|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
378-568 |
7.91e-87 |
|
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: 268.02 E-value: 7.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 378 TQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKN 457
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 458 EAELLREKVNLLEQELMELRAQAALHPAPLGPPGVGLTFSE-------DIPALQRELDRLRAELKEERQGHDQMSSGFQH 530
Cdd:pfam06818 81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKeqrqeeaDLGSLRREVERLRAELREERQRRERQASSFEQ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 568955328 531 ERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQ 568
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
242-551 |
8.93e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 242 PGKADKGASCVRSPLSTDECTIQELEQKLLQRETALQKLQRSFDEKefasgqtfEERPRRTRDELECLEPKSKLkppsqk 321
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL--------EEELEQLRKELEELSRQISA------ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 322 sqrtqqvlqlqvlqLQQEKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQL 401
Cdd:TIGR02168 731 --------------LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 402 EVNTKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAA 481
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 482 LHpaplgppgvgltfSEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQ 551
Cdd:TIGR02168 877 AL-------------LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-571 |
6.54e-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: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 419 DTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhpaplgppgvglTFSE 498
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE-------------RLQQ 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955328 499 DIPALQRELDRL-RAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQsylAMYQRNQRLEKALQQLA 571
Cdd:TIGR02168 422 EIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ---ALDAAERELAQLQARLD 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-572 |
2.36e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 419 DTRGKLDGMELKTQDLEsalRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQaalhpaplgppgvgltfse 498
Cdd:COG4942 101 AQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------------- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955328 499 dipalQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLAR 572
Cdd:COG4942 159 -----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-590 |
3.30e-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: 60.08 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFDEKEfasgQTFEERPRRTRD--ELECLEPKSKLKppSQKSQRTQQVLQLqvlqlqqek 340
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIE----QLLEELNKKIKDlgEEEQLRVKEKIG--ELEAEIASLERSI--------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDT 420
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 421 RGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQaalhpaplgppgvgltfsedI 500
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE--------------------I 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 501 PALQRELDRLRAELKEERQghdqmssgfQHERLvwKEEKEKVIQYQRQLQQSYlamyqrnQRLEKALQQLARGDGPGEPF 580
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQ---------ELYDL--KEEYDRVEKELSKLQREL-------AEAEAQARASEERVRGGRAV 512
|
330
....*....|
gi 568955328 581 EIDLeGADIP 590
Cdd:TIGR02169 513 EEVL-KASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-572 |
3.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQW-------EVCQKSGEISLLKQQLKESQLEVNTKASEIL 411
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyellaELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 412 SLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNE-AELLREKVNLLEQELMELRAQAALhpaplgpp 490
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElAEAEEELEELAEELLEALRAAAEL-------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 491 gvgLTFSEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQL 570
Cdd:COG1196 399 ---AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
..
gi 568955328 571 AR 572
Cdd:COG1196 476 EA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-578 |
4.09e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDL--------------LETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVN 404
Cdd:COG1196 268 ELEELRLELEELELELEEaqaeeyellaelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 405 TKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhp 484
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 485 aplgppgvglTFSEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLE 564
Cdd:COG1196 425 ----------ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250
....*....|....
gi 568955328 565 KALQQLARGDGPGE 578
Cdd:COG1196 495 LLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-572 |
6.49e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTnfapaleetqwevcQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELA--------------ELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 419 DTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhpaplgppgvgltfse 498
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----------------- 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955328 499 dipALQRELDRLRAELKEERQGHDQmssgFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLAR 572
Cdd:COG1196 362 ---EAEEALLEAEAELAEAEEELEE----LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-541 |
3.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETqwevcqksgEISLLKQQLKESQLEVNTKASEILSLKAQLKDT 420
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 421 RGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhpaplgppgvglTFSEDI 500
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-------------DLESRL 884
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568955328 501 PALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEK 541
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
265-570 |
6.34e-08 |
|
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: 55.29 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 265 ELEQKLLQRetALQKLQRSFDEKEFASGQTFEERPRRTRDELECLEPKSKLKPPSQKSQRtqqvlqlqvlqlqqEKRQLR 344
Cdd:pfam07888 30 ELLQNRLEE--CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE--------------ELRQSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 345 QELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGKL 424
Cdd:pfam07888 94 EKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 425 DGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELM--------------ELR-AQAALHPAPLGP 489
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeaenealleELRsLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 490 PGVGltfsEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQ 569
Cdd:pfam07888 254 EGLG----EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
.
gi 568955328 570 L 570
Cdd:pfam07888 330 L 330
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
262-526 |
8.30e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 262 TIQELEQKLLQRETALQKLQRSFDEKEfasgQTFEERPRRTRDELECLEpksklkppsqKSQRTQQVLQLQVLQLQQEKR 341
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELE----LELEEAQAEEYELLAELA----------RLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTR 421
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 422 GKLDGMELKTQDLESALRTKGLELEvcENELQRKKNEAELLREKVNLLEQELMELRAQAALhpaplgppgvgLTFSEDIP 501
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELE--ELEEALAELEEEEEEEEEALEEAAEEEAELEEEE-----------EALLELLA 466
|
250 260
....*....|....*....|....*
gi 568955328 502 ALQRELDRLRAELKEERQGHDQMSS 526
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAA 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-571 |
3.72e-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: 53.10 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 419 DTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAALhpaplgppgvgltFSE 498
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-------------LKE 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955328 499 DIPALQRELDRLRAELKEERQGHDQMSSGFQHERLvwKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLA 571
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKDDFELKKENL--EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-538 |
1.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 352 KEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEvntkasEILSLKAQLKDTRGKLDGMELKT 431
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 432 QDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhpaplgppgvgltfsEDIPALQRELDRLR 511
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE----------------AALRDLRRELRELE 425
|
170 180
....*....|....*....|....*..
gi 568955328 512 AELKEERQGHDQMSSGFQHERLVWKEE 538
Cdd:COG4913 426 AEIASLERRKSNIPARLLALRDALAEA 452
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
339-483 |
1.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEvcQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955328 419 DTRGKLD-GMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAALH 483
Cdd:COG4717 174 ELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-516 |
4.77e-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: 49.67 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFDEKEFASG-------------QTFEERPRRTRDELECLEPK------------SKLKP 317
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISalrkdlarleaevEQLEERIAQLSKELTELEAEieeleerleeaeEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 318 PSQKSQRTQQVLQLQVLQLQQEKRQ---LRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQ 394
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREAldeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 395 QLKESQLEVNTKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELevceNELQRKKNEAELLREKVNL----LE 470
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR----SELRRELEELREKLAQLELrlegLE 935
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568955328 471 QELMELRAQ-AALHPAPLGPPG-VGLTFSEDIPALQRELDRLRAELKE 516
Cdd:TIGR02168 936 VRIDNLQERlSEEYSLTLEEAEaLENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-514 |
6.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFDEKEFASGQtfeerprrTRDELECLEpKSKLKPPSQKSQRtqqvlqlqvlqlqqEKRQ 342
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHK--------LEEALNDLE-ARLSHSRIPEIQA--------------ELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 343 LRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRG 422
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 423 KLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELraqAALHPAPLGPPGVGLtfseDIPA 502
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI---EDPKGEDEEIPEEEL----SLED 955
|
250
....*....|..
gi 568955328 503 LQRELDRLRAEL 514
Cdd:TIGR02169 956 VQAELQRVEEEI 967
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-572 |
1.13e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 343 LRQELESLMKEQDLLETKLRSYeREKTNFAPAleetqwevcqkSGEISLLKQQLKEsqlevntkaseilsLKAQLKDTRG 422
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEF-RQKNGLVDL-----------SEEAKLLLQQLSE--------------LESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 423 KLDGMELKTQDLESALRTKGLEL-EVCENELQRKkneaelLREKVNLLEQELMELRAQ-AALHPaplgppgvgltfseDI 500
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALpELLQSPVIQQ------LRAQLAELEAELAELSARyTPNHP--------------DV 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955328 501 PALQRELDRLRAELKEERQghdQMSSGFQHERLVWKEEKEkviQYQRQLQQsYLAMYQRNQRLEKALQQLAR 572
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREA---SLQAQLAQ-LEARLAELPELEAELRRLER 358
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-516 |
1.16e-05 |
|
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: 46.84 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLK--ESQLEVNTKASEILSLKAQ 416
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 417 lkdtrgkLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELmelraqaalhpaplgppgvgltf 496
Cdd:COG1579 98 -------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL----------------------- 147
|
170 180
....*....|....*....|
gi 568955328 497 SEDIPALQRELDRLRAELKE 516
Cdd:COG1579 148 DEELAELEAELEELEAEREE 167
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
339-518 |
1.35e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQ--------------KSGEISLLKQQLKESQLEVN 404
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglDDADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 405 TKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAALHP 484
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
170 180 190
....*....|....*....|....*....|....*
gi 568955328 485 APLGppgvGLT-FSEDipaLQRELDRLRAELKEER 518
Cdd:PRK02224 405 VDLG----NAEdFLEE---LREERDELREREAELE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
262-473 |
1.40e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 262 TIQELEQKLLQRETALQKLQRSFDEKEFASgQTFEERPRRTRDELECLE-PKSKLKPPSQKSQRTQQVLQLQVLQLQQEK 340
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEI-EKLKKENQSYKQEIKNLEsQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALE---------ETQWEVCqkSGEISLLKQQLKESQLEVNTKASEIL 411
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntreslETQLKVL--SRSINKIKQNLEQKQKELKSKEKELK 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955328 412 SLKAQLKDTRGKLDgmELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQEL 473
Cdd:TIGR04523 500 KLNEEKKELEEKVK--DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
350-480 |
2.35e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 350 LMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKA---QLKDTRGKLDG 426
Cdd:pfam15905 161 LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEK 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568955328 427 MELKTQDLESALRTKGLELEVCENELQRKKNE----AELLREKVNLLEQELMELRAQA 480
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQElskqIKDLNEKCKLLESEKEELLREY 298
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-524 |
3.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDL--LETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNT--KASEILSLKAQ 416
Cdd:COG3206 192 EEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 417 LKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRK--------KNEAELLREKVNLLEQELMELRAQAAlhpaplg 488
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqrilaslEAELEALQAREASLQAQLAQLEARLA------- 344
|
170 180 190
....*....|....*....|....*....|....*.
gi 568955328 489 ppgvgltfseDIPALQRELDRLRAELKEERQGHDQM 524
Cdd:COG3206 345 ----------ELPELEAELRRLEREVEVARELYESL 370
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-572 |
3.76e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFDEKEFASGQ--TFEERPRRTRDELECLEPKSKLKPPSQksqrtqqvlqlqvlqlqqEK 340
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQLLPLYQ------------------EL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYERektnfapaLEEtqwevcqksgEISLLKQQLKESQLEVNTKASEI-LSLKAQLKD 419
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRE--------LEE----------ELEELEAELAELQEELEELLEQLsLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 420 TRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKvNLLEQELMELRAQAALH----------PAPLGP 489
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLallglggsllSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 490 PGVGLTFSEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQ 569
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
...
gi 568955328 570 LAR 572
Cdd:COG4717 356 AEE 358
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
341-495 |
4.53e-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: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLetklrSYERektnfapaLEETQWEVCQKSGEISLLKQQLKESQLEVNtkasEILSLKAQLKDT 420
Cdd:COG0542 421 EQLEIEKEALKKEQDEA-----SFER--------LAELRDELAELEEELEALKARWEAEKELIE----EIQELKEELEQR 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 421 RGKLDGMELKTQDLESALRTKG--LELEVCENELQR-----------KKNEAEllREKVNLLEQELME------------ 475
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAplLREEVTEEDIAEvvsrwtgipvgKLLEGE--REKLLNLEEELHErvigqdeaveav 561
|
170 180 190
....*....|....*....|....*....|..
gi 568955328 476 ----LRAQAALHPA--P------LGPPGVGLT 495
Cdd:COG0542 562 adaiRRSRAGLKDPnrPigsflfLGPTGVGKT 593
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
341-479 |
5.54e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDT 420
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955328 421 RGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQ 479
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
264-571 |
5.94e-05 |
|
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: 46.12 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 264 QELEQKLLQRETALQKLQRSFDEKEF-------ASGQTFEERPRR---TRDELECLEPKSKLKPPSQKSQRTQQVLQLQV 333
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDIlqreqatIDTRTSAFRDLQgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 334 LQLQQEKRQLRQELESLMKEQDLLEtklrSYEREKTNFAPALEETQWEVCqksgeisllkqQLKESQLEVNTKASEILSL 413
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHL----QETRKKAVVLARLLELQEEPC-----------PLCGSCIHPNPARQDIDNP 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 414 KAqlkdTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELraqaalhpaplgppgvg 493
Cdd:TIGR00618 524 GP----LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS----------------- 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 494 ltfSEDIPALQRELDRLRAELKEERQgHDQMSSGFQHERLVWKEEK---EKVIQYQRQLQqsylamyQRNQRLEKALQQL 570
Cdd:TIGR00618 583 ---KEDIPNLQNITVRLQDLTEKLSE-AEDMLACEQHALLRKLQPEqdlQDVRLHLQQCS-------QELALKLTALHAL 651
|
.
gi 568955328 571 A 571
Cdd:TIGR00618 652 Q 652
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-585 |
1.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKEsqleVNTKASEILSLKAQLKDT 420
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 421 RGKLDGMELKTQDLESALRTKGLELEvcenELQRKKNEAELLREKVNLLEqELMELRAQaalhpaplgppgvgltFSEDI 500
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAEEYI-KLSEFYEE----------------YLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 501 PALQRELDRLRAELKEERQGHDQMSSgfQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLARGDGPGEPF 580
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
....*
gi 568955328 581 EIDLE 585
Cdd:PRK03918 388 KLEKE 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-573 |
1.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKtnfapaleetqwevcqksgEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQR-------------------RLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 419 DTRGKLDgmelktqDLESALRTKGLE-LEVCENELQRkkneaelLREKVNLLEQELMELRAQAAlhpaplgppGVGLTfs 497
Cdd:COG4913 320 ALREELD-------ELEAQIRGNGGDrLEQLEREIER-------LERELEERERRRARLEALLA---------ALGLP-- 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955328 498 edIPALQRELDRLRAELKEERQGhdqmssgfqherlvWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLARG 573
Cdd:COG4913 375 --LPASAEEFAALRAEAAALLEA--------------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
445-572 |
1.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 445 LEVCENELQRKKNEAELLREKVNLLEQELMELRAQAALHPAPLgppgvGLTFSE-DIPALQRELDRLRAELKEERQGHDQ 523
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-----EYSWDEiDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568955328 524 MssgfqhERLvwKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLAR 572
Cdd:COG4913 687 L------AAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
393-519 |
1.33e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 393 KQQLKESQLEVNTKA--------SEILSLKAQL----KDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAE 460
Cdd:PRK12704 41 KRILEEAKKEAEAIKkealleakEEIHKLRNEFekelRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955328 461 LLREKVNLLEQELMELRAQAalhpaplgppgvgLTFSEDIPALQRE------LDRLRAELKEERQ 519
Cdd:PRK12704 121 QKQQELEKKEEELEELIEEQ-------------LQELERISGLTAEeakeilLEKVEEEARHEAA 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-516 |
1.64e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 385 KSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLRE 464
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568955328 465 KVNLLEQELMELRAQAALHPAPLGPPGVGLTFSEDipALQRELDRLRAELKE 516
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLE--ELERELERLEREIEA 778
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
343-440 |
2.46e-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: 42.50 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 343 LRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEislLKQQLKESQLEVNTKASEILSLKAQLKDTRG 422
Cdd:pfam06785 95 LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLE---SEEQLAEKQLLINEYQQTIEEQRSVLEKRQD 171
|
90
....*....|....*...
gi 568955328 423 KLDGMELKTQDLESALRT 440
Cdd:pfam06785 172 QIENLESKVRDLNYEIKT 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-575 |
3.16e-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: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYER-EKTNFAPA-LEETQWEVCQK----------SGEISLLKQQLKESQLEVNTK 406
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRlAEYSWDEIdVASAEREIAELeaelerldasSDDLAALEEQLEELEAELEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 407 ASEILSLKAQLKDTRGKLDGMELKTQDLESAL-----------------RTKGLELEVCENELQRK-KNEAELLREKVNL 468
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLeaaedlarlelralleeRFAAALGDAVERELRENlEERIDALRARLNR 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 469 LEQELMELRAQAALH-PAPLGPPGVGLtfsEDIPALQRELDRLRAE-LKEERQghdqmssgfQHERLVWKEEKEKVIQYQ 546
Cdd:COG4913 785 AEEELERAMRAFNREwPAETADLDADL---ESLPEYLALLDRLEEDgLPEYEE---------RFKELLNENSIEFVADLL 852
|
250 260
....*....|....*....|....*....
gi 568955328 547 RQLQQSYLAMYQRNQRLEKALQQLARGDG 575
Cdd:COG4913 853 SKLRRAIREIKERIDPLNDSLKRIPFGPG 881
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
428-572 |
4.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 428 ELKTQDLESALrtkgLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhpaplgppgvglTFSEDIPALQREL 507
Cdd:COG1196 221 ELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELE-------------ELRLELEELELEL 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955328 508 DRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLAR 572
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
347-572 |
5.06e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 347 LESLMKEQDLLETKLRSYEREKTNF-APALEETQWEVCQKSGEISLLKQQLKESQlEVNTKASEILSLKAQLKDTRGKL- 424
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNLEELEKkAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELl 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 425 -----------DGMELKTQDLESA------LRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAAlhpapl 487
Cdd:PRK03918 577 keleelgfesvEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE------ 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 488 gppGVGLTFSED--------IPALQRELDRLRAELKEERQGHDQMSSGFqhERLvwKEEKEKVIQYQRQLqqsylamyqr 559
Cdd:PRK03918 651 ---ELEKKYSEEeyeelreeYLELSRELAGLRAELEELEKRREEIKKTL--EKL--KEELEEREKAKKEL---------- 713
|
250
....*....|...
gi 568955328 560 nQRLEKALQQLAR 572
Cdd:PRK03918 714 -EKLEKALERVEE 725
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
341-477 |
5.54e-04 |
|
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: 43.09 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDT 420
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955328 421 RGKLDgmELKTQ-------DLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELR 477
Cdd:TIGR04523 294 KSEIS--DLNNQkeqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
458-572 |
8.28e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 458 EAELLREKVNLLEQELMELRAQAALHPAPLGP--PGVgltfsediPALQRELDRLRAELKEERQghdQMSSGFQHERLVw 535
Cdd:COG3524 215 TAEALLQLIATLEGQLAELEAELAALRSYLSPnsPQV--------RQLRRRIAALEKQIAAERA---RLTGASGGDSLA- 282
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568955328 536 keekEKVIQYQR-QLQQSYlamyqRNQRLEKALQQL--AR 572
Cdd:COG3524 283 ----SLLAEYERlELEREF-----AEKAYTSALAALeqAR 313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
263-486 |
1.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFD------EKEFASGQTFEERPRRTRDELECLEPKSKLKppSQKSQRTQQVLQLQVLQL 336
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGlvdlseEAKLLLQQLSELESQLAEARAELAEAEARLA--ALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 337 QQEKRQLRQELESLMKEQDLLETKLrsyerekTNFAPALEETQwevcqksGEISLLKQQLK-ESQLEVNTKASEILSLKA 415
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARY-------TPNHPDVIALR-------AQIAALRAQLQqEAQRILASLEAELEALQA 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955328 416 QLKDTRGKLDGMELKTQDLESAlrtkglelevcENELQRKKNEAELLREKVNLLEQELMELRAQAALHPAP 486
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEL-----------EAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
262-568 |
1.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 262 TIQELEQKLLQRETALQKLQRSFDEKEfasgqTFEERPRRTRDELECLEpksklkppsqksqrtqqvlqlqvlqlqQEKR 341
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELE-----QLEEELEQARSELEQLE---------------------------EELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTR 421
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 422 GKLDGMELKTQDLESALRTKglELEVCENELQRKKNEAELLREKVNLLEQELMElRAQAALHPAPLGPPGVGLTFSEDIP 501
Cdd:COG4372 164 EELAALEQELQALSEAEAEQ--ALDELLKEANRNAEKEEELAEAEKLIESLPRE-LAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955328 502 ALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQ 568
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-481 |
1.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEqKLLQRETALQKLQRSfDEKEFASG----QTFEERPRRTRDELECLEPK----SKLKPPSQKSQRTQQVLQLQVL 334
Cdd:PRK03918 178 IERLE-KFIKRTENIEELIKE-KEKELEEVlreiNEISSELPELREELEKLEKEvkelEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 335 QLQQEKRQLRQELESLMKEQDLLETKLRSYE--REKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILS 412
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 413 LKAQLKDTRGKLDGMELKTQDLESALRT------------------KGLELEVCENELQRKKNEAELLREKVNLLEQELM 474
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkkrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
....*..
gi 568955328 475 ELRAQAA 481
Cdd:PRK03918 416 ELKKEIK 422
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
340-567 |
1.52e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 340 KRQLRQELESLmkeQDLLETKLRSYEREktnFAPALEE--TQWEVCQKSG--EISLLKQQLKESQLEVNtkaseilsLKA 415
Cdd:pfam03528 99 KSQWQEEVASL---QAIMKETVREYEVQ---FHRRLEQerAQWNQYRESAerEIADLRRRLSEGQEEEN--------LED 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 416 QLKdtRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQElMELRAQAALHPAPLGPPGVGLt 495
Cdd:pfam03528 165 EMK--KAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAE-KSCRTDLEMYVAVLNTQKSVL- 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955328 496 fSEDIPALQRELDRLRAELKEERQGHDQMssgfqheRLVWKEEKEKVIQYQRQLQQSYlamyqrnQRLEKAL 567
Cdd:pfam03528 241 -QEDAEKLRKELHEVCHLLEQERQQHNQL-------KHTWQKANDQFLESQRLLMRDM-------QRMESVL 297
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
263-504 |
1.64e-03 |
|
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: 41.64 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFDEKEFASGQTFEERP------RRTRDELECLEP-----KSKLKPPSQKSQRTQQVLQL 331
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDqllnevKTSRNELNSLSEdyevlKRNFRNKSEEMETTTNKLKM 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 332 QVLQLQQEKRQLRQELESL-------------MKEQ--------DLLETKLRSYEREKTNfapaleetqwevcqKSGEIS 390
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMegsdghamkvamgMQKQitakrgqiDALQSKIQFLEEAMTN--------------ANKEKH 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 391 LLKQQLKESQLEVNTKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLE 470
Cdd:pfam15921 766 FLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDV 845
|
250 260 270
....*....|....*....|....*....|....*.
gi 568955328 471 QELM--ELRAQAALHPAPLGPPGVGLTFSeDIPALQ 504
Cdd:pfam15921 846 KELQgpGYTSNSSMKPRLLQPASFTRTHS-NVPSSQ 880
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-479 |
1.83e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKE------------SQLEVNTK 406
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleekvkdltkkiSSLKEKIE 527
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955328 407 A--SEILSLKAQLKDTRGKLDGM--ELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQ 479
Cdd:TIGR04523 528 KleSEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
256-572 |
2.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 256 LSTDECTIQELEQKLLQRETALQKLQRSFDEKEFASGQTFEERPRRTRDELECLEpksklkppSQKSQRTQqvlqlqvlq 335
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ--------QRLAELEE--------- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 336 lqqEKRQLRQELESLMKEQDLLETKLRSYE-------------------------------------------------- 365
Cdd:COG4717 214 ---ELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallglggsllsliltiagvlflvlgllallf 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 366 ----REKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGKLDGMElktqDLESALRTK 441
Cdd:COG4717 291 lllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE----ELEEELQLE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 442 GLELEVCENELQRKKNEAELLREKVNLLE--QELMELRAQAALHPAPLGPPGVGLTFSEDIPALQRELDRLRAELKEERQ 519
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568955328 520 GHDQMssgfqherlvwKEEKEKVIQYQRQLQQS--YLAMYQRNQRLEKALQQLAR 572
Cdd:COG4717 447 ELEEL-----------REELAELEAELEQLEEDgeLAELLQELEELKAELRELAE 490
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
345-475 |
3.40e-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: 40.58 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 345 QELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGKL 424
Cdd:pfam10174 338 QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQL 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568955328 425 DGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELME 475
Cdd:pfam10174 418 AGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE 468
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
339-573 |
3.93e-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: 40.34 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNfapaLEETQWevcQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLK 418
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ----ELKLKE---QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 419 DTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEA-ELLREKVNLLEQELMELRAQAALhpaplgppgVGLTFS 497
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkKLQEEELKLLAKEEEELKSELLK---------LERRKV 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955328 498 EDIPALQRELDRLRAELKEERQGHDQMSSgFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLARG 573
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEE-LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
342-579 |
4.08e-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: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEEtqweVCQKSGEISllKQQLKESQLEVNTKASEILSLKAQLKDTR 421
Cdd:COG3096 445 AFRAKEQQATEEVLELEQKLSVADAARRQFEKAYEL----VCKIAGEVE--RSQAWQTARELLRRYRSQQALAQRLQQLR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 422 GKLDGMElktQDLESALRTKGLELEVCEnELQRKKNEAELLREKVNLLEQELMELRAQAAlhpaplgppgvglTFSEDIP 501
Cdd:COG3096 519 AQLAELE---QRLRQQQNAERLLEEFCQ-RIGQQLDAAEELEELLAELEAQLEELEEQAA-------------EAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 502 ALQRELDRLRAELKEERQG--------------HDQMSSGFQHERLVwKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKAL 567
Cdd:COG3096 582 ELRQQLEQLRARIKELAARapawlaaqdalerlREQSGEALADSQEV-TAAMQQLLEREREATVERDELAARKQALESQI 660
|
250
....*....|..
gi 568955328 568 QQLARGDGPGEP 579
Cdd:COG3096 661 ERLSQPGGAEDP 672
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-476 |
5.95e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 263 IQELEQKLLQRETALQKLQRSFDEKEfasgQTFEERPRRTRDELECLEpksKLKPPSQKSQRTQQVLQLQVLQLQQEKRQ 342
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATE----RRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNERAS 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 343 LRQELESLMKEQDLLETKLRSYEREKTNfapaleetqwevcqksgeislLKQQLKEsqlevntkaseilsLKAQLKDTRG 422
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE---------------------LRRELEE--------------LREKLAQLEL 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955328 423 KLDGMELKTQDLESALRTKG-LELEVCENELQRKKNEAELLREKVNLLEQELMEL 476
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
264-515 |
9.62e-03 |
|
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: 38.95 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 264 QELEQKLLQRETALQKLQRsfdeKEFASGQTFEerprRTRDELECLEPKSKLKppsQKSQRTQQVLQLQVLQLQQEKRQL 343
Cdd:pfam05557 16 NEKKQMELEHKRARIELEK----KASALKRQLD----RESDRNQELQKRIRLL---EKREAEAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 344 RQELESLMKEQDLLETKLRSYEREKTNfapaleetqwevcqksgEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGK 423
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKN-----------------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955328 424 LDGMELKTQDLESALRtkglelEVCENELQRKKNEAELlrekvNLLEQELMELR-AQAALhpaplgppgvgltfsEDIPA 502
Cdd:pfam05557 148 ASEAEQLRQNLEKQQS------SLAEAEQRIKELEFEI-----QSQEQDSEIVKnSKSEL---------------ARIPE 201
|
250
....*....|...
gi 568955328 503 LQRELDRLRAELK 515
Cdd:pfam05557 202 LEKELERLREHNK 214
|
|
| |
