|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
361-519 |
5.67e-47 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 162.47 E-value: 5.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 361 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHS------------------- 421
Cdd:pfam06818 3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 422 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEAREgAEQLRAELLQERLRGQEQALRFEQE 482
Cdd:pfam06818 83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 31981859 483 RQTWQEEKERVLRYQREIQGSYMDMYRRNQALEHELR 519
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-523 |
2.40e-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: 66.62 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 296 ERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADPNARPEEEARW---------EVCQK 366
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeeriaqlskELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 367 TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPR-EEAPGSCETDDCKSRGL 445
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 446 LGEAggSEAREGAEQLRAELLQERLRGQEQALRFEQERQTWQEEKERVLRYQREIQGSYMDMY-------RRNQALEHEL 518
Cdd:TIGR02168 840 LEDL--EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeelreleSKRSELRREL 917
|
....*
gi 31981859 519 RLLRE 523
Cdd:TIGR02168 918 EELRE 922
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-523 |
5.06e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 257 EAREELKRDLGDQDVSNSFTQVLEERQRLWLSELkrlyvERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGL 336
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 337 APEprtsgssmeadpNARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLR 416
Cdd:COG1196 311 RRE------------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 417 EAVHSLQEQAPREEApgscETDDCKSRgllgEAGGSEAREGAEQLRAELLQERLRGQEQALRFEQERQTWQEEKERVLRY 496
Cdd:COG1196 379 EELEELAEELLEALR----AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260
....*....|....*....|....*..
gi 31981859 497 QREIQGSYMDMYRRNQALEHELRLLRE 523
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEA 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-432 |
5.25e-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: 45.53 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 248 TTEEVAVLPEAREELKRDLGDqdvsnsfTQVLEERQRLWLSELKRLYVERLhevaQKAERSERNLQLQLFMAQQEQRRLR 327
Cdd:COG4942 67 LARRIRALEQELAALEAELAE-------LEKEIAELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 328 KELRAQQGLAPEPRTSGSSMEADPNARPEEEARWEvcQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQA 407
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELE--AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
170 180
....*....|....*....|....*
gi 31981859 408 QDAELARLREAVHSLQEQAPREEAP 432
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-492 |
1.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 289 ELKRLYVERLHEVAQKAERsERNlqlqlfMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADpNARPEEEARW--EVCQK 366
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEE-DKN------MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIkaEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 367 TAEISLLKQQLREAQAELAQKlAEifslktQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEapgscETDDCKSRGLL 446
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKK-AE------ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE-----EDEKKAAEALK 1695
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31981859 447 GEAggsEAREGAEQLRAELLQERlRGQEQALRFEQERQTWQEEKER 492
Cdd:PTZ00121 1696 KEA---EEAKKAEELKKKEAEEK-KKAEELKKAEEENKIKAEEAKK 1737
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
287-422 |
8.38e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 37.74 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 287 LSELKRLYVERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLApeprtsgSSMEADPNARPEEEARWEVCQK 366
Cdd:pfam04012 2 FKRLGRLVRANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQ-------KQLERRLEQQTEQAKKLEEKAQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 31981859 367 TAeisllkqqLREAQAELAQK-LAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSL 422
Cdd:pfam04012 75 AA--------LTKGNEELAREaLAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAAL 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
361-519 |
5.67e-47 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 162.47 E-value: 5.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 361 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHS------------------- 421
Cdd:pfam06818 3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 422 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEAREgAEQLRAELLQERLRGQEQALRFEQE 482
Cdd:pfam06818 83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 31981859 483 RQTWQEEKERVLRYQREIQGSYMDMYRRNQALEHELR 519
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-523 |
2.40e-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: 66.62 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 296 ERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADPNARPEEEARW---------EVCQK 366
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeeriaqlskELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 367 TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPR-EEAPGSCETDDCKSRGL 445
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 446 LGEAggSEAREGAEQLRAELLQERLRGQEQALRFEQERQTWQEEKERVLRYQREIQGSYMDMY-------RRNQALEHEL 518
Cdd:TIGR02168 840 LEDL--EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeelreleSKRSELRREL 917
|
....*
gi 31981859 519 RLLRE 523
Cdd:TIGR02168 918 EELRE 922
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-523 |
5.06e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 257 EAREELKRDLGDQDVSNSFTQVLEERQRLWLSELkrlyvERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGL 336
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 337 APEprtsgssmeadpNARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLR 416
Cdd:COG1196 311 RRE------------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 417 EAVHSLQEQAPREEApgscETDDCKSRgllgEAGGSEAREGAEQLRAELLQERLRGQEQALRFEQERQTWQEEKERVLRY 496
Cdd:COG1196 379 EELEELAEELLEALR----AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260
....*....|....*....|....*..
gi 31981859 497 QREIQGSYMDMYRRNQALEHELRLLRE 523
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEA 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-523 |
8.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 261 ELKRDLGDQDVS---NSFTQVLEERQRLwLSELKRLYVERLHEVAQKAERSERNLQLQLFM--AQQEQRRLRKELRAQQG 335
Cdd:TIGR02168 217 ELKAELRELELAllvLRLEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVseLEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 336 LApeprtsgSSMEADPNARPEEEARWEVCQK--TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELA 413
Cdd:TIGR02168 296 EI-------SRLEQQKQILRERLANLERQLEelEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 414 RLREAVHSLQEQAPREEApgscETDDCKSRGLLGEAGGSEAREGAEQL--RAELLQERLRGQEQALRfEQERQTWQEEKE 491
Cdd:TIGR02168 369 ELESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLedRRERLQQEIEELLKKLE-EAELKELQAELE 443
|
250 260 270
....*....|....*....|....*....|..
gi 31981859 492 RVLRYQREIQGSYMDMYRRNQALEHELRLLRE 523
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-520 |
1.69e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 294 YVERLHEVAQKAERSERNL------------QLQLFMAQQEQ----RRLRKELRAQQG---------------------- 335
Cdd:TIGR02168 170 YKERRKETERKLERTRENLdrledilnelerQLKSLERQAEKaeryKELKAELRELELallvlrleelreeleelqeelk 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 336 --------LAPEPRTSGSSMEADPNARPEEEARWEVCQK-----TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSR 402
Cdd:TIGR02168 250 eaeeeleeLTAELQELEEKLEELRLEVSELEEEIEELQKelyalANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 403 AQAQAQDAELARLREAVHSLQEQapREEAPGSCETDDCKSRGLlgEAGGSEAREGAEQLRAELLQERLRGQEQALRFEQE 482
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEE--LESLEAELEELEAELEEL--ESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270
....*....|....*....|....*....|....*...
gi 31981859 483 RQTWQEEKERVLRYQREIQGSYMDMyRRNQALEHELRL 520
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKL-EEAELKELQAEL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-523 |
2.11e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 249 TEEVAVLPEAREELKRDLGDQDVSnsfTQVLEERQRLWLSELKRLYVERLHEVAQKAERSERNLQLQLFMAQQEQRR--L 326
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKD---LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 327 RKELRAQQGLAPEPRTSGSSMEADPNARPEE--EARWEVCQKTAEISLLKQQLREAQAELAQKLAEIfslkTQLRGSRAQ 404
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEaaNLRERLESLERRIAATERRLEDLEEQIEELSEDI----ESLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 405 AQAQDAELARlrEAVHSLQEQAPREEAPGSCETDDCKSRGLLGEAGG--SEAREGAEQLRAELLQERLRGQEQALRFEQE 482
Cdd:TIGR02168 864 LEELIEELES--ELEALLNERASLEEALALLRSELEELSEELRELESkrSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 31981859 483 RQTWQEEKERVLryqREIQGSYMDMYRRNQALEHELRLLRE 523
Cdd:TIGR02168 942 QERLSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-432 |
5.25e-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: 45.53 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 248 TTEEVAVLPEAREELKRDLGDqdvsnsfTQVLEERQRLWLSELKRLYVERLhevaQKAERSERNLQLQLFMAQQEQRRLR 327
Cdd:COG4942 67 LARRIRALEQELAALEAELAE-------LEKEIAELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 328 KELRAQQGLAPEPRTSGSSMEADPNARPEEEARWEvcQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQA 407
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELE--AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
170 180
....*....|....*....|....*
gi 31981859 408 QDAELARLREAVHSLQEQAPREEAP 432
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-522 |
1.66e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 260 EELKRDLgdqDVSNSFTQVLEERQRLWLSELKRLYVE-----RLHEVAQKAERSERNLQLQLF-MAQQEQRRLRKELRAQ 333
Cdd:pfam12128 600 EELRERL---DKAEEALQSAREKQAAAEEQLVQANGElekasREETFARTALKNARLDLRRLFdEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 334 QGLAPEPRTSgssMEADPNARPEEEARWEVCQKtaeisllkQQLREAQAELAQKLAEIFSlktqlrgsraqaqAQDAELA 413
Cdd:pfam12128 677 KDSANERLNS---LEAQLKQLDKKHQAWLEEQK--------EQKREARTEKQAYWQVVEG-------------ALDAQLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 414 RLREAVHSLQEQAPREEApgSCETD---DCKSRGLLGEAGGSEAR---------EGAEQLRAELLQERLRGQEQalrFEQ 481
Cdd:pfam12128 733 LLKAAIAARRSGAKAELK--ALETWykrDLASLGVDPDVIAKLKReirtlerkiERIAVRRQEVLRYFDWYQET---WLQ 807
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 31981859 482 ERQTWQEEKERVLRYQREIQGSY----MDMYRRNQALEHELRLLR 522
Cdd:pfam12128 808 RRPRLATQLSNIERAISELQQQLarliADTKLRRAKLEMERKASE 852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-492 |
1.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 289 ELKRLYVERLHEVAQKAERsERNlqlqlfMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADpNARPEEEARW--EVCQK 366
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEE-DKN------MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIkaEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 367 TAEISLLKQQLREAQAELAQKlAEifslktQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEapgscETDDCKSRGLL 446
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKK-AE------ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE-----EDEKKAAEALK 1695
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31981859 447 GEAggsEAREGAEQLRAELLQERlRGQEQALRFEQERQTWQEEKER 492
Cdd:PTZ00121 1696 KEA---EEAKKAEELKKKEAEEK-KKAEELKKAEEENKIKAEEAKK 1737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-517 |
2.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 289 ELKRLYVERLHEVAQKAERSERNLQLQlFMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADpNARPEEEARW--EVCQK 366
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIkaEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 367 TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEAPGSCETDDCKSRGLL 446
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31981859 447 GEAGGSEAREgAEQLRAELLQERLRGQEQALRFEQERQTWQE------EKERVLRYQREIQGSYMDMYRRNQALEHE 517
Cdd:PTZ00121 1708 KKKEAEEKKK-AEELKKAEEENKIKAEEAKKEAEEDKKKAEEakkdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-473 |
2.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 280 EERQRLWLSELKRLYVERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKE---LRAQQGLAPEPRTSGSSMEADPNARPE 356
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleeLRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 357 E--EARWEvcQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEApgS 434
Cdd:COG4913 327 EleAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE--A 402
|
170 180 190
....*....|....*....|....*....|....*....
gi 31981859 435 CETDDCKSRGLLgeaggSEAREGAEQLRAELlqERLRGQ 473
Cdd:COG4913 403 LEEALAEAEAAL-----RDLRRELRELEAEI--ASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
319-523 |
3.30e-04 |
|
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: 43.21 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 319 AQQEQRRLRKELRAQQGlapeprtsgssmEADPNARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQL 398
Cdd:COG4942 25 AEAELEQLQQEIAELEK------------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 399 RGSRAQAQAQDAELARLREAVHSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEAREGAEQLRA----------ELLQE 468
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAdlaelaalraELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 31981859 469 RLRGQEQALRFEQERQTWQEEKERVLRYQREIQGSYMDMYRRNQALEHELRLLRE 523
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-502 |
4.26e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 248 TTEEVAVLPEAREELKRDLGD-QDVSNSFTQVLEErqrlwLSELKRLYVERLHEVAQKAERSERNLQlQLFMAQQEQRRL 326
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEElQKELYALANEISR-----LEQQKQILRERLANLERQLEELEAQLE-ELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 327 RKELRAQQGLAPEPRTSGSS-MEADPNARPEEEARWEVCQKTAEisllkqQLREAQAELAQKLAeifSLKTQLRGSRAQA 405
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAeLEELEAELEELESRLEELEEQLE------TLRSKVAQLELQIA---SLNNEIERLEARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 406 QAQDAELARLReavhslQEQAPREEAPGSCETDDCKSRGLLGEAGGSEAREGAEQLRAEL--LQERLRGQEQALR-FEQE 482
Cdd:TIGR02168 410 ERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALeeLREELEEAEQALDaAERE 483
|
250 260
....*....|....*....|
gi 31981859 483 RQTWQEEKERVLRYQREIQG 502
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEG 503
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
305-431 |
5.60e-04 |
|
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: 42.03 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 305 AERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADPNARPEEEARWEvcQKTAEISLLKQQLR------ 378
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVK--AAQAQLAQAQIDLArrrvla 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31981859 379 -----------EAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSlQEQAPREEA 431
Cdd:pfam00529 134 piggisreslvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELS-GAQLQIAEA 196
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
280-517 |
5.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 280 EERQRLWLSELKRLYVERLHEVAQKAERSERNLQlQLFMAQQEQRRlRKELRAQqglAPEPRTSGSSMEADPNARPEEEA 359
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKK-ADEAKKK---AEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 360 RWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEAPGSCETDD 439
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 440 CKSRGLLGEAGGSEAREGAEQLR-AELLQ--ERLRGQEQALRFEQERQTWQEEKERVLRYQREIQGSYMDMYRRNQALEH 516
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKkAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
.
gi 31981859 517 E 517
Cdd:PTZ00121 1610 E 1610
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
295-492 |
5.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 295 VERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEprtsgSSMEADPNARPEEEARWEVcQKTA------ 368
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----SWDEIDVASAEREIAELEA-ELERldassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 369 EISLLKQQLREAQAELAQklaeifsLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPReeapgscetddcksrglLGE 448
Cdd:COG4913 686 DLAALEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEA-----------------AED 741
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 31981859 449 AGGSEAREGAEQLRAELLQERLRGQEQAlRFEQERQTWQEEKER 492
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNR 784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-492 |
8.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 289 ELKRLYVERLHEVAQKAERSERNLQLQLFMAQQ-EQRRLRKELRAQQGL--APEPRTSGSSMEADPNARPEEEAR-WEVC 364
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKkkADEAKKAEEKKKADEAKKKAEEAKkADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 365 QKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLR---------EAVHSLQEQAPREEAPGSC 435
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeakkkadAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 31981859 436 ETDDCKSRGLLGEAggsEAREGAEQLRAEllQERLRGQEQALRFEQERQTWQEEKER 492
Cdd:PTZ00121 1401 EEDKKKADELKKAA---AAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKK 1452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
244-431 |
9.68e-04 |
|
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: 41.67 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 244 FSCPTTEEVAVLPEAREELKRDLGDQDVSNSFTQVLEERQRLWLSELKRL--YVERLHEVAQKAERSERNLQLQLFMAQQ 321
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 322 EQRRLRKELRAQQG-LAPEPRTSGSSMEADP------NARPEEEARWEVCQKTAEISLLKQ--QLREAQAELAQKLAEIF 392
Cdd:COG4942 91 EIAELRAELEAQKEeLAELLRALYRLGRQPPlalllsPEDFLDAVRRLQYLKYLAPARREQaeELRADLAELAALRAELE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 31981859 393 SLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEA 431
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
251-501 |
2.03e-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: 40.65 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 251 EVAVLPEAREELKRDLGdqdVSNSFTQVLEERQRLWLSELKRLYVERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKEL 330
Cdd:pfam07888 74 QRRELESRVAELKEELR---QSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 331 RAQQgLAPEPRTSGSSMEADPNARPEEEARWEVCQktAEISLLKQQLREAQAELAQKLAEIFSLK---TQLRGSRAQAQA 407
Cdd:pfam07888 151 ELER-MKERAKKAGAQRKEEEAERKQLQAKLQQTE--EELRSLSKEFQELRNSLAQRDTQVLQLQdtiTTLTQKLTTAHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 408 QDAELARLREAVHSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSE---AREGAEQLRAELLQERLRGQEQALRFEQERQ 484
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAElhqARLQAAQLTLQLADASLALREGRARWAQERE 307
|
250 260
....*....|....*....|.
gi 31981859 485 TWQE----EKERVLRYQREIQ 501
Cdd:pfam07888 308 TLQQsaeaDKDRIEKLSAELQ 328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
280-492 |
3.37e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 280 EERQRLwlSELKRlyVERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRTSGSSMEADPNARPEEEA 359
Cdd:PTZ00121 1221 EDAKKA--EAVKK--AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 360 RWEVCQKTAEislLKQQLREA-QAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEApgscETD 438
Cdd:PTZ00121 1297 KAEEKKKADE---AKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA----EAA 1369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 31981859 439 DCKSrgllgeaggSEAREGAEQLRAElLQERLRGQEQALRFEQERQTWQEEKER 492
Cdd:PTZ00121 1370 EKKK---------EEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKA 1413
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
294-532 |
4.74e-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: 39.94 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 294 YVERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRTSgssmEADPNARpEEEARWEVCQKTAE-ISL 372
Cdd:COG3096 442 YLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERS----QAWQTAR-ELLRRYRSQQALAQrLQQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 373 LKQQLREAQAEL-----AQKLAEIFSLktQLRGSRAQAQAQDAELARLREAVHSLQEQApreeapgscetddcksrgllg 447
Cdd:COG3096 517 LRAQLAELEQRLrqqqnAERLLEEFCQ--RIGQQLDAAEELEELLAELEAQLEELEEQA--------------------- 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 448 eaggSEAREGAEQLRAELLQ-----ERLRGQEQALRFEQER---------------QTWQEEKERVLRYQREIQGSYMDM 507
Cdd:COG3096 574 ----AEAVEQRSELRQQLEQlrariKELAARAPAWLAAQDAlerlreqsgealadsQEVTAAMQQLLEREREATVERDEL 649
|
250 260
....*....|....*....|....*
gi 31981859 508 YRRNQALEHELRLLREPPTSWSPRL 532
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDPRL 674
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
279-533 |
6.14e-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: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 279 LEERQRlwlsELKRLyveRLHEVAQKAERSERNLQLQLfMAQQEQRRLRKELRAqqglapeprtsgssmeADPNARPEEE 358
Cdd:pfam17380 355 QEERKR----ELERI---RQEEIAMEISRMRELERLQM-ERQQKNERVRQELEA----------------ARKVKILEEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 359 ARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAPREEAPGSCETD 438
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 439 DCKSRGLLGEAGGSEAREGAEQLRAELLQERLRGQEQALRFEQERQTWQEE--KERVLRYQREIQGSYM---DMYRRNQA 513
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErrKQQEMEERRRIQEQMRkatEERSRLEA 570
|
250 260
....*....|....*....|
gi 31981859 514 LEHELRLLREPPTSWSPRLE 533
Cdd:pfam17380 571 MEREREMMRQIVESEKARAE 590
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
300-427 |
7.25e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 300 EVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPepRTSGSSMEADpnarpeeearwevcQKTAEISLLKQQLRE 379
Cdd:COG1566 103 EAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYK--KGAVSQQELD--------------EARAALDAAQAQLEA 166
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 31981859 380 AQAELAQKLAEIfSLKTQLRGSRAQAQAQDAELARLREAVHSLQEQAP 427
Cdd:COG1566 167 AQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAELNLARTTIRAP 213
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
369-485 |
7.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 369 EISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAE----LARLREAVHSLQEQAPREEAPGSCETDDCKSRG 444
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 31981859 445 LLGEAGGSEAREGAEQLRAELLQERLRGQEQALRFEQERQT 485
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
287-422 |
8.38e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 37.74 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981859 287 LSELKRLYVERLHEVAQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLApeprtsgSSMEADPNARPEEEARWEVCQK 366
Cdd:pfam04012 2 FKRLGRLVRANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQ-------KQLERRLEQQTEQAKKLEEKAQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 31981859 367 TAeisllkqqLREAQAELAQK-LAEIFSLKTQLRGSRAQAQAQDAELARLREAVHSL 422
Cdd:pfam04012 75 AA--------LTKGNEELAREaLAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAAL 123
|
|
| |
