi 2024348544 365 ELFIIQLLEKISFLE 379
Cdd:COG2433 485 RERIEELKRKLERLK 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-338 |
7.28e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 74 QLKEEMNYIKEVRATLEKVRKKMYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDLQ 153
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 154 KTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMtrklyNQYEEKMRE 233
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL-----RELESKRSE 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 234 EEQKHKAEKEILLEETNRLLKA-IEESNKKMQITE---TSIKEKDQRIGELDRLIERMEEERHQLQKQL-ELNEIQLSgA 308
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLeVRIDNLQERLSEeysLTLEEAEALENKIEDDEEEARRRLKRLENKIkELGPVNLA-A 991
|
250 260 270
....*....|....*....|....*....|
gi 2024348544 309 KSESNSDSERSQHLEEVAASLRERIKHLDD 338
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-339 |
4.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 82 IKEVRATLEKVRKKMYGEYDEMKR-KIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDLQKTLVDVT 160
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 161 LENTDIREQIRNLKHTHEQSMEKLREKQKQLEtaQIENQLLKLKVESSQ-EANAEVMREMTRKLYNQYEEKmREEEQKHK 239
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALR--DLESRLGDLKKERDElEAQLRELERKIEELEAQIEKK-RKRLSELK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 240 AEKEILLEEtnrlLKAIEESNKKMQitetSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERS 319
Cdd:TIGR02169 924 AKLEALEEE----LSEIEDPKGEDE----EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
250 260
....*....|....*....|
gi 2024348544 320 QHLEEVAASLRERIKHLDDM 339
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKK 1015
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-392 |
7.78e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 73 DQLKEEMNYIKEVRATLEKVRKKMYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDL 152
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 153 QKtlvdvtlENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEA--NAEVMREMTRKLYNQYEEK 230
Cdd:PRK02224 355 EE-------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 231 MREEEQKHKAEKEILlEETNRLLKA---------IEESnkkmQITETsIKEKDQRIGELDRLIERMEEERHQLQKQLELN 301
Cdd:PRK02224 428 EAELEATLRTARERV-EEAEALLEAgkcpecgqpVEGS----PHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 302 EiQLSGAKSESNSDSERSQHLEEVAASLRERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECE 381
Cdd:PRK02224 502 E-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
330
....*....|.
gi 2024348544 382 NKELQDKLEYL 392
Cdd:PRK02224 581 LAELKERIESL 591
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-392 |
8.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 165 DIREQIRNLKHTHEQSMEKLREKQKQL-----ETAQIENQLLKLKVESSQEANAEVMREMTRKLYNQYEEKMRE-EEQKH 238
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELpelreELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRElEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 239 KAEKEI-LLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLElneiQLSGAKSESNSDSE 317
Cdd:PRK03918 270 ELKKEIeELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 318 RSQHLEEVAASLRERIKHLDDMVHCQQKKVKH-----------MVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQ 386
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELERLkkrltgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
....*.
gi 2024348544 387 DKLEYL 392
Cdd:PRK03918 426 KAIEEL 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
164-389 |
9.63e-05 |
|
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: 45.01 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 164 TDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVES--SQEANAEVMREMTRKLYNQYEEKMREEEQkhkaE 241
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNleSQINDLESKIQNQEKLNQQKDEQIKKLQQ----E 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 242 KEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEE--------------ERHQLQKQLELNEIQLSG 307
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsrsinkikqNLEQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 308 AKSESNSDSERSQHLEEVAASLRERIKHLDDMVHCQQKKVKHMVEEI---------EMLRKKVKEKELFIIQLLEKISFL 378
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSL 580
|
250
....*....|.
gi 2024348544 379 ECENKELQDKL 389
Cdd:TIGR04523 581 KKKQEEKQELI 591
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
93-366 |
1.46e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 93 RKKMYGEYDEMkrkIQQLTNELKVTNAHQESLENHVRVQAAAL-DSFSEMNSSLTSASIDLQKTLVDVTLEN-------- 163
Cdd:COG5022 808 SRKEYRSYLAC---IIKLQKTIKREKKLRETEEVEFSLKAEVLiQKFGRSLKAKKRFSLLKKETIYLQSAQRvelaerql 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 164 TDIREQIRNLKHTHEQSME---KLREKQKQLETAQIENqlLKLKVESS-------QEANAEVMREMTRKLY------NQY 227
Cdd:COG5022 885 QELKIDVKSISSLKLVNLElesEIIELKKSLSSDLIEN--LEFKTELIarlkkllNNIDLEEGPSIEYVKLpelnklHEV 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 228 EEKMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQ-ITETS-----IKEKDQRIGELDRLIERMEEERHQLQKQLELN 301
Cdd:COG5022 963 ESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKeLAELSkqygaLQESTKQLKELPVEVAELQSASKIISSESTEL 1042
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024348544 302 EIQLSGAKSESNSDSERSQHLEEVAA-SLRERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKEL 366
Cdd:COG5022 1043 SILKPLQKLKGLLLLENNQLQARYKAlKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNL 1108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-334 |
1.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 165 DIREQIRNLKHTHEQsMEKLREKQKQLEtaQIENQLLKLKVESSQEANAEVMREMTRKLYNQYE-EKMREEEQKHKAEKE 243
Cdd:COG4913 229 ALVEHFDDLERAHEA-LEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 244 ILLEETNRLLKAIEESNKKMQITETSIKEKD-QRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHL 322
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170
....*....|..
gi 2024348544 323 EEVAASLRERIK 334
Cdd:COG4913 386 RAEAAALLEALE 397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
229-429 |
3.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 229 EKMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLE--LNEIQLS 306
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 307 GA---------KSESNSD-----------SERSQHLEEVAASLRERIKHLDDMVHCQQKKVKHMVEEIEMLRK----KVK 362
Cdd:COG3883 99 GGsvsyldvllGSESFSDfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAeleaQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024348544 363 EKELFIIQLLEKISFLECENKELQDKLEYLMENQPKTNVETRDAGVGCDLPSSTSNDNGRSPESTRP 429
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
262-394 |
3.92e-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: 41.83 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 262 KMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLRERIKHLDDmvh 341
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2024348544 342 cqQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKLEYLME 394
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-363 |
4.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 168 EQIRNLKHTHEQSMEKLREKQKQLetAQIENQLLKLKVESSQEANAEVMRemTRKLYNQYEEKmreeeQKHKAEKEILLE 247
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEEL--AELLKELEELGFESVEELEERLKE--LEPFYNEYLEL-----KDAEKELEREEK 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 248 ETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIErmEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAA 327
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024348544 328 SLRERIKHLDDmVHCQQKKVKHMVEEIEMLRKKVKE 363
Cdd:PRK03918 698 KLKEELEEREK-AKKELEKLEKALERVEELREKVKK 732
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
178-390 |
6.33e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 178 EQSMEKLREkqkqLETAQIENqllkLKVESSQEANAEVMREMT---RKLynqyeEKMREEEQKHKAEKEILLE-ETNRLL 253
Cdd:PRK05771 19 DEVLEALHE----LGVVHIED----LKEELSNERLRKLRSLLTklsEAL-----DKLRSYLPKLNPLREEKKKvSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 254 KAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQ--KQLELNEIQLSGAKS--------ESNSDSERSQHLE 323
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvfvgtvPEDKLEELKLESD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024348544 324 EVAASLRERIKHLDDMVHCQQKKVKHMVEEI----EMLRKKVKEKELF---IIQLLEKISFLECENKELQDKLE 390
Cdd:PRK05771 166 VENVEYISTDKGYVYVVVVVLKELSDEVEEElkklGFERLELEEEGTPselIREIKEELEEIEKERESLLEELK 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-333 |
6.87e-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: 42.36 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 72 ADQLKEEMNYIKEVRATL-EKVRKKMYGEYDEMKRKIQQLTNELkvtnahqeslENHVRVQAAALDSFSEMNSSLTSASI 150
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEI----------ASLERSIAEKERELEDAEERLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 151 DLQKTLvdvtLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKlkvESSQEANAEVMREMTRKlynqyeEK 230
Cdd:TIGR02169 330 EIDKLL----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKL------EK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 231 MREEEQKHKAEKEILLEETNRLLKAIEESNKKmqitetsIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKS 310
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260
....*....|....*....|...
gi 2024348544 311 ESNSDSERSQHLEEVAASLRERI 333
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQREL 492
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
153-298 |
7.40e-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: 42.03 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 153 QKTLVDVTLENTDIREQIRNLKHTHEQSMEKlrEKQKQLETAQIENQLLKLKVESSQEANAEVMREMTRKLYNQYEEKMR 232
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024348544 233 EEEQKHKAEKEilLEETNRllKAIEESNKK------MQITETSIKEKDQ-RIGELDRLIERMEEERHQLQKQL 298
Cdd:pfam17380 490 EEQRRKILEKE--LEERKQ--AMIEEERKRkllekeMEERQKAIYEEERrREAEEERRKQQEMEERRRIQEQM 558
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
233-396 |
7.84e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 233 EEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERME--EERHQLQKQLELNEIQLSGAKS 310
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 311 ESNSDSERSQHLEEVAASLRERIKHLDDMVHC----QQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQ 386
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|
gi 2024348544 387 DKLEYLMENQ 396
Cdd:COG4717 234 NELEAAALEE 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
78-313 |
7.96e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 78 EMNYIKEVRATLEKVR--KKMYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFS-EMNSSLTSASIDLQK 154
Cdd:pfam15921 631 ELEKVKLVNAGSERLRavKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTnKLKMQLKSAQSELEQ 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 155 TlvdvtlentdiREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEA--NAEVMREMTRKLYNQYEEKMR 232
Cdd:pfam15921 711 T-----------RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAmtNANKEKHFLKEEKNKLSQELS 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 233 E---EEQKHKAEKEILLEETNRLlkaieesNKKMQITETSIKEKDQRIGELDRLIERMEEE--RHQLQKQLELNEIQLSG 307
Cdd:pfam15921 780 TvatEKNKMAGELEVLRSQERRL-------KEKVANMEVALDKASLQFAECQDIIQRQEQEsvRLKLQHTLDVKELQGPG 852
|
....*.
gi 2024348544 308 AKSESN 313
Cdd:pfam15921 853 YTSNSS 858
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
176-372 |
8.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 176 THEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEvmREMTRKLYNQYEEKMREEEQKHKAEKeiLLEETNRLLKA 255
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKLEKLLQLLP--LYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 256 IEESNKKMQitetSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSES-NSDSERSQHLEEVAASLRERIK 334
Cdd:COG4717 141 LAELPERLE----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024348544 335 HLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLL 372
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-390 |
9.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 167 REQIRNLKHTHEQSMEKLREKQKQLEtaQIENQLLKLKvessqeanaEVMREMTRKLYNQYEEKMREEEQKHK-AEKEIL 245
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELE--EVLREINEIS---------SELPELREELEKLEKEVKELEELKEEiEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 246 LEETNRLLKAIEEsnkKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIqLSGAKSESNSDSERSQHLEEV 325
Cdd:PRK03918 247 LESLEGSKRKLEE---KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024348544 326 AASLRERIKHLDDMVhcqqKKVKHMVEEIEMLRKKVKEKELFiIQLLEKISFLECENKELQDKLE 390
Cdd:PRK03918 323 INGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLT 382
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-389 |
1.66e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 158 DVTLENTDIREQIRNLKHTHEQsMEKLREKQKQLETAQIENQLLKLKVESsQEANAEVMREMTRKLYNQYEEKMREEEQK 237
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAE-RRETIEEKRERAEELRERAAELEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 238 HKAEKEiLLEETNRLLKAIEESNKKMQITETSIkEKDQRIGELDRLIERMEEERHQLQKQLElneiqlsgAKSESNSdsE 317
Cdd:PRK02224 557 REAAAE-AEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKRE--------ALAELND--E 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024348544 318 RSQHLEEvaasLRERIKHLDDmvhcqqkkvKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKL 389
Cdd:PRK02224 625 RRERLAE----KRERKRELEA---------EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
90-303 |
3.01e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 90 EKVRKKMYgeydEMKRKIQQLTNELKVTNAHQESLENHVRVQAAAldsfsemNSSLTSASIDLQKTLVDVTLENTDIREQ 169
Cdd:PRK11281 159 ERAQAALY----ANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQA-------EQALLNAQNDLQRKSLEGNTQLQDLLQK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 170 IRNLkhtheqsmekLREKQKQLETaqiENQLLklkvessQEAnaevmreMTRKLYNQYEEKMREEEQKHKA--------- 240
Cdd:PRK11281 228 QRDY----------LTARIQRLEH---QLQLL-------QEA-------INSKRLTLSEKTVQEAQSQDEAariqanplv 280
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024348544 241 --EKEILLEETNRLLKAIEESNkkmQITETSIKEKDQrigeLDRLI--ER-MEEERHQLQKQLELNEI 303
Cdd:PRK11281 281 aqELEINLQLSQRLLKATEKLN---TLTQQNLRVKNW----LDRLTqsERnIKEQISVLKGSLLLSRI 341
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
148-275 |
3.08e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 39.64 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 148 ASIDLQKTLVDVTLENTDIREQI-----------------RNLKHTHEQSMEKLREKQKQLetaqiENQLLKLKVESSQE 210
Cdd:smart00435 229 ASITLQEQLKELTAKDGNVAEKIlaynranrevailcnhqRTVSKTHEKSMEKLQEKIKAL-----KYQLKRLKKMILLF 303
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024348544 211 ANAEVMREMTRKLYNQYEEKMREEEQKHKAEKEILLEETnrllKAIEESNKKMQITETSIKEKDQ 275
Cdd:smart00435 304 EMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKK----KQIERLEERIEKLEVQATDKEE 364
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
176-288 |
3.32e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 176 THEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMtRKLYNQYEEKMREEEQKHKAEKEILLEETNRLLKa 255
Cdd:cd16269 185 AILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL-EDQERSYEEHLRQLKEKMEEERENLLKEQERALE- 262
|
90 100 110
....*....|....*....|....*....|...
gi 2024348544 256 ieesNKKMQITETSIKEKDQRIGELDRLIERME 288
Cdd:cd16269 263 ----SKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
83-385 |
3.34e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 83 KEVRATLEKVRKKMYGEYDEMKRKIQQLTNElkvtnaHQESLENHVRVQAAALDSFSEMNSSLTSASIDLQKTLVDVTLE 162
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEDHEKIQHLEEE------YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 163 NTDIREQIRNLKhtheQSMEKLREKQKQLETAQIENQllklKVESSQEANAEVMREMTRKLYNQYEEKMREEEQKHKAE- 241
Cdd:pfam05483 274 EEKTKLQDENLK----ELIEKKDHLTKELEDIKMSLQ----RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKa 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 242 ----------------KEILLEETNRLlkaiEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQL 305
Cdd:pfam05483 346 ahsfvvtefeattcslEELLRTEQQRL----EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 306 SGAKSESNSDSERSQHLEEVAASLRERIKHLDDM---VHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECEN 382
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
...
gi 2024348544 383 KEL 385
Cdd:pfam05483 502 KEL 504
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
173-336 |
3.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 173 LKHTHEQSMEKLREKQKQ-LETAQIENQLLKlkvessQEANAEVmREMTRKLYNQYEEKMREEEQKHKAEKEILLEETNR 251
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRiLEEAKKEAEAIK------KEALLEA-KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 252 LLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLElneiQLSGAKSEsnsdSERSQHLEEVAASLRE 331
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE----RISGLTAE----EAKEILLEKVEEEARH 169
|
....*
gi 2024348544 332 RIKHL 336
Cdd:PRK12704 170 EAAVL 174
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
115-298 |
4.37e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 39.66 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 115 KVTNAHQESLENH----VRVQAAALDSFSEMNSSLTSASIDLQKTLVDVTLENT---DIREQIRNLKHTHEQS----MEK 183
Cdd:pfam13166 264 PLPAERKAALEAHfddeFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSafeLDVEDIESEAEVLNSQldglRRA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 184 LREKQKQL----ETAQIENQLLKLKvESSQEANAEVmremtrKLYNQYEEKMreEEQKHKAEKEILLEETNRLLKAIEES 259
Cdd:pfam13166 344 LEAKRKDPfksiELDSVDAKIESIN-DLVASINELI------AKHNEITDNF--EEEKNKAKKKLRLHLVEEFKSEIDEY 414
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024348544 260 NKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQL 298
Cdd:pfam13166 415 KDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQL 453
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
178-396 |
4.99e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 178 EQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMTRKLYNQYEEKM-REEEQKHKAEKEILLEETNRLLKAI 256
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLkESEKEKKKAEKELKKEKEEIEELEK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 257 EESNKKMQITETSIKEKDQR------IGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLR 330
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEklqeklEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024348544 331 ERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLECENKELQDKLEYLMENQ 396
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-304 |
5.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 103 MKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEmnssltsasidlQKTLVDVTLENTDIREQIRNLkhthEQSME 182
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSEL----ESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 183 KLREKQKQLET--AQIENQLLKLKVESSQEANAEVMREMTRKLyNQYEEKMREEEQK----H----KAEKEIllEETNRL 252
Cdd:COG3206 230 EARAELAEAEArlAALRAQLGSGPDALPELLQSPVIQQLRAQL-AELEAELAELSARytpnHpdviALRAQI--AALRAQ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024348544 253 LKaiEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQL-QKQLELNEIQ 304
Cdd:COG3206 307 LQ--QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpELEAELRRLE 357
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
83-304 |
5.68e-03 |
|
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: 39.34 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 83 KEVRATLEKVRKKMYGEyDEMKRKIQQLTNELKVTNAHQESlENHVRVQAAALDSFSEMNSsltsasidlqktlvdVTLE 162
Cdd:pfam17380 392 ERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEE-ARQREVRRLEEERAREMER---------------VRLE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 163 NTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMTRK---LYNQYEEKMR---EEEQ 236
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKrklLEKEMEERQKaiyEEER 534
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024348544 237 KHKAEKEILLEETNRLLKAIEESNKKMQiTETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQ 304
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQEQMRKAT-EERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-363 |
6.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 74 QLKEEMNYIKEVRATLEKVRKKmYGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASIDLQ 153
Cdd:PRK03918 208 EINEISSELPELREELEKLEKE-VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 154 --KTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMTR--KLYNQYEE 229
Cdd:PRK03918 287 elKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 230 KMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQK--------QLELN 301
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcGRELT 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024348544 302 EIQ----LSGAKSESNSDSERSQHLEEVAASLRERIKHLDDMVHCQQK--KVKHMVEEIEMLRKKVKE 363
Cdd:PRK03918 447 EEHrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKK 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-340 |
6.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 152 LQKTLVDVTLENTDIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMREMTRKLYNQYEEKM 231
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 232 REEEQKHKAE--KEILLEETNRLLKAIEESNKKMQITETSIKEKDQRIGELDRLIERME-------------EERHQ-LQ 295
Cdd:COG1196 722 EEEALEEQLEaeREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnllaieeyeelEERYDfLS 801
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024348544 296 KQLElneiqlsgaksesnsDsersqhLEEVAASLRERIKHLDDMV 340
Cdd:COG1196 802 EQRE---------------D------LEEARETLEEAIEEIDRET 825
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
73-407 |
7.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 73 DQLKEEMNYIKEVRATLEKVRKKM--YGEYDEMKRKIQQLTNELKVTNAHQESLENHVRVQAAALDSFSEMNSSLTSASI 150
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 151 DLQKTLVDVTLENtdiREQIRNLKHTHEQSMEKLREKQKQLETAQ-----IENQLLKLKVESSQEANAEVMREMTR---- 221
Cdd:COG4717 178 ELEELLEQLSLAT---EEELQDLAEELEELQQRLAELEEELEEAQeeleeLEEELEQLENELEAAALEERLKEARLllli 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 222 -------------------------------------KLYNQYEEKMREEEQKHKAEKEILLEETnRLLKAIEESNKKMQ 264
Cdd:COG4717 255 aaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEE-ELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 265 ITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAA--SLRERIKHLDDMVHc 342
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLE- 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024348544 343 qqkkvKHMVEEIEMLRKKVKEkelfiiQLLEKISFLECENKELQDKLEYLMENQPKTNVETRDAG 407
Cdd:COG4717 413 -----ELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-406 |
7.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 167 REQIRNLKHTHEQSMEKLREKQKQLETAQIENQLL------KLKVESSQEANAEVMREMTRKLYNQYEEKMREEEQKHKA 240
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 241 EKEILLEETnrlLKAIEESNKKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQ 320
Cdd:PTZ00121 1671 EEDKKKAEE---AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 321 HLeEVAASLRERIKHLDDMVHCQQKKVKHMVEEIemLRKKVKEKELFIIQLLEKisflecENKELQDKLEYLMENQPKTN 400
Cdd:PTZ00121 1748 EA-KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDK------KIKDIFDNFANIIEGGKEGN 1818
|
....*.
gi 2024348544 401 VETRDA 406
Cdd:PTZ00121 1819 LVINDS 1824
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
246-390 |
7.29e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 38.72 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 246 LEETNRLLKAIEESN----KKMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQH 321
Cdd:pfam07888 40 LQERAELLQAQEAANrqreKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024348544 322 LEEVAASLRERIKHLDDMVHCQQKKVKHMVEEIEMLRKKVKEkelFIIQLLEKisflECENKELQDKLE 390
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK---AGAQRKEE----EAERKQLQAKLQ 181
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
182-379 |
7.54e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 182 EKLREKQKQLETAQIENQLLKLKvESSQEANAEVMREMTRKLYNQYEEKMReEEQKHKAEKEILLEETNRLLKAIEESNK 261
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLK-EQAKKALEYYQLKEKLELEEEYLLYLD-YLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 262 KMQITETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNEIQLSGAKSESNSDSERSQHLEEVAASLrerikhlddmvh 341
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA------------ 326
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024348544 342 cqQKKVKHMVEEIEMLRKKVKEKELFIIQLLEKISFLE 379
Cdd:pfam02463 327 --EKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
|
| cdk7 |
TIGR00570 |
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ... |
158-299 |
8.40e-03 |
|
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129661 [Multi-domain] Cd Length: 309 Bit Score: 38.25 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 158 DVTLEN-TDIREQIRNLKHTHEQSMEKLREKQKQLEtaQIENQLLKL-----------KVESSQEANAEV-MREMTRKLY 224
Cdd:TIGR00570 65 DPTVEKeVDIRKRVLKIYNKREEDFPSLREYNDYLE--EVEDIVYNLtnnidlentkkKIETYQKENKDViQKNKEKSTR 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024348544 225 NQYE-EKMREEEQKHKAEKEILLEETNRLLKAIEESNKKMQITETSIKEKDqrigeLDRLIERMEEERHQLQKQLE 299
Cdd:TIGR00570 143 EQEElEEALEFEKEEEEQRRLLLQKEEEEQQMNKRKNKQALLDELETSTLP-----AAELIAQHKKNSVKLEMQVE 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-341 |
9.08e-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: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 72 ADQLKEEMNYIKEVRATLEKVRKKM---------YGEYDEMKRKIQQLtnelkvtnahqESLENHVRVQAAALdsfsemn 142
Cdd:COG4913 227 ADALVEHFDDLERAHEALEDAREQIellepirelAERYAAARERLAEL-----------EYLRAALRLWFAQR------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 143 ssltsaSIDLqktlvdvtlentdIREQIRNLKHTHEQSMEKLREKQKQLETAQIENQLLKLKVESSQEANAEVMremtrk 222
Cdd:COG4913 289 ------RLEL-------------LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL------ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024348544 223 lynqyeEKMREEEQKHKAEKEILLEETNRLLKAIEESnkkmqiTETSIKEKDQRIGELDRLIERMEEERHQLQKQLELNE 302
Cdd:COG4913 344 ------EREIERLERELEERERRRARLEALLAALGLP------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
250 260 270
....*....|....*....|....*....|....*....
gi 2024348544 303 IQLSGAKsesnsdsERSQHLEEVAASLRERIKHLDDMVH 341
Cdd:COG4913 412 AALRDLR-------RELRELEAEIASLERRKSNIPARLL 443
|
|
| |
