|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
268-364 |
1.44e-36 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 132.79 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 268 AWVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSkG 347
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 564388374 348 IDPPQVLSPDMVPPSER 364
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
121-214 |
1.16e-31 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 118.92 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 121 WAVRVEEKAKFDGIFESLLP-VNGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 199
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 564388374 200 VPSVLPPPLIPPSKR 214
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
131-196 |
5.51e-25 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 98.83 E-value: 5.51e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 131 FDGIFESLLPVN-GLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 196
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
279-345 |
6.21e-24 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 95.75 E-value: 6.21e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 279 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVS 345
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
127-192 |
3.50e-21 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 89.35 E-value: 3.50e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 127 EKAKFDGIFESLLPVNGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVY 192
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIF 73
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
8.68e-21 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 86.89 E-value: 8.68e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 19 YESYYKQVDPAYTGRVGASEAALFLKKSGLSDIVLGKIWDLADPEGKGFLDKQGFYVALRLVACAQS 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
7.57e-20 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 85.02 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 13 PSGNPLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIVLGKIWDLADPEGKGFLDKQGFYVALRLVACAQSGHEVTLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 564388374 93 NLGLTMPPPKF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-545 |
3.43e-18 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 87.65 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 381 TGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA-----GRAQLETILRSLKC 535
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeAEQALDELLKEANR 194
|
170
....*....|
gi 564388374 536 TQDDINQARS 545
Cdd:COG4372 195 NAEKEEELAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-566 |
1.81e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR 544
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|..
gi 564388374 545 SKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEE 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-563 |
2.22e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170 180
....*....|....*....|
gi 564388374 544 RSKLSQLQESHLEAHRSLEQ 563
Cdd:COG1196 462 LELLAELLEEAALLEAALAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-563 |
3.90e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180
....*....|....*....|
gi 564388374 544 RSKLSQLQESHLEAHRSLEQ 563
Cdd:COG1196 448 AEEEAELEEEEEALLELLAE 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-566 |
1.22e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180
....*....|....*....|...
gi 564388374 544 RSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-563 |
1.27e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 455
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC 535
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180
....*....|....*....|....*...
gi 564388374 536 TQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-566 |
1.63e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 471
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 472 DETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 551
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170
....*....|....*
gi 564388374 552 ESHLEAHRSLEQYDQ 566
Cdd:COG1196 393 RAAAELAAQLEELEE 407
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-613 |
1.04e-15 |
|
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: 82.03 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 463 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRAQLETILRSLKCTQDDINQ 542
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 543 ARSKLSQLQESHLEAHRSLEQYDQVPDGVSGtslpDLATLNEGILLAERgGFGAMDDPFKNKALLFSNNSQ 613
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAER----ELAQLQARLDSLER-LQENLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-563 |
1.84e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180
....*....|....*....|
gi 564388374 544 RSKLSQLQESHLEAHRSLEQ 563
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEA 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-563 |
2.40e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 388 DISQEIAQLQREKYSLEqdIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVR 467
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-------LEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 468 QKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKL 547
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170
....*....|....*.
gi 564388374 548 SQLQESHLEAHRSLEQ 563
Cdd:COG1196 368 LEAEAELAEAEEELEE 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-563 |
5.96e-15 |
|
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: 79.72 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdqqkAKLRDML 463
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180
....*....|....*....|
gi 564388374 544 RSKLSQLQESHLEAHRSLEQ 563
Cdd:TIGR02168 858 AAEIEELEELIEELESELEA 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-566 |
7.32e-15 |
|
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: 79.33 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrQK 469
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 470 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 549
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170
....*....|....*..
gi 564388374 550 LQEShlEAHRSLEQYDQ 566
Cdd:TIGR02168 433 AELK--ELQAELEELEE 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-569 |
9.05e-15 |
|
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: 78.95 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQ 455
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisrLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQKcQDETQTI-SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 534
Cdd:TIGR02168 318 LEELEAQLEELESK-LDELAEElAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190
....*....|....*....|....*....|....*
gi 564388374 535 CTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 569
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-563 |
2.01e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 388 DISQEIAQLQREK---YSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1196 261 ELAELEAELEELRlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR 544
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170
....*....|....*....
gi 564388374 545 SKLSQLQESHLEAHRSLEQ 563
Cdd:COG1196 421 EELEELEEALAELEEEEEE 439
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-566 |
4.21e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.94 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 407 IREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcqdetqtISSLKTQIQS 486
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 487 QESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
385-567 |
7.57e-14 |
|
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: 71.88 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVR-----QKCQDEtqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDD 539
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180
....*....|....*....|....*...
gi 564388374 540 INQARSKLsqlqESHLEAhRSLEQYDQV 567
Cdd:COG1579 161 LEAEREEL----AAKIPP-ELLALYERI 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-566 |
7.66e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 463 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL----NRLQQEETQL---EQSIQAGRAQLETILRSLKC 535
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALleaEAELAEAEEELEELAEELLE 390
|
170 180 190
....*....|....*....|....*....|.
gi 564388374 536 TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-566 |
9.09e-14 |
|
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: 75.86 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 469
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 470 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 549
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170
....*....|....*..
gi 564388374 550 LQESHLEAHRSLEQYDQ 566
Cdd:TIGR02168 829 LERRIAATERRLEDLEE 845
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-552 |
1.17e-13 |
|
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: 73.64 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 456
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSIQAGRAQLETILRSLKCT 536
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170
....*....|....*.
gi 564388374 537 QDDINQARSKLSQLQE 552
Cdd:COG4942 212 AAELAELQQEAEELEA 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-552 |
1.24e-13 |
|
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: 75.06 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELNRLQQE----ETQLEQSIQagraQLETI 529
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEisntQTQLNQLKD----EQNKI 265
|
170 180
....*....|....*....|...
gi 564388374 530 LRSLKCTQDDINQARSKLSQLQE 552
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEK 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-593 |
1.36e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRdml 463
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLE--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 sDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:COG1196 404 -ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564388374 544 RSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGG 593
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-553 |
1.95e-13 |
|
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: 72.87 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 463
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 S-----------DVRQKCQDETQTISSLK-------------TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 519
Cdd:COG4942 111 RalyrlgrqpplALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190
....*....|....*....|....*....|....
gi 564388374 520 QAGRAQLETILRSLkctQDDINQARSKLSQLQES 553
Cdd:COG4942 191 EALKAERQKLLARL---EKELAELAAELAELQQE 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-551 |
2.16e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.03 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 DMLSDVRQKcqdeTQTISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDD 539
Cdd:COG4717 160 ELEEELEEL----EAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170
....*....|....
gi 564388374 540 --INQARSKLSQLQ 551
Cdd:COG4717 236 leAAALEERLKEAR 249
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
383-534 |
2.48e-13 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 73.90 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 461 DMLSDVRQKCQDETQTI-SSLKTQI---QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 534
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-553 |
2.57e-13 |
|
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: 74.32 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 471
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 472 DETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 551
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
..
gi 564388374 552 ES 553
Cdd:TIGR02168 393 LQ 394
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-563 |
3.12e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQ--DIREKEEAIRQKASEVQELQNDLDRETSS---------LQELEAQKQDAQDRLDEM 452
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQrrlelleaeLEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 DQQKAKLRDMLSDVRQKC-QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILR 531
Cdd:COG4913 315 EARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 532 SLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-566 |
3.67e-13 |
|
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: 73.94 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 S-------DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRAQLETILRSL 533
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALL 892
|
170 180 190
....*....|....*....|....*....|....*..
gi 564388374 534 KC----TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:TIGR02168 893 RSeleeLSEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-566 |
6.35e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 393 IAQLQREKYSLE-----------QDIREKEEAIRQ---KASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDMLSdvRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRAQLETILRSLKCTQ 537
Cdd:COG4717 128 LPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*....
gi 564388374 538 DDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
385-563 |
1.17e-12 |
|
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: 72.02 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 dvRQKCQDETQTISSLKTQIQSQESDLKSQEddlnrakSELNRLQQEETQLEQSIQ---------------------AGR 523
Cdd:TIGR02169 790 --HSRIPEIQAELSKLEEEVSRIEARLREIE-------QKLNRLTLEKEYLEKEIQelqeqridlkeqiksiekeieNLN 860
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564388374 524 AQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-552 |
1.92e-12 |
|
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: 71.20 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLKCTQDD---- 539
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEKlese 532
|
170
....*....|...
gi 564388374 540 INQARSKLSQLQE 552
Cdd:TIGR04523 533 KKEKESKISDLED 545
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-596 |
1.99e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.86 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQEL--EAQKQDAQ--------------- 446
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSvsyldvllgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 447 --DRLDEMDQQKAKLRDMLSDVrqkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRA 524
Cdd:COG3883 117 flDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388374 525 QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGGFGA 596
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
385-532 |
2.50e-12 |
|
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: 71.25 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 465 DVRQKCQDETQTISSLktqiqsqesdlksqEDDLNRAKSELNRLQQEETQLEQSIQAGRAQlETILRS 532
Cdd:TIGR02169 466 KYEQELYDLKEEYDRV--------------EKELSKLQRELAEAEAQARASEERVRGGRAV-EEVLKA 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-552 |
3.68e-12 |
|
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: 70.43 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
....*....
gi 564388374 544 RSKLSQLQE 552
Cdd:TIGR04523 495 EKELKKLNE 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
384-527 |
5.67e-12 |
|
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: 66.49 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 463
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 464 SDVRQKCQDEtqtISSLKTQIQSQESDLKSQEDDLNRAKSELN----RLQQEETQLEQSIQAGRAQLE 527
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAAKIP 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
390-563 |
1.45e-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: 67.10 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 469
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 470 CQDETQTISSL-----KTQIQSQESDLKSQED--DLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkctQDDINQ 542
Cdd:COG4942 99 LEAQKEELAELlralyRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------RAELEA 171
|
170 180
....*....|....*....|.
gi 564388374 543 ARSKLSQLQESHLEAHRSLEQ 563
Cdd:COG4942 172 ERAELEALLAELEEERAALEA 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-521 |
2.70e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 380 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 459 LRDMLSDVRQKCQDETQTISSLKTQIQSQ----ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-567 |
3.53e-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: 67.39 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRET-------SSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealallrSELEELSEELRELESKRSELRREL 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLksQEDDL---NRAKSELNRLQQEETQLEQSIQA-GRAQLETI--- 529
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT--LEEAEaleNKIEDDEEEARRRLKRLENKIKElGPVNLAAIeey 995
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564388374 530 ------LRSLKCTQDDINQARSKLSQL-QESHLEAH-RSLEQYDQV 567
Cdd:TIGR02168 996 eelkerYDFLTAQKEDLTEAKETLEEAiEEIDREAReRFKDTFDQV 1041
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-568 |
7.20e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 65.24 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 460
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 -------------------DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQA 521
Cdd:COG3883 103 syldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE-------LEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564388374 522 GRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVP 568
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-565 |
1.29e-10 |
|
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: 65.47 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAqkQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDV-----------------RQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAK----SELNRLQQEETQLEQS---I 519
Cdd:TIGR02169 808 SRIearlreieqklnrltleKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKeeleEELEELEAALRDLESRlgdL 887
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564388374 520 QAGRAQLETILRSLKCTQDDIN----QARSKLSQLQESHLEAHRSLEQYD 565
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIE 937
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
392-557 |
2.51e-10 |
|
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: 64.38 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKEEAIRQkasEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 471
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 472 DETQTISSLKTQIQSQESDLKSQEDD---LNRAKSELNRLQQEETQLEQsIQAGRAQLETILRSLKCTQDDINQARSKLS 548
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 564388374 549 QLQESHLEA 557
Cdd:pfam05557 239 REEKYREEA 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-554 |
2.79e-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: 64.31 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 408 REKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQ 487
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 488 ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH 554
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-562 |
2.87e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKASEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 459
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 460 RDMLSDVRQKCQDETQTISSLK---TQIQSQESDLKSQ----EDDLNRAKSELNRLQQEETQLEQSIQAGRAQ------- 525
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRedaDDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERfgdapvd 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388374 526 ---LETILRSLKCTQDDINQA----RSKLSQLQESHLEAHRSLE 562
Cdd:PRK02224 407 lgnAEDFLEELREERDELREReaelEATLRTARERVEEAEALLE 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-567 |
4.64e-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: 63.54 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ---EETQLEQSIQAgrAQLETILRSLKCTQDDIN 541
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlsEEYSLTLEEAE--ALENKIEDDEEEARRRLK 975
|
170 180
....*....|....*....|....*.
gi 564388374 542 QARSKLSQLQESHLEAhrsLEQYDQV 567
Cdd:TIGR02168 976 RLENKIKELGPVNLAA---IEEYEEL 998
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-572 |
4.75e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 398 REKYSLEQDIREKEEAIRQkasEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMdQQKAKLRDMLSDVRQkCQDETQTI 477
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVAS-AEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 478 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEA 557
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170
....*....|....*
gi 564388374 558 HRSLEQYDQVPDGVS 572
Cdd:COG4913 754 RFAAALGDAVERELR 768
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
387-563 |
5.93e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.11 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQDIREKEEAI---RQK------ASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 457
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKnglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 458 KLRDMLSDVRQkcqdeTQTISSLKTQIQSQESDLKSQED-------DLNRAKSELN----RLQQEETQLEQSIQAGRAQL 526
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAalraQLQQEAQRILASLEAELEAL 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 564388374 527 ETILRSLkctQDDINQARSKLSQLQESHLEAhRSLEQ 563
Cdd:COG3206 326 QAREASL---QAQLAQLEARLAELPELEAEL-RRLER 358
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-584 |
6.03e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIR--QKASEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAK 458
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQsiQAGRAQLETILRSLkct 536
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAA--ALGDAVERELRENL--- 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564388374 537 QDDINQARSKLSQLqESHLEahRSLEQYDQVPDGVSGTSLPDLATLNE 584
Cdd:COG4913 772 EERIDALRARLNRA-EEELE--RAMRAFNREWPAETADLDADLESLPE 816
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
440-567 |
7.29e-10 |
|
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: 61.70 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 519
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564388374 520 QAGRAQLETILRSLkctQDDINQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:COG4942 100 EAQKEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYL 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-552 |
7.33e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQndldretSSLQELEAQKQdaqdRLDEMdQQKAKLRDM 462
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVK----ELKEL-KEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 463 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIqagrAQLETILRSLkctqddiNQ 542
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL----EELEERHELY-------EE 366
|
170
....*....|
gi 564388374 543 ARSKLSQLQE 552
Cdd:PRK03918 367 AKAKKEELER 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-563 |
1.04e-09 |
|
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: 62.35 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKASEVQE-------LQNDLDRETSSLQELEAQKQDAQDRLDEMD 453
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISElkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 454 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ---SQESDLKSQ--EDDLNRAKSEL----NRLQQEETQLEQSIQagra 524
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELknqeKKLEEIQNQISQNNK---- 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 564388374 525 qletILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:TIGR04523 336 ----IISQLN---EQISQLKKELTNSESENSEKQRELEE 367
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
384-567 |
1.04e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 62.18 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKeeairqkasEVQELQNDLDRETSSLQELEAqkQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDK---------EIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 ---SDVRQKCQDETQTISSLKTQIQSQESDLKS-----------QEDDLNRAKS---ELNRLQQEETQLEQSIQAG---- 522
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEelervqqsytlNENELERVRGlekQLEELEKRYDEIVERLEEKevay 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564388374 523 ---RAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:pfam06160 360 selQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLE 407
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
378-460 |
1.39e-09 |
|
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: 59.55 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 378 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 457
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 564388374 458 KLR 460
Cdd:COG1579 160 ELE 162
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-563 |
2.84e-09 |
|
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: 60.80 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdml 463
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIqagrAQLETILRSLKCTQDDINQa 543
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD----SVKELIIKNLDNTRESLET- 468
|
170 180
....*....|....*....|
gi 564388374 544 rsKLSQLQESHLEAHRSLEQ 563
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQ 486
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
385-563 |
4.13e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.23 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKASEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 452
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 ---DQQKAKLRDMLSDVRQKCQ-----------------DETQTISSLKTQIQSQESDLKSQEDDLNRAK---SEL-NRL 508
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKEQNKelkeeidrvkqsytlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaySELqEEL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 509 QQEETQLEQsIQAGRAQLETILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:PRK04778 386 EEILKQLEE-IEKEQEKLSEMLQGLR---KDELEAREKLERYRNKLHEIKRYLEK 436
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-590 |
7.37e-09 |
|
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: 59.97 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQkaseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVRQKCQdetqtisslktQIQSQESDLKSQEDDLNRAKSELNRLQ-QEETQLE--QSIQAGRAQLETILRSLKCTQDDIN 541
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLReQSGEALAdsQEVTAAMQQLLEREREATVERDELA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564388374 542 QARSKLSQlqeshlEAHRsLEQydqvPDGVSGTSLPDLATLNEGILLAE 590
Cdd:COG3096 651 ARKQALES------QIER-LSQ----PGGAEDPRLLALAERLGGVLLSE 688
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
384-556 |
9.08e-09 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 56.93 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMLSDVRQKCQDETQT-ISSLKTQIQSQESDLKSQEDDL--NRAKSELNRLQQEETQLEQsiqagrAQLETILRSL 533
Cdd:pfam12795 130 QQIRNRLNGPAPPGEPLSEAqRWALQAELAALKAQIDMLEQELlsNNNRQDLLKARRDLLTLRI------QRLEQQLQAL 203
|
170 180
....*....|....*....|...
gi 564388374 534 kctQDDINQARSKLSQLQESHLE 556
Cdd:pfam12795 204 ---QELLNEKRLQEAEQAVAQTE 223
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-553 |
9.81e-09 |
|
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: 59.26 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNR---------LQQEETQLEQ---SIQAGRA 524
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQtqkSLKKKQE 585
|
170 180
....*....|....*....|....*....
gi 564388374 525 QLETILRSLKCTQDDINQARSKLSQLQES 553
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-557 |
1.41e-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: 58.91 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEI-AQLQR--------EKYsleqdiREKEEAIRQK-----ASEVQELQNDLDRETSSLQELEAQKQDAQDRLDE 451
Cdd:TIGR02168 191 LEDILNELeRQLKSlerqaekaERY------KELKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 452 MDQQKAKLRDmlsdvrqkcqdetqTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILR 531
Cdd:TIGR02168 265 LEEKLEELRL--------------EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180
....*....|....*....|....*.
gi 564388374 532 SLKCTQDDINQARSKLSQLQESHLEA 557
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESL 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-563 |
1.64e-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: 58.54 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQND-----------LDRETSSLQELEAQKQDAQDRLDEM 452
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeLEAEIASLERSIAEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 DQQ-KAKLRDMLSDVRQkcqdetqtissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILR 531
Cdd:TIGR02169 324 LAKlEAEIDKLLAEIEE-----------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 532 SLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
391-563 |
1.93e-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: 57.98 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDiREKEEAIRQKA---SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 468 QKCQDETQTISSLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEETQLEQSiQAGRAQLETILRSLKCT----------- 536
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSLSKEfqelrnslaqr 204
|
170 180 190
....*....|....*....|....*....|....
gi 564388374 537 -------QDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:pfam07888 205 dtqvlqlQDTITTLTQKLTTAHRKEAENEALLEE 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
386-566 |
2.03e-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: 58.54 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIREKEEAIR----QKASEVQELQN------DLDRETSSLQ----ELEAQKQDAQDRLDE 451
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENlngkkeELEEELEELEaalrDLESRLGDLKKERDE 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 452 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSE------LNRLQQEETQLEQSIQAgraq 525
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA---- 969
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564388374 526 LETIlrSLKCTQD-DINQARskLSQLQESH--LEAHRS-----LEQYDQ 566
Cdd:TIGR02169 970 LEPV--NMLAIQEyEEVLKR--LDELKEKRakLEEERKailerIEEYEK 1014
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
384-552 |
2.71e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.47 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIR------EKEEAIRQKA-SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ-Q 455
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRLAAEdfrqkyEDELNLRTSAeNDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQ----------KCQDETQTISSLKTQ---------------IQSQESDLKSQ----EDDLNRAKSELN 506
Cdd:pfam00038 141 EEEVRELQAQVSDtqvnvemdaaRKLDLTSALAEIRAQyeeiaaknreeaeewYQSKLEELQQAaarnGDALRSAKEEIT 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564388374 507 ----RLQQEETQLeQSIQAGRAQLETILRSLKCTQD-DINQARSKLSQLQE 552
Cdd:pfam00038 221 elrrTIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISELEA 270
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
394-554 |
3.51e-08 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 57.01 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQrekySLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 473
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 474 TQTISSLKTQIQSQESDLKSQEDDLNRaKSELNRLQ----QEETQLEQSIQA-----GRAQLETIlRSLKCTQDDINQAR 544
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETI-AELKQTREELAAQK 186
|
170
....*....|
gi 564388374 545 SKLSQLQESH 554
Cdd:PRK11637 187 AELEEKQSQQ 196
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
388-566 |
4.96e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 388 DISQEIAQLQREKYsLEQDIREKEEAIRQKAS----EVQELQNDLD---------RETSSLQELEAQKQDAQDRLDEMDQ 454
Cdd:COG3206 148 ELAAAVANALAEAY-LEQNLELRREEARKALEfleeQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 455 QKAKLRDMLSDVRQKcqdetqtISSLKTQIQSQESDLKSQEDD--LNRAKSELNRLQQEETQLEQ-------SIQAGRAQ 525
Cdd:COG3206 227 QLAEARAELAEAEAR-------LAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQ 299
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564388374 526 LETILRSLKC-TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG3206 300 IAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
387-576 |
5.00e-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: 56.44 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 466
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 467 RQKCQDetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSK 546
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
170 180 190
....*....|....*....|....*....|
gi 564388374 547 LSQLQESHLEAHRSLEQYDQVPDGVSGTSL 576
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASL 293
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
391-525 |
5.04e-08 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 52.26 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDIREKEEAIrqkasevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 471 QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSelnRLQQEETQLEQSIQAGRAQ 525
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
371-537 |
5.12e-08 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 55.53 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 371 SSSALGSGEFTGVKELddisqEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQE--------LEAQK 442
Cdd:pfam09787 32 EGSGVEGLDSSTALTL-----ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 443 QDAQDRLDEMDQQKAKLRDMLSDVRQ-------KCQDETQTISSLKTQIQSQeSDLKSQEDDL-NRAKSELNRLQQEETQ 514
Cdd:pfam09787 107 SARREAEAELERLQEELRYLEEELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELeNRLHQLTETLIQKQTM 185
|
170 180
....*....|....*....|....*..
gi 564388374 515 LEqSIQAGRA----QLETILRSLKCTQ 537
Cdd:pfam09787 186 LE-ALSTEKNslvlQLERMEQQIKELQ 211
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
387-564 |
5.43e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.30 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 467 RQKCQDETQTISSLKTQIQSQESDLKSqeddLNRAKSELNRL---QQ-------EETQLEQSIQAGRAQLETILRSLKcT 536
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERLewrQQtevlspeEEKELVEKIKELEKELEKAKKALE-K 158
|
170 180
....*....|....*....|....*...
gi 564388374 537 QDDINQARSKLSQLQESHLEAHRSLEQY 564
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKEL 186
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
384-566 |
5.69e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQR--EKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLD----------- 450
Cdd:COG3206 182 EQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellq 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 451 -----EMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDD-LNRAKSELNRLQQEEtqleQSIQAGRA 524
Cdd:COG3206 262 spviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQARE----ASLQAQLA 337
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564388374 525 QLETILRSLkctqddiNQARSKLSQLQEshlEAHRSLEQYDQ 566
Cdd:COG3206 338 QLEARLAEL-------PELEAELRRLER---EVEVARELYES 369
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
394-569 |
6.30e-08 |
|
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: 56.29 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQREKYSLEQDIREKEEAIRQKASEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 448
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS 518
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564388374 519 IQagraQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 569
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPE 201
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-567 |
7.76e-08 |
|
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: 56.18 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQE----IAQLQREKYSLEQD---IREKEEAIRQKASEVQEL----QNDLDRETSS-LQELEAQKQDAQDRLDE 451
Cdd:TIGR04523 253 TQLNQLKDEqnkiKKQLSEKQKELEQNnkkIKELEKQLNQLKSEISDLnnqkEQDWNKELKSeLKNQEKKLEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 452 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGR---AQLET 528
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEklnQQKDE 412
|
170 180 190
....*....|....*....|....*....|....*....
gi 564388374 529 ILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
391-590 |
7.83e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 471 QdetqtisslktQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLE-QSIQAGRAQLETILRSLKctqddinQARSKL 547
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLREQsgEEFEDsQDVTEYMQQLLERERELT-------VERDEL 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564388374 548 SQLQESHLEAHRSLEQYDqvpdgvsGTSLPDLATLNE---GILLAE 590
Cdd:PRK04863 651 AARKQALDEEIERLSQPG-------GSEDPRLNALAErfgGVLLSE 689
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-534 |
1.03e-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: 56.23 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENLNGKKEELEEE 869
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388374 463 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 534
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
387-569 |
1.52e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 460
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 DMLSDVRQKCQDETQTISSlKTQIQSQESDLKSQEDDLNRAKSE----LNRLQQEETQLEQSIQAGRAQLETILRSLKCT 536
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190
....*....|....*....|....*....|...
gi 564388374 537 QDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 569
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-593 |
1.73e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 457
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 458 KLRDMLSDVRQKC-----QDET--QTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 530
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 531 RSLKCTQDDINQARSKLSQLqESHLEAHRslEQYDQVPdgvsgTSLPDLATLNEgILLAERGG 593
Cdd:PRK02224 370 SELEEAREAVEDRREEIEEL-EEEIEELR--ERFGDAP-----VDLGNAEDFLE-ELREERDE 423
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-561 |
1.83e-07 |
|
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: 55.34 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREkysLEQdIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQkqDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG3096 837 ELAALRQRRSELERE---LAQ-HRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVRQKCQdetqTISSLKTQIQSQESDLKSQED---DLNRAKSELNRLQQEETQLEQSIQ---------------AGRAQL 526
Cdd:COG3096 911 FIQQHGK----ALAQLEPLVAVLQSDPEQFEQlqaDYLQAKEQQRRLKQQIFALSEVVQrrphfsyedavgllgENSDLN 986
|
170 180 190
....*....|....*....|....*....|....*
gi 564388374 527 ETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 561
Cdd:COG3096 987 EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL 1021
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
373-555 |
2.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 373 SALGSGEFTGVKELDDISQEIAQLQRekysLEQDIREKEEAIRQKASEvQELQNDLDR-ETSSLQELEA---QKQDAQDR 448
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 LDEMDQQKAKLRDMLSDVRQkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE----ET-----QLEQSI 519
Cdd:COG4717 401 KEELEELEEQLEELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAEleqlEEdgelaELLQEL 478
|
170 180 190
....*....|....*....|....*....|....*....
gi 564388374 520 QAGRAQLETILR---SLKCTQDDINQARSKLSQLQESHL 555
Cdd:COG4717 479 EELKAELRELAEewaALKLALELLEEAREEYREERLPPV 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-559 |
3.04e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 463
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETqleqsiQAGRAQLEtilrslkctqdDINQA 543
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET------ADLDADLE-----------SLPEY 817
|
170
....*....|....*.
gi 564388374 544 RSKLSQLQESHLEAHR 559
Cdd:COG4913 818 LALLDRLEEDGLPEYE 833
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
340-510 |
3.10e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.09 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 340 IQQKVSKGIDPPQVLSpDMVppseRGTPIpdsSSALGSGEFtgvKELDDISQEIaqlQREKYSLEQDIREKEEAIRQKAS 419
Cdd:COG2433 355 VEKKVPPDVDRDEVKA-RVI----RGLSI---EEALEELIE---KELPEEEPEA---EREKEHEERELTEEEEEIRRLEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 420 EVQELqndldretsslqelEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQT---ISSLKTQIQSQESDLKSQED 496
Cdd:COG2433 421 QVERL--------------EAEVEELEAELEEKDERIERLERELSEARSEERREIRKdreISRLDREIERLERELEEERE 486
|
170
....*....|....
gi 564388374 497 DLNRAKSELNRLQQ 510
Cdd:COG2433 487 RIEELKRKLERLKE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-532 |
3.15e-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: 54.30 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEA----------IRQKASEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMD 453
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdelkdYREKLEKLKREINELKRELDRLQEE---LQRLSEELADLN 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 454 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 532
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-552 |
4.07e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKASEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 536
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170
....*....|....*.
gi 564388374 537 QDDINQARSKLSQLQE 552
Cdd:pfam01576 179 SKLKNKHEAMISDLEE 194
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
383-550 |
4.10e-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: 53.87 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 453
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 454 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSiqagraqLETILRSL 533
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170
....*....|....*..
gi 564388374 534 KCTQDDINQARSKLSQL 550
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEI 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
396-552 |
5.60e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 396 LQREKYSLEQDIREKEEAIRQKASEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 460
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 ---------DMLSDVRQKC------QDETQTISSLKTQIQSQESDLKSQEDDLNRA--KSELNRLQQEETQLEQ---SIQ 520
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEeleELR 452
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 521 AGRAQLETILRSLKcTQDDINQARSKLSQLQE 552
Cdd:COG4717 453 EELAELEAELEQLE-EDGELAELLQELEELKA 483
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-552 |
5.77e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEvQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR 460
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQQaaKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRA---QLETILRSLKCTQ 537
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLI 901
|
170
....*....|....*
gi 564388374 538 DDINQARSKLSQLQE 552
Cdd:TIGR00606 902 REIKDAKEQDSPLET 916
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-562 |
6.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 463 LSDVRQKCQDEtqtissLKTQIQSQES------DLKSQEDDLnraKSELNRLQQEETQLEQSiqagRAQLETILRSLKCT 536
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPfyneylELKDAEKEL---EREEKELKKLEEELDKA----FEELAETEKRLEEL 645
|
170 180 190
....*....|....*....|....*....|.
gi 564388374 537 QDDINQARSKLSQ-----LQESHLEAHRSLE 562
Cdd:PRK03918 646 RKELEELEKKYSEeeyeeLREEYLELSRELA 676
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
377-560 |
6.62e-07 |
|
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: 53.29 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 377 SGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELE---AQKQ--------- 443
Cdd:pfam10174 379 AGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEriierlkeq 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 444 ---DAQDRLDEMDQQKAKLRDM---LSDVRQKCQDETQTISSLKTQIQSQESD-------LKSQEDDLNRAKSELNRLQ- 509
Cdd:pfam10174 459 rerEDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLEn 538
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 510 -------QEET------------QLEQSIQ-----AGRAQ--LETILRSLKCTQDDINQARSKLSQLQESHLEAHRS 560
Cdd:pfam10174 539 qlkkahnAEEAvrtnpeindrirLLEQEVArykeeSGKAQaeVERLLGILREVENEKNDKDKKIAELESLTLRQMKE 615
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
383-554 |
7.82e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.71 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDdisQEIAQLQREKYSLEQDIREKEEAI-RQKAS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:PHA02562 176 IRELN---QQIQTLDMKIDHIQQQIKTYNKNIeEQRKKngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDMLSDVRQK-----------------------CQDETQTISS---LKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 512
Cdd:PHA02562 253 PSAALNKLNTAaakikskieqfqkvikmyekggvCPTCTQQISEgpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564388374 513 TQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH 554
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
385-566 |
8.00e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.91 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQkaseVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVRQKCQD------ETQTISSLKTQIQSQESDLKSQE--DDLNRAKSELNRLQQEETQLEQsIQAGRAQLETILRSL--K 534
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHKELEEELEA-HEPRLKSLNELAEELleE 175
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 535 CTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:cd00176 176 GHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-479 |
9.51e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
90
....*....|....*.
gi 564388374 464 SDVRQKCQDETQTISS 479
Cdd:COG4942 230 ARLEAEAAAAAERTPA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-566 |
1.07e-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: 52.76 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQeIAQLQREKysleQDIREKEEAIRQKASEVQ----ELQNDLDR-------------------ET------SS 434
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI------------------QSQESDLKSQED 496
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 497 DLNR-----------AKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYD 565
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
.
gi 564388374 566 Q 566
Cdd:TIGR02169 392 E 392
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
384-516 |
1.08e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKASEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 454
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388374 455 QKAKLRDMlsdvRQKCQDETQTISSLkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 516
Cdd:PRK12704 129 KEEELEEL----IEEQLQELERISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
379-614 |
1.17e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.27 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 379 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 454
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 455 QKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQEsdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRAQLETILRSLk 534
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRAKL- 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 535 ctQDDINQARSKLSQLQES--HLEAHRSLEQYDQVPDGVSGTSL-PDLATLNEGILLAERGGFGamDDPFKNKALLFSNN 611
Cdd:COG5185 509 --ERQLEGVRSKLDQVAESlkDFMRARGYAHILALENLIPASELiQASNAKTDGQAANLRTAVI--DELTQYLSTIESQQ 584
|
...
gi 564388374 612 SQE 614
Cdd:COG5185 585 ARE 587
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
384-550 |
1.18e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelaekrdELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMlsdvRQKCQDETQTISSLKTQIQS-----QESDL-KSQEDDL----NRAKSELNRLQQEETQ------LEQSIQ 520
Cdd:COG1340 95 DELRKE----LAELNKAGGSIDKLRKEIERlewrqQTEVLsPEEEKELvekiKELEKELEKAKKALEKneklkeLRAELK 170
|
170 180 190
....*....|....*....|....*....|
gi 564388374 521 AGRAQLETILRSLKCTQDDINQARSKLSQL 550
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQELHEEMIEL 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-566 |
1.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 411 EEAIRQKASEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQTISSLKTQI 484
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 485 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRAQLETILRslkctqdDINQARSKLSQLQeshleahRSLEQ 563
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER-------EIERLERELEERE-------RRRAR 363
|
...
gi 564388374 564 YDQ 566
Cdd:COG4913 364 LEA 366
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-557 |
1.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAiRQKASEVQELQNDLDRETssLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQ-------------------IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgra 524
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK--- 491
|
170 180 190
....*....|....*....|....*....|...
gi 564388374 525 qlETILRSLKCTQDDINQARSKLSQLQESHLEA 557
Cdd:PRK03918 492 --ESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
382-542 |
1.60e-06 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 51.40 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 382 GVKEL-----DDISQEIAQLQREKYSLEQDIREKEEAIR----------------------------------------- 415
Cdd:pfam03148 130 GIQELlqrtlEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeewekftqdn 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 416 -QKA-SEVQ---ELQNDLD--RETSSlQELEAQKQDA----QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 484
Cdd:pfam03148 210 iERAeKERAasaQLRELIDsiLEQTA-NDLRAQADAVnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAI 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 485 QSQESDLK-SQ---EDDLNRAKSEL------NRLQQEETQLEQSIQAGRAQL---ETILRSLKCTQDDINQ 542
Cdd:pfam03148 289 RDKEAPLKlAQtrlENRTYRPNVELcrdeaqYGLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
397-517 |
1.77e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 47.61 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 397 QREKYSLEQDIREKEEAIRQKasevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQT 476
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564388374 477 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQ 517
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
385-559 |
1.94e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 51.23 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKASEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 448
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 ---LD-----------------EMDQQKAKLR---DMLSDVRQKcqdetqTISSLK---TQIQSQEsdlKSQEDDLNRAK 502
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQE------TIAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 503 SELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHR 559
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
405-566 |
2.38e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.71 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 405 QDIREKEEAIRQkasEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 484
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 485 QSQESDLKSQEDDLN-----RAKSELNR------LQQEETQLEQSI------QAGRAQLETILRSLKCTQDDinQARSKL 547
Cdd:pfam01576 267 RELEAQISELQEDLEseraaRNKAEKQRrdlgeeLEALKTELEDTLdttaaqQELRSKREQEVTELKKALEE--ETRSHE 344
|
170 180
....*....|....*....|...
gi 564388374 548 SQLQE---SHLEAHRSL-EQYDQ 566
Cdd:pfam01576 345 AQLQEmrqKHTQALEELtEQLEQ 367
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
383-511 |
2.51e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 50.40 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREkeeaIRQKASEVQEL-QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQ----LKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 564388374 462 MLSDVRQKCQDetqtissLKTQIQSQESDLKS----QEDDLNRAKSELNRLQQE 511
Cdd:smart00787 240 KIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-499 |
2.68e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110
....*....|....*....|....*....|....*....
gi 564388374 464 SDVRQKCQ---DETQTISSLKTQIQSQESDLKSQEDDLN 499
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDII 679
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
387-560 |
2.86e-06 |
|
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: 51.28 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 455
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQK--CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSL 533
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSY 438
|
170 180
....*....|....*....|....*..
gi 564388374 534 kcTQDDINQARSKLsqlqeSHLEAHRS 560
Cdd:pfam05557 439 --SKEEVDSLRRKL-----ETLELERQ 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
386-502 |
2.94e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREkysLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 465
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 564388374 466 VRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAK 502
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
391-544 |
3.05e-06 |
|
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: 51.49 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDiREKEEAIRQKASEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 451
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 452 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL------------NRAKSELNRLQQE-------E 512
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 513 TQLEQSIQAGRAQLETILRSLKCTQDDINQAR 544
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-551 |
3.34e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 379 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKASEVQELQNDLDRET-SSLQELEAQKQ---------- 443
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneyl 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 444 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESdlKSQEDDLNRAKSELNRLQQEETQLEQSIQ 520
Cdd:PRK03918 606 elkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|....
gi 564388374 521 AGRAQLETI---LRSLKCTQDDINQARSKLSQLQ 551
Cdd:PRK03918 684 ELEKRREEIkktLEKLKEELEEREKAKKELEKLE 717
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
384-547 |
3.51e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 446
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 447 DRLDEMDQQ--KAK---------LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE--- 512
Cdd:pfam05667 415 QRLVELAGQweKHRvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564388374 513 --TQ--LE--QSIQAGRAQLETILRSLKCTQDDINQARSKL 547
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-566 |
3.51e-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: 51.22 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 402 SLEQDIREKEEAI--------------RQKASEVQELQNDLdretsslQELEAQKQDAQDRLDE----MDQQKAKLRD-- 461
Cdd:TIGR02169 643 TLEGELFEKSGAMtggsraprggilfsRSEPAELQRLRERL-------EGLKRELSSLQSELRRienrLDELSQELSDas 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 462 -MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLkcTQDDI 540
Cdd:TIGR02169 716 rKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRI 793
|
170 180
....*....|....*....|....*.
gi 564388374 541 NQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQ 819
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
404-528 |
3.90e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 50.23 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 404 EQDIREKEEAIRQKASEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDET 474
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPNSPQVRQLR 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 475 QTISSLKTQIQSQESDL--KSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLET 528
Cdd:COG3524 256 RRIAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
384-569 |
4.44e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180
....*....|....*....|....*.
gi 564388374 544 RSKLSQLQESHLEAHRSLEQYDQVPD 569
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELEL 265
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
363-552 |
4.90e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 363 ERGTPIPDSSSalgsgeftgVKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKASEVQELQNDLDRetsslqeLEAQK 442
Cdd:PRK02224 456 ECGQPVEGSPH---------VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 443 QDAQDRLDEMDQQKAKLRDMLSDVRQKCQDetqtissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAg 522
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES- 590
|
170 180 190
....*....|....*....|....*....|
gi 564388374 523 RAQLETILRSLKCTQDDINQARSKLSQLQE 552
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREALAE 620
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
291-364 |
5.03e-06 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 45.83 E-value: 5.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 291 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 364
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
416-557 |
5.29e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.84 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 416 QKASEVQELQNDLdretSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQTISSLKTQIQ 485
Cdd:pfam12795 14 AKKKLLQDLQQAL----SLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLEELEQRLL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 486 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI---LRSLKCTQDDINQARSKLSQLQESHLEA 557
Cdd:pfam12795 89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrnrLNGPAPPGEPLSEAQRWALQAELAALKA 163
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
393-544 |
5.33e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 393 IAQLQREKYSLEQDiREKEEAIRQKASEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 453
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 454 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLN------------RAKSELNRLQQE-------ETQ 514
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgaeeRARARRDELHARlsanrsrRNQ 1078
|
170 180 190
....*....|....*....|....*....|
gi 564388374 515 LEQSIQAGRAQLETILRSLKCTQDDINQAR 544
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
384-552 |
5.83e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 48.14 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEqdiREKEEAIRQKASEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLE---RRLEQQTEQAKKLEEKAQAALTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 463 LSDVRQKCQDETQTISSLKTQIQ---SQESDLKSQED--------DLNRAKSELNRLQQEETQLEQSIQAgRAQLETIL- 530
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNllkARLKAAKAQEAvqtslgslSTSSATDSFERIEEKIEEREARADA-AAELASAVd 191
|
170 180
....*....|....*....|....
gi 564388374 531 RSLKCTQDDINQARSK--LSQLQE 552
Cdd:pfam04012 192 LDAKLEQAGIQMEVSEdvLARLKA 215
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
388-531 |
5.84e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.07 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 388 DISQEIAQLQREKYSLeqdiREK-EEAIRQKASEVQELqndLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:pfam05622 279 EIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQ 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 467 RQKCQDEtqtiSSLKtqiqsqeSDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQ----LETILR 531
Cdd:pfam05622 352 GSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkideLQEALR 409
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
384-486 |
6.86e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 46.02 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKAsevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKKE---QELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|...
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQS 486
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLEE 105
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
6.87e-06 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 45.44 E-value: 6.87e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564388374 32 GRVGASEAALFLKKSGLSDIVLGKIWDLADPEGKGFLDKQGFYVALRLV 80
Cdd:pfam12763 24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
402-552 |
7.18e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 402 SLEQDIREKEEAIRQkasEVQELQNDLDRETSSL-------QELEAQKQDAQDRLDEMdQQKAKL----------RDMLS 464
Cdd:COG1842 16 ALLDKAEDPEKMLDQ---AIRDMEEDLVEARQALaqvianqKRLERQLEELEAEAEKW-EEKARLalekgredlaREALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVrqkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQlETILRSLkcTQDDINQAR 544
Cdd:COG1842 92 RK----AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEAL--SGIDSDDAT 164
|
....*...
gi 564388374 545 SKLSQLQE 552
Cdd:COG1842 165 SALERMEE 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-605 |
7.37e-06 |
|
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: 50.12 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 459
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 460 RDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlqqeetqleQSIQAGRAQLETILRSLKCTQDD 539
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL-----------QEFKILKDKKDAKIRELEARVSD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 540 INQARSKLSQLQESHLEAHRSLEQ-YDQVPDGVSgTSLPDLATLNEGILLAERGgfgamddpFKNKA 605
Cdd:pfam15921 630 LELEKVKLVNAGSERLRAVKDIKQeRDQLLNEVK-TSRNELNSLSEDYEVLKRN--------FRNKS 687
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-563 |
8.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQK--ASEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKelAEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 462 MLSDVrQKCQDETQTISSLKTQIQSQESDLK-----------SQEDDLNRAKSELNRLQQEETQLEQSiqagRAQLETIL 530
Cdd:PRK03918 544 LKKEL-EKLEELKKKLAELEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDA----EKELEREE 618
|
170 180 190
....*....|....*....|....*....|...
gi 564388374 531 RSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
453-533 |
8.09e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 532
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 564388374 533 L 533
Cdd:COG3883 95 L 95
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
435-563 |
8.24e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.86 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 435 LQELEAQKQDAQDRLDEMDQQKAKLRD---MLSDVRQKCQDETQTISSLKTQIQSQESDLKS-QEDDLNRAKSELNRLQQ 510
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKeleLLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564388374 511 EETQLEQSIqagrAQLETILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:smart00787 219 EIMIKVKKL----EELEEELQELE---SKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
418-554 |
8.62e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.86 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 418 ASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQtisslktqiqSQESDLKSQEDD 497
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 498 LNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR----SKLSQLQESH 554
Cdd:smart00787 220 IMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQL 280
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
387-549 |
8.81e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQE----------LEAQKQDAQDRlDEMDQqk 456
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNrwrekvfalmVQLKAQDLEHR-DSVKQ-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 akLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 536
Cdd:pfam07111 336 --LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
170
....*....|...
gi 564388374 537 QDDINQARSKLSQ 549
Cdd:pfam07111 414 QIWLETTMTRVEQ 426
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
383-511 |
1.00e-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: 48.65 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKASEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 462
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564388374 463 lsdvrqkcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 511
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
427-553 |
1.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 427 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL-NRAKSE- 504
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALy 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 505 ---------------------------LNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQES 553
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
392-552 |
1.20e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKE--EAIRQKASEVQELQNDLDRETSSL----QELEAQKQD-------AQDRLDEMdQQKAK 458
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEdhEKIQHLEEEYKKEINDKEKQVSLLliqiTEKENKMKDltflleeSRDKANQL-EEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDM-LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE-ETQLEQSIQAGRAQ----------- 525
Cdd:pfam05483 279 LQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEkEAQMEELNKAKAAHsfvvtefeatt 358
|
170 180 190
....*....|....*....|....*....|....*..
gi 564388374 526 --LETILRS----LKCTQDDIN----QARSKLSQLQE 552
Cdd:pfam05483 359 csLEELLRTeqqrLEKNEDQLKiitmELQKKSSELEE 395
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
302-573 |
1.30e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 302 IFMHSGLTQNL-------LAHIWALADTRQTGKLSKEQFALAMYFIQ--QKVSKGIDPPQVLSPDmvPPSERGTPIPDSS 372
Cdd:COG5022 726 VFFKAGVLAALedmrdakLDNIATRIQRAIRGRYLRRRYLQALKRIKkiQVIQHGFRLRRLVDYE--LKWRLFIKLQPLL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 373 SALGSGEFTG--VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQK--QDAQDR 448
Cdd:COG5022 804 SLLGSRKEYRsyLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQrvELAERQ 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 LDEMDQQKAKL------------------RDMLSDVRQKCQDETQTISSLKTQIQsqESDLKSQEDDLNRAKSELNRLQQ 510
Cdd:COG5022 884 LQELKIDVKSIsslklvnleleseiielkKSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHE 961
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 511 EETQLEQSIQagraQLETILRSLKCTQDDINQARSKLSQLQEShLEAHRSleQYDQVPDGVSG 573
Cdd:COG5022 962 VESKLKETSE----EYEDLLKKSTILVREGNKANSELKNFKKE-LAELSK--QYGALQESTKQ 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-567 |
1.60e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqqkakLRDML 463
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE-------LREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKcqdetqtisslktqIQSQESDLKSQEDDLNRAKselnRLQQE------ETQLEQSIQAG--------RAQLETI 529
Cdd:PRK02224 422 DELRER--------------EAELEATLRTARERVEEAE----ALLEAgkcpecGQPVEGSPHVEtieedrerVEELEAE 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 564388374 530 LRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL 521
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-549 |
1.80e-05 |
|
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: 48.58 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQ-------LQREKYSLEQDIREKEEAIRQ-------KASEVQELQ---NDLDRETSSL-----QELEAQ 441
Cdd:pfam15921 569 QQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEfkilkdkKDAKIRELEarvSDLELEKVKLvnagsERLRAV 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 442 KQDAQDR---LDEMDQQKAKLRDMLSD-------VRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 511
Cdd:pfam15921 649 KDIKQERdqlLNEVKTSRNELNSLSEDyevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564388374 512 ETQLEQSIQAGRAQLETILRSLKCTQDDINQA----------RSKLSQ 549
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkekhflkeeKNKLSQ 776
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
386-566 |
1.93e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQEL-QNDLDRET------SSLQELEA-------QKQDAQDRLDE 451
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqQAKQDSEHkrkkleGQLQELQArlseserQRAELAEKLSK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 452 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLksQEDdlNRAK----SELNRLQQEET----QLEQSIQAGR 523
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL--QEE--TRQKlnlsTRLRQLEDERNslqeQLEEEEEAKR 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564388374 524 A---QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:pfam01576 514 NverQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
394-531 |
1.98e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.42 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQREKYslEQDIREKEEAIRQKASEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 473
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388374 474 TQTIsslktQIQSQESDLKSQEDD----LNRAKselnRLQQEetqlEQSIQAGRAQLETILR 531
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-552 |
2.12e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 455
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 -------------KAKLRDM---LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSI 519
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190
....*....|....*....|....*....|...
gi 564388374 520 QAGRAQLETILRSLKCTQDDINQARSKLSQLQE 552
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-567 |
2.56e-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: 48.04 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSL----------------QELEAQKQDAQDR 448
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehalsirvlpKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 LDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNRLQ------------ 509
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassSLGSDLAAREDALNQSLKELMHQArtvlkarteahf 764
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 510 -------------QEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSklSQLQESHLEAHRSLEQYDQV 567
Cdd:TIGR00618 765 nnneevtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP--SDEDILNLQCETLVQEEEQF 833
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
381-657 |
2.72e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 381 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 D------MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRA-KSELNRLQQEETQLEQSIQAGRAQLETILRSL 533
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 534 KCTQDDINQAR-----SKLSQLQESHLEAHRSL--------EQYDQVPDGVSGtslpDLATLNEGILLAER--GGFGAMD 598
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVrskkedlnEELTQIESRVST----LKATLEKLRAKLERqlEGVRSKL 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 599 DPFKNKALLFSNNSQELHPDPFQAEDPFKSdpFKGADPFKGDPFQSDPFSEQQTAVTDP 657
Cdd:COG5185 520 DQVAESLKDFMRARGYAHILALENLIPASE--LIQASNAKTDGQAANLRTAVIDELTQY 576
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
384-552 |
2.74e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQndldrETSSLQELEAQKQDAQDR-------LDEMDQQK 456
Cdd:PRK10929 72 QVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQ-----VSSQLLEKSRQAQQEQDRareisdsLSQLPQQQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMLSDVRQKCQDETQTISSLK----TQIQSQESDLKSQEDDLNRA------KSELNRLQQE-----ETQLEQSIQA 521
Cdd:PRK10929 147 TEARRQLNEIERRLQTLGTPNTPLAqaqlTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQA 226
|
170 180 190
....*....|....*....|....*....|.
gi 564388374 522 GRAQLeTILRslkctQDDINQARSKLSQLQE 552
Cdd:PRK10929 227 LRNQL-NSQR-----QREAERALESTELLAE 251
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
384-549 |
2.80e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 453
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 454 QQKAKLRDMLSDVRqkcQDETQTISSLKTQIQSqESDLKSQEDDLNRAK-------SELNRLQQEETQLEQsiqagrAQL 526
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRKSlegntqlQDLLQKQRDYLTARI------QRL 239
|
170 180
....*....|....*....|...
gi 564388374 527 ETILRSLkctQDDINQARSKLSQ 549
Cdd:PRK11281 240 EHQLQLL---QEAINSKRLTLSE 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-528 |
3.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDIREkeeaIRQKASEVQELQNDLD-RETSSLQELEAQKQDAQDRLDEMDQQKAKLRDmlsdvrqk 469
Cdd:COG4913 338 DRLEQLEREIERLERELEE----RERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEE-------- 405
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 470 cqdetqtissLKTQIQSQESDLKSQEDDLnraKSELNRLQQEETQLEQSIQAGRAQLET 528
Cdd:COG4913 406 ----------ALAEAEAALRDLRRELREL---EAEIASLERRKSNIPARLLALRDALAE 451
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
367-515 |
3.85e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 367 PIPDSSSALGsgEFTgvKELDDISQEIAQLQREKYSLE---------QDIREKEEAIrqkasevQELQNDLDRETSSLQE 437
Cdd:PHA02562 249 DIEDPSAALN--KLN--TAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI-------TKIKDKLKELQHSLEK 317
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 438 LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:PHA02562 318 LDTAIDELEEIMDEFNEQSKKLLELKNKIST----NKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-615 |
4.22e-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: 47.66 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQD---IREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 462 MLSDVRQKCQDETQtissLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEetQLEQSIQAGRAQLETILRSLKCTQDDIN 541
Cdd:TIGR00618 630 VRLHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSIRVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388374 542 QARSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERggfgAMDDPFKNKALLFSNNSQEL 615
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH----QARTVLKARTEAHFNNNEEV 770
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
284-561 |
4.27e-05 |
|
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: 47.42 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 284 LKTDLDLDGYVSGQEVKEIFM-HSGLTQnllaHIWA-LADTRQ-TGKLSKEQFALA-MYF--IQQKVSKGIdppQVLSPD 357
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLsHEGVLQ----EIRSiLVDFEEaSGKKIYEHDSMStMHFrsLGSAISKIL---RELDTE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 358 MVPPSERGTPIPDSSSALGSGEFTGVKEL-----DDISQEIAQLQREKYSLEQ---DIREKEEAIRQKASEVQEL---QN 426
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLlqqhqDRIEQLISEHEVEITGLTEkasSARSQANSIQSQLEIIQEQarnQN 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 427 --------DLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDD 497
Cdd:pfam15921 313 smymrqlsDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 498 LNRAKSELNRLQQEETQLEQSIQAGRAQ----------LETILRSLKC-TQDDINQARSKLSQLQEShLEAHRSL 561
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRElddrnmevqrLEALLKAMKSeCQGQMERQMAAIQGKNES-LEKVSSL 466
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
392-572 |
4.46e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETS-------SLQELEAQKQDAQDRLDEMDQQKAK------ 458
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAqknnalkKIRELEAQISELQEDLESERAARNKaekqrr 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 --------LRDMLSDVrqkcQDETQTISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEET--------QLEQ---- 517
Cdd:pfam01576 296 dlgeeleaLKTELEDT----LDTTAAQQELRSKREQEVTELKkALEEETRSHEAQLQEMRQKHTqaleelteQLEQakrn 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 518 ---------SIQAGRAQLETILRSLKCTQDDINQARSKL-SQLQESHLEAHRSLEQYDQVPDGVS 572
Cdd:pfam01576 372 kanlekakqALESENAELQAELRTLQQAKQDSEHKRKKLeGQLQELQARLSESERQRAELAEKLS 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-562 |
4.75e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAI------RQKASE-VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ-- 454
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFgdapvdLGNAEDfLEELREERDELREREAELEATLRTARERVEEAEAll 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 455 ------------QKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEdDLNRAKSELNRLQQEETQLEQSIQAG 522
Cdd:PRK02224 450 eagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAER 528
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564388374 523 RAQLETilRSLKCTQ-----DDIN-QARSKLSQLQESHLEAHRSLE 562
Cdd:PRK02224 529 RETIEE--KRERAEElreraAELEaEAEEKREAAAEAEEEAEEARE 572
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-562 |
5.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQdaqdRLDEMDQQKAKLRDML 463
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKS---------ELNRLQQEETQLEQSIQAGRAQLETILRSLK 534
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180
....*....|....*....|....*...
gi 564388374 535 CTQDDINQARSKLSQLQESHLEAHRSLE 562
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLE 355
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
382-477 |
5.57e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.11 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 382 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 460
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 564388374 461 DMLSDVRQKCQDETQTI 477
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-552 |
5.76e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 382 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQ---NDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDMLSDVRQKCQDETQTISSLKTQ----IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAqletilRSLK 534
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD------DYLK 973
|
170
....*....|....*...
gi 564388374 535 CTQDDINQARSKLSQLQE 552
Cdd:TIGR00606 974 QKETELNTVNAQLEECEK 991
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
386-556 |
5.77e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 458
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LrDMLSDvRQKCQ----DETQTISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELNRLQQEETQLeQSIQ 520
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*..
gi 564388374 521 AGRAQLETILRSLKCTQDDINQARS-KLSQLQESHLE 556
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvALDNWRQVHEQ 725
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
387-563 |
5.86e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKySLEQDirekEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 467 RQKcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL--NRLQQEETQLEQSIQAGRAQ-LETILRSLKCTQDDINQA 543
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAQAALYANSQRLQqIRNLLKGGKVGGKALRPS 192
|
170 180
....*....|....*....|
gi 564388374 544 RSKLSQLQESHLEAHRSLEQ 563
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR 212
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
414-566 |
6.16e-05 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 43.93 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 414 IRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDemdqqkaklrdmlsDVRQKCQDETQTISSlktQIQSQESDLKs 493
Cdd:pfam07321 5 LRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQ--------------DYRAWRPQEEQRLYA---EIQGKLVLLK- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 494 qedDLNRAKSELNRLQQEETQLEQSIQAGRAQLEtilrslkctqddinQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:pfam07321 67 ---ELEKVKQQVALLRENEADLEKQVAEARQQLE--------------AEREALRQARQALAEARRAVEKFAE 122
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
482-566 |
6.32e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 482 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 561
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
....*
gi 564388374 562 EQYDQ 566
Cdd:COG4372 104 ESLQE 108
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
419-562 |
6.32e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.82 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 419 SEVQELQNDLDRETSSlQELEAQKQDAQDRLDEMD------QQKA-KLRDMLSDVRQKCQDETQTISSLKTQIQSQ--ES 489
Cdd:cd22656 94 AEILELIDDLADATDD-EELEEAKKTIKALLDDLLkeakkyQDKAaKVVDKLTDFENQTEKDQTALETLEKALKDLltDE 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 490 DLKSQEDDLNRAKSELNRLQQEET-QLEQSIQAGRAQLETI---LRSLKCTQDDINQARSKLSQLQESHLEAHRSLE 562
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYAaKLKAKIDELKALIADDeakLAAALRLIADLTAADTDLDNLLALIGPAIPALE 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
386-563 |
7.50e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKASEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 457
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 458 KLRDMLSDVRQKCQDEtqtisslKTQIQSQESDLKSQEDDLNrAKSELnRLQQEETQLEqsIQAGRAQLETILRSLKCTQ 537
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQAT-ATPEL-LLQLENFDER--IERAREEQEAANAEVERLQ 491
|
170 180
....*....|....*....|....*.
gi 564388374 538 DDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEE 517
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
384-521 |
7.60e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.82 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIR---QKASE-VQELQNDLDRET-SSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEkweEKARLaLEKGREDLAREAlERKAELEAQAEALEAQLAQLEEQVEK 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 459 LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE----DDLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:COG1842 117 LKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA 183
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
384-544 |
7.89e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.74 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNdlDRETSSLQELEAQK--QDAQDRLDEMDQQKAKLRD 461
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAE--ERRQRLEEALDLQQffRDADDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 462 MLSDvrqkcqDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE-----TQLEQSIQAGRAQLETILRSLKCT 536
Cdd:cd00176 132 EDLG------KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdadEEIEEKLEELNERWEELLELAEER 205
|
....*...
gi 564388374 537 QDDINQAR 544
Cdd:cd00176 206 QKKLEEAL 213
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
482-552 |
9.36e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 9.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 482 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQE 552
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
384-564 |
9.52e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQkASEVQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQ-LTEEKEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ----QEETQLEQsiqagRAQLETILRSLKCTQDD 539
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 564388374 540 IN---QARSKLSQLQESHLEAHRSLEQY 564
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
390-599 |
1.11e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 469
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 470 CQDETQT----------ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLkctQDD 539
Cdd:pfam06008 119 DLSRMLAeaqrmlgeirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDL---REL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388374 540 INQARSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEG--ILLAERGGFGAMDD 599
Cdd:pfam06008 196 LREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTArdSLDAANLLLQEIDD 257
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
384-504 |
1.12e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKASEVQELQNDLD-----------RETSSLQELEAQKQ-- 443
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 444 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDL------KSQEddLNRAKSE 504
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-565 |
1.21e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------ASEVQELQNDLDRETSSLQEL 438
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 439 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 512
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 513 TQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH--LEAHRSLEQYD 565
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIreLEAQISELQED 279
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
384-553 |
1.23e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIR---------EKE-EAIRQKASEVQELQNDLDRetsSLQELEAQKQ---------- 443
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDrvkqsytlnESElESVRQLEKQLESLEKQYDE---ITERIAEQEIayselqeele 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 444 DAQDRLDEMDQQKAKLRDMLSDVRqkcQDET---QTISSLKTQIQS-----QESDL----KSQEDDLNRAKSELNRLqqe 511
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLR---KDELearEKLERYRNKLHEikrylEKSNLpglpEDYLEMFFEVSDEIEAL--- 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564388374 512 ETQLEQsiqaGRAQLETILRSLKCTQDDINQARSKLSQLQES 553
Cdd:PRK04778 461 AEELEE----KPINMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
394-527 |
1.32e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 42.19 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQREKysleQDIREKEEAIRQ---KASEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEEKEIEL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 471 QDETQTISSLKTQIQSqesdlksqeddlnrAKSELNRLQQeetQLEQSIQAGRAQLE 527
Cdd:pfam18595 74 RELERREERLQRQLEN--------------AQEKLERLRE---QAEEKREAAQARLE 113
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
403-511 |
1.41e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.25 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 403 LEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLkt 482
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 564388374 483 qiqsqESDLKSQEDDLNRAKSELNRLQQE 511
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
384-552 |
1.45e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEaIRQkasEVQELQNDLDRETSSL--------------QELEAQKQ--DAQD 447
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDK-LRK---EIERLEWRQQTEVLSPeeekelvekikeleKELEKAKKalEKNE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 448 RLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSqesdLKSQEDDLNRaksELNRLQQEETQLEQSIQAGRAQLE 527
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRK---EADELHKEIVEAQEKADELHEEII 233
|
170 180
....*....|....*....|....*
gi 564388374 528 TILRSLKCTQDDINQARSKLSQLQE 552
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALKR 258
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
384-552 |
1.47e-04 |
|
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: 44.80 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 463
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 sdvrqkcqdetQTISSLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 543
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*....
gi 564388374 544 RSKLSQLQE 552
Cdd:pfam15905 320 EQEHQKLQQ 328
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
390-508 |
1.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 469
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110
....*....|....*....|....*....|....*....
gi 564388374 470 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 508
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-526 |
1.58e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEeaiRQKASEVQElqndlDREtssLQELEAQKQDAQDRLDEMDQQKAKLRdml 463
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAER-----EEE---EFERMLRKQAEDEEIEQEEAEKRRMK--- 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 464 sdvRQKCQDEtqtissLKTQIQSQEsdlKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQL 526
Cdd:pfam13868 288 ---RLEHRRE------LEKQIEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
391-563 |
1.65e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQRekySLEQDIREKEEAI---RQK-ASEVQELQNDLD---RETSSL----QELEAQKQDAQDRL-------DEM 452
Cdd:pfam01576 327 QEVTELKK---ALEEETRSHEAQLqemRQKhTQALEELTEQLEqakRNKANLekakQALESENAELQAELrtlqqakQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 532
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 564388374 533 -------LKCTQDDinqaRSKLSQLQESHLEAHRSLEQ 563
Cdd:pfam01576 484 klnlstrLRQLEDE----RNSLQEQLEEEEEAKRNVER 517
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
403-551 |
1.86e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 403 LEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQTISSLKT 482
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 483 QIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQAGRAQLETILRSLkctqdDINQARSKLSQLQ 551
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQ-------IAALRRQLAALEAAL-----DASEKRDRESQAK 173
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
385-514 |
1.88e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSL--EQDIREKEEAIRQKAsEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRdm 462
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkkEQDEASFERLAELRD-ELAELEEELE-------ALKARWEAEKELIEEIQELKEELE-- 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 463 lsdvrqkcqDETQTISSLKTQIQSQESDLKSQEDDLNRAKSE--------------LNRLQQEETQ 514
Cdd:COG0542 482 ---------QRYGKIPELEKELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGERE 538
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
403-554 |
1.88e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.23 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 403 LEQDIREKEEAIRQKASEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQ 475
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 476 TISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRAQLETILRSLKCTQDDINQARSK---LSQLQ 551
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKRELESEIKKLTHDIKLKEEQIRELEIKvqeLRKYK 559
|
...
gi 564388374 552 ESH 554
Cdd:pfam09726 560 ESE 562
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
341-538 |
1.88e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 341 QQKVSKGIDPPQVLSPDMVPPSERgtpiPDSSSALGSGEFTGVKELDDISQEIAQLQREKYSLE---QDIREKEEAI--- 414
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSE----LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 415 -RQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR---DMLSDVRQKCqdeTQTISSLKTQIQSQESD 490
Cdd:pfam05483 445 lQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcDKLLLENKEL---TQEASDMTLELKKHQED 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564388374 491 LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQD 538
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD 569
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-526 |
2.04e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 452
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 ---DQQKAKLRD-MLSDVRQKCQDETQTISSLKTQIQSQEsdlKSQEDDLNRAKSELNRL---QQEETQLEQSIQAGRAQ 525
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQEEAEKRRM 286
|
.
gi 564388374 526 L 526
Cdd:pfam13868 287 K 287
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
385-567 |
2.27e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKASEVQELQND---LDRET--SSLQELEAQKQDAQD--------- 447
Cdd:PRK04863 838 ELRQLNRRRVELERAladHESQEQQQRSQLEQAKEGLSALNRLLPRlnlLADETlaDRVEEIREQLDEAEEakrfvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 448 -RLDEMDQQKAKLRdmlsdvrqkcQDETQtISSLK---TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQleqSIQAGR 523
Cdd:PRK04863 918 nALAQLEPIVSVLQ----------SDPEQ-FEQLKqdyQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAA---EMLAKN 983
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388374 524 AQLETILRSlkctqdDINQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:PRK04863 984 SDLNEKLRQ------RLEQAEQERTRAREQLRQAQAQLAQYNQV 1021
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
432-563 |
2.34e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.34 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 432 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELN-- 506
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPig 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 507 -RLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQ--------ARSKLSQLQESHLEAHRSLEQ 563
Cdd:pfam00529 137 gISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaenqaeVRSELSGAQLQIAEAEAELKL 202
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
434-552 |
2.41e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.83 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 434 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQTISSLKTQIQS--QESDLKSQEDDL 498
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 499 NRAKSEL-NRLQQEETQLeQSIQAGRAQLETILRSLkctQDDINQARSKLSQLQE 552
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQNQLAQLNSQLIEL---QTRPERAQQQLSEARQ 127
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
396-563 |
2.48e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 396 LQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS---DVRQKCQD 472
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQateDAKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 473 ETQtisSLKTQIqsqESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIqAGRAQLETILRSLKCTQDDINQAR 544
Cdd:pfam01576 721 NMQ---ALKAQF---ERDLQARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGR 793
|
170 180
....*....|....*....|...
gi 564388374 545 S----KLSQLQESHLEAHRSLEQ 563
Cdd:pfam01576 794 EeavkQLKKLQAQMKDLQRELEE 816
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
384-527 |
2.49e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLqREKysLEQDIREKEEAIRQKA---SEVQELQNDLDRETSSLQELEAQKQDAQDRLD-------EMD 453
Cdd:pfam13851 47 KLMSEIQQENKRL-TEP--LQKAQEEVEELRKQLEnyeKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQrfekverERD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 454 QQKAKLRDMLSDVRQKCQDETQtisSLKTQIQSQESDLKSQEDDLN----RAKSELNRLQQEETQLEQSIQAGRAQLE 527
Cdd:pfam13851 124 ELYDKFEAAIQDVQQKTGLKNL---LLEKKLQALGETLEKKEAQLNevlaAANLDPDALQAVTEKLEDVLESKNQLIK 198
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
446-552 |
2.56e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 446 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQ 525
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100
....*....|....*....|....*..
gi 564388374 526 LETILRSLKCTQDDINQARSKLSQLQE 552
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEA 158
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
386-507 |
2.71e-04 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 42.68 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLeqdiREKEEAIRQKAsevQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 465
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564388374 466 VRqkCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNR 507
Cdd:pfam16043 81 VS--RDQFDETLEELNQMLQELLDKLEGQEDAWKKALETLSE 120
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
397-567 |
2.75e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 397 QREKYSLEQDIREKEEAIRQkasevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 474
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 475 -QTISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELNRLQQEETQLEQSIQA--GRAQLETI 529
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 530 LR-------SLKCTQD-------------DINQARSKLSQLQE--SHLEAHRSLEQYDQV 567
Cdd:PRK11281 342 LYqqqqalpSADLIEGladriadlrleqfEINQQRDALFQPDAyiDKLEAGHKSEVTDEV 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-521 |
2.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRL 449
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 450 DEMDQ-----QKAK-LRDMLSDVRQKCQDEtqTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:PRK03918 355 EELEErhelyEEAKaKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
395-561 |
2.83e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 395 QLQREKYSLEQdIREKEEAIRQKasEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLrDMLSDVRQKCQD 472
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 473 ETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ---EETQLEQSIQAGRAQLETILRslKCTQDDINQARSKLSQ 549
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKaiyEEERRREAEEERRKQQEMEER--RRIQEQMRKATEERSR 567
|
170
....*....|..
gi 564388374 550 LQEshLEAHRSL 561
Cdd:pfam17380 568 LEA--MEREREM 577
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
381-551 |
2.86e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 381 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKAS-------EVQELQNDLDRETSSLQELEAQKQDAQDR- 448
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI--QSQESDLKSQEDDLNRAKSELNRLQ--- 509
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQvlq 1051
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388374 510 --QEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 551
Cdd:TIGR00606 1052 mkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
394-551 |
2.86e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQREKYSLEQDIREKEEAirqkASEVQELQNDLDRETSSLQE--------------LEAQKQDAQDRLDEMDQQK--- 456
Cdd:pfam01576 412 GQLQELQARLSESERQRAEL----AEKLSKLQSELESVSSLLNEaegkniklskdvssLESQLQDTQELLQEETRQKlnl 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 -AKLRDMLSD---VRQKCQDETQTISSLKTQIQS---QESDLKSQ-----------EDDLNRAKSELNRLQQ---EETQL 515
Cdd:pfam01576 488 sTRLRQLEDErnsLQEQLEEEEEAKRNVERQLSTlqaQLSDMKKKleedagtlealEEGKKRLQRELEALTQqleEKAAA 567
|
170 180 190
....*....|....*....|....*....|....*.
gi 564388374 516 EQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 551
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
385-566 |
2.93e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 465 DVR--QKCQDETQTISSLKTQIQSqesdlKSQEDDLNRAKSELNRLQQEETQLEQSIQagrAQLETILRSLKCTQDDINQ 542
Cdd:TIGR00606 790 DVTimERFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVV---SKIELNRKLIQDQQEQIQH 861
|
170 180
....*....|....*....|....
gi 564388374 543 ARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQ 885
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
369-552 |
3.26e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 369 PDSSSALGSGEFTGVKELDDISQEIAQLQRekySLEQDIREKEEAIRQKASEVQELQNDLDRETsslQELEAQKQDAQDR 448
Cdd:pfam04108 156 LSSPSESISLIPTLLKELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 LDEMDQQKAKLRDMLS---DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAK-------SELNRLQQEETQLEQS 518
Cdd:pfam04108 230 LDEMENNYERLQKLLEqknSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKetiedylSELEDLREFYEGFPSA 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388374 519 -----IQAGR-----AQLETILRSLkctqddinqaRSKLSQLQE 552
Cdd:pfam04108 310 ygsllLEVERrrewaEKMKKILRKL----------AEELDRLQE 343
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
383-518 |
3.62e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQE-------LQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 455
Cdd:PRK04863 977 AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQynqvlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEE 1056
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 456 KAKLR-----DMLSDVRQKCqdetqtiSSLKTQIQSQESDLKSQEddlNRAKSELNRLQQEETQLEQS 518
Cdd:PRK04863 1057 RARARrdelhARLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA 1114
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
385-552 |
3.70e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLE----QDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 ------------------------------DMLSDVRQKCQDETQTISSLKTQIQsqesDLKSQEDDLNRAKSELNRLQQ 510
Cdd:PHA02562 269 skieqfqkvikmyekggvcptctqqisegpDRITKIKDKLKELQHSLEKLDTAID----ELEEIMDEFNEQSKKLLELKN 344
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564388374 511 EETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQE 552
Cdd:PHA02562 345 KISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
399-520 |
4.14e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 399 EKYSLEQDIREKEEAIRQKASEVQELQNDldretsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTIS 478
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564388374 479 slktQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQ 520
Cdd:COG0542 472 ----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
384-564 |
4.29e-04 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 43.02 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEV---QEL------------QNDLDRETSSLQELEAQkqdAQDR 448
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEK---EESK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 LDEMDQQKAKLRDMLsdvrQKCQDETQT---------------ISSLKTQIQsqesDLK-SQEDDLNraksELNRLQQEE 512
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEELNFlstykdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 513 TQ-LEQSIQAGRAQLETIL--RSLKCTQDDInQARSKLSQLQESHLEAHRSLEQY 564
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQESL-LQKTRDNQVMLKEIEQFREFIDE 204
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
435-556 |
4.54e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 435 LQELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL---------------- 498
Cdd:pfam00261 3 MQQIKEELDEAEERLKE-------AMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLaealekleeaekaade 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 499 ---------NRAKSELNRLQQEETQLEQSIQ----AGRaQLETILRSLKCTQDDINQARSKLSQLQE--SHLE 556
Cdd:pfam00261 76 sergrkvleNRALKDEEKMEILEAQLKEAKEiaeeADR-KYEEVARKLVVVEGDLERAEERAELAESkiVELE 147
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
164-337 |
4.69e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 41.32 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 164 LGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEPVPsvlppplippskrkktvfagavpvlpaspppkdslrstpshg 243
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADT------------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 244 svsslNSTGSLSPKHSVKQTQPPVAWVVPVADKMRFDEIflktDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTR 323
Cdd:COG5126 45 -----DGDGRISREEFVAGMESLFEATVEPFARAAFDLL----DTDGDGKISADEFRRLLTALGVSEEEADELFARLDTD 115
|
170
....*....|....
gi 564388374 324 QTGKLSKEQFALAM 337
Cdd:COG5126 116 GDGKISFEEFVAAV 129
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-563 |
4.72e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYsLEQDIREKEEAIRQKASEVQELQNDL-DRETSSLQELEAQKQDAQDRL---------DEMD 453
Cdd:pfam13868 39 KEEERRLDEMMEEERERA-LEEEEEKEEERKEERKRYRQELEEQIeEREQKRQEEYEEKLQEREQMDeiveriqeeDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 454 -QQKAKLRDMLSDVRQKCQDETQTISSLKtQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL---EQSIQAGRAQLETI 529
Cdd:pfam13868 118 aEEKLEKQRQLREEIDEFNEEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKA 196
|
170 180 190
....*....|....*....|....*....|....
gi 564388374 530 LRslkcTQDDINQARSKLsqLQESHLEAHRSLEQ 563
Cdd:pfam13868 197 QD----EKAERDELRAKL--YQEEQERKERQKER 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-559 |
5.08e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 452
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 DQQKAKLRDMLSDVRQKCqDETQT--------ISSL---KTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ---S 518
Cdd:PRK04863 389 EEEVDELKSQLADYQQAL-DVQQTraiqyqqaVQALeraKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsV 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564388374 519 IQAGRAQLETILRSLKCTQDDI------NQARSKLSQLQESHLEAHR 559
Cdd:PRK04863 468 AQAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAEQ 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
381-562 |
5.14e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 381 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKASEVQELQNDLDRETSS-------------- 434
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL-------NR 507
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLaaserarRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 508 LQQEETQLEQSIQAGRAQletilRSLkcTQDDINQARSKLSQLQESHLEAHRSLE 562
Cdd:pfam01576 859 AQQERDELADEIASGASG-----KSA--LQDEKRRLEARIAQLEEELEEEQSNTE 906
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
405-552 |
5.63e-04 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family consists of the coiled-coil (alpha) domain of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). STAT3 continuously shuttles between nuclear and cytoplasmic compartments. The coiled-coil domain (CCD) of STAT3 appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the STAT3 CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 in the testis, and importin-alpha6 NLS adapters in most cells. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment.
Pssm-ID: 341078 [Multi-domain] Cd Length: 180 Bit Score: 41.90 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 405 QDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 484
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 485 QSQESDLKSQE-DDLNRakselnRLQQEETQLEQSIQAGRaqLETILRSLKCTQDDINQARSKLSQLQE 552
Cdd:cd16853 91 EYVQKNLTDEElADWKR------RQQIACIGGPPNICLDR--LENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
381-589 |
5.72e-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: 43.80 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 381 TGVKEldDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK---- 456
Cdd:TIGR00618 693 TYWKE--MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNneev 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 -------AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNrakSELNRLQQEETQLEQSIQAGRAQLETI 529
Cdd:TIGR00618 771 taalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN---LQCETLVQEEEQFLSRLEEKSATLGEI 847
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 530 LRSLKCTQDDINQARSKLSQLQESHLEAHRsLEQYDQVPDGVSGTSLPDLA---TLNEGILLA 589
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDK-LNGINQIKIQFDGDALIKFLheiTLYANVRLA 909
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
385-522 |
6.36e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqkasEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEMDQQKAKL 459
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKEAKKEADEI 589
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 460 rdmlsdVRQKCQDETQTISSLKTQiqsqesDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAG 522
Cdd:PRK00409 590 ------IKELRQLQKGGYASVKAH------ELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
392-515 |
6.58e-04 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 41.28 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 463
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
471-566 |
6.75e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.79 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 471 QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL-RSLKCTQDDINQARSKLSQ 549
Cdd:TIGR04320 250 PNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALAN 329
|
90
....*....|....*..
gi 564388374 550 LQESHLEAHRSLEQYDQ 566
Cdd:TIGR04320 330 AEARLAKAKEALANLNA 346
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
433-557 |
7.25e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 433 SSLQELEAQKQDAQDRLDEMDQQKAKLRDmlsDVRQKCQDETQTISSLKTQIQSQESDLKSqeddLNRAKSELNRLQQEE 512
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQE---DLEKQAEIAREAQQNYERELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 513 TQLEQSIQAGRAQLETILRSLKCT----QDDINQARSKLSQLQE------SHLEA 557
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNEqnkllhDQLES 128
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
384-567 |
7.70e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIRE---KEEAIRQKASE--VQELQNDLDRETSSLQELeaQKQDAQDRLDEMDQQKAK 458
Cdd:pfam06008 75 AESERTLGHAKELAEAIKNLIDNIKEineKVATLGENDFAlpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAELKA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDMLSDVR---QKCQDETQTissLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQS---IQAGRAQLETILRS 532
Cdd:pfam06008 153 AQDLLSRIQtwfQSPQEENKA---LANALRDSLAEYEAKLSDLR------ELLREAAAKTRDAnrlNLANQANLREFQRK 223
|
170 180 190
....*....|....*....|....*....|....*
gi 564388374 533 LKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:pfam06008 224 KEEVSEQKNQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
371-559 |
7.98e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 41.90 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 371 SSSALGSGEFTGVKE-LDDISQEIAQLQREKYSLEQDIR-EKEEAIRQKASEVQELQNDLDretSSLQELEAQKQDAqdr 448
Cdd:cd07651 46 SRKSLGGSEEGGLKNsLDTLRLETESMAKSHLKFAKQIRqDLEEKLAAFASSYTQKRKKIQ---SHMEKLLKKKQDQ--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 449 ldEMDQQKAklrdmlsdvRQKCQDETQTISSLktqiQSQESDLKSQEDDLNRAKseLNRLQQeetqleqSIQAGRAQLET 528
Cdd:cd07651 120 --EKYLEKA---------REKYEADCSKINSY----TLQSQLTWGKELEKNNAK--LNKAQS-------SINSSRRDYQN 175
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 529 ILRSLKCTQDDINQA-RSKLSQLQesHLEAHR 559
Cdd:cd07651 176 AVKALRELNEIWNREwKAALDDFQ--DLEEER 205
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
390-561 |
8.10e-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: 43.42 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQRekysLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 466
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 467 ---RQKCQDETQTISSLKTQIQSQESDLKSQE-------DDLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLKCT 536
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQETRK 488
|
170 180 190
....*....|....*....|....*....|.
gi 564388374 537 QDDINQARSKLSQL------QESHLEAHRSL 561
Cdd:TIGR00618 489 KAVVLARLLELQEEpcplcgSCIHPNPARQD 519
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
384-449 |
8.15e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 8.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDretsslQELEAQKQDAQDRL 449
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
405-544 |
8.29e-04 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 40.76 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 405 QDIREKEEaiRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqtissLKTQI 484
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 485 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRAQLETILRSLKCTQ---DDINQAR 544
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEKLKE--KKQKEYRAEEAKREQkemDELATQR 138
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
387-517 |
8.91e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 40.36 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQdirEKEEAIRQKAS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 463
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 464 sdvrqkCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL-NRLQQEETQLEQ 517
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-563 |
9.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQND-----LDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 459 LRDMLSDVRqkcqdetqTISSLKT---QIQSQESDLKS-QEDDLNRAKSELNRLQQEETQLEqsiqagrAQLETILRSLK 534
Cdd:PRK03918 485 LEKVLKKES--------ELIKLKElaeQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLK-------GEIKSLKKELE 549
|
170 180 190
....*....|....*....|....*....|..
gi 564388374 535 CTQDDINQAR---SKLSQLQESHLEAHRSLEQ 563
Cdd:PRK03918 550 KLEELKKKLAeleKKLDELEEELAELLKELEE 581
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-563 |
9.76e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQN-----------DLDRETSSLQELEAQKQ--------- 443
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 444 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE---DDLNRAKSELNRLQQEETQLEQ 517
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564388374 518 SiqagrAQLETILR---SLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:TIGR00606 493 N-----SLTETLKKevkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
369-515 |
9.80e-04 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 41.63 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 369 PDSSSALGSGEFTGVKELDDISQEIAQLQrekysleQDIREKEEAIRQKASEVQELQNDLDRETSSLQEL--EAQKQDA- 445
Cdd:cd21116 76 PDLIELADNLIKGDQGAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAv 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 446 ----QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ--SQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:cd21116 149 lnalKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
354-563 |
1.11e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 354 LSPDMVPPSErgtPIPDSSSALGSGEFTGVKELDDISQEI-AQLQRekySLEQDIREKEEAIRQKASEVQELqndLDRET 432
Cdd:pfam10168 471 LLIDAVPPSP---PLLCSKEDVTVDEPLRGLQEDSFEDHIkSILQR---SVSNPILSADKLSSPSPQECLQL---LSRAT 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 433 SSLQELEAQKQDA-----QDRLDEMDQQKAK-LRDMlsdvrQKCQDETQTISSLKTQIQSQESDLK-SQEDDLNRAKSEL 505
Cdd:pfam10168 542 QVFREEYLKKHDLareeiQKRVKLLKLQKEQqLQEL-----QSLEEERKSLSERAEKLAEKYEEIKdKQEKLMRRCKKVL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 506 NRLQqeeTQLEQSIQAGRA---QLETILRSLKCTQDDINQARSKLSQlQESHLEAHRSLEQ 563
Cdd:pfam10168 617 QRLN---SQLPVLSDAEREmkkELETINEQLKHLANAIKQAKKKMNY-QRYQIAKSQSIRK 673
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
411-520 |
1.13e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.15 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 411 EEAIRQKASEVQELqndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV-------------RQK------CQ 471
Cdd:pfam03148 246 NFALRKRIEETEDA----------KNKLEWQLKKTLQEIAELEKNIEALEKAIRDKeaplklaqtrlenRTYrpnvelCR 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564388374 472 DETQtiSSLK---TQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQ 520
Cdd:pfam03148 316 DEAQ--YGLVdevKELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-555 |
1.13e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQkasevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 460
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGR-----LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 461 DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIQAGRaQLETILRS 532
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielkkeiLEKKQEELKFVIKELQ-QLEGSSDR 472
|
170 180
....*....|....*....|...
gi 564388374 533 LKCTQDDINQARSKLSQLQESHL 555
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKNSL 495
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
386-530 |
1.13e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 40.97 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 465
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 466 vrqkcqdETQTISSLktqiqsqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 530
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
384-534 |
1.14e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 41.75 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKASEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 456
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 457 aKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDdLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLK 534
Cdd:COG5325 144 -FLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEE-LEYQQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
342-494 |
1.21e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 42.27 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 342 QKVSKGIDPPQVLSPDMVPPSERGTPIpDSSSALGSGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEV 421
Cdd:pfam17060 99 SFISALELKEDVKSSPRSEADSLGTPI-KVDLLRNLKPQESPETPRRINRKYKSLELRVESMKDELEFKDETIMEKDREL 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388374 422 QELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQ 494
Cdd:pfam17060 178 TELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIISELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
387-585 |
1.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKysLEQDIREKE--EAIRQKASEVQELQNDLDRETSSLQEL--------EAQKQDAqDRLDEMDQQK 456
Cdd:pfam12128 209 DGVVPPKSRLNRQQ--VEHWIRDIQaiAGIMKIRPEFTKLQQEFNTLESAELRLshlhfgykSDETLIA-SRQEERQETS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 457 AKLRDMLSdvrqkcQDETQtissLKTQIQSQESDLKSQEDDLNRAKSELNRLqqeETQLEQSIQAGraqletiLRSLKCT 536
Cdd:pfam12128 286 AELNQLLR------TLDDQ----WKEKRDELNGELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAAD 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564388374 537 QDDINQARSKLSQLQESH---LEAHRSLEQ-YDQVPDGVSGTSLPDLATLNEG 585
Cdd:pfam12128 346 QEQLPSWQSELENLEERLkalTGKHQDVTAkYNRRRSKIKEQNNRDIAGIKDK 398
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
385-532 |
1.37e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKysleqdirekEEAIRQKASEVQELqndlDRETSSLQELE-----AQKQDAQDRldeMDQQKAKL 459
Cdd:pfam05701 43 ELEKVQEEIPEYKKQS----------EAAEAAKAQVLEEL----ESTKRLIEELKlnlerAQTEEAQAK---QDSELAKL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 460 RdmLSDVRQKCQDETQTISslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRAQlETILRS 532
Cdd:pfam05701 106 R--VEEMEQGIADEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSAS 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
493-563 |
1.40e-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: 42.06 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 493 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
387-554 |
1.49e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 41.74 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 387 DDISQEIAQLQREKYSLEQ----------------------DIREKEEAIRQKASEVQELQNDLDRETSSL--------Q 436
Cdd:pfam09755 110 NDLSRKLTQLRQEKVELEQtleqeqeyqvnklmrkiekleaETLNKQTNLEQLRREKVELENTLEQEQEALvnrlwkrmD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 437 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDvRQKCQDETQTISSLKTQIQSQESDLKSQEDDlnrAKSELNRLQQEETQL- 515
Cdd:pfam09755 190 KLEAEKRLLQEKLDQPVSAPPSPRDSTSE-GDTAQNLTAHIQYLRKEVERLRRQLATAQQE---HTEKMAQYAQEERHIr 265
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564388374 516 EQSIQAGRA-QLETILRSLKCTQddINQARSKLSQLQESH 554
Cdd:pfam09755 266 EENLRLQRKlQLEMERREALCRH--LSESESSLEMDEERY 303
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
394-461 |
1.55e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 40.03 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388374 394 AQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
389-561 |
1.55e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 389 ISQEIAQLQREKYSLEQDIREKEEAIRQkasEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 465
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVLNELKKDFKQ---LLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 466 --VRQKCQdetQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ-------------QEETQLEQSI----------- 519
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMasllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 520 ----QAGR-----------------AQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 561
Cdd:pfam04108 192 dqcvTAVKlteggraemlevlendaRELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
396-534 |
1.58e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.32 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 396 LQREKYSLEQDIREKEEAIRQKASEVQELQNDLdreTSSLQELEAQKQDAQDRLDEmdqqkaklrdmlsdVRQkcQDETQ 475
Cdd:PRK07352 48 LEERREAILQALKEAEERLRQAAQALAEAQQKL---AQAQQEAERIRADAKARAEA--------------IRA--EIEKQ 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 476 TISSLKTQIQSQESDLKSQEDdlnRAKSELNR------LQQEETQLEQSIQAGrAQLETILRSLK 534
Cdd:PRK07352 109 AIEDMARLKQTAAADLSAEQE---RVIAQLRReaaelaIAKAESQLPGRLDED-AQQRLIDRSIA 169
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
384-552 |
1.58e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLE--QDIREKEEAIRQKASEVqeLQNDLDRetsSLQELEAQ--------KQDAQDRLDEMD 453
Cdd:pfam07111 162 EALSSLTSKAEGLEKSLNSLEtkRAGEAKQLAEAQKEAEL--LRKQLSK---TQEELEAQvtlveslrKYVGEQVPPEVH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 454 QQ-----KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS-IQAGRAQLE 527
Cdd:pfam07111 237 SQtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSlLNRWREKVF 316
|
170 180
....*....|....*....|....*....
gi 564388374 528 TILRSLKCT----QDDINQARSKLSQLQE 552
Cdd:pfam07111 317 ALMVQLKAQdlehRDSVKQLRGQVAELQE 345
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
390-562 |
1.66e-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: 42.12 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQK 469
Cdd:pfam10174 543 AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQ 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 470 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEEtqleqsiqagraQLETILRSLKCTQDDINQARSKLSQ 549
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL------------QLEELMGALEKTRQELDATKARLSS 680
|
170
....*....|...
gi 564388374 550 LQESHLEAHRSLE 562
Cdd:pfam10174 681 TQQSLAEKDGHLT 693
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
390-517 |
1.73e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 41.51 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 390 SQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQD--------------RLDEMDQQ 455
Cdd:pfam14915 150 SQQLSKAESKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDkvnkyigkqesleeRLAQLQSE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 456 KAKLRDMLSDVRQK----------CQDETQTISSlKTQIQSQESDLKSQEddlnRAK---SELNRLQQEETQLEQ 517
Cdd:pfam14915 230 NMLLRQQLEDAQNKadakektvidIQDQFQDIVK-KLQAESEKQVLLLEE----RNKeliNECNHLKERLYQYEK 299
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
383-472 |
1.76e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 39.28 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRqkasEVQELQNDLD------------RETSSLQELEAQKQDAQDRLD 450
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALE----ELEKLPDDTPiykivgnllvkvDKTKVEKELKERKELLELRSR 88
|
90 100
....*....|....*....|..
gi 564388374 451 EMDQQKAKLRDMLSDVRQKCQD 472
Cdd:PRK09343 89 TLEKQEKKLREKLKELQAKINE 110
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
479-549 |
1.79e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.99 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 479 SLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 549
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-552 |
1.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 381 TGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA--- 457
Cdd:PRK02224 509 DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 458 -------KLRDMLSDvRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL------NRL---QQEETQLEQSIqa 521
Cdd:PRK02224 586 eriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeARIeeaREDKERAEEYL-- 662
|
170 180 190
....*....|....*....|....*....|....*
gi 564388374 522 grAQLETILRSLKCTQDD----INQARSKLSQLQE 552
Cdd:PRK02224 663 --EQVEEKLDELREERDDlqaeIGAVENELEELEE 695
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
385-528 |
1.82e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.05 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQ-REKYSLEQDIREKEEAIRQKASEV------------QELQNDLDRETSSLQ---------ELEAQK 442
Cdd:pfam09731 295 EIDQLSKKLAELKkREEKHIERALEKQKEELDKLAEELsarleevraadeAQLRLEFEREREEIResyeeklrtELERQA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 443 QDAQDRL-DEMDQQKAKL-RDMLSDVRQKCQDE----TQTISSLKTQIQSQE---SDLKSQEDDLNRAKselnrlqqeet 513
Cdd:pfam09731 375 EAHEEHLkDVLVEQEIELqREFLQDIKEKVEEEragrLLKLNELLANLKGLEkatSSHSEVEDENRKAQ----------- 443
|
170
....*....|....*
gi 564388374 514 QLEQSIQAGRAQLET 528
Cdd:pfam09731 444 QLWLAVEALRSTLED 458
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
440-563 |
1.94e-03 |
|
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: 40.68 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 519
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564388374 520 QAGRAQletilRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 563
Cdd:COG1579 83 GNVRNN-----KEYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
456-564 |
2.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQKCQD---ETQTISSLK-TQIQSQESDLKSQ-EDDLNRAKSEL----NRLQQEETQLE---QSIQAGR 523
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEakkEAEAIKKEAlLEAKEEIHKLRNEfEKELRERRNELqkleKRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564388374 524 AQLETILRSLKCTQDDINQARSKLSQLQESHLEAhrsLEQY 564
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERI 147
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
394-556 |
2.09e-03 |
|
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.
Pssm-ID: 407241 [Multi-domain] Cd Length: 360 Bit Score: 41.33 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQREKYSLEQD-IREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD 472
Cdd:pfam17097 121 ASLEDEVSQLEDDtLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECWELLNELERLRDQRITVEEQTSN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 473 ETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE--QSIQAGRAQL-ETILRSLKCTQDDINQARSK-LS 548
Cdd:pfam17097 201 EKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEkvDKSSINRTQNdEESIQNTVQLNLLIDMWKSKfII 280
|
....*...
gi 564388374 549 QLQESHLE 556
Cdd:pfam17097 281 HEKISNLE 288
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
419-553 |
2.14e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.47 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 419 SEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL 498
Cdd:cd21116 73 SYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 499 NRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQES 553
Cdd:cd21116 143 QAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESS 197
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-566 |
2.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdETQtISSLKTQ---------IQSQESDLksqedDLNRAKSELNRLQQ 510
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGEL------ERQ-LEPLERQaekaeryreLKEELKEL-----EAELLLLKLRELEA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 511 EETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
384-481 |
2.36e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAI-----RQKASEVQELQNDLDrETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKEMEERQKAIyeeerRREAEEERRKQQEME-ERRRIQEQMRKATEERSRLEAMEREREM 577
|
90 100
....*....|....*....|....
gi 564388374 459 LRDMLSDVRQKCQDETQT-ISSLK 481
Cdd:pfam17380 578 MRQIVESEKARAEYEATTpITTIK 601
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
386-563 |
2.51e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQrekyslEQDIREKEEAIRQKASEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 465
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 466 VRQKCQDETQTI-SSLKTQIQSQESDLKSQEDDL-NRAKSELNRLQqeeTQLEQSIQAGRAQLETILRSLKCTQDDI--- 540
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAPYaee 147
|
170 180
....*....|....*....|....*
gi 564388374 541 --NQARSKLSQLQESHLEAHRSLEQ 563
Cdd:pfam01442 148 vqAQLSQRLQELREKLEPQAEDLRE 172
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
389-543 |
2.69e-03 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 39.43 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 389 ISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSlqeleaqkqdaqDRLDEMDQQKAKLRDMLSDVRQ 468
Cdd:pfam16789 23 VKDKKRALEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------------DKILQMKRYIKVVKERLKQEEK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388374 469 KCQDEtqtisslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkcTQDDINQA 543
Cdd:pfam16789 91 KVQDQ-------KEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEER------EQDEIGSA 152
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
384-454 |
2.72e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388374 384 KELDDISQEIAQLQREKysleQDIREKEEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 454
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
384-553 |
2.73e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQrEKYSL----EQDIREKEEAIRQKASEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEM 452
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAyselqeeLEEILEQLEEIEEEQEEF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 453 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSqeSDL----KSQEDDLNRAKSELNRLQQeetQLEQSiqagRAQLET 528
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEV----PLNMDE 454
|
170 180
....*....|....*....|....*
gi 564388374 529 ILRSLKCTQDDINQARSKLSQLQES 553
Cdd:pfam06160 455 VNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
392-554 |
2.93e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.03 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 392 EIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRetsslQELEAQKQDAQdRLDEMDQQ--------KAKLRDML 463
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE-----RELKAEAEHRQ-RVVELSREveeakrafEEKLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKS-ELNRLQQEetqLEQSIQAGRAQLETiLRSLKctQDDINQ 542
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVED-LRKEK--KKLAEE 194
|
170
....*....|..
gi 564388374 543 ARSKLSQLQESH 554
Cdd:pfam15665 195 YEQKLSKAQAFY 206
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-616 |
2.94e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLEtiLRSLKCTQdDINQA 543
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE--LKKEILEK-KQEEL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388374 544 RSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGGFGAMDDPFKNKALLFSNNSQELH 616
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
384-563 |
2.98e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQREKYSLEQDIREKEEAiRQKASEVQELQNDLDRetssLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAA-ALQPGEEEELEEERRR----LSNAEKLREALQEALEALSGGEGGALDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 SDVRQKCQDetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE----ETQLEQsIQAGRAQLETILRSLKCTQDD 539
Cdd:COG0497 247 GQALRALER----LAEYDPSLAELAERLESALIELEEAASELRRYLDSlefdPERLEE-VEERLALLRRLARKYGVTVEE 321
|
170 180 190
....*....|....*....|....*....|
gi 564388374 540 I----NQARSKLSQLQ--ESHLEAhrsLEQ 563
Cdd:COG0497 322 LlayaEELRAELAELEnsDERLEE---LEA 348
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
456-566 |
3.05e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 41.38 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC 535
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQ 81
|
90 100 110
....*....|....*....|....*....|.
gi 564388374 536 TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 566
Cdd:COG5283 82 LSAAQRRLRSSLEQTNRQLERQQQRLARLGA 112
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
410-558 |
3.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 410 KEEAIRQKASEVQELQNDLDREtsslqeleaqkqdAQDRLDEMDQQKAKLRdmlsdvrQKcqdetqtisslKTQIQSQES 489
Cdd:PRK12704 55 KKEALLEAKEEIHKLRNEFEKE-------------LRERRNELQKLEKRLL-------QK-----------EENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 490 DLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSL-KCTQDD-----INQARSKL-----SQLQESHLEAH 558
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEEakeilLEKVEEEArheaaVLIKEIEEEAK 183
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
383-558 |
3.61e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 40.76 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 455
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 456 KAKLRDMLSDVRQKCQdetQTISSLKTQIQSQESDLK----SQEDDLNRAKSELNRLQQEETQLEQS-IQAGRAQLETIL 530
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
170 180
....*....|....*....|....*....
gi 564388374 531 RSL-KCTQDDINQARSKLSQLQESHLEAH 558
Cdd:pfam03999 298 DKLfYSTEQRKRFIPFFEELYTEDLLELH 326
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
391-542 |
3.68e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDIrekeEAIRQKASEVQELQnDLDRETSSLQE--LEAQKQDAQDRLDEMDQQKAKLrdmlsdvrq 468
Cdd:pfam12128 768 DVIAKLKREIRTLERKI----ERIAVRRQEVLRYF-DWYQETWLQRRprLATQLSNIERAISELQQQLARL--------- 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 469 kcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELN------------RLQQEETQLEQSIQAGRAQLETILRSLKCT 536
Cdd:pfam12128 834 --------IADTKLRRAKLEMERKASEKQQVRLSENLRglrcemsklatlKEDANSEQAQGSIGERLAQLEDLKLKRDYL 905
|
....*.
gi 564388374 537 QDDINQ 542
Cdd:pfam12128 906 SESVKK 911
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
478-558 |
3.69e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.48 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 478 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEA 557
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLAT 322
|
.
gi 564388374 558 H 558
Cdd:TIGR04320 323 A 323
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
386-463 |
3.86e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSL-QELEAQKQDAQDRLD---EMDQQKAKLRD 461
Cdd:pfam00038 226 IQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETrQEMARQLREYQELLNvklALDIEIATYRK 305
|
..
gi 564388374 462 ML 463
Cdd:pfam00038 306 LL 307
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
410-517 |
3.98e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 410 KEEAIRQKASEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqtisslk 481
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 564388374 482 tqiQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQ 517
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLER 142
|
|
| ClyA_MakA-like |
cd22655 |
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
403-529 |
4.04e-03 |
|
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.
Pssm-ID: 439153 [Multi-domain] Cd Length: 342 Bit Score: 40.34 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 403 LEQDIREKEEAIRQKASevqelqndldretSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVRQKCQDETQTISSLKT 482
Cdd:cd22655 84 FKALPTAPDDAQVEQII-------------ALLQALQKPVQEIISNIAAYQGK-------LKAWGDKMQAAHDNLTTGAA 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564388374 483 QIQSQESDLKSQEDDLNRAKSELNR-LQQEETQLEQS-IQAGRAQLETI 529
Cdd:cd22655 144 QIQAAETDLQADIDKINNAIANLNAeIAKDNKAIAAAqIAIGVGIFELV 192
|
|
| MIP-T3_C |
pfam17749 |
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ... |
409-547 |
4.07e-03 |
|
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.
Pssm-ID: 465481 [Multi-domain] Cd Length: 154 Bit Score: 38.97 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 409 EKEEAIRQKASEVQELQNDLDRE------TSSLQELEAQKqdaqdrldEMDQQKAKLrdmlSDVRQKCQDETQTISSLKT 482
Cdd:pfam17749 4 DAQGGLVKKILETKKEYEKGGAEaepgesDRSLQESSAKK--------GRTVSASDI----NQLRESIQTLTKSANPLGK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 483 QIQSQESDLKSQEDDLNRAKSELNR----LQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKL 547
Cdd:pfam17749 72 LLDFIQDDIDSMQRELQMWRSEYRQnaqaLQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQI 140
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
486-554 |
4.66e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 37.16 E-value: 4.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 486 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkctQDDI-------NQARSKLSQLQESH 554
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL-------NDELialqienNLLEEKLRKLQEEN 69
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
386-517 |
4.90e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 37.93 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLdretsslqeLEAQKqdaqdrldemdqqkaklrdMLSD 465
Cdd:pfam05103 27 LDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTL---------ILAQE-------------------TAEE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564388374 466 VRQKCQDETQTISSlKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQLEQ 517
Cdd:pfam05103 79 VKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
425-554 |
5.18e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 425 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcQDETQ------------TISSLKTQIQSQESDLk 492
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL-YRELRksllanrfsfgpALDELEKQLENLEEEF- 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 493 SQEDDLN------RAKSELNRLQQEETQLEQSIQagraQLETILRSLKCT-QDDINQARSKLSQLQESH 554
Cdd:PRK04778 182 SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAGYRELVEEG 246
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
385-472 |
5.75e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.22 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQLQREKYSLEQDIREKEEAI---------RQKASEVqEL-----QNDLDRETSSLQE----LEAQKQDAQ 446
Cdd:pfam03148 266 QLKKTLQEIAELEKNIEALEKAIRDKEAPLklaqtrlenRTYRPNV-ELcrdeaQYGLVDEVKELEEtieaLKQKLAEAE 344
|
90 100 110
....*....|....*....|....*....|...
gi 564388374 447 DRLDEMDQQKAKLRDMLSDV-------RQKCQD 472
Cdd:pfam03148 345 ASLQALERTRLRLEEDIAVKanslfidREKCMG 377
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
384-509 |
6.29e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 384 KELDDISQEIAQLQR---EKYSLEQDIREKEEAIRQKASEVQELQNDLDretsslQELEAQKQdaqdrldEMDQQKAKLR 460
Cdd:pfam02841 183 QSKEAVEEAILQTDQaltAKEKAIEAERAKAEAAEAEQELLREKQKEEE------QMMEAQER-------SYQEHVKQLI 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564388374 461 DMLSDVRQKCQDETQTISSLKTQIQ---SQESdLKSQEDDLNRaksELNRLQ 509
Cdd:pfam02841 250 EKMEAEREQLLAEQERMLEHKLQEQeelLKEG-FKTEAESLQK---EIQDLK 297
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
408-523 |
6.51e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.05 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 408 REKEEAIR---QKASEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD---ML----SDVRQKCQDETQTI 477
Cdd:pfam19220 272 RDRDEAIRaaeRRLKEASIERDTLERR---LAGLEADLERRTQQFQEMQRARAELEEraeMLtkalAAKDAALERAEERI 348
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564388374 478 SSLKTQIQSQESDLKSQEDDL---NRA-KSELNRLQQEETQLEQSIQAGR 523
Cdd:pfam19220 349 ASLSDRIAELTKRFEVERAALeqaNRRlKEELQRERAERALAQGALEIAR 398
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
411-548 |
6.65e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 38.89 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 411 EEAIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKL----RDMLSdvrqkcQDETQTISSLKTQIQS 486
Cdd:pfam04012 21 EDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLeekaQAALT------KGNEELAREALAEKKS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388374 487 QESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC--TQDDINQARSKLS 548
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLS 158
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
406-468 |
7.18e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 38.77 E-value: 7.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388374 406 DIREKEEAIRQKASEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 468
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
386-471 |
7.23e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 37.63 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 386 LDDISQEIAQLQREKYSLEQDIRE----KEEAIRQKASEVQELQNDLD-RETSSLQELEAQKqdaQDRLDEMDQQKAKLR 460
Cdd:smart00502 9 LTKLRKKAAELEDALKQLISIIQEveenAADVEAQIKAAFDELRNALNkRKKQLLEDLEEQK---ENKLKVLEQQLESLT 85
|
90
....*....|.
gi 564388374 461 DMLSDVRQKCQ 471
Cdd:smart00502 86 QKQEKLSHAIN 96
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
388-569 |
7.65e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 388 DISQEIAQLQREKYSLEQ------DIREK-----------EEAIRQKASEVQELQN---DLDRETSSLQELEAQKQDAQD 447
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQykekacEIRDQitskeaqlessREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 448 RLDEMDQQKAKLRDMLSDVRQKCQDEtqtissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS-----IQAG 522
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEktellVEQG 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564388374 523 RAQLetilrslkctQDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 569
Cdd:TIGR00606 351 RLQL----------QADRHQEHIRARDSLIQSLATRLELDGFERGPF 387
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
391-564 |
7.87e-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: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDIREKEEAIRQKASEVQELQNDLDRETSSLQELE----AQKQDAQDRldemDQQKAKLRDML--- 463
Cdd:pfam10174 95 QDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMElrieTQKQTLGAR----DESIKKLLEMLqsk 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 464 ---SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL---NRLQQEETQ---LEQSIQAGRAQLETILRSLK 534
Cdd:pfam10174 171 glpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaLQTVIEMKDTKISSLERNIR 250
|
170 180 190
....*....|....*....|....*....|
gi 564388374 535 CTQDDINQARSKLSQLQESHLEAHRSLEQY 564
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
380-567 |
7.97e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 380 FTGVKELDDIsqeIAQLQREKYSLEQDIREKEEaIRQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKL 459
Cdd:PRK01156 134 FVGQGEMDSL---ISGDPAQRKKILDEILEINS-LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 460 RDMLSDVRQKcqdetqtisslktqIQSQESDLKSQEDDLNRAKSELNRLQqeetqleqsiqagrAQLETILRslkcTQDD 539
Cdd:PRK01156 210 EKSHSITLKE--------------IERLSIEYNNAMDDYNNLKSALNELS--------------SLEDMKNR----YESE 257
|
170 180
....*....|....*....|....*...
gi 564388374 540 INQARSKLSQLQESHLEAHRSLEQYDQV 567
Cdd:PRK01156 258 IKTAESDLSMELEKNNYYKELEERHMKI 285
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
412-520 |
8.03e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 37.24 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 412 EAIRQKASEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQTISSLKTQIQSQ 487
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLisiiQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKENK 73
|
90 100 110
....*....|....*....|....*....|...
gi 564388374 488 ESDLKSQeddlnrakseLNRLQQEETQLEQSIQ 520
Cdd:smart00502 74 LKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| DUF5082 |
pfam16888 |
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized. |
391-508 |
8.36e-03 |
|
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized.
Pssm-ID: 407125 [Multi-domain] Cd Length: 122 Bit Score: 37.28 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 391 QEIAQLQREKYSLEQDIREKEEAiRQKASEVQElqndldretsslqELEAQKQDAQDRLDEMD----QQKAKLRDMLSDV 466
Cdd:pfam16888 10 AQIAQLRSEIAALEEKIERLKEA-KTKLDAEKE-------------SLHDKKTKLQGPLNSSEswngSNENNYDGIRSNL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564388374 467 RQKCQ---DET-QTISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 508
Cdd:pfam16888 76 ETSYQnyvDELdELIDAIEEEITRLENQINEAQGVIDTLQSQLNSL 121
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
402-533 |
9.00e-03 |
|
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.
Pssm-ID: 396537 [Multi-domain] Cd Length: 199 Bit Score: 38.51 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 402 SLEQDIREKEEAIRQKASEvqELQNDLDRetsslqeLEAQKQDAQDRLDEMDQQKAklrdmlsDVRQKcqdetQTISSLK 481
Cdd:pfam01991 1 FIRQEAEEKAEEIRAKAEE--EFAIEKAE-------LVQEAEEKIDEIYEKKEKQA-------EMQKK-----IIISNAK 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564388374 482 tqIQSQESDLKSQEDDLNRAkseLNRLQQEETQLEQSiqagRAQLETILRSL 533
Cdd:pfam01991 60 --NEARLKVLEAREEILDEV---FNEAEKKLAELEED----TDEYKDLLRKL 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-560 |
9.05e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 385 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKASEVQELQNDLDRETSSLQ------- 436
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 437 ELEAQKQDAQDRLDEMDQQ-KAKLRdmlsdvrqkcqdetQTISSLKTQIQSQESDLKsQEddlNRAKSELNRL-QQEETQ 514
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFK--------------SSIAALEAKIAQLEEQLE-QE---SRERQAANKLvRRTEKK 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564388374 515 LEQSIqagrAQLETILRSLKCTQDDINQARSKLS----QLQESHLEAHRS 560
Cdd:pfam01576 1004 LKEVL----LQVEDERRHADQYKDQAEKGNSRMKqlkrQLEEAEEEASRA 1049
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
415-560 |
9.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 415 RQKASEVQELQNDLDRETSSLQE-LEAQKQDAQDRLDEMDQQKAKLRdmlsdvRQKCQDETQTISSLKTQIQSQESDLKS 493
Cdd:PRK12705 29 QRLAKEAERILQEAQKEAEEKLEaALLEAKELLLRERNQQRQEARRE------REELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388374 494 QEDDLNRAKSELN--------RLQQEETQLEQSIQAGRAQL-ETILRSLKCTQDDINQARSKLsQLQESHLEAHRS 560
Cdd:PRK12705 103 LENQLEEREKALSareleleeLEKQLDNELYRVAGLTPEQArKLLLKLLDAELEEEKAQRVKK-IEEEADLEAERK 177
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
426-552 |
9.40e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 37.59 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 426 NDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQES-DLKSQEDDLNRAKSE 504
Cdd:cd12923 1 DDVEKLAKKLKEINKEYLDKSREYDELYEKYNKLSQEIQLKRQALEAFEEAVKMFEEQLRTQEKfQKEAQPHEKQRLMEN 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564388374 505 LNRLQQEETQLEQSiqagRAQLETILR----SLKCTQDDINQARSKLSQLQE 552
Cdd:cd12923 81 NELLKSRLKELEES----KEQLEEDLRkqvaYNRELEREMNSLKPELMQLRK 128
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
394-563 |
9.91e-03 |
|
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: 39.95 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 394 AQLQREKYSLEQDIREKEEairQKASEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQde 473
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMP---DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 474 tqtisslktQIQSQESDLKSQEDDLNRAKSELnRLQQEETQLEQSiqagRAQLETILRSLKCTQDDINQARSKLSQL--Q 551
Cdd:TIGR00618 271 ---------ELRAQEAVLEETQERINRARKAA-PLAAHIKAVTQI----EQQAQRIHTELQSKMRSRAKLLMKRAAHvkQ 336
|
170
....*....|..
gi 564388374 552 ESHLEAHRSLEQ 563
Cdd:TIGR00618 337 QSSIEEQRRLLQ 348
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
388-485 |
9.94e-03 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 38.06 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388374 388 DISQEIAQLQREKYSLEQDIREKEEAiRQKASEVQELQNDLDRETSSLQELEAQKQ-----DAQDRLDEMDQQKAKLRDM 462
Cdd:pfam03280 76 SAEEKQQRLAALRAQLPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQRAAWQQR 154
|
90 100
....*....|....*....|....*.
gi 564388374 463 LSD---VRQKCQDETQTISSLKTQIQ 485
Cdd:pfam03280 155 LDDylaERQQINAAGLSEQERQAAIA 180
|
|
| |
