|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
380-565 |
3.54e-86 |
|
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: 266.48 E-value: 3.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 380 TQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKN 459
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 460 EAELLREKVNLLEQELQELRAQAALARDMGPPTFPE------------DVPALQRELERLRAELREERQGHDQMSSGFQH 527
Cdd:pfam06818 81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYEsdeakeqrqeeaDLGSLRREVERLRAELREERQRRERQASSFEQ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 10440566 528 ERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQ 565
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-567 |
5.81e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 235 GGSKLGHSNKADKGPSCVRSPISTDECSIQELEQKLLEREGALQKLQRSFE--EKELASSLAYEERPRRCRDELEGPEPK 312
Cdd:TIGR02168 658 GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEelEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 313 GGNKLKQASQKSQRAQQVLHLQVLQLQQEKRQL---RQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSG 389
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 390 EISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVN 469
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 470 LLEQELQELRaqaalardmgpptfpEDVPALQRELERLRAELREERQGHDQMSSGFQH--ERL--VWKEEKEKVIQYQKQ 545
Cdd:TIGR02168 898 ELSEELRELE---------------SKRSELRRELEELREKLAQLELRLEGLEVRIDNlqERLseEYSLTLEEAEALENK 962
|
330 340
....*....|....*....|..
gi 10440566 546 LQQSYVAMYQRNQRLEKALQQL 567
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
263-523 |
6.81e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 263 IQELEQKLLEREGALQKLQRSFEEKELASSLAYEERprrcrdelegpepkggNKLKQASQKSQRAQQVLHLQVLQLQQEK 342
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEE----------------YELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDT 422
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 423 RGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARdmgpptfpEDVPALQR 502
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL--------ELLAELLE 470
|
250 260
....*....|....*....|.
gi 10440566 503 ELERLRAELREERQGHDQMSS 523
Cdd:COG1196 471 EAALLEAALAELLEELAEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
264-592 |
1.11e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 264 QELEQKLLEREGALQKLQRSFEEKELAsslAYEERPRRCRDELEgpepkggnKLKQASQKSQRAQQVLHLQVLQLQQEKR 343
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELE---ELEAELEELEAELE--------ELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 344 QLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTR 423
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 424 GKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARdmgpptfpEDVPALQRE 503
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE--------EALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 504 LERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLE--KALQQLARGDSAGEPLEVDL 581
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLllLEAEADYEGFLEGVKAALLL 516
|
330
....*....|.
gi 10440566 582 EGADIPYEDII 592
Cdd:COG1196 517 AGLRGLAGAVA 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-513 |
5.65e-11 |
|
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: 65.86 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 260 ECSIQELEQKLLEREGALQKLQRSFEEKELAsslaYEERPRRCRDELEGPEPKGGN-----KLKQASQKSQRAQQVLHLq 334
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSI- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 335 vlqlqqekRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILG 414
Cdd:TIGR02169 311 --------AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 415 LKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDmGPPTFP 494
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-KLEQLA 461
|
250
....*....|....*....
gi 10440566 495 EDVPALQRELERLRAELRE 513
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDR 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
341-569 |
7.64e-11 |
|
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: 64.01 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLK 420
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 DTRGKLEGLeLRTQDLEGalRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQaalardmgpptfpedvpal 500
Cdd:COG4942 101 AQKEELAEL-LRALYRLG--RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------------- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10440566 501 QRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLAR 569
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-584 |
2.37e-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: 63.92 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLK 420
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 DTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDmGPPTFPEDVPAL 500
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE-QLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 501 QRELERLRAELRE-ERQGHDQmssgfQHERLVWKEEKEKVIQYQKQLQQSYVAMY--QRNQRLEKALQQLARGDSAGEPL 577
Cdd:TIGR02168 392 ELQIASLNNEIERlEARLERL-----EDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEEL 466
|
....*..
gi 10440566 578 EVDLEGA 584
Cdd:TIGR02168 467 REELEEA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-583 |
6.42e-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: 62.38 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 264 QELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGpepkggnklkqASQKSQRAQQVLHLQVLQLQQEKR 343
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTA-----------ELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 344 QLRQELESLMKEQDLLETKLRSYEREktsfgpaLEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTR 423
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 424 GKLEGLELRTQDLEGALRTkglelevCENELQRKKNEAELLREKVNLLEQELQELRAQAAlardmgpptfpedvpALQRE 503
Cdd:TIGR02168 358 AELEELEAELEELESRLEE-------LEEQLETLRSKVAQLELQIASLNNEIERLEARLE---------------RLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 504 LERLRAELREERQGHDQMSSGFQHERLVWK--------EEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSAGE 575
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELeeeleelqEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
....*...
gi 10440566 576 PLEVDLEG 583
Cdd:TIGR02168 496 RLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-584 |
8.38e-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: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLK 420
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 DTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDmGPPTFPEDVPAL 500
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE-RLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 501 QRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSAGEPLEVD 580
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
....
gi 10440566 581 LEGA 584
Cdd:TIGR02168 917 LEEL 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-538 |
7.97e-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: 58.93 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 267 EQKLLEREGALQKlQRSFEEKELASSlayEERPRRCRDELEGPEPKGGNKLKQASQKSQRAQQVLHLQVLQLQqEKRQLR 346
Cdd:TIGR02169 676 LQRLRERLEGLKR-ELSSLQSELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-DLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 347 QELESLMKEQDLLETKLRSYEREKTSFGPALEETqwevcqksgEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKL 426
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 427 EGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQaalARDMGpptfpEDVPALQRELER 506
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA---LRDLE-----SRLGDLKKERDE 893
|
250 260 270
....*....|....*....|....*....|..
gi 10440566 507 LRAELREERQGHDQMSSGFQHERLVWKEEKEK 538
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
341-535 |
1.77e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSY--EREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEV--------NAKAS 410
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeleaqirGNGGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 411 EILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDmgp 490
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR--- 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 10440566 491 ptfpedvpALQRELERLRAELREERQGHDQMSSGFQHERLVWKEE 535
Cdd:COG4913 416 --------DLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-486 |
4.10e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 263 IQELEQKLLEREGALQKLQRSFEEKElASSLAYEERPRRCRDELEGPEPKGgNKLKQASQKSQRAQQVLHLQVLQLQQEK 342
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLE-QQKQILRERLANLERQLEELEAQL-EELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKdt 422
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-- 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10440566 423 rgkleglELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALAR 486
Cdd:TIGR02168 432 -------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-569 |
6.68e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 342 KRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKD 421
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 422 TRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALardmgpptfpedvpaLQ 501
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE---------------LK 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 502 RELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQsyvamyQRNQ--RLEKALQQLAR 569
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS------LNNEieRLEARLERLED 414
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
341-567 |
1.01e-07 |
|
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: 54.90 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLK 420
Cdd:pfam07888 88 ELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 DTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLL--------------EQELQELRA--QAAL 484
Cdd:pfam07888 168 EEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqklttahrkeaenEALLEELRSlqERLN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 485 ARDMGPPTFPEDVPALQRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKAL 564
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAEL 327
|
...
gi 10440566 565 QQL 567
Cdd:pfam07888 328 QRL 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-512 |
1.33e-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: 54.69 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 263 IQELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKqaSQKSQRAQQVLHLQVLQLQQEK 342
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS--KLEEEVSRIEARLREIEQKLNR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQE-LESLMKEqdlLETKLRSYEREKTSFGPALEETQwevcqksGEISLLKQQLKESQTEVNAKASEILGLKAQLKD 421
Cdd:TIGR02169 824 LTLEKEyLEKEIQE---LQEQRIDLKEQIKSIEKEIENLN-------GKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 422 TRGKLEGLELRTQDLEGalrtkglelevcenELQRKKNEAELLREKVNLLEQELQELraQAALARDMGPPTFPEDVPALQ 501
Cdd:TIGR02169 894 LEAQLRELERKIEELEA--------------QIEKKRKRLSELKAKLEALEEELSEI--EDPKGEDEEIPEEELSLEDVQ 957
|
250
....*....|.
gi 10440566 502 RELERLRAELR 512
Cdd:TIGR02169 958 AELQRVEEEIR 968
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
341-568 |
1.55e-07 |
|
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: 54.26 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLK 420
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 DTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALardmgpptFPEDVPAL 500
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS--------LKEKIEKL 529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10440566 501 QRELERLRAELREERQGHDQMSSGFQHERLvwKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLA 568
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELKKENL--EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
341-515 |
4.85e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFgpaleetqwevcqkSGEISLLKQQLKEsqtevnaKASEILGLKAQLK 420
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREEL--------------AEEVRDLRERLEE-------LEEERDDLLAEAG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 DTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAA-LARDMgpPTFPEDVPA 499
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAeLESEL--EEAREAVED 381
|
170
....*....|....*.
gi 10440566 500 LQRELERLRAELREER 515
Cdd:PRK02224 382 RREEIEELEEEIEELR 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
345-569 |
7.57e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 345 LRQELESLMKEQDLLETKLRSYEREKTSFGPaleetqwevcqkSGEISLLKQQLKEsqtevnakaseilgLKAQLKDTRG 424
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDL------------SEEAKLLLQQLSE--------------LESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 425 KLEGLELRTQDLEGALRTKGLEL-EVCENELQRKkneaelLREKVNLLEQELQELRAQAAlardmgpPTFPeDVPALQRE 503
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALpELLQSPVIQQ------LRAQLAELEAELAELSARYT-------PNHP-DVIALRAQ 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10440566 504 LERLRAELREERQghdQMSSGFQHERLVWKEEkekviqyQKQLQQSYVAMYQRNQRLEKALQQLAR 569
Cdd:COG3206 300 IAALRAQLQQEAQ---RILASLEAELEALQAR-------EASLQAQLAQLEARLAELPELEAELRR 355
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-509 |
1.01e-06 |
|
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: 50.31 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQT---------EVNAKASE 411
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 412 ILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEaelLREKVNLLEQELQELRAQAALARdmgpP 491
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA----A 170
|
170
....*....|....*...
gi 10440566 492 TFPEDvpaLQRELERLRA 509
Cdd:COG1579 171 KIPPE---LLALYERIRK 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
390-578 |
1.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 390 EISLLKQQLKESQtevnAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAEL--LREK 467
Cdd:COG4717 72 ELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELaeLPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 468 VNLLEQELQELRAQAalardmgpptfpEDVPALQRELERLRAELREERQGHDQMssgfQHERLV-WKEEKEKVIQYQKQL 546
Cdd:COG4717 148 LEELEERLEELRELE------------EELEELEAELAELQEELEELLEQLSLA----TEEELQdLAEELEELQQRLAEL 211
|
170 180 190
....*....|....*....|....*....|..
gi 10440566 547 QQSYVAMYQRNQRLEKALQQLARGDSAGEPLE 578
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-569 |
1.58e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 403 TEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKglELEVCENELQRKKNEAELLREKVNLLEQELQELRAQa 482
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA--ELEELRAELARLEAELERLEARLDALREELDELEAQ- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 483 aLARDMGpptfpEDVPALQRELERLRAELREERQGHDQMS--------------SGFQHERLVWKEEKEKVIQYQKQLQQ 548
Cdd:COG4913 332 -IRGNGG-----DRLEQLEREIERLERELEERERRRARLEallaalglplpasaEEFAALRAEAAALLEALEEELEALEE 405
|
170 180
....*....|....*....|.
gi 10440566 549 SYVAMYQRNQRLEKALQQLAR 569
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEA 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
341-487 |
2.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEvcQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLK 420
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10440566 421 DTRGKL-EGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARD 487
Cdd:COG4717 174 ELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-596 |
2.42e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 390 EISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVN 469
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 470 LLEQELQELRAQAALARDmGPPTFPEDVPALQRELERLRAELREERQGHDQMSSGFQheRLVWKEEKEKVIQYQKQLQQS 549
Cdd:COG4372 119 ELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAEQALDELLKEANRN 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 10440566 550 YVAMYQRNQRLEKALQQLARGDSAGEPLEVDLEGADIPYEDIIATEI 596
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
390-556 |
4.31e-06 |
|
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: 48.38 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 390 EISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKN---------E 460
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 461 AELLREKVNLLEQELQELRAQAALARdmgpptfpEDVPALQRELERLRAELREERQGHDQMSSGFQHERlvwKEEKEKVI 540
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELE--------EELAELEAELAELEAELEEKKAELDEELAELEAEL---EELEAERE 166
|
170
....*....|....*.
gi 10440566 541 QYQKQLQQSYVAMYQR 556
Cdd:COG1579 167 ELAAKIPPELLALYER 182
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
398-569 |
4.32e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 49.08 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 398 LKESQTEVNaKASEILGlKAQLKDTRGKLEGLELRTQDLEGALRtkglelevcenELQRKKN------EAELLREKVNLL 471
Cdd:COG3524 160 LAESEELVN-QLSERAR-EDAVRFAEEEVERAEERLRDAREALL-----------AFRNRNGildpeaTAEALLQLIATL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 472 EQELQELRAQAALARDMGPPTFPEdVPALQRELERLRAELREERQghdQMSSGFQHERLVwkeekEKVIQYQK-QLQQSY 550
Cdd:COG3524 227 EGQLAELEAELAALRSYLSPNSPQ-VRQLRRRIAALEKQIAAERA---RLTGASGGDSLA-----SLLAEYERlELEREF 297
|
170 180
....*....|....*....|.
gi 10440566 551 vamyqRNQRLEKALQQL--AR 569
Cdd:COG3524 298 -----AEKAYTSALAALeqAR 313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
344-488 |
6.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 344 QLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQwevcqKSGEISLLKQQLKESQTEVNAKAS-------EILGLK 416
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSArytpnhpDVIALR 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10440566 417 AQLKDTRGKLEGlelRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDM 488
Cdd:COG3206 298 AQIAALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
387-513 |
1.24e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 387 KSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLRE 466
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 10440566 467 KVNLLEQELQELR---AQAALARDMGPPTFPEDVPALQRELERLRAELRE 513
Cdd:COG1196 729 QLEAEREELLEELleeEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
395-516 |
1.41e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 395 KQQLKESQTEVNAKASEILgLKAQ-------------LKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEA 461
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEAL-LEAKeeihklrnefekeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10440566 462 ELLREKVNLLEQELQELRAQA--ALardmgpptfpEDVPALQRE------LERLRAELREERQ 516
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQlqEL----------ERISGLTAEeakeilLEKVEEEARHEAA 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-578 |
1.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYEREKTsfgpaleetqwevcQKSGEISLLKQQLKESQTEVNAKASEilglKAQLKDT 422
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELE--------------EVLREINEISSELPELREELEKLEKE----VKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 423 RGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVnlleQELQELRAQAALARDMGppTFPEDVPALQR 502
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV----KELKELKEKAEEYIKLS--EFYEEYLDELR 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10440566 503 ELERLRAELREERQG-HDQMSSGFQHE-RLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLaRGDSAGEPLE 578
Cdd:PRK03918 311 EIEKRLSRLEEEINGiEERIKELEEKEeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL-KKRLTGLTPE 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-575 |
1.59e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 263 IQELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEgpepkggnKLKQASQKSQRaqqvlhlqvlqlqqEK 342
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE--------ELQQRLAELEE--------------EL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYEREKTsfgpaLEETQWEVCQKSG--EISLLKQQLKESQTEVNAKASEILGL----- 415
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER-----LKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLlallf 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 416 ------KAQLKDTRGKLEGL----ELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALA 485
Cdd:COG4717 291 lllareKASLGKEAEELQALpaleELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 486 R-----DMGPPTFPEDVPA----------LQRELERLRAELREERQGHDQMSSGFQHERLvwKEEKEKVIQYQKQLQQSY 550
Cdd:COG4717 371 EiaallAEAGVEDEEELRAaleqaeeyqeLKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEL 448
|
330 340
....*....|....*....|....*
gi 10440566 551 VAMYQRNQRLEKALQQLARGDSAGE 575
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAE 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-569 |
1.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 252 VRSPISTDECSIQELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKSQRAQQVL 331
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 332 HLQVLQLQQEKRQLRqeLESLMKEQDLLETKLRSYEREKTSF-GPALEETQWEVCQKSGEISLLKQQLKESQ------TE 404
Cdd:PRK03918 483 RELEKVLKKESELIK--LKELAEQLKELEEKLKKYNLEELEKkAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkklAE 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 405 VNAKASEILGLKAQLKDTRGKL-----EGLELRTQDLEGA------LRTKGLELEVCENELQRKKNEAELLREKVNLLEQ 473
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 474 ELQELRAQ-AALARDMGPPTFP---EDVPALQRELERLRAELREERQGHDQMSSGFqhERLvwKEEKEKVIQYQKQLqqs 549
Cdd:PRK03918 641 RLEELRKElEELEKKYSEEEYEelrEEYLELSRELAGLRAELEELEKRREEIKKTL--EKL--KEELEEREKAKKEL--- 713
|
330 340
....*....|....*....|
gi 10440566 550 yvamyqrnQRLEKALQQLAR 569
Cdd:PRK03918 714 --------EKLEKALERVEE 725
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
269-513 |
2.80e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 269 KLLEREGALQKLQRSFEEKELASslayeerpRRCRDELEGPEPKGGNKLKQASQKSQRAQQVLHLQVLQLQQEKRQLRQE 348
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH--------KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 349 LESLMKEQDLLETkLRSYEREKTSFGPALEETQWEvcqKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEG 428
Cdd:pfam05557 75 AELNRLKKKYLEA-LNKKLNEKESQLADAREVISC---LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 429 LELRTQDLEGA--------LRTKGLELEVC----------------------ENELQRKKNEAELLRE---KVNLLEQEL 475
Cdd:pfam05557 151 AEQLRQNLEKQqsslaeaeQRIKELEFEIQsqeqdseivknskselaripelEKELERLREHNKHLNEnieNKLLLKEEV 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 10440566 476 QELRAQaaLARDMGpptFPEDVPALQRELERLRAELRE 513
Cdd:pfam05557 231 EDLKRK--LEREEK---YREEAATLELEKEKLEQELQS 263
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
343-596 |
3.17e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDT 422
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 423 RGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMgpptfpedvpALQR 502
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA----------EAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 503 ELERLRAELREerqghdQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSAGEPLEVDLE 582
Cdd:COG4372 184 ALDELLKEANR------NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250
....*....|....
gi 10440566 583 GADIPYEDIIATEI 596
Cdd:COG4372 258 KEIEELELAILVEK 271
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-483 |
3.85e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 262 SIQELEqKLLEREGALQKLQRSfEEKELASSL----AYEERPRRCRDELEG--PEPKGGNKLKQASQKSQRAQQVLHLQV 335
Cdd:PRK03918 177 RIERLE-KFIKRTENIEELIKE-KEKELEEVLreinEISSELPELREELEKleKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 336 LQLQQEKRQLRQELESLMKEQDLLETKLRSYE--REKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEIL 413
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 414 GLKAQLKDTRGKLEGLELRTQDLEGALRT------------------KGLELEVCENELQRKKNEAELLREKVNLLEQEL 475
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkkrlTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
....*...
gi 10440566 476 QELRAQAA 483
Cdd:PRK03918 415 GELKKEIK 422
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
343-477 |
4.57e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLetklrSYERektsfgpaLEETQWEVCQKSGEISLLKQQLKESQTEVNakasEILGLKAQLKDT 422
Cdd:COG0542 421 EQLEIEKEALKKEQDEA-----SFER--------LAELRDELAELEEELEALKARWEAEKELIE----EIQELKEELEQR 483
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10440566 423 RGKLEGLELRTQDLEGALRTKG--LELEVCENELQR-----------KKNEAEllREKVNLLEQELQE 477
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAplLREEVTEEDIAEvvsrwtgipvgKLLEGE--REKLLNLEEELHE 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-489 |
5.45e-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: 46.20 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 260 ECSIQELEQKLLEREGALQKLQRSFEE--KELASSLAYEERPRRCRDELEgpepkggNKLKQASQKSQRAqqvlhlqvlq 337
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEElkEELESLEAELEELEAELEELE-------SRLEELEEQLETL---------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 338 lQQEKRQLRQELESLMKEQDLLETKLRSYEREKtsfgpaleeTQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKA 417
Cdd:TIGR02168 385 -RSKVAQLELQIASLNNEIERLEARLERLEDRR---------ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10440566 418 QLKDTRGKLEGLELRTQDLEGALRTKglelevcENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMG 489
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAA-------ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
315-574 |
5.56e-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: 45.91 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 315 NKLKQASQKSQRAQQVLHLQVLqlqqEKRQLRQELESLMKEQDLLETKLRSYEREktsfgpaLEETQWEVCQKSGEISLL 394
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRALEQE-------LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 395 KQQLKESQTEVnakaSEILGlKAQLKDTRGKLEGLeLRTQDLEGALRTkgleLEVCENELQRKKNEAELLREKVNLLEQE 474
Cdd:COG4942 96 RAELEAQKEEL----AELLR-ALYRLGRQPPLALL-LSPEDFLDAVRR----LQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 475 LQELRAQAALARdmgpptfpedvpALQRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMY 554
Cdd:COG4942 166 RAELEAERAELE------------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|
gi 10440566 555 QRNQRLEKALQQLARGDSAG 574
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKG 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-485 |
7.76e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 263 IQELEQKLLEREGALQKLQRSFEEKElasslAYEERPRRCRDELEgpepkggnklkqaSQKSQRAQQVLHLQVLQLQQEK 342
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAELE-------------ELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYERektsfgpaLEEtqwevcqksgEISLLKQQLKESQTEVNAKASEI-LGLKAQLKD 421
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRE--------LEE----------ELEELEAELAELQEELEELLEQLsLATEEELQD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10440566 422 TRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKvNLLEQELQELRAQAALA 485
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALL 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
341-510 |
1.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGpALEETQWEV-----CQK---------------SGEISLLKQQLKE 400
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEidvasAEReiaeleaelerldasSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 401 SQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGAL-----------------RTKGLELEVCENELQRK-KNEAE 462
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaedlarlelralleeRFAAALGDAVERELRENlEERID 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 10440566 463 LLREKVNLLEQELQELRAQ-----AALARDMGPptFPEDVPALQRELERLRAE 510
Cdd:COG4913 777 ALRARLNRAEEELERAMRAfnrewPAETADLDA--DLESLPEYLALLDRLEED 827
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
258-568 |
1.99e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 258 TDECSIQELEQKLlerEGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKS----QRAQQVLHL 333
Cdd:TIGR00618 376 TLTQHIHTLQQQK---TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYaelcAAAITCTAQ 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 334 QVLQLQQEKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQksgeisllkqqLKESQTEVNAKASEIL 413
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP-----------LCGSCIHPNPARQDID 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 414 GLKAqlkdTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRaqaalardmgpptf 493
Cdd:TIGR00618 522 NPGP----LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK-------------- 583
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10440566 494 pEDVPALQRELERLRAELREERQgHDQMSSGFQHERLVWKEEKEKVIQyqkqlqqsyVAMYQRNQRLEKALQQLA 568
Cdd:TIGR00618 584 -EDIPNLQNITVRLQDLTEKLSE-AEDMLACEQHALLRKLQPEQDLQD---------VRLHLQQCSQELALKLTA 647
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
341-568 |
3.01e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYERektsfgpALEETQWEVCQKSGEISLLKQQLKESQTEVnAKASEILGLKAQLK 420
Cdd:PRK10246 420 EQRPLRQRLVALHGQIVPQQKRLAQLQV-------AIQNVTQEQTQRNAALNEMRQRYKEKTQQL-ADVKTICEQEARIK 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 421 D---TRGKLE--------------------GLEL-----RTQDLE---GALRTKGL----ELEVCENELQRKKNEAELLR 465
Cdd:PRK10246 492 DleaQRAQLQagqpcplcgstshpaveayqALEPgvnqsRLDALEkevKKLGEEGAalrgQLDALTKQLQRDESEAQSLR 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 466 EKVNLLEQELQELRAQAALARDMGpptfpEDVPALQRELERLRAELREERQGHDQMSSGFQHERLvwkeekekVIQYQKQ 545
Cdd:PRK10246 572 QEEQALTQQWQAVCASLNITLQPQ-----DDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQ--------IIQYQQQ 638
|
250 260
....*....|....*....|...
gi 10440566 546 LQqsyvamyQRNQRLEKALQQLA 568
Cdd:PRK10246 639 IE-------QRQQQLLTALAGYA 654
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-479 |
4.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 260 ECSIQELEQKLLEREGALQKLQRSFEE-----KELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKSQRAQQVLHLQ 334
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEEleekvKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 335 VLQLQQEKR--QLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEI 412
Cdd:PRK03918 331 KELEEKEERleELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 413 LGLKAQLKDTRGKLE----------------GLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQ 476
Cdd:PRK03918 411 TARIGELKKEIKELKkaieelkkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
...
gi 10440566 477 ELR 479
Cdd:PRK03918 491 KES 493
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
471-593 |
6.57e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 471 LEQELQELRAQAALARDmgpptfpEDVPALQRELERLRAELREERQGHDQMssgfqheRLVWKEEKEKVIQYQKqLQQSY 550
Cdd:COG0542 416 LERRLEQLEIEKEALKK-------EQDEASFERLAELRDELAELEEELEAL-------KARWEAEKELIEEIQE-LKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 10440566 551 VAMYQRNQRLEKALQQLARGDSAGEPL---EVDlegadipyEDIIA 593
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLlreEVT--------EEDIA 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
316-531 |
7.41e-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: 42.80 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 316 KLKQASQKSQRAQQVLHLQVLQLQQEKRQLRQELESLMKEQDLLETKLRSYEREktsfgpaLEETQwevcqksgeiSLLK 395
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEE-------METTT----------NKLK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 396 QQLKESQTEVNAKASEI--------------LGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEA 461
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLksmegsdghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 462 ELLREKVNLLEQELQELRAQA----------ALARDMGPPTFPEDVPALQR-ELERLRAELR-----EERQGHDQMSSGF 525
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQErrlkekvanmEVALDKASLQFAECQDIIQRqEQESVRLKLQhtldvKELQGPGYTSNSS 858
|
....*.
gi 10440566 526 QHERLV 531
Cdd:pfam15921 859 MKPRLL 864
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
345-442 |
7.73e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.96 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 345 LRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEislLKQQLKESQTEVNAKASEILGLKAQLKDTRG 424
Cdd:pfam06785 95 LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLE---SEEQLAEKQLLINEYQQTIEEQRSVLEKRQD 171
|
90
....*....|....*...
gi 10440566 425 KLEGLELRTQDLEGALRT 442
Cdd:pfam06785 172 QIENLESKVRDLNYEIKT 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
416-568 |
8.48e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 416 KAQLKDTRGKLEGLELR----TQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMGpp 491
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK-- 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10440566 492 tfpedvpALQRELERLRAELREERQGHDQMSSGFQHERLVwkEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLA 568
Cdd:TIGR00618 264 -------QLRARIEELRAQEAVLEETQERINRARKAAPLA--AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
264-538 |
8.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 264 QELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKsQRAQQVLHLQVLQLQQEKR 343
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKK 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 344 QLRQEleslMKEQDLLETKLRSYEREKTsfgpALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEIlglkAQLKDTR 423
Cdd:PTZ00121 1565 KAEEA----KKAEEDKNMALRKAEEAKK----AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL----KKAEEEK 1632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 424 GKLEGLELRT-QDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMGPPTFPEDVPALQR 502
Cdd:PTZ00121 1633 KKVEQLKKKEaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
250 260 270
....*....|....*....|....*....|....*.
gi 10440566 503 ELERLRAELREERQghdqmSSGFQHERLVWKEEKEK 538
Cdd:PTZ00121 1713 EEKKKAEELKKAEE-----ENKIKAEEAKKEAEEDK 1743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-515 |
1.17e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 383 EVCQKSGEI----------SLLKQQLKESQTEVNAkasEILGLKAQLKDTRGKLEGLELRT-------QDLEGALRTKGL 445
Cdd:TIGR02169 647 ELFEKSGAMtggsraprggILFSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLdelsqelSDASRKIGEIEK 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10440566 446 ELEVCENELQRKKNEAELLREKVNLLEQELQELRA-QAALARDMGPPTfpEDVPALQRELERLRAELREER 515
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSeLKELEARIEELE--EDLHKLEEALNDLEARLSHSR 792
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
315-586 |
1.41e-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: 41.88 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 315 NKLKQASQKSQRAQQVLHLQVLQLQQEKRQLRQELESLMKEQDLLETKLR-SYEREKTSFGPALEETQWEVCQKSGEISL 393
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYlLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 394 LKQQLK---ESQTEVNAKASEILGLKAQLKDTRGKL----EGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLRE 466
Cdd:pfam02463 256 SKQEIEkeeEKLAQVLKENKEEEKEKKLQEEELKLLakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 467 KVNLLEQELQELRAQAALARDMgpptfPEDVPALQRELERLRAELREERQGHDQMSSgfQHERLVWKEEKEKVIQYQKQL 546
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEE-----EEELEKLQEKLEQLEEELLAKKKLESERLS--SAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 10440566 547 QQSYVAMYQRNQRLEKALQQLARGDSAGEPLEVDLEGADI 586
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
265-541 |
1.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 265 ELEQKLLEREGALQKL--QRSF--EEKELASSL--AYEERprrcRDELEgpepkggnKLKQASQKSQRAQQVLHLQVLQL 338
Cdd:PRK02224 210 GLESELAELDEEIERYeeQREQarETRDEADEVleEHEER----REELE--------TLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 339 QQEKRQLRQELESLMKE--------------QDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQ---QLKES 401
Cdd:PRK02224 278 AEEVRDLRERLEELEEErddllaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREdadDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 402 QTEVNAKA----SEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQE 477
Cdd:PRK02224 358 AEELREEAaeleSELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 478 LRAQAALARDM---------GPPTfpEDVPALQR---------ELERLRAELREERQGHDQmssgfQHERLVWKEEKEKV 539
Cdd:PRK02224 438 ARERVEEAEALleagkcpecGQPV--EGSPHVETieedrerveELEAELEDLEEEVEEVEE-----RLERAEDLVEAEDR 510
|
..
gi 10440566 540 IQ 541
Cdd:PRK02224 511 IE 512
|
|
| DUF2730 |
pfam10805 |
Protein of unknown function (DUF2730); This family of proteins with unknown function appears ... |
457-522 |
1.64e-03 |
|
Protein of unknown function (DUF2730); This family of proteins with unknown function appears to be restricted to Gammaproteobacteria.
Pssm-ID: 402439 Cd Length: 101 Bit Score: 38.14 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10440566 457 KKNEAELLREKVNLLEQELQELRAQAAlardmGPPTfPEDVPALQRELERLRAELREERQGHDQMS 522
Cdd:pfam10805 31 KREDLEKLADKVEEHDKRLTELEIKVD-----NLPT-AKDLHRLQLLLTDLRGELKALRAEIRQIS 90
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
407-569 |
2.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 407 AKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAAlar 486
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 487 dmgpptfpedvpALQRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQ 566
Cdd:COG4942 94 ------------ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
...
gi 10440566 567 LAR 569
Cdd:COG4942 162 LAA 164
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
343-569 |
4.22e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 343 RQLRQELESLMKEQDLLETKLRSYERE-KTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKD 421
Cdd:pfam10174 6 RDLQRENELLRRELDIKESKLGSSMNSiKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 422 TRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQEL------RAQAALARDmgpptfpe 495
Cdd:pfam10174 86 QRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMelrietQKQTLGARD-------- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10440566 496 dvPALQRELERLRAelreerQGHDQMSSGFQHERlvwkeeKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLAR 569
Cdd:pfam10174 158 --ESIKKLLEMLQS------KGLPKKSGEEDWER------TRRIAEAEMQLGHLEVLLDQKEKENIHLREELHR 217
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
446-516 |
4.48e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 4.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10440566 446 ELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMGPPTFPED--VPALQRELERLRAELREERQ 516
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDreISRLDREIERLERELEEERE 486
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
390-573 |
4.64e-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: 40.32 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 390 EISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLE--------LRTQDLEG---ALRTKGLELEVCENELQRKK 458
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADETLADrleELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 459 NEAELLREKVNLLEQElqelraqaalardmgpptfPEDVPALQRELERLRAELREERQGHDQMSSGFQH-ERLVWKEE-- 535
Cdd:COG3096 917 KALAQLEPLVAVLQSD-------------------PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrPHFSYEDAvg 977
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 10440566 536 ------------KEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSA 573
Cdd:COG3096 978 llgensdlneklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS 1027
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
263-564 |
4.71e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 39.70 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 263 IQELEQKLLEREGALQKLQRSFEEKELASS---LAYEERPRRCRDELEGPEPKGG---NKLKQASQKSQR----AQQVLH 332
Cdd:pfam03528 10 VAELEKENAEFYRLKQQLEAEFNQKRAKFKelyLAKEEDLKRQNAVLQEAQVELDalqNQLALARAEMENikavATVSEN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 333 LQVLQLQQEKRQLRQELESLmkeQDLLETKLRSYEREktsFGPALEE--TQWEVCQKSG--EISLLKQQLKESQTEVNak 408
Cdd:pfam03528 90 TKQEAIDEVKSQWQEEVASL---QAIMKETVREYEVQ---FHRRLEQerAQWNQYRESAerEIADLRRRLSEGQEEEN-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 409 aseilgLKAQLKDTRGKLEGLELRTQDLEGALRTkgLELEVCENELQRKKNEAELLREKVNLLEQELQ---ELRAQAALA 485
Cdd:pfam03528 162 ------LEDEMKKAQEDAEKLRSVVMPMEKEIAA--LKAKLTEAEDKIKELEASKMKELNHYLEAEKScrtDLEMYVAVL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10440566 486 rDMGPPTFPEDVPALQRELERLRAELREERQGHDQMssgfqheRLVWKEEKEKVIQYQKQLQQSYvamyqrnQRLEKAL 564
Cdd:pfam03528 234 -NTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQL-------KHTWQKANDQFLESQRLLMRDM-------QRMESVL 297
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
341-481 |
5.97e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 341 EKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQK--------------SGEISLLKQQLKESQTEVN 406
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKekelkklneekkelEEKVKDLTKKISSLKEKIE 527
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10440566 407 AKASEILGLKAQLKDTRGKLEGL--ELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQ 481
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
347-477 |
6.71e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10440566 347 QELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKL 426
Cdd:pfam10174 338 QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQL 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 10440566 427 EGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQE 477
Cdd:pfam10174 418 AGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE 468
|
|
| |
