|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
266-362 |
1.21e-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: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 266 AWVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSkG 345
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 568955195 346 IDPPQVLSPDMVPPSER 362
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
121-200 |
3.07e-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: 117.38 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 121 WAVRVEEKAKFDGIFESLLP-VNGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 199
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
.
gi 568955195 200 V 200
Cdd:smart00027 82 I 82
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
131-196 |
5.20e-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: 5.20e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 131 FDGIFESLLPVN-GLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 196
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
277-343 |
5.75e-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: 5.75e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 277 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVS 343
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 |
3.47e-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: 3.47e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 127 EKAKFDGIFESLLPVNGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVY 192
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIF 73
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
4.29e-21 |
|
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: 88.49 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 13 PGGNPLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQSGHEVTLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 568955195 93 SLSLTMPPPKF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
1.40e-20 |
|
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: 86.12 E-value: 1.40e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 19 YESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQS 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
371-543 |
3.14e-18 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 87.65 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 371 STLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 450
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA-----GRAQLE 525
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeAEQALD 186
|
170
....*....|....*...
gi 568955195 526 TILRSLKCTQDDINQARS 543
Cdd:COG4372 187 ELLKEANRNAEKEEELAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-564 |
1.80e-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: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|..
gi 568955195 543 SKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEE 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-561 |
2.40e-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: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170 180
....*....|....*....|
gi 568955195 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 462 LELLAELLEEAALLEAALAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-561 |
4.37e-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: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180
....*....|....*....|
gi 568955195 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 448 AEEEAELEEEEEALLELLAE 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-566 |
6.05e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180
....*....|....*....|....*
gi 568955195 542 RSKLSQLQESHLEAHRSLEQYDQDD 566
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEAL 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
390-564 |
1.32e-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: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 469
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 470 DETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170
....*....|....*
gi 568955195 550 ESHLEAHRSLEQYDQ 564
Cdd:COG1196 393 RAAAELAAQLEELEE 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-565 |
5.26e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 453
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC 533
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190
....*....|....*....|....*....|..
gi 568955195 534 TQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-565 |
2.12e-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: 81.26 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGR-----AQLETILRSLKCTQ 535
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQ 453
|
170 180 190
....*....|....*....|....*....|
gi 568955195 536 DDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-565 |
2.28e-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: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 386 DISQEIAQLQREKYSLEqdIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVR 465
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-------LEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 466 QKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180
....*....|....*....|
gi 568955195 546 SQLQESHLEAHRSLEQYDQD 565
Cdd:COG1196 368 LEAEAELAEAEEELEELAEE 387
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-561 |
2.51e-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: 80.87 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdqqkAKLRDML 461
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180
....*....|....*....|
gi 568955195 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR02168 858 AAEIEELEELIEELESELEA 877
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-561 |
2.69e-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: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180
....*....|....*....|
gi 568955195 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-565 |
8.64e-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: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQ 453
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisrLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQKcQDETQTI-SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:TIGR02168 318 LEELEAQLEELESK-LDELAEElAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190
....*....|....*....|....*....|...
gi 568955195 533 CTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-561 |
1.20e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 386 DISQEIAQLQREK---YSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG1196 261 ELAELEAELEELRlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170
....*....|....*....
gi 568955195 543 SKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 421 EELEELEEALAELEEEEEE 439
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-564 |
1.30e-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: 78.56 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrQK 467
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 468 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170
....*....|....*..
gi 568955195 548 LQEShlEAHRSLEQYDQ 564
Cdd:TIGR02168 433 AELK--ELQAELEELEE 447
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
405-566 |
4.91e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.94 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 405 IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcqdetqtISSLKTQIQS 484
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 485 QESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
..
gi 568955195 565 DD 566
Cdd:COG4372 179 AE 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-566 |
7.00e-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: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL----NRLQQEETQLEQSIQAGRAQLETILRslkcTQD 536
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALLEAEAELAEAEEELEE----LAE 386
|
170 180 190
....*....|....*....|....*....|
gi 568955195 537 DINQARSKLSQLQESHLEAHRSLEQYDQDD 566
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-582 |
8.93e-14 |
|
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: 74.03 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 461
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 S-----------DVRQKCQDETQTISSLK-------------TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 517
Cdd:COG4942 111 RalyrlgrqpplALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 518 QAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQDDPFKNKALLFSNNSQEL 582
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
383-563 |
1.02e-13 |
|
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: 71.49 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 DVR-----QKCQDEtqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDD 537
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180
....*....|....*....|....*.
gi 568955195 538 INQARSKLsqlqESHLEAhRSLEQYD 563
Cdd:COG1579 161 LEAEREEL----AAKIPP-ELLALYE 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-551 |
1.59e-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: 75.09 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 469
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 470 DETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
..
gi 568955195 550 ES 551
Cdd:TIGR02168 393 LQ 394
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-564 |
2.54e-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: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 467
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 468 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170
....*....|....*..
gi 568955195 548 LQESHLEAHRSLEQYDQ 564
Cdd:TIGR02168 829 LERRIAATERRLEDLEE 845
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-549 |
2.61e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 458
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 459 DMLSDVRQKcqdeTQTISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDD 537
Cdd:COG4717 160 ELEEELEEL----EAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170
....*....|....
gi 568955195 538 --INQARSKLSQLQ 549
Cdd:COG4717 236 leAAALEERLKEAR 249
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
381-532 |
2.63e-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: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 458
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 459 DMLSDVRQKCQDETQTI-SSLKTQI---QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-550 |
3.57e-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: 73.52 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELNRLQQE----ETQLEQSIQagraQLETI 527
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEisntQTQLNQLKD----EQNKI 265
|
170 180
....*....|....*....|...
gi 568955195 528 LRSLKCTQDDINQARSKLSQLQE 550
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEK 288
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
391-565 |
4.01e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 391 IAQLQREKYSLE-----------QDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 457 LRDMLSdvRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRAQLETILRSLKCTQ 535
Cdd:COG4717 128 LPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|
gi 568955195 536 DDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-565 |
4.30e-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: 73.55 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 S-------DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRAQLETILRSL 531
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALL 892
|
170 180 190
....*....|....*....|....*....|....*...
gi 568955195 532 KC----TQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:TIGR02168 893 RSeleeLSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-561 |
5.02e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKTSEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 446
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 LDEMDQQKAKLRDMLSDVRQKC-QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLE 525
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 568955195 526 TILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-530 |
1.32e-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: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 463 DVRQKCQDETQTISSLktqiqsqesdlksqEDDLNRAKSELNRLQQEETQLEQSIQAGRAQlETILRS 530
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 ... |
382-550 |
2.48e-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: 70.82 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
....*....
gi 568955195 542 RSKLSQLQE 550
Cdd:TIGR04523 495 EKELKKLNE 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-550 |
2.65e-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: 70.82 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLKCTQDD---- 537
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEKlese 532
|
170
....*....|...
gi 568955195 538 INQARSKLSQLQE 550
Cdd:TIGR04523 533 KKEKESKISDLED 545
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-565 |
2.91e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD-- 459
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEEle 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 460 -MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLkctqDDI 538
Cdd:COG1196 407 eAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL----AEL 482
|
170 180
....*....|....*....|....*..
gi 568955195 539 NQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-561 |
2.98e-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: 70.87 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 dvRQKCQDETQTISSLKTQIQSQESDLKSQEddlnrakSELNRLQQEETQLEQSIQ---------------------AGR 521
Cdd:TIGR02169 790 --HSRIPEIQAELSKLEEEVSRIEARLREIE-------QKLNRLTLEKEYLEKEIQelqeqridlkeqiksiekeieNLN 860
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568955195 522 AQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
382-582 |
4.33e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 68.78 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLksQEDDLNRAKSELNRLQQE-ETQLEQSIQAGRAQLETILRSLKCTQDDINQ 540
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEaNRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955195 541 ARSKLSQLQESHLEAHRSLEQYDQDDPFKNKALLFSNNSQEL 582
Cdd:COG4372 224 KDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
382-628 |
5.82e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 68.32 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQ--------------- 444
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSvsyldvllgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 445 --DRLDEMDQQKAKLRDMLSDVrqkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRA 522
Cdd:COG3883 117 flDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 523 QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQDDPFKNKALLFSNNSQELHPDPFQAEDPFKSDPFKGAD 602
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAA 272
|
250 260
....*....|....*....|....*.
gi 568955195 603 PFKGDPFQSDPFSEQQTAATDPFGGD 628
Cdd:COG3883 273 GAGAAAASAAGGGAGGAGGGGGGGGA 298
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
382-525 |
6.87e-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: 66.10 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 461
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 462 SDVRQKCQDEtqtISSLKTQIQSQESDLKSQEDDLNRAKSELN----RLQQEETQLEQSIQAGRAQLE 525
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
378-519 |
2.29e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 378 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 457 LRDMLSDVRQKCQDETQTISSLKTQIQSQ----ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-547 |
6.40e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD-------QQK 454
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskrselrREL 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLksQEDDL---NRAKSELNRLQQEETQLEQSIQA-GRAQLETI--- 527
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT--LEEAEaleNKIEDDEEEARRRLKRLENKIKElGPVNLAAIeey 995
|
170 180
....*....|....*....|....*.
gi 568955195 528 ------LRSLKCTQDDINQARSKLSQ 547
Cdd:TIGR02168 996 eelkerYDFLTAQKEDLTEAKETLEE 1021
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
382-561 |
9.84e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.47 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 458
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 459 -------------------DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQA 519
Cdd:COG3883 103 syldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE-------LEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955195 520 GRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-567 |
1.13e-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: 65.85 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRE-------TSSLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 456 KLRDMLSDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 528
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170 180 190
....*....|....*....|....*....|....*....
gi 568955195 529 RSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQDDP 567
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-560 |
1.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKTSEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 457
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 458 RDMLSDVRQKCQDETQTISSLK---TQIQSQESDLKSQ----EDDLNRAKSELNRLQQEETQLEQSIQAGRAQ------- 523
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRedaDDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERfgdapvd 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568955195 524 ---LETILRSLKCTQDDINQA----RSKLSQLQESHLEAHRSLE 560
Cdd:PRK02224 407 lgnAEDFLEELREERDELREReaelEATLRTARERVEEAEALLE 450
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
390-555 |
2.30e-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: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 390 EIAQLQREKYSLEQDIREKEEAIRQKTSevqELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 469
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELS---ELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 470 DETQTISSLKTQIQSQESDLKSQEDD---LNRAKSELNRLQQEETQLEQsIQAGRAQLETILRSLKCTQDDINQARSKLS 546
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 568955195 547 QLQESHLEA 555
Cdd:pfam05557 239 REEKYREEA 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-552 |
2.41e-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: 64.69 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 406 REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQ 485
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 486 ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH 552
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-582 |
4.52e-10 |
|
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: 63.50 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdml 461
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIqagrAQLETILRSLKCTQDDINQa 541
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD----SVKELIIKNLDNTRESLET- 468
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955195 542 rsKLSQLQESHLEAHRSLEQYDQDDPFKNKALL-FSNNSQEL 582
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQKQKELKSKEKELKkLNEEKKEL 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-561 |
5.31e-10 |
|
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: 63.12 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKTSEVQE-------LQNDLDRETSSLQELEAQKQDAQDRLDEMD 451
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISElkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ---SQESDLKSQ--EDDLNRAKSEL----NRLQQEETQLEQSIQagra 522
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELknqeKKLEEIQNQISQNNK---- 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 568955195 523 qletILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR04523 336 ----IISQLN---EQISQLKKELTNSESENSEKQRELEE 367
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
385-561 |
5.78e-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: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKT------SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 456 KLRDMLSDVRQkcqdeTQTISSLKTQIQSQESDLKSQED-------DLNRAKSELN----RLQQEETQLEQSIQAGRAQL 524
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAalraQLQQEAQRILASLEAELEAL 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 568955195 525 ETILRSLkctQDDINQARSKLSQLQESHLEAhRSLEQ 561
Cdd:COG3206 326 QAREASL---QAQLAQLEARLAELPELEAEL-RRLER 358
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-568 |
6.78e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIR--QKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAK 456
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 457 LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQsiQAGRAQLETILRSLkct 534
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAA--ALGDAVERELRENL--- 771
|
170 180 190
....*....|....*....|....*....|....
gi 568955195 535 QDDINQARSKLSQLqESHLEahRSLEQYDQDDPF 568
Cdd:COG4913 772 EERIDALRARLNRA-EEELE--RAMRAFNREWPA 802
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
382-565 |
9.71e-10 |
|
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: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKeeairqktsEVQELQNDLDRETSSLQELEAqkQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDK---------EIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 ---SDVRQKCQDETQTISSLKTQIQSQESDLKS-----------QEDDLNRAKS---ELNRLQQEETQLEQSIQAG---- 520
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEelervqqsytlNENELERVRGlekQLEELEKRYDEIVERLEEKevay 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955195 521 ---RAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:pfam06160 360 selQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLE 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-550 |
9.95e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQdaqdRLDEMdQQKAKLRDM 460
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVK----ELKEL-KEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIqagrAQLETILRSLkctqddiNQ 540
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL----EELEERHELY-------EE 366
|
170
....*....|
gi 568955195 541 ARSKLSQLQE 550
Cdd:PRK03918 367 AKAKKEELER 376
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
382-567 |
1.04e-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: 59.62 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 AKLRDMLSDVRQKCQDETQT-ISSLKTQIQSQESDLKSQEDDL--NRAKSELNRLQQEETQLEQsiqagrAQLETILRSL 531
Cdd:pfam12795 130 QQIRNRLNGPAPPGEPLSEAqRWALQAELAALKAQIDMLEQELlsNNNRQDLLKARRDLLTLRI------QRLEQQLQAL 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 568955195 532 kctQDDINQARSKLSQLQESHLEahRSLEQYDQDDP 567
Cdd:pfam12795 204 ---QELLNEKRLQEAEQAVAQTE--QLAEEAAGDHP 234
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
376-458 |
1.05e-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: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 376 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 455
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 568955195 456 KLR 458
Cdd:COG1579 160 ELE 162
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
438-531 |
1.32e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 517
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|....
gi 568955195 518 QAGRAQLETILRSL 531
Cdd:COG4942 100 EAQKEELAELLRAL 113
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
383-561 |
2.71e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.62 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKTSEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 450
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 ---DQQKAKLRDMLSDVRQKCQ-----------------DETQTISSLKTQIQSQESDLKSQEDDLNRAK---SEL-NRL 506
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKEQNKelkeeidrvkqsytlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaySELqEEL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 507 QQEETQLEQsIQAGRAQLETILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:PRK04778 386 EEILKQLEE-IEKEQEKLSEMLQGLR---KDELEAREKLERYRNKLHEIKRYLEK 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-566 |
3.39e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 396 REKYSLEQDIREKEEAIRQktsEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDmLSDVRQKCQDetqtI 475
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEEL-------AEAEERLEALEAELDALQERREALQR-LAEYSWDEID----V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 476 SSLKTQIQSQESDLksqeDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:COG4913 664 ASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170
....*....|.
gi 568955195 556 HRSLEQYDQDD 566
Cdd:COG4913 740 EDLARLELRAL 750
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-551 |
1.39e-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: 58.49 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNR---------LQQEETQLEQ---SIQAGRA 522
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQtqkSLKKKQE 585
|
170 180
....*....|....*....|....*....
gi 568955195 523 QLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
386-582 |
1.87e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 386 DISQEIAQLQREKYsLEQDIREKEEAIRQKTS----EVQELQNDLD---------RETSSLQELEAQKQDAQDRLDEMDQ 452
Cdd:COG3206 148 ELAAAVANALAEAY-LEQNLELRREEARKALEfleeQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 453 QKAKLRDMLSDVRQKcqdetqtISSLKTQIQSQESDLKSQEDD--LNRAKSELNRLQQEETQLEQ-------SIQAGRAQ 523
Cdd:COG3206 227 QLAEARAELAEAEAR-------LAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQ 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 524 LETILRSLKC-TQDDINQARSKLSQLQESHLEAHRSLEQYdqddpfKNKALLFSNNSQEL 582
Cdd:COG3206 300 IAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQL------EARLAELPELEAEL 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-555 |
1.92e-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: 58.53 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEI-AQLQR--------EKYsleqdiREKEEAIRQK-----TSEVQELQNDLDRETSSLQELEAQKQDAQDRLDE 449
Cdd:TIGR02168 191 LEDILNELeRQLKSlerqaekaERY------KELKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 450 MDQQKAKLRDmlsdvrqkcqdetqTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILR 529
Cdd:TIGR02168 265 LEEKLEELRL--------------EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180
....*....|....*....|....*.
gi 568955195 530 SLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESL 356
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
389-561 |
2.07e-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: 57.60 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDiREKEEAIRQKT---SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 465
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 466 QKCQDETQTISSLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEETQLEQSiQAGRAQLETILRSLKCT----------- 534
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSLSKEfqelrnslaqr 204
|
170 180 190
....*....|....*....|....*....|....
gi 568955195 535 -------QDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam07888 205 dtqvlqlQDTITTLTQKLTTAHRKEAENEALLEE 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
382-564 |
3.23e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQR--EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----------- 448
Cdd:COG3206 182 EQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellq 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 449 -----EMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDD-LNRAKSELNRLQQEEtqleQSIQAGRA 522
Cdd:COG3206 262 spviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQARE----ASLQAQLA 337
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955195 523 QLETILRSLkctqddiNQARSKLSQLQEShLEAHRslEQYDQ 564
Cdd:COG3206 338 QLEARLAEL-------PELEAELRRLERE-VEVAR--ELYES 369
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
392-552 |
3.55e-08 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 56.63 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 392 AQLQrekySLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 471
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 472 TQTISSLKTQIQSQESDLKSQEDDLNRaKSELNRLQ----QEETQLEQSIQA-----GRAQLETIlRSLKCTQDDINQAR 542
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETI-AELKQTREELAAQK 186
|
170
....*....|
gi 568955195 543 SKLSQLQESH 552
Cdd:PRK11637 187 AELEEKQSQQ 196
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
382-550 |
4.07e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.08 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLE---QDIREK-EEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ-Q 453
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRlaaEDFRQKyEDELNLRTSaenDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQ----------KCQDETQTISSLKTQ---------------IQSQESDLKSQ----EDDLNRAKSELN 504
Cdd:pfam00038 141 EEEVRELQAQVSDtqvnvemdaaRKLDLTSALAEIRAQyeeiaaknreeaeewYQSKLEELQQAaarnGDALRSAKEEIT 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568955195 505 ----RLQQEETQLeQSIQAGRAQLETILRSLKCTQD-DINQARSKLSQLQE 550
Cdd:pfam00038 221 elrrTIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISELEA 270
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
385-558 |
4.36e-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: 56.83 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 464
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 465 RQKCQDetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSK 544
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
170
....*....|....
gi 568955195 545 LSQLQESHLEAHRS 558
Cdd:pfam07888 264 AAQRDRTQAELHQA 277
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
369-535 |
6.54e-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: 55.15 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 369 SSSTLASGEFTGVKELddisqEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE--------LEAQK 440
Cdd:pfam09787 32 EGSGVEGLDSSTALTL-----ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 441 QDAQDRLDEMDQQKAKLRDMLSDVRQ-------KCQDETQTISSLKTQIQSQeSDLKSQEDDL-NRAKSELNRLQQEETQ 512
Cdd:pfam09787 107 SARREAEAELERLQEELRYLEEELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELeNRLHQLTETLIQKQTM 185
|
170 180
....*....|....*....|....*..
gi 568955195 513 LEqSIQAGRA----QLETILRSLKCTQ 535
Cdd:pfam09787 186 LE-ALSTEKNslvlQLERMEQQIKELQ 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-564 |
6.67e-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: 56.61 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLEQDIREKEEAIR----QKTSEVQELQN------DLDRETSSLQ----ELEAQKQDAQDRLDE 449
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENlngkkeELEEELEELEaalrDLESRLGDLKKERDE 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 450 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSE------LNRLQQEETQLEQSIQAgraq 523
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA---- 969
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955195 524 LETIlrSLKCTQD-DINQARskLSQLQESH--LEAHRS-----LEQYDQ 564
Cdd:TIGR02169 970 LEPV--NMLAIQEyEEVLKR--LDELKEKRakLEEERKailerIEEYEK 1014
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
389-523 |
6.79e-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: 51.87 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDIREKEEAIrqktsevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 468
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 469 QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSelnRLQQEETQLEQSIQAGRAQ 523
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
385-583 |
8.71e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 464
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 465 RQKCQDETQTISSLKTQIQSQESDLKSqeddLNRAKSELNRL---QQ-------EETQLEQSIQAGRAQLETILRSLKcT 534
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERLewrQQtevlspeEEKELVEKIKELEKELEKAKKALE-K 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955195 535 QDDINQARSKLSQLQESHLEAHRSLEQYdqddpfknkallfSNNSQELH 583
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKEL-------------AEEAQELH 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-532 |
1.05e-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: 55.84 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENLNGKKEELEEE 869
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955195 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-547 |
1.08e-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: 56.11 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 DVRQKCQdetqtisslktQIQSQESDLKSQEDDLNRAKSELNRLQ-QEETQLE--QSIQAGRAQLETILRSLKCTQDDIN 539
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLReQSGEALAdsQEVTAAMQQLLEREREATVERDELA 650
|
....*...
gi 568955195 540 QARSKLSQ 547
Cdd:COG3096 651 ARKQALES 658
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-571 |
1.13e-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: 55.80 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQE----IAQLQREKYSLEQD---IREKEEAIRQKTSEVQEL----QNDLDRETSS-LQELEAQKQDAQDRLDE 449
Cdd:TIGR04523 253 TQLNQLKDEqnkiKKQLSEKQKELEQNnkkIKELEKQLNQLKSEISDLnnqkEQDWNKELKSeLKNQEKKLEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 450 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGR---AQLET 526
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEklnQQKDE 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568955195 527 ILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEqyDQDDPFKNK 571
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT--NQDSVKELI 455
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-565 |
1.20e-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: 55.95 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 458
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 459 DMLSDVRQKCQDETQTISSlKTQIQSQESDLKSQEDDLNRAKSE----LNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190
....*....|....*....|....*....|.
gi 568955195 535 QDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQE 862
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-557 |
1.84e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 461
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETqleqsiQAGRAQLEtilrslkctqdDINQA 541
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET------ADLDADLE-----------SLPEY 817
|
170
....*....|....*.
gi 568955195 542 RSKLSQLQESHLEAHR 557
Cdd:COG4913 818 LALLDRLEEDGLPEYE 833
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
368-558 |
2.09e-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: 54.83 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 368 DSSSTLAsGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE---AQKQ-- 441
Cdd:pfam10174 373 EEKSTLA-GEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEri 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 442 ----------DAQDRLDEMDQQKAKLRDM---LSDVRQKCQDETQTISSLKTQIQSQESD-------LKSQEDDLNRAKS 501
Cdd:pfam10174 452 ierlkeqrerEDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 502 ELNRLQ--------QEET------------QLEQSIQ-----AGRAQ--LETILRSLKCTQDDINQARSKLSQLQESHLE 554
Cdd:pfam10174 532 ECSKLEnqlkkahnAEEAvrtnpeindrirLLEQEVArykeeSGKAQaeVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
....
gi 568955195 555 AHRS 558
Cdd:pfam10174 612 QMKE 615
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
392-551 |
2.34e-07 |
|
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: 54.75 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 392 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 446
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS 516
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 568955195 517 IQagraQLETILRSLKCTQDDINQARSKLsQLQES 551
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEI-QSQEQ 184
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
382-550 |
2.49e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 456 KLRDMLSDVRQKC-----QDET--QTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 528
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180
....*....|....*....|..
gi 568955195 529 RSLKCTQDDINQARSKLSQLQE 550
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEE 391
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
382-583 |
2.75e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDI---REKEEAIRQKT----SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELkelAEKRDELNAQVkelrEEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 AKLRDMlsdvRQKCQDETQTISSLKTQIQS-----QESDL-KSQEDDL----NRAKSELNRLQQEETQLEQsIQagraQL 524
Cdd:COG1340 95 DELRKE----LAELNKAGGSIDKLRKEIERlewrqQTEVLsPEEEKELvekiKELEKELEKAKKALEKNEK-LK----EL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955195 525 ETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL-----EQYDQDDPFKNKALLFSNNSQELH 583
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELykeadELRKEADELHKEIVEAQEKADELH 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
382-530 |
3.13e-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: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEA----------IRQKTSEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMD 451
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdelkdYREKLEKLKREINELKRELDRLQEE---LQRLSEELADLN 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 530
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
399-508 |
3.75e-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: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 399 YSLEQDIR---------EKEEAIRQKTSEVQELQnDLDRETSSL----QELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 465
Cdd:COG2433 376 LSIEEALEeliekelpeEEPEAEREKEHEERELT-EEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568955195 466 QKCQDETQT---ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ 508
Cdd:COG2433 455 SEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
381-548 |
5.97e-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: 53.49 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 451
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSiqagraqLETILRSL 531
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170
....*....|....*..
gi 568955195 532 KCTQDDINQARSKLSQL 548
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEI 664
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
377-581 |
7.44e-07 |
|
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: 53.04 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 377 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 452
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 453 QKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQEsdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRAQLETILRSLk 532
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRAKL- 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 533 ctQDDINQARSKLSQLQES-------HLEAHRSLEQYDQDDPFKNKALLFSNNSQE 581
Cdd:COG5185 509 --ERQLEGVRSKLDQVAESlkdfmraRGYAHILALENLIPASELIQASNAKTDGQA 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-532 |
8.36e-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: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 443 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRA 522
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|
gi 568955195 523 QLETILRSLK 532
Cdd:COG4942 98 ELEAQKEELA 107
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
383-564 |
9.51e-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: 50.52 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 DVRQKCQD------ETQTISSLKTQIQSQESDLKSQE--DDLNRAKSELNRLQQEETQLEQsIQAGRAQLETILRSL--K 532
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHKELEEELEA-HEPRLKSLNELAEELleE 175
|
170 180 190
....*....|....*....|....*....|..
gi 568955195 533 CTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:cd00176 176 GHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-550 |
9.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 394 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 458
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 459 ---------DMLSDVRQKC------QDETQTISSLKTQIQSQESDLKSQEDDLNRA--KSELNRLQQEETQLEQ---SIQ 518
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEeleELR 452
|
170 180 190
....*....|....*....|....*....|..
gi 568955195 519 AGRAQLETILRSLKcTQDDINQARSKLSQLQE 550
Cdd:COG4717 453 EELAELEAELEQLE-EDGELAELLQELEELKA 483
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
382-514 |
1.03e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 452
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955195 453 QKAKLRDMlsdvRQKCQDETQTISSLkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 514
Cdd:PRK12704 129 KEEELEEL----IEEQLQELERISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-580 |
1.04e-06 |
|
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: 52.74 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM----------- 450
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimerfqmelk 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 ------DQQKAKLRDM-----LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:TIGR00606 803 dverkiAQQAAKLQGSdldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955195 520 GRA---QLETILRSLKCTQDDINQARSKLSqlqeshleahrSLEQYDQDDPFKNKALLFSNNSQ 580
Cdd:TIGR00606 883 RQQfeeQLVELSTEVQSLIREIKDAKEQDS-----------PLETFLEKDQQEKEELISSKETS 935
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
381-565 |
1.05e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDdisQEIAQLQREKYSLEQDIREKEEAI---RQKTSE-VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:PHA02562 176 IRELN---QQIQTLDMKIDHIQQQIKTYNKNIeeqRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 457 LRDMLSDVRQK-----------------------CQDETQTISS---LKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 510
Cdd:PHA02562 253 PSAALNKLNTAaakikskieqfqkvikmyekggvCPTCTQQISEgpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 511 TQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
382-564 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQeIAQLQREKysleQDIREKEEAIRQKTSEVQ----ELQNDLDR-------------------ET------SS 432
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 433 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI------------------QSQESDLKSQED 494
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 495 DLNR-----------AKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYD 563
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
.
gi 568955195 564 Q 564
Cdd:TIGR02169 392 E 392
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
414-582 |
1.33e-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: 50.38 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 414 QKTSEVQELQNDLdretSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQTISSLKTQIQ 483
Cdd:pfam12795 14 AKKKLLQDLQQAL----SLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLEELEQRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 484 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI---LRSLKCTQDDINQARSKLSQLQESHLEAhrSLE 560
Cdd:pfam12795 89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrnrLNGPAPPGEPLSEAQRWALQAELAALKA--QID 166
|
170 180
....*....|....*....|..
gi 568955195 561 QYDQddpfknkALLFSNNSQEL 582
Cdd:pfam12795 167 MLEQ-------ELLSNNNRQDL 181
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
403-585 |
1.45e-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: 52.10 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 403 QDIREKEEAIRQktsEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 482
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 483 QSQESDLKSQEDDLN-----RAKSELNR------LQQEETQLEQSI------QAGRAQLETILRSLKCTQDDinQARSKL 545
Cdd:pfam01576 267 RELEAQISELQEDLEseraaRNKAEKQRrdlgeeLEALKTELEDTLdttaaqQELRSKREQEVTELKKALEE--ETRSHE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955195 546 SQLQE---SHLEAHRSL-EQYDQDDPF-----KNKALLFSNNsQELHPD 585
Cdd:pfam01576 345 AQLQEmrqKHTQALEELtEQLEQAKRNkanleKAKQALESEN-AELQAE 392
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
438-573 |
1.53e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcqdetqtisslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 517
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQA-----------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 518 QAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQDDPFKNKAL 573
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
389-542 |
1.60e-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: 52.26 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 449
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 450 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL------------NRAKSELNRLQQE-------E 510
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190
....*....|....*....|....*....|..
gi 568955195 511 TQLEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-560 |
1.61e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 461 LSDVRQKCQDEtqtissLKTQIQSQES------DLKSQEDDLnraKSELNRLQQEETQLEQSiqagRAQLETILRSLKCT 534
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPfyneylELKDAEKEL---EREEKELKKLEEELDKA----FEELAETEKRLEEL 645
|
170 180 190
....*....|....*....|....*....|.
gi 568955195 535 QDDINQARSKLSQ-----LQESHLEAHRSLE 560
Cdd:PRK03918 646 RKELEELEKKYSEeeyeeLREEYLELSRELA 676
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-555 |
1.66e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAiRQKTSEVQELQNDLDRETssLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQ-------------------IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgra 522
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK--- 491
|
170 180 190
....*....|....*....|....*....|...
gi 568955195 523 qlETILRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:PRK03918 492 --ESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
383-557 |
1.87e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 51.23 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 446
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 ---LD-----------------EMDQQKAKLR---DMLSDVRQKcqdetqTISSLK---TQIQSQEsdlKSQEDDLNRAK 500
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQE------TIAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 501 SELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHR 557
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
382-545 |
1.93e-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: 51.57 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 444
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 445 DRLDEMDQQKAK-----------LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE--- 510
Cdd:pfam05667 415 QRLVELAGQWEKhrvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568955195 511 --TQ--LE--QSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-553 |
2.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQRekysLEQDIREKEEAIRQKTSEvQELQNDLDR-ETSSLQELEA---QKQDAQDRLDEMDQQKAK 456
Cdd:COG4717 336 PEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 457 LRDMLSDVRQkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE----ET-----QLEQSIQAGRAQLETI 527
Cdd:COG4717 411 LEELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAEleqlEEdgelaELLQELEELKAELREL 488
|
170 180
....*....|....*....|....*....
gi 568955195 528 LR---SLKCTQDDINQARSKLSQLQESHL 553
Cdd:COG4717 489 AEewaALKLALELLEEAREEYREERLPPV 517
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
395-515 |
2.07e-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: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 395 QREKYSLEQDIREKEEAIRQKtsevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQT 474
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568955195 475 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQ 515
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-582 |
2.30e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKT--SEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 459
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 460 MLSDVrQKCQDETQTISSLKTQIQSQESDLK-----------SQEDDLNRAKSELNRLQQEETQLEQSiqagRAQLETIL 528
Cdd:PRK03918 544 LKKEL-EKLEELKKKLAELEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDA----EKELEREE 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 529 RSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ----YDQDDpFKNKALLFSNNSQEL 582
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEElekkYSEEE-YEELREEYLELSREL 675
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
380-540 |
2.31e-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: 51.01 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 380 GVKEL-----DDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKTSEV 419
Cdd:pfam03148 130 GIQELlqrtlEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 420 -----QELQN--DLdRET--SSLQ----ELEAQKQDA----QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 482
Cdd:pfam03148 210 ieraeKERAAsaQL-RELidSILEqtanDLRAQADAVnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAI 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 483 QSQESDLK-SQ---EDDLNRAKSEL------NRLQQEETQLEQSIQAGRAQL---ETILRSLKCTQDDINQ 540
Cdd:pfam03148 289 RDKEAPLKlAQtrlENRTYRPNVELcrdeaqYGLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
382-550 |
2.43e-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: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKTSEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170
....*....|....*.
gi 568955195 535 QDDINQARSKLSQLQE 550
Cdd:pfam01576 179 SKLKNKHEAMISDLEE 194
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
385-578 |
2.48e-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: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 453
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQK--CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLET----- 526
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLadpsy 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 527 ---ILRSLKCTQDDINQARSKLSQlQESHLE---AHRSLEQydQDDPFKNKALLFSNN 578
Cdd:pfam05557 439 skeEVDSLRRKLETLELERQRLRE-QKNELEmelERRCLQG--DYDPKKTKVLHLSMN 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
400-565 |
2.59e-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: 51.61 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 400 SLEQDIREKEEAI--------------RQKTSEVQELQNDLdretsslQELEAQKQDAQDRLDE----MDQQKAKLRD-- 459
Cdd:TIGR02169 643 TLEGELFEKSGAMtggsraprggilfsRSEPAELQRLRERL-------EGLKRELSSLQSELRRienrLDELSQELSDas 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 460 -MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLkcTQDDI 538
Cdd:TIGR02169 716 rKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRI 793
|
170 180
....*....|....*....|....*..
gi 568955195 539 NQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQK 820
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
363-529 |
2.89e-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: 50.84 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 363 GTPIPDSSSTLAsgeftgvKEL--DDISQEIAQLQREKYSLeqdiREK-EEAIRQKTSEVQELqndLDRETSSLQELEAQ 439
Cdd:pfam05622 261 LSPSSDPGDNLA-------AEImpAEIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 440 KQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDEtqtiSSLKtqiqsqeSDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:pfam05622 327 NRLANQRILELQQQVEELQKALQEQGSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDS 395
|
170
....*....|....
gi 568955195 520 GRAQ----LETILR 529
Cdd:pfam05622 396 NLAQkideLQEALR 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
466-579 |
2.95e-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: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 466 QKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110
....*....|....*....|....*....|....
gi 568955195 546 SQLQESHLEAHRSLEQYDQDDPFKnkaLLFSNNS 579
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLA---LLLSPED 130
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
381-509 |
3.43e-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: 50.02 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREkeeaIRQKTSEVQEL-QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 459
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQ----LKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568955195 460 MLSDVRQKCQDetqtissLKTQIQSQESDLKS----QEDDLNRAKSELNRLQQE 509
Cdd:smart00787 240 KIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
433-583 |
3.66e-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: 50.02 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 433 LQELEAQKQDAQDRLDEMDQQKAKLRD---MLSDVRQKCQDETQTISSLKTQIQSQESDLKS-QEDDLNRAKSELNRLQQ 508
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKeleLLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 509 EETQLEQSIqagrAQLETILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQYDQDDPFK-NKALLFSNNSQELH 583
Cdd:smart00787 219 EIMIKVKKL----EELEEELQELE---SKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEiEKLKEQLKLLQSLT 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
377-549 |
4.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 377 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKTSEVQELQNDLDRET-SSLQELEAQKQ---------- 441
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneyl 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 442 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESdlKSQEDDLNRAKSELNRLQQEETQLEQSIQ 518
Cdd:PRK03918 606 elkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|....
gi 568955195 519 AGRAQLETI---LRSLKCTQDDINQARSKLSQLQ 549
Cdd:PRK03918 684 ELEKRREEIkktLEKLKEELEEREKAKKELEKLE 717
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-497 |
4.40e-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: 50.40 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110
....*....|....*....|....*....|....*....
gi 568955195 462 SDVRQKCQ---DETQTISSLKTQIQSQESDLKSQEDDLN 497
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDII 679
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
289-362 |
4.88e-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: 4.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 289 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 362
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
391-542 |
5.16e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 391 IAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 451
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLN------------RAKSELNRLQQE-------ETQ 512
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgaeeRARARRDELHARlsanrsrRNQ 1078
|
170 180 190
....*....|....*....|....*....|
gi 568955195 513 LEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
402-526 |
5.46e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 49.46 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 402 EQDIREKEEAIRQKTSEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDET 472
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPNSPQVRQLR 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 473 QTISSLKTQIQSQESDL--KSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLET 526
Cdd:COG3524 256 RRIAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
409-564 |
5.69e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 409 EEAIRqktsEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQTISSLKTQI 482
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 483 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRAQLETILRslkctqdDINQARSKLSQLQeshleahRSLEQ 561
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER-------EIERLERELEERE-------RRRAR 363
|
...
gi 568955195 562 YDQ 564
Cdd:COG4913 364 LEA 366
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
400-550 |
7.63e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 400 SLEQDIREKEEAIRQktsEVQELQNDLDRETSSL-------QELEAQKQDAQDRLDEMdQQKAKL----------RDMLS 462
Cdd:COG1842 16 ALLDKAEDPEKMLDQ---AIRDMEEDLVEARQALaqvianqKRLERQLEELEAEAEKW-EEKARLalekgredlaREALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 463 DVrqkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQlETILRSLkcTQDDINQAR 542
Cdd:COG1842 92 RK----AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEAL--SGIDSDDAT 164
|
....*...
gi 568955195 543 SKLSQLQE 550
Cdd:COG1842 165 SALERMEE 172
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
382-547 |
7.92e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 451
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQKAKLRDMLSDVRqkcQDETQTISSLKTQIQSqESDLKSQEDDLNRAK-------SELNRLQQEETQLEQsiqagrAQL 524
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRKSlegntqlQDLLQKQRDYLTARI------QRL 239
|
170 180
....*....|....*....|...
gi 568955195 525 ETILRSLkctQDDINQARSKLSQ 547
Cdd:PRK11281 240 EHQLQLL---QEAINSKRLTLSE 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
451-531 |
8.18e-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: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 530
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 568955195 531 L 531
Cdd:COG3883 95 L 95
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
385-547 |
8.24e-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: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE----------LEAQKQDAQDRlDEMDQqk 454
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNrwrekvfalmVQLKAQDLEHR-DSVKQ-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 akLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam07111 336 --LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
170
....*....|...
gi 568955195 535 QDDINQARSKLSQ 547
Cdd:pfam07111 414 QIWLETTMTRVEQ 426
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
381-573 |
9.16e-06 |
|
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: 49.84 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 453
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 -------------KAKLRDM---LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSI 517
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 518 QAGRAQLETILRSLKCTQDDINQARSKLSQLQE--SHLEAHRSLEQYDQDDPFKNKAL 573
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMSklATLKEDANSEQAQGSIGERLAQL 895
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
382-550 |
1.00e-05 |
|
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: 47.37 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 461 LSDVRQKCQDETQTISSLKTQIQ---SQESDLKSQED--------DLNRAKSELNRLQQEETQLEQSIQAgRAQLETIL- 528
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNllkARLKAAKAQEAvqtslgslSTSSATDSFERIEEKIEEREARADA-AAELASAVd 191
|
170 180
....*....|....*....|....
gi 568955195 529 RSLKCTQDDINQARSK--LSQLQE 550
Cdd:pfam04012 192 LDAKLEQAGIQMEVSEdvLARLKA 215
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
416-552 |
1.11e-05 |
|
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: 48.48 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 416 TSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQtisslktqiqSQESDLKSQEDD 495
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 496 LNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR----SKLSQLQESH 552
Cdd:smart00787 220 IMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQL 280
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
425-551 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 425 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL-NRAKSE- 502
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALy 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 503 ---------------------------LNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
382-484 |
1.47e-05 |
|
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: 44.87 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKtseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKK---EQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|...
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQS 484
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLEE 105
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
382-581 |
1.54e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQT-----ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILrslkcTQD 536
Cdd:COG4372 167 AALEQELQALSEAeaeqaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL-----LDA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568955195 537 DINQARSKLSQLQESHLEAHRSLEQYDQDDPFKNKALLFSNNSQE 581
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
390-580 |
1.59e-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: 48.56 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 390 EIAQLQREKYSLEQDIREKE--EAIRQKTSEVQELQNDLDRETSSL----QELEAQKQD-------AQDRLDEMdQQKAK 456
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEdhEKIQHLEEEYKKEINDKEKQVSLLliqiTEKENKMKDltflleeSRDKANQL-EEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 457 LRDM-LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE-ETQLEQSIQAGRAQ----------- 523
Cdd:pfam05483 279 LQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEkEAQMEELNKAKAAHsfvvtefeatt 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 524 --LETILRS----LKCTQDDIN----QARSKLSQLQE-SHLEAHRSLEQYDQDDPFKNKALLFSNNSQ 580
Cdd:pfam05483 359 csLEELLRTeqqrLEKNEDQLKiitmELQKKSSELEEmTKFKNNKEVELEELKKILAEDEKLLDEKKQ 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
382-547 |
1.67e-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: 48.96 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQ-------LQREKYSLEQDIREKEEAIRQ-------KTSEVQELQ---NDLDRETSSL-----QELEAQ 439
Cdd:pfam15921 569 QQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEfkilkdkKDAKIRELEarvSDLELEKVKLvnagsERLRAV 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 440 KQDAQDR---LDEMDQQKAKLRDMLSD-------VRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 509
Cdd:pfam15921 649 KDIKQERdqlLNEVKTSRNELNSLSEDyevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955195 510 ETQLEQSIQAGRAQLETILRSLKCTQDDINQA----------RSKLSQ 547
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkekhflkeeKNKLSQ 776
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
384-554 |
1.70e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.64 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 456
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 457 LrDMLSDvRQKCQ----DETQTISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELNRLQQEETQLeQSIQ 518
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*..
gi 568955195 519 AGRAQLETILRSLKCTQDDINQARS-KLSQLQESHLE 554
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvALDNWRQVHEQ 725
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
381-572 |
1.78e-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: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 457
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 458 RDMLSDVRQKCQDETQTI--------------SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE----QSIQA 519
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNA 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 520 GRAQLETIlRSLKCTQD----DINQARSKLSQLQESHLEAHRSleqydqddpFKNKA 572
Cdd:pfam15921 641 GSERLRAV-KDIKQERDqllnEVKTSRNELNSLSEDYEVLKRN---------FRNKS 687
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
1.80e-05 |
|
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: 44.29 E-value: 1.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568955195 32 GRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLV 80
Cdd:pfam12763 24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-565 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLEQDIREKEeairqktSEVQELQNDL--------DRET------SSLQELEA-------QKQD 442
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALE-------SENAELQAELrtlqqakqDSEHkrkkleGQLQELQArlseserQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 443 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLksQEDdlNRAK----SELNRLQQEET----QLE 514
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL--QEE--TRQKlnlsTRLRQLEDERNslqeQLE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568955195 515 QSIQAGRA---QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:pfam01576 507 EEEEAKRNverQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
382-582 |
2.14e-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: 48.43 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslqELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----EAEDMLACEQHALLRKLQPEQDLQDVR 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLK------TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ----------LEQSIQAGRAQLE 525
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHalqltlTQERVREHALSIRVLPKELLASRQLALQKMQSEkeqltywkemLAQCQTLLRELET 711
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 526 TILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQDDPFKNKALLF--SNNSQEL 582
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEahFNNNEEV 770
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
400-550 |
2.26e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 400 SLEQDIREKEEAIRQK------TSEVQELQNDLDRETSSLQELEAQKQDAQDR-------LDEMDQQKAKLRDMLSDVRQ 466
Cdd:PRK10929 79 KLSAELRQQLNNERDEprsvppNMSTDALEQEILQVSSQLLEKSRQAQQEQDRareisdsLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 467 KCQDETQTISSLK----TQIQSQESDLKSQEDDLNRA------KSELNRLQQE-----ETQLEQSIQAGRAQLeTILRsl 531
Cdd:PRK10929 159 RLQTLGTPNTPLAqaqlTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQALRNQL-NSQR-- 235
|
170
....*....|....*....
gi 568955195 532 kctQDDINQARSKLSQLQE 550
Cdd:PRK10929 236 ---QREAERALESTELLAE 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
389-545 |
2.39e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 468
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 469 QdetqtisslktQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLE-QSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLREQsgEEFEDsQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-559 |
2.61e-05 |
|
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: 48.41 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQ-------LQREKYSLEQDIREK---------EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQ----- 441
Cdd:COG3096 793 ERDELAEQYAKasfdvqkLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeq 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 442 -----------------DAQDRLDEMDQQKAKLRDMLSDVRQKCqdetQTISSLKTQIQSQESDLKSQED---DLNRAKS 501
Cdd:COG3096 873 lqllnkllpqanlladeTLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLVAVLQSDPEQFEQlqaDYLQAKE 948
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955195 502 ELNRLQQEETQLEQSIQ---------------AGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 559
Cdd:COG3096 949 QQRRLKQQIFALSEVVQrrphfsyedavgllgENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL 1021
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
382-562 |
2.66e-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: 48.18 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ----QEETQLEQsiqagRAQLETILRSLKCTQDD 537
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 568955195 538 IN---QARSKLSQLQESHLEAHRSLEQY 562
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
381-509 |
2.73e-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: 47.11 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 460
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568955195 461 lsdvrqkcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 509
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-565 |
2.76e-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: 48.12 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYS---------LEQDIREKEEAIRQKTSEVQELQ-----------------NDLDRETSSLQEL 436
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGsdldrtvqqVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktNELKSEKLQIGTN 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 437 EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQ----IQSQESDLKSQEDDLNRAKSELNRLQQEETQ 512
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568955195 513 LEQSIQAGRAqletilRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:TIGR00606 960 IENKIQDGKD------DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-550 |
2.83e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 361 ERGTPIPDSSStlasgeftgVKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKTSEVQELQNDLDRetsslqeLEAQK 440
Cdd:PRK02224 456 ECGQPVEGSPH---------VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 441 QDAQDRLDEMDQQKAKLRDMLSDVRQKCQDetqtissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAg 520
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES- 590
|
170 180 190
....*....|....*....|....*....|
gi 568955195 521 RAQLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREALAE 620
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
382-563 |
4.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqqkakLRDML 461
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE-------LREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKcqdetqtisslktqIQSQESDLKSQEDDLNRAKselnRLQQE------ETQLEQSIQAG--------RAQLETI 527
Cdd:PRK02224 422 DELRER--------------EAELEATLRTARERVEEAE----ALLEAgkcpecGQPVEGSPHVEtieedrerVEELEAE 483
|
170 180 190
....*....|....*....|....*....|....*.
gi 568955195 528 LRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYD 563
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE 519
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
386-513 |
4.39e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 386 DISQEIAQLQREKYSLE---------QDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQ-------HSLEKLDTAIDELEEIMDEFNEQSKK 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 457 LRDMLSDVRQkcqdETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 513
Cdd:PHA02562 339 LLELKNKIST----NKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-559 |
4.82e-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: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQ----------LETILRSL 531
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRElddrnmevqrLEALLKAM 438
|
170 180
....*....|....*....|....*....
gi 568955195 532 KC-TQDDINQARSKLSQLQEShLEAHRSL 559
Cdd:pfam15921 439 KSeCQGQMERQMAAIQGKNES-LEKVSSL 466
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
382-542 |
4.87e-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: 45.51 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNdlDRETSSLQELEAQK--QDAQDRLDEMDQQKAKLRD 459
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAE--ERRQRLEEALDLQQffRDADDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 460 MLSDvrqkcqDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE-----TQLEQSIQAGRAQLETILRSLKCT 534
Cdd:cd00176 132 EDLG------KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdadEEIEEKLEELNERWEELLELAEER 205
|
....*...
gi 568955195 535 QDDINQAR 542
Cdd:cd00176 206 QKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-564 |
4.89e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 408 KEEAIRQ--KTSE----VQELQNDLDRETSSLQ----------ELEAQKQDAQ-----DRLDEMDQQKAKLRDMLSDVRQ 466
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELERQLKSLErqaekaerykELKAELRELElallvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 467 KCQDETQTISslKTQIQSQESDLKSQEDDlnrakSELNRLQQE--ETQ-----LEQSIQAGRAQLETILRSLKCTQDDIN 539
Cdd:TIGR02168 254 ELEELTAELQ--ELEEKLEELRLEVSELE-----EEIEELQKElyALAneisrLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180
....*....|....*....|....*
gi 568955195 540 QARSKLSQLQEshlEAHRSLEQYDQ 564
Cdd:TIGR02168 327 ELESKLDELAE---ELAELEEKLEE 348
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
385-561 |
5.04e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKySLEQDirekEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 464
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 465 RQKcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL--NRLQQEETQLEQSIQAGRAQ-LETILRSLKCTQDDINQA 541
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAQAALYANSQRLQqIRNLLKGGKVGGKALRPS 192
|
170 180
....*....|....*....|
gi 568955195 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR 212
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
392-529 |
5.17e-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: 44.26 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 392 AQLQREKYslEQDIREKEEAIRQKTSEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 471
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955195 472 TQTIsslktQIQSQESDLKSQEDD----LNRAKselnRLQQEetqlEQSIQAGRAQLETILR 529
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
480-565 |
5.23e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 480 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 559
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
....*.
gi 568955195 560 EQYDQD 565
Cdd:COG4372 104 ESLQEE 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-560 |
5.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQdaqdRLDEMDQQKAKLRDML 461
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKS---------ELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180
....*....|....*....|....*...
gi 568955195 533 CTQDDINQARSKLSQLQESHLEAHRSLE 560
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLE 355
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
382-550 |
6.12e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYS---LEQDIREKEEaiRQKTSEV-QELQNDLDRETSSL-QELEAQKQ--DAQDRLDEMDQQK 454
Cdd:COG1340 92 EELDELRKELAELNKAGGSidkLRKEIERLEW--RQQTEVLsPEEEKELVEKIKELeKELEKAKKalEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSqesdLKSQEDDLNRaksELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRK---EADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
170
....*....|....*.
gi 568955195 535 QDDINQARSKLSQLQE 550
Cdd:COG1340 243 RKELKKLRKKQRALKR 258
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
469-573 |
6.53e-05 |
|
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: 46.26 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 469 QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL-RSLKCTQDDINQARSKLSQ 547
Cdd:TIGR04320 250 PNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALAN 329
|
90 100
....*....|....*....|....*.
gi 568955195 548 LQESHLEAHRSLEQYDQDDPFKNKAL 573
Cdd:TIGR04320 330 AEARLAKAKEALANLNADLAKKQAAL 355
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
382-572 |
7.44e-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: 46.71 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------TSEVQELQNDLDRETSSLQEL 436
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 437 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 510
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 511 TQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH--LEAHRS--LEQYDQDDPFKNKA 572
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIreLEAQISelQEDLESERAARNKA 290
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
432-564 |
7.66e-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: 43.54 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 432 SLQELEAQKQ--DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSlktQIQSQESDLKsqedDLNRAKSELNRLQQE 509
Cdd:pfam07321 9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRLYA---EIQGKLVLLK----ELEKVKQQVALLREN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 510 ETQLEQSIQAGRAQLEtilrslkctqddinQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:pfam07321 82 EADLEKQVAEARQQLE--------------AEREALRQARQALAEARRAVEKFAE 122
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
417-560 |
7.99e-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: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 417 SEVQELQNDLDRETSSlQELEAQKQDAQDRLDEMD------QQKA-KLRDMLSDVRQKCQDETQTISSLKTQIQSQ--ES 487
Cdd:cd22656 94 AEILELIDDLADATDD-EELEEAKKTIKALLDDLLkeakkyQDKAaKVVDKLTDFENQTEKDQTALETLEKALKDLltDE 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 488 DLKSQEDDLNRAKSELNRLQQEET-QLEQSIQAGRAQLETI---LRSLKCTQDDINQARSKLSQLQESHLEAHRSLE 560
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYAaKLKAKIDELKALIADDeakLAAALRLIADLTAADTDLDNLLALIGPAIPALE 249
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
382-550 |
8.12e-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: 45.57 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 461
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 sdvrqkcqdetQTISSLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*....
gi 568955195 542 RSKLSQLQE 550
Cdd:pfam15905 320 EQEHQKLQQ 328
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
382-551 |
8.14e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIR---------EKE-EAIRQKTSEVQELQNDLDRetsSLQELEAQKQ---------- 441
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDrvkqsytlnESElESVRQLEKQLESLEKQYDE---ITERIAEQEIayselqeele 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 442 DAQDRLDEMDQQKAKLRDMLSDVRqkcQDET---QTISSLKTQIQS-----QESDL----KSQEDDLNRAKSELNRLqqe 509
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLR---KDELearEKLERYRNKLHEikrylEKSNLpglpEDYLEMFFEVSDEIEAL--- 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955195 510 ETQLEQsiqaGRAQLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:PRK04778 461 AEELEE----KPINMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-554 |
8.23e-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: 46.65 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 373 LASGEFTGVK-ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndLDRETSSLQELEAQKQDAQDRLDEMD 451
Cdd:pfam15921 353 LANSELTEARtERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL---WDRDTGNSITIDHLRRELDDRNMEVQ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQKAKLRDMLSDVRQKCQDETQTIS----SLKtQIQSQESDLKSQEDDLNRAKSELNrlqQEETQLEQS---IQAGRAQL 524
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQMAAIQgkneSLE-KVSSLTAQLESTKEMLRKVVEELT---AKKMTLESSertVSDLTASL 505
|
170 180 190
....*....|....*....|....*....|..
gi 568955195 525 ETILRSLKCTQDDINQARSKLS-QLQE-SHLE 554
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDlKLQElQHLK 537
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-560 |
8.64e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 361 ERGTPIPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK 440
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 441 QDAQDRLDEMDQ--------------QKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEdDLNRAKSELNRL 506
Cdd:PRK02224 436 RTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERL 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 507 QQEETQLEQSIQAGRAQLETilRSLKCTQ-----DDIN-QARSKLSQLQESHLEAHRSLE 560
Cdd:PRK02224 515 EERREDLEELIAERRETIEE--KRERAEElreraAELEaEAEEKREAAAEAEEEAEEARE 572
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
480-550 |
9.39e-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: 9.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 480 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-526 |
9.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREkysleqdIREKEEAIRQKTSEVQELQNDLDR----ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDmlsdv 464
Cdd:COG4913 338 DRLEQLERE-------IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEE----- 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955195 465 rqkcqdetqtissLKTQIQSQESDLKSQEDDLnraKSELNRLQQEETQLEQSIQAGRAQLET 526
Cdd:COG4913 406 -------------ALAEAEAALRDLRRELREL---EAEIASLERRKSNIPARLLALRDALAE 451
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
382-502 |
9.62e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKTSEVQELQNDLD-----------RETSSLQELEAQKQ-- 441
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 442 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDL------KSQEddLNRAKSE 502
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
430-565 |
1.04e-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: 45.49 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 430 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELN-- 504
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPig 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 505 -RLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQ--------ARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:pfam00529 137 gISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaenqaeVRSELSGAQLQIAEAEAELKLAKLD 206
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
389-561 |
1.04e-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: 46.32 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQRekySLEQDIREKEEAI---RQK-TSEVQELQNDLD---RETSSL----QELEAQKQDAQDRL-------DEM 450
Cdd:pfam01576 327 QEVTELKK---ALEEETRSHEAQLqemRQKhTQALEELTEQLEqakRNKANLekakQALESENAELQAELrtlqqakQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 530
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 568955195 531 -------LKCTQDDinqaRSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam01576 484 klnlstrLRQLEDE----RNSLQEQLEEEEEAKRNVER 517
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
388-555 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV-RQ 466
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALpSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 467 KCQDETQTISSLKTQIQSQesDLKSQ----EDDLNRAKSELNRLQqeetQLEQSIQagrAQLETILRSLKctqDDINQAR 542
Cdd:pfam06008 119 DLSRMLAEAQRMLGEIRSR--DFGTQlqnaEAELKAAQDLLSRIQ----TWFQSPQ---EENKALANALR---DSLAEYE 186
|
170
....*....|...
gi 568955195 543 SKLSQLQESHLEA 555
Cdd:pfam06008 187 AKLSDLRELLREA 199
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
392-525 |
1.16e-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: 42.57 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 392 AQLQREKysleQDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDVRQKC 468
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEEKEIEL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 469 QDETQTISSLKTQIQSqesdlksqeddlnrAKSELNRLQQeetQLEQSIQAGRAQLE 525
Cdd:pfam18595 74 RELERREERLQRQLEN--------------AQEKLERLRE---QAEEKREAAQARLE 113
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
383-564 |
1.41e-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: 45.73 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL----------------QELEAQKQDAQDR 446
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehalsirvlpKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 LDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNRLQ------------ 507
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassSLGSDLAAREDALNQSLKELMHQArtvlkarteahf 764
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 508 -------------QEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSklSQLQESHLEAHRSLEQYDQ 564
Cdd:TIGR00618 765 nnneevtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP--SDEDILNLQCETLVQEEEQ 832
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
401-549 |
1.45e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 401 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQTISSLKT 480
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 481 QIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQAGRAQLETILRSLkctqdDINQARSKLSQLQ 549
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQ-------IAALRRQLAALEAAL-----DASEKRDRESQAK 173
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-509 |
1.47e-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: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 370 SSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDR 446
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 447 LDEMdqqKAKLRDMLSDV------RQKCQDEtqtISSLKTQIQSQEsdlkSQEDDLNRAKselNRLQQE 509
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLealeegKKRLQRE---LEALTQQLEEKA----AAYDKLEKTK---NRLQQE 581
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
300-549 |
1.49e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 300 IFMHSGLTQNL-------LAHIWALADTRQTGKLSKEQFALAMYFIQ--QKVSKGIDPPQVLSPDmvPPSERGTPIPDSS 370
Cdd:COG5022 726 VFFKAGVLAALedmrdakLDNIATRIQRAIRGRYLRRRYLQALKRIKkiQVIQHGFRLRRLVDYE--LKWRLFIKLQPLL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 371 STLASGEFTG--VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK--QDAQDR 446
Cdd:COG5022 804 SLLGSRKEYRsyLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQrvELAERQ 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 LDEMDQQKAKL------------------RDMLSDVRQKCQDETQTISSLKTQIQsqESDLKSQEDDLNRAKSELNRLQQ 508
Cdd:COG5022 884 LQELKIDVKSIsslklvnleleseiielkKSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHE 961
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568955195 509 EETQLEQSIQagraQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:COG5022 962 VESKLKETSE----EYEDLLKKSTILVREGNKANSELKNFK 998
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
379-561 |
1.51e-04 |
|
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: 45.33 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 379 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 458
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 459 D------MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRA-KSELNRLQQEETQLEQSIQAGRAQLETILRSL 531
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190
....*....|....*....|....*....|....*
gi 568955195 532 KCTQDDINQAR-----SKLSQLQESHLEAHRSLEQ 561
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVRS 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
438-565 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVR----------------QKCQDETQT--ISSLKTQIQSQESDLKSQEDDLNRA 499
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGELErqleplerqaekaeryRELKEELKEleAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 500 KSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
401-509 |
1.67e-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: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 401 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLkt 480
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 568955195 481 qiqsqESDLKSQEDDLNRAKSELNRLQQE 509
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
384-566 |
1.67e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKTSEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 455
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 456 KLRDMLSDVRQKCQDEtqtisslKTQIQSQESDLKSQEDDLNrAKSELnRLQQEETQLEqsIQAGRAQLETILRSLKCTQ 535
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQAT-ATPEL-LLQLENFDER--IERAREEQEAANAEVERLQ 491
|
170 180 190
....*....|....*....|....*....|.
gi 568955195 536 DDINQARSKLSQLQESHLEAHRSLEQYDQDD 566
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSAL 522
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
339-536 |
1.76e-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: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 339 QQKVSKGIDPPQVLSPDMVPPSERgtpiPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLE---QDIREKEEAI--- 412
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSE----LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 413 -RQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR---DMLSDVRQKCqdeTQTISSLKTQIQSQESD 488
Cdd:pfam05483 445 lQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcDKLLLENKEL---TQEASDMTLELKKHQED 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955195 489 LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQD 536
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD 569
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
403-550 |
1.79e-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: 43.45 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 403 QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 482
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 483 QSQESDLKSQE-DDLNRakselnRLQQEETQLEQSIQAGRaqLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:cd16853 91 EYVQKNLTDEElADWKR------RQQIACIGGPPNICLDR--LENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
401-552 |
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 568955195 401 LEQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQ 473
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 474 TISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRAQLETILRSLKCTQDDINQARSK---LSQLQ 549
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKRELESEIKKLTHDIKLKEEQIRELEIKvqeLRKYK 559
|
...
gi 568955195 550 ESH 552
Cdd:pfam09726 560 ESE 562
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
383-512 |
2.01e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSL--EQDIREKEEAIRQKTsEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRdm 460
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkkEQDEASFERLAELRD-ELAELEEELE-------ALKARWEAEKELIEEIQELKEELE-- 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 461 lsdvrqkcqDETQTISSLKTQIQSQESDLKSQEDDLNRAKSE--------------LNRLQQEETQ 512
Cdd:COG0542 482 ---------QRYGKIPELEKELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGERE 538
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
380-475 |
2.08e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 42.19 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 380 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 458
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 568955195 459 DMLSDVRQKCQDETQTI 475
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
388-586 |
2.11e-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: 45.34 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 388 SQEIAQLQRekysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSDVRQK 467
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-KTTLTQKLQSLCKELDILQREQAT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 468 CQDETQTISSLKTQIQSQESDLKSQeddlnraKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQ-------QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568955195 548 LQESH-LEAHRSLEQYDQDDPFKnkallfsnnSQELHPDP 586
Cdd:TIGR00618 485 ETRKKaVVLARLLELQEEPCPLC---------GSCIHPNP 515
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
382-519 |
2.22e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQEL----QNDLDRET-SSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAlekgREDLAREAlERKAELEAQAEALEAQLAQLEEQVEK 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 457 LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE----DDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:COG1842 117 LKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA 183
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
444-550 |
2.31e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 444 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQ 523
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100
....*....|....*....|....*..
gi 568955195 524 LETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEA 158
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
384-505 |
2.35e-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: 43.06 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLeqdiREKEEAIRQKTsevQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 463
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568955195 464 VRqkCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNR 505
Cdd:pfam16043 81 VS--RDQFDETLEELNQMLQELLDKLEGQEDAWKKALETLSE 120
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
397-518 |
2.45e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 397 EKYSLEQDIREKEEAIRQKTSEVQELQNDldretsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTIS 476
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568955195 477 slktQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQ 518
Cdd:COG0542 472 ----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
432-550 |
2.46e-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: 43.44 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 432 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQTISSLKTQIQS--QESDLKSQEDDL 496
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 497 NRAKSEL-NRLQQEETQLeQSIQAGRAQLETILRSLkctQDDINQARSKLSQLQE 550
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQNQLAQLNSQLIEL---QTRPERAQQQLSEARQ 127
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
366-564 |
2.65e-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: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 366 IPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQD 445
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 446 RLDEMDQQKAKLRDMLSDVR--QKCQDETQTISSLKTQIQSqesdlKSQEDDLNRAKSELNRLQQEETQLEQSIQagrAQ 523
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDVTimERFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVV---SK 844
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568955195 524 LETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
393-559 |
2.98e-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: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 393 QLQREKYSLEQdIREKEEAIRQKtsEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLrDMLSDVRQKCQD 470
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 471 ETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ---EETQLEQSIQAGRAQLETILRslKCTQDDINQARSKLSQ 547
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKaiyEEERRREAEEERRKQQEMEER--RRIQEQMRKATEERSR 567
|
170
....*....|..
gi 568955195 548 LQEshLEAHRSL 559
Cdd:pfam17380 568 LEA--MEREREM 577
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
394-561 |
3.10e-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: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 394 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS---DVRQKCQD 470
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQateDAKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 471 ETQtisSLKTQIqsqESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIqAGRAQLETILRSLKCTQDDINQAR 542
Cdd:pfam01576 721 NMQ---ALKAQF---ERDLQARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGR 793
|
170 180
....*....|....*....|...
gi 568955195 543 S----KLSQLQESHLEAHRSLEQ 561
Cdd:pfam01576 794 EeavkQLKKLQAQMKDLQRELEE 816
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
395-574 |
3.40e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 395 QREKYSLEQDIREKEEAIRQktsevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 472
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 473 -QTISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELNRLQQEETQLEQSIQA--GRAQLETI 527
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 528 LR-------SLKCTQD-------------DINQARSKLSQLQE--SHLEAHrsleQYDQDDPFKNKALL 574
Cdd:PRK11281 342 LYqqqqalpSADLIEGladriadlrleqfEINQQRDALFQPDAyiDKLEAG----HKSEVTDEVRDALL 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
389-584 |
3.52e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDIrekeEAIRQKTSEVQELQnDLDRETSSLQE--LEAQKQDAQDRLDEMDQQKAKLrdmlsdvrq 466
Cdd:pfam12128 768 DVIAKLKREIRTLERKI----ERIAVRRQEVLRYF-DWYQETWLQRRprLATQLSNIERAISELQQQLARL--------- 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 467 kcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELN------------RLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam12128 834 --------IADTKLRRAKLEMERKASEKQQVRLSENLRglrcemsklatlKEDANSEQAQGSIGERLAQLEDLKLKRDYL 905
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568955195 535 QDDINQARSKLSQLQESHL--EAHRSLEQYDQDDPFKNKALLFSNNSQELHP 584
Cdd:pfam12128 906 SESVKKYVEHFKNVIADHSgsGLAETWESLREEDHYQNDKGIRLLDYRKLVP 957
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
379-549 |
3.54e-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: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 379 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKTS-------EVQELQNDLDRETSSLQELEAQKQDAQDR- 446
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI--QSQESDLKSQEDDLNRAKSELNRLQ--- 507
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQvlq 1051
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568955195 508 --QEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:TIGR00606 1052 mkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
385-516 |
3.63e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 459
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 460 MLSDVRQKCqdetqtiSSLKTQIQSQESDLKSQEddlNRAKSELNRLQQEETQLEQS 516
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA 1114
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
382-592 |
4.09e-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: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEV---QEL------------QNDLDRETSSLQELEAQKQDaqdR 446
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEKEES---K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 LDEMDQQKAKLRDMLsdvrQKCQDETQT---------------ISSLKTQIQsqesDLK-SQEDDLNraksELNRLQQEE 510
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEELNFlstykdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 511 TQ-LEQSIQAGRAQLETIL--RSLKCTQDDInQARSKLSQLQESHLEAHRSLEQYdqddpFKNKALLFSNNSQELHpdpF 587
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQESL-LQKTRDNQVMLKEIEQFREFIDE-----LEEEIPKLKAEVQQLQ---A 221
|
....*
gi 568955195 588 QAEDP 592
Cdd:pfam15397 222 QRQEP 226
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-506 |
4.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 467
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110
....*....|....*....|....*....|....*....
gi 568955195 468 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 506
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
384-557 |
4.68e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 450
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 DQQKAKLRDMLSDVRQKCqDETQT--------ISSL---KTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ---S 516
Cdd:PRK04863 389 EEEVDELKSQLADYQQAL-DVQQTraiqyqqaVQALeraKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsV 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568955195 517 IQAGRAQLETILRSLKCTQDDI------NQARSKLSQLQESHLEAHR 557
Cdd:PRK04863 468 AQAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAEQ 514
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
367-550 |
4.68e-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: 43.53 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 367 PDSSSTLASGEFTGVKELDDISQEIAQLQRekySLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDR 446
Cdd:pfam04108 156 LSSPSESISLIPTLLKELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 447 LDEMDQQKAKLRDMLS---DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAK-------SELNRLQQEETQLEQS 516
Cdd:pfam04108 230 LDEMENNYERLQKLLEqknSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKetiedylSELEDLREFYEGFPSA 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568955195 517 -----IQAGR-----AQLETILRSLkctqddinqaRSKLSQLQE 550
Cdd:pfam04108 310 ygsllLEVERrrewaEKMKKILRKL----------AEELDRLQE 343
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
390-513 |
4.80e-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: 41.66 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 461
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 513
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
433-581 |
5.27e-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: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 433 LQELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL---------------- 496
Cdd:pfam00261 3 MQQIKEELDEAEERLKE-------AMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLaealekleeaekaade 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 497 ---------NRAKSELNRLQQEETQLEQSIQ----AGRaQLETILRSLKCTQDDINQARSKLSQLQE--SHLEAH----- 556
Cdd:pfam00261 76 sergrkvleNRALKDEEKMEILEAQLKEAKEiaeeADR-KYEEVARKLVVVEGDLERAEERAELAESkiVELEEElkvvg 154
|
170 180 190
....*....|....*....|....*....|...
gi 568955195 557 ---RSLE-----QYDQDDPFKNKALLFSNNSQE 581
Cdd:pfam00261 155 nnlKSLEaseekASEREDKYEEQIRFLTEKLKE 187
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
372-564 |
5.50e-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: 42.78 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 372 TLASGEFTGvKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLD 448
Cdd:pfam06008 66 TLAKAQQVN-AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 449 EMDQQKAKLRDMLSDVR---QKCQDETQtisSLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQS---IQAGRA 522
Cdd:pfam06008 145 NAEAELKAAQDLLSRIQtwfQSPQEENK---ALANALRDSLAEYEAKLSDLR------ELLREAAAKTRDAnrlNLANQA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955195 523 QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:pfam06008 216 NLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLLLQEIDD 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-582 |
5.66e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAI-------RQKTSEvqELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 AKLRDMLSDVRqkcqdetqTISSLKT---QIQSQESDLKS--------QEDDLNRAKSELNRLQQEETQLEQSIQAGRAq 523
Cdd:PRK03918 483 RELEKVLKKES--------ELIKLKElaeQLKELEEKLKKynleelekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE- 553
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 524 LETILRSLKCTQDDINQARSKL-SQLQESHLEAHRSLEQYDQD-DPFKNKALLFSNNSQEL 582
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKElEPFYNEYLELKDAEKEL 614
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
401-550 |
5.87e-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: 42.40 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 401 LEQDIREKEEAIRQKTSEVQELQNDLDRetsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKT 480
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTK----------KQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNA 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955195 481 qIQSQESDLKSQEDDlnrAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT--QDDINQARSKLSQLQE 550
Cdd:cd21116 152 -LKNQLNSLAEQIDA---AIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAflQADLKAAKADWNQLYE 219
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
338-565 |
6.56e-04 |
|
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: 43.66 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 338 IQQKVSkgidppqVLSPDMVPPSERGTPIPDSSSTLASgefTGVKELDDISQ-EIA-----------QLQREK-YSLEQD 404
Cdd:pfam10174 480 LKEKVS-------ALQPELTEKESSLIDLKEHASSLAS---SGLKKDSKLKSlEIAveqkkeecsklENQLKKaHNAEEA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 405 IREKEE---AIRQKTSEVQ-------ELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQKCQDETQT 474
Cdd:pfam10174 550 VRTNPEindRIRLLEQEVArykeesgKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQMKEQNKK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 475 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEEtqleqsiqagraQLETILRSLKCTQDDINQARSKLSQLQESHLE 554
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL------------QLEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
250
....*....|.
gi 568955195 555 AHRSLEQYDQD 565
Cdd:pfam10174 688 KDGHLTNLRAE 698
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
383-520 |
6.77e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEMDQQKAKL 457
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKEAKKEADEI 589
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955195 458 rdmlsdVRQKCQDETQTISSLKTQiqsqesDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAG 520
Cdd:PRK00409 590 ------IKELRQLQKGGYASVKAH------ELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
164-335 |
6.80e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 40.55 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 164 LGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEpvpsilppplippskrkktvfagavpvlpaspppkdslrstpshg 243
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSE--------------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 244 svSSLNSTGSLSP---KHSVKQPPVAWVVPVADKMrFDEIflktDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADT 320
Cdd:COG5126 42 --ADTDGDGRISReefVAGMESLFEATVEPFARAA-FDLL----DTDGDGKISADEFRRLLTALGVSEEEADELFARLDT 114
|
170
....*....|....*
gi 568955195 321 RQTGKLSKEQFALAM 335
Cdd:COG5126 115 DGDGKISFEEFVAAV 129
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
388-515 |
6.81e-04 |
|
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: 42.67 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQD--------------RLDEMDQQ 453
Cdd:pfam14915 150 SQQLSKAESKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDkvnkyigkqesleeRLAQLQSE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 454 KAKLRDMLSDVRQK----------CQDETQTISSlKTQIQSQESDLKSQEddlnRAK---SELNRLQQEETQLEQ 515
Cdd:pfam14915 230 NMLLRQQLEDAQNKadakektvidIQDQFQDIVK-KLQAESEKQVLLLEE----RNKeliNECNHLKERLYQYEK 299
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
382-524 |
7.21e-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: 42.60 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAI-RQKTSEVQELQNDLdretsslqeleaQKQDAQDRLDEMDQQKAKLRdm 460
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEQIELKERRLaEEAEREEEEFERML------------RKQAEDEEIEQEEAEKRRMK-- 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955195 461 lsdvRQKCQDEtqtissLKTQIQSQEsdlKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQL 524
Cdd:pfam13868 288 ----RLEHRRE------LEKQIEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
392-554 |
8.04e-04 |
|
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: 42.87 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 392 AQLQREKYSLEQD-IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD 470
Cdd:pfam17097 121 ASLEDEVSQLEDDtLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECWELLNELERLRDQRITVEEQTSN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 471 ETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE--QSIQAGRAQL-ETILRSLKCTQDDINQARSK-LS 546
Cdd:pfam17097 201 EKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEkvDKSSINRTQNdEESIQNTVQLNLLIDMWKSKfII 280
|
....*...
gi 568955195 547 QLQESHLE 554
Cdd:pfam17097 281 HEKISNLE 288
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-583 |
8.05e-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: 43.50 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQktsevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 458
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGR-----LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 459 DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIQAGRaQLETILRS 530
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielkkeiLEKKQEELKFVIKELQ-QLEGSSDR 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 531 LKCTQDDINQARSKLSQLQESHLEAHRSLE----QYDQDDPFKNKALLFSNNSQELH 583
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKNSLTETLKKEvkslQNEKADLDRKLRKLDQEMEQLNH 529
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
382-561 |
8.44e-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: 42.60 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSeVQELQNDL-DRETSSLQELEAQKQDAQDRL---------DEMD 451
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIeEREQKRQEEYEEKLQEREQMDeiveriqeeDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 -QQKAKLRDMLSDVRQKCQDETQTISSLKtQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL---EQSIQAGRAQLETI 527
Cdd:pfam13868 118 aEEKLEKQRQLREEIDEFNEEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKA 196
|
170 180 190
....*....|....*....|....*....|....
gi 568955195 528 LRslkcTQDDINQARSKLsqLQESHLEAHRSLEQ 561
Cdd:pfam13868 197 QD----EKAERDELRAKL--YQEEQERKERQKER 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-519 |
8.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL 447
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 448 DEMDQ-----QKAK-LRDMLSDVRQKCQDEtqTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:PRK03918 355 EELEErhelyEEAKaKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-580 |
8.69e-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: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-----------DLDRETSSLQELEAQKQ--------- 441
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 442 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE---DDLNRAKSELNRLQQEETQLEQ 515
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 516 SiqagrAQLETILR---SLKCTQDDINQARSKLSQLQES---HLEAHRSLEQYDQDDPFKNKAlLFSNNSQ 580
Cdd:TIGR00606 493 N-----SLTETLKKevkSLQNEKADLDRKLRKLDQEMEQlnhHTTTRTQMEMLTKDKMDKDEQ-IRKIKSR 557
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
431-555 |
8.87e-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: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 431 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISslkTQIQSQESDLKSqeddLNRAKSELNRLQQEE 510
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 511 TQLEQSIQAGRAQLETILRSLKCT----QDDINQARSKLSQLQE------SHLEA 555
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNEqnkllhDQLES 128
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
382-524 |
9.13e-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: 42.60 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 450
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 ---DQQKAKLRD-MLSDVRQKCQDETQTISSLKTQIQSQEsdlKSQEDDLNRAKSELNRL---QQEETQLEQSIQAGRAQ 523
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQEEAEKRRM 286
|
.
gi 568955195 524 L 524
Cdd:pfam13868 287 K 287
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
379-560 |
9.50e-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: 43.24 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 379 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKTSEVQELQNDLDRETSS-------------- 432
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 433 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL-------NR 505
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLaaserarRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 506 LQQEETQLEQSIQAGRAQletilRSLkcTQDDINQARSKLSQLQESHLEAHRSLE 560
Cdd:pfam01576 859 AQQERDELADEIASGASG-----KSA--LQDEKRRLEARIAQLEEELEEEQSNTE 906
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-557 |
9.61e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 386 DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 460
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 461 LSDVRQkcqdETQTISSLKTQ---IQSQESDLKSQEDDLNRAKSELNRLQQEETQL--------------EQSIQAGRAQ 523
Cdd:PRK04863 910 KRFVQQ----HGNALAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALtevvqrrahfsyedAAEMLAKNSD 985
|
170 180 190
....*....|....*....|....*....|....*
gi 568955195 524 LETILRS-LKCTQDDINQARSKLSQLQESHLEAHR 557
Cdd:PRK04863 986 LNEKLRQrLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
382-532 |
1.05e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 42.14 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKTSEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 454
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 455 aKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDdLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLK 532
Cdd:COG5325 144 -FLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEE-LEYQQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
385-515 |
1.07e-03 |
|
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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQdirEKEEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 461
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 462 sdvrqkCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL-NRLQQEETQLEQ 515
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
392-549 |
1.13e-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: 42.85 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 392 AQLQREKYSLEQDIREKEEAirqkTSEVQELQNDLDRETSSLQE--------------LEAQKQDAQDRLDEMDQQK--- 454
Cdd:pfam01576 412 GQLQELQARLSESERQRAEL----AEKLSKLQSELESVSSLLNEaegkniklskdvssLESQLQDTQELLQEETRQKlnl 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 455 -AKLRDMLSD---VRQKCQDETQTISSLKTQIQS---QESDLKSQ-----------EDDLNRAKSELNRLQQ---EETQL 513
Cdd:pfam01576 488 sTRLRQLEDErnsLQEQLEEEEEAKRNVERQLSTlqaQLSDMKKKleedagtlealEEGKKRLQRELEALTQqleEKAAA 567
|
170 180 190
....*....|....*....|....*....|....*.
gi 568955195 514 EQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
384-528 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 463
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 464 vrqkcqdETQTISSLktqiqsqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 528
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
368-550 |
1.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 368 DSSSTLASGEfTGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL 447
Cdd:PRK02224 499 ERAEDLVEAE-DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 448 DEMDQQKA----------KLRDMLSDvRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL------NRL---QQ 508
Cdd:PRK02224 575 AELNSKLAelkeriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeARIeeaRE 653
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568955195 509 EETQLEQSIqagrAQLETILRSLKCTQDD----INQARSKLSQLQE 550
Cdd:PRK02224 654 DKERAEEYL----EQVEEKLDELREERDDlqaeIGAVENELEELEE 695
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
387-492 |
1.46e-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: 41.88 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 387 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 462
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 568955195 463 DVRQKCQDETQTISSLKTQIQSQESDLKSQ 492
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
383-530 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 458
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955195 459 dmlsdvrqkcqDETQTISslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRAQlETILRS 530
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSAS 175
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
382-513 |
1.53e-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: 40.86 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQrekysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 454
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQ--SQESDLKSQEDDLNRAKSELNRLQQEETQL 513
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
382-565 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQREKYSLE--QDIREKEEAIRQKTSEVqeLQNDLDRetsSLQELEAQ--------KQDAQDRLDEMD 451
Cdd:pfam07111 162 EALSSLTSKAEGLEKSLNSLEtkRAGEAKQLAEAQKEAEL--LRKQLSK---TQEELEAQvtlveslrKYVGEQVPPEVH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQ-----KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS-IQAGRAQLE 525
Cdd:pfam07111 237 SQtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSlLNRWREKVF 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568955195 526 TILRSLKCT----QDDINQARSKLSQLQE---SHLEAHRSLEQYDQD 565
Cdd:pfam07111 317 ALMVQLKAQdlehRDSVKQLRGQVAELQEqvtSQSQEQAILQRALQD 363
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
384-469 |
1.63e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.56 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKYSLEQDIRE----KEEAIRQKTSEVQELQNDLD-RETSSLQELEAQKqdaQDRLDEMDQQKAKLR 458
Cdd:smart00502 9 LTKLRKKAAELEDALKQLISIIQEveenAADVEAQIKAAFDELRNALNkRKKQLLEDLEEQK---ENKLKVLEQQLESLT 85
|
90
....*....|.
gi 568955195 459 DMLSDVRQKCQ 469
Cdd:smart00502 86 QKQEKLSHAIN 96
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
394-532 |
1.65e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.32 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 394 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdreTSSLQELEAQKQDAQDRLDEmdqqkaklrdmlsdVRQkcQDETQ 473
Cdd:PRK07352 48 LEERREAILQALKEAEERLRQAAQALAEAQQKL---AQAQQEAERIRADAKARAEA--------------IRA--EIEKQ 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 474 TISSLKTQIQSQESDLKSQEDdlnRAKSELNR------LQQEETQLEQSIQAGrAQLETILRSLK 532
Cdd:PRK07352 109 AIEDMARLKQTAAADLSAEQE---RVIAQLRReaaelaIAKAESQLPGRLDED-AQQRLIDRSIA 169
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
392-459 |
1.70e-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: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 392 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 459
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
408-556 |
1.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 408 KEEAIRQKTSEVQELQNDLDREtsslqeleaqkqdAQDRLDEMDQQKAKLRdmlsdvrQKcqdetqtisslKTQIQSQES 487
Cdd:PRK12704 55 KKEALLEAKEEIHKLRNEFEKE-------------LRERRNELQKLEKRLL-------QK-----------EENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 488 DLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSL-KCTQDD-----INQARSKL-----SQLQESHLEAH 556
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEEakeilLEKVEEEArheaaVLIKEIEEEAK 183
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
387-559 |
1.81e-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: 41.60 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 387 ISQEIAQLQREKYSLEQDIREKEEAIRQktsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 463
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVLNELKKDFKQ---LLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 464 --VRQKCQdetQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ-------------QEETQLEQSIQA--------- 519
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMASllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955195 520 ------------GRA-----------QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 559
Cdd:pfam04108 192 dqcvtavkltegGRAemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
438-565 |
1.82e-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: 41.06 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 517
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568955195 518 QAGRAQletilRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQD 565
Cdd:COG1579 83 GNVRNN-----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEE 125
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
381-571 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDD---ISQEIAQLQREKYSLEQDIREKEEAIRQKTSE-VQELQNDLDRET-------SSLQELE----AQKQDAQD 445
Cdd:pfam10174 76 IQALQDelrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAkelfllrKTLEEMElrieTQKQTLGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 446 RldemDQQKAKLRDML------SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL---NRLQQEETQ---L 513
Cdd:pfam10174 156 R----DESIKKLLEMLqskglpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaL 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 514 EQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQDDPF-KNK 571
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFmKNK 290
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
403-518 |
1.95e-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: 41.38 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 403 QDIREKEEAIRQKTSEVQELQND-----LDR---ETSS-LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV--------- 464
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADavnfaLRKrieETEDaKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKeaplklaqt 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955195 465 ----RQK------CQDETQtiSSLK---TQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQ 518
Cdd:pfam03148 301 rlenRTYrpnvelCRDEAQ--YGLVdevKELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
454-562 |
2.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQKCQD---ETQTISSLK-TQIQSQESDLKSQ-EDDLNRAKSEL----NRLQQEETQLE---QSIQAGR 521
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEakkEAEAIKKEAlLEAKEEIHKLRNEfEKELRERRNELqkleKRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568955195 522 AQLETILRSLKCTQDDINQARSKLSQLQESHLEAhrsLEQY 562
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERI 147
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
385-552 |
2.02e-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: 41.35 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 385 DDISQEIAQLQREKYSLEQ----------------------DIREKEEAIRQKTSEVQELQNDLDRETSSL--------Q 434
Cdd:pfam09755 110 NDLSRKLTQLRQEKVELEQtleqeqeyqvnklmrkiekleaETLNKQTNLEQLRREKVELENTLEQEQEALvnrlwkrmD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 435 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDvRQKCQDETQTISSLKTQIQSQESDLKSQEDDlnrAKSELNRLQQEETQL- 513
Cdd:pfam09755 190 KLEAEKRLLQEKLDQPVSAPPSPRDSTSE-GDTAQNLTAHIQYLRKEVERLRRQLATAQQE---HTEKMAQYAQEERHIr 265
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568955195 514 EQSIQAGRA-QLETILRSLKCTQddINQARSKLSQLQESH 552
Cdd:pfam09755 266 EENLRLQRKlQLEMERREALCRH--LSESESSLEMDEERY 303
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
477-547 |
2.02e-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: 39.61 E-value: 2.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 477 SLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
384-561 |
2.09e-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: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQrekyslEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 463
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 464 VRQKCQDETQTI-SSLKTQIQSQESDLKSQEDDL-NRAKSELNRLQqeeTQLEQSIQAGRAQLETILRSLKCTQDDI--- 538
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAPYaee 147
|
170 180
....*....|....*....|....*
gi 568955195 539 --NQARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam01442 148 vqAQLSQRLQELREKLEPQAEDLRE 172
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
381-470 |
2.10e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 38.90 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLD------------RETSSLQELEAQKQDAQDRLD 448
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALE----ELEKLPDDTPiykivgnllvkvDKTKVEKELKERKELLELRSR 88
|
90 100
....*....|....*....|..
gi 568955195 449 EMDQQKAKLRDMLSDVRQKCQD 470
Cdd:PRK09343 89 TLEKQEKKLREKLKELQAKINE 110
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
382-447 |
2.15e-03 |
|
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: 39.48 E-value: 2.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRL 447
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
403-542 |
2.19e-03 |
|
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: 39.22 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 403 QDIREKEEaiRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqtissLKTQI 482
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955195 483 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRAQLETILRSLKCTQ---DDINQAR 542
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEKLKE--KKQKEYRAEEAKREQkemDELATQR 138
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
417-551 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 417 SEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL 496
Cdd:cd21116 73 SYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 497 NRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:cd21116 143 QAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESS 197
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
352-561 |
2.33e-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: 41.57 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 352 LSPDMVPPSErgtPIPDSSSTLASGEFTGVKELDDISQEI-AQLQRekySLEQDI--REKEEAIRQKtsEVQELqndLDR 428
Cdd:pfam10168 471 LLIDAVPPSP---PLLCSKEDVTVDEPLRGLQEDSFEDHIkSILQR---SVSNPIlsADKLSSPSPQ--ECLQL---LSR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 429 ETSSLQELEAQKQDA-----QDRLDEMDQQKAK-LRDMlsdvrQKCQDETQTISSLKTQIQSQESDLK-SQEDDLNRAKS 501
Cdd:pfam10168 540 ATQVFREEYLKKHDLareeiQKRVKLLKLQKEQqLQEL-----QSLEEERKSLSERAEKLAEKYEEIKdKQEKLMRRCKK 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955195 502 ELNRLQqeeTQLEQSIQAGRA---QLETILRSLKCTQDDINQARSKLSQlQESHLEAHRSLEQ 561
Cdd:pfam10168 615 VLQRLN---SQLPVLSDAEREmkkELETINEQLKHLANAIKQAKKKMNY-QRYQIAKSQSIRK 673
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
382-551 |
2.39e-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: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQrEKYSL----EQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEM 450
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAyselqeeLEEILEQLEEIEEEQEEF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSqeSDL----KSQEDDLNRAKSELNRLQQeetQLEQSiqagRAQLET 526
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEV----PLNMDE 454
|
170 180
....*....|....*....|....*
gi 568955195 527 ILRSLKCTQDDINQARSKLSQLQES 551
Cdd:pfam06160 455 VNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
400-460 |
2.49e-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: 37.93 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 400 SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 460
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
454-564 |
2.51e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 41.76 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC 533
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQ 81
|
90 100 110
....*....|....*....|....*....|.
gi 568955195 534 TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG5283 82 LSAAQRRLRSSLEQTNRQLERQQQRLARLGA 112
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
373-561 |
2.58e-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: 41.49 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 373 LASGEFTGVKELD-DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEaqkqdaqdRLDEMD 451
Cdd:TIGR00618 181 LALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT--------QKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 452 QQKAKLRDMLSDVRQKCQdetqtisslktQIQSQESDLKSQEDDLNRAKSELnRLQQEETQLEQSiqagRAQLETILRSL 531
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIE-----------ELRAQEAVLEETQERINRARKAA-PLAAHIKAVTQI----EQQAQRIHTEL 316
|
170 180 190
....*....|....*....|....*....|..
gi 568955195 532 KCTQDDINQARSKLSQL--QESHLEAHRSLEQ 561
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHvkQQSSIEEQRRLLQ 348
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
339-552 |
2.73e-03 |
|
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: 41.55 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 339 QQKVSKGIDppQVLSPDMVPPSERGTPIPDSSSTLAS--GEFTGVKELDDISQEIAQLQR-EKYSLEQDIREKEEAIRQK 415
Cdd:pfam05667 245 RTKLLKRIA--EQLRSAALAGTEATSGASRSAQDLAEllSSFSGSSTTDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 416 TSEVQELQNDLDRETSSLQEleaqkqdaqdRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE-- 493
Cdd:pfam05667 323 VETEEELQQQREEELEELQE----------QLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKkt 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 494 -DDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI-------LRSLKCTQDD-INQARSKLSQLQESH 552
Cdd:pfam05667 393 lDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHrvplieeYRALKEAKSNkEDESQRKLEEIKELR 460
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
382-452 |
3.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 382 KELDDISQEIAQLQREKysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 452
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
384-561 |
3.10e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 455
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 456 KLRDMLSDVRQKCQDETQTISSLKTQIQSQ-------ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI- 527
Cdd:COG0497 223 KLREALQEALEALSGGEGGALDLLGQALRAlerlaeyDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVe 302
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955195 528 -----LRSLK----CTQDDI----NQARSKLSQLQ--ESHLEAhrsLEQ 561
Cdd:COG0497 303 erlalLRRLArkygVTVEELlayaEELRAELAELEnsDERLEE---LEA 348
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
404-466 |
3.19e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 39.93 E-value: 3.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 404 DIREKEEAIRQKTSEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 466
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
409-567 |
3.34e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 409 EEAIRQKTSEVQELQNDLDRETSSLQELEAQkqdaqdrLDEMDQQKAKLRDMLSDVRQ-KCQDETQtissLKTQIQSQEs 487
Cdd:pfam05911 687 KEEFEQLKSEKENLEVELASCTENLESTKSQ-------LQESEQLIAELRSELASLKEsNSLAETQ----LKCMAESYE- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 488 DLKSQEDDLnraKSELNRLQQEETQLEQSIQAGRaqletilrslKCTQDDInqARSKLSQLQ-ESHLEAHRSLEQYDQDD 566
Cdd:pfam05911 755 DLETRLTEL---EAELNELRQKFEALEVELEEEK----------NCHEELE--AKCLELQEQlERNEKKESSNCDADQED 819
|
.
gi 568955195 567 P 567
Cdd:pfam05911 820 K 820
|
|
| ClyA_MakA-like |
cd22655 |
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
416-527 |
3.56e-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: 40.73 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 416 TSEVQELQNDL-DRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE 493
Cdd:cd22655 77 TSQILNIFKALpTAPDDAQvEQIIALLQALQKPVQEIISNIAAYQGKLKAWGDKMQAAHDNLTTGAAQIQAAETDLQADI 156
|
90 100 110
....*....|....*....|....*....|....*.
gi 568955195 494 DDLNRAKSELNR-LQQEETQLEQS-IQAGRAQLETI 527
Cdd:cd22655 157 DKINNAIANLNAeIAKDNKAIAAAqIAIGVGIFELV 192
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
387-541 |
3.57e-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: 39.05 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 387 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSlqeleaqkqdaqDRLDEMDQQKAKLRDMLSDVRQ 466
Cdd:pfam16789 23 VKDKKRALEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------------DKILQMKRYIKVVKERLKQEEK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955195 467 KCQDEtqtisslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkcTQDDINQA 541
Cdd:pfam16789 91 KVQDQ-------KEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEER------EQDEIGSA 152
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
401-546 |
3.64e-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: 39.66 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 401 LEQDIREKEEAIRQKTSEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQTISSLKT 480
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955195 481 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC--TQDDINQARSKLS 546
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLS 158
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
476-556 |
3.93e-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: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 476 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLAT 322
|
.
gi 568955195 556 H 556
Cdd:TIGR04320 323 A 323
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
390-552 |
3.98e-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: 39.64 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRetsslQELEAQKQDAQdRLDEMDQQ--------KAKLRDML 461
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE-----RELKAEAEHRQ-RVVELSREveeakrafEEKLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKS-ELNRLQQEetqLEQSIQAGRAQLETiLRSLKctQDDINQ 540
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVED-LRKEK--KKLAEE 194
|
170
....*....|..
gi 568955195 541 ARSKLSQLQESH 552
Cdd:pfam15665 195 YEQKLSKAQAFY 206
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
381-531 |
3.99e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 40.76 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 453
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 454 KAKLRDMLSDVRQKCQdetQTISSLKTQIQSQESDLK----SQEDDLNRAKSELNRLQQEETQLEQS-IQAGRAQLETIL 528
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
...
gi 568955195 529 RSL 531
Cdd:pfam03999 298 DKL 300
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
408-515 |
4.31e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 408 KEEAIRQKTSEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqtisslk 479
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 568955195 480 tqiQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQ 515
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLER 142
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
484-552 |
4.80e-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: 4.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955195 484 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkctQDDI-------NQARSKLSQLQESH 552
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL-------NDELialqienNLLEEKLRKLQEEN 69
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
423-552 |
5.85e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 423 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcQDETQ------------TISSLKTQIQSQESDLk 490
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL-YRELRksllanrfsfgpALDELEKQLENLEEEF- 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 491 SQEDDLN------RAKSELNRLQQEETQLEQSIQagraQLETILRSLKCT-QDDINQARSKLSQLQESH 552
Cdd:PRK04778 182 SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAGYRELVEEG 246
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
389-557 |
6.69e-03 |
|
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: 39.21 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDIREKEEAIRQKT---SEVQELQNDLDretSSLQELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDV 464
Cdd:cd07651 22 EELRSFYKERASIEEEYAKRLEKLSRKSlggSEEGGLKNSLD---TLRLETESMAKSHLKFAKQIRQDlEEKLAAFASSY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 465 RQKCQDETQTISSLKTQIQSQESDL-KSQ---EDDLNRAKS-----------ELNRLQQEETQLEQSIQAGRAQLETILR 529
Cdd:cd07651 99 TQKRKKIQSHMEKLLKKKQDQEKYLeKARekyEADCSKINSytlqsqltwgkELEKNNAKLNKAQSSINSSRRDYQNAVK 178
|
170 180
....*....|....*....|....*....
gi 568955195 530 SLKCTQDDINQA-RSKLSQLQesHLEAHR 557
Cdd:cd07651 179 ALRELNEIWNREwKAALDDFQ--DLEEER 205
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
382-507 |
7.40e-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: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 382 KELDDISQEIAQLQR---EKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQdaqdrldEMDQQKAKLR 458
Cdd:pfam02841 183 QSKEAVEEAILQTDQaltAKEKAIEAERAKAEAAEAEQELLREKQKEEE------QMMEAQER-------SYQEHVKQLI 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568955195 459 DMLSDVRQKCQDETQTISSLKTQIQ---SQESdLKSQEDDLNRaksELNRLQ 507
Cdd:pfam02841 250 EKMEAEREQLLAEQERMLEHKLQEQeelLKEG-FKTEAESLQK---EIQDLK 297
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
383-526 |
7.53e-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: 40.13 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQLQ-REKYSLEQDIREKEEAIRQ------------KTSEVQELQNDLDRETSSLQ---------ELEAQK 440
Cdd:pfam09731 295 EIDQLSKKLAELKkREEKHIERALEKQKEELDKlaeelsarleevRAADEAQLRLEFEREREEIResyeeklrtELERQA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 441 QDAQDRL-DEMDQQKAKL-RDMLSDVRQKCQDE----TQTISSLKTQIQSQE---SDLKSQEDDLNRAKselnrlqqeet 511
Cdd:pfam09731 375 EAHEEHLkDVLVEQEIELqREFLQDIKEKVEEEragrLLKLNELLANLKGLEkatSSHSEVEDENRKAQ----------- 443
|
170
....*....|....*
gi 568955195 512 QLEQSIQAGRAQLET 526
Cdd:pfam09731 444 QLWLAVEALRSTLED 458
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
383-558 |
7.73e-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: 40.16 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 383 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKTSEVQELQNDLDRETSSLQ------- 434
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 435 ELEAQKQDAQDRLDEMDQQ-KAKLRdmlsdvrqkcqdetQTISSLKTQIQSQESDLKsQEddlNRAKSELNRL-QQEETQ 512
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFK--------------SSIAALEAKIAQLEEQLE-QE---SRERQAANKLvRRTEKK 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568955195 513 LEQSIqagrAQLETILRSLKCTQDDINQARSKLS----QLQESHLEAHRS 558
Cdd:pfam01576 1004 LKEVL----LQVEDERRHADQYKDQAEKGNSRMKqlkrQLEEAEEEASRA 1049
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
416-561 |
8.00e-03 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 38.53 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 416 TSEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetQTISSLKtqiQSQE-SD----LK 490
Cdd:pfam15272 3 TSEYLELLDKLDKNNRALHLL---NKDVRERDEHYQLQETSYKKKYLQTRN------ELINELK---QSKKlYDnyykLY 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955195 491 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLEtilRSLKCTQDDINQarsklSQLQESHLEAHRSLEQ 561
Cdd:pfam15272 71 SKYQQLKKISNESLDLQSTITNLESQLVDQAIDKD---REIHNLNEKILS-----LELRNQELETKREIDK 133
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
384-515 |
8.20e-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: 37.55 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 384 LDDISQEIAQLQREKysleqdirekeeairqktsevqelqndldretsslQELEAQKQDAQDRLDEMDQQKAKLRDML-- 461
Cdd:pfam05103 27 LDQVAEDYEALIREN-----------------------------------AELKEKIEELEEKLAHYKNLEETLQNTLil 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955195 462 -----SDVRQKCQDETQTISSlKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQLEQ 515
Cdd:pfam05103 72 aqetaEEVKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| DUF5082 |
pfam16888 |
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized. |
389-506 |
9.11e-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: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 389 QEIAQLQREKYSLEQDIREKEEAiRQKTSEVQElqndldretsslqELEAQKQDAQDRLDEMD----QQKAKLRDMLSDV 464
Cdd:pfam16888 10 AQIAQLRSEIAALEEKIERLKEA-KTKLDAEKE-------------SLHDKKTKLQGPLNSSEswngSNENNYDGIRSNL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568955195 465 RQKCQ---DET-QTISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 506
Cdd:pfam16888 76 ETSYQnyvDELdELIDAIEEEITRLENQINEAQGVIDTLQSQLNSL 121
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
410-518 |
9.27e-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: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 410 EAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQTISSLKTQIQSQ 485
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLisiiQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKENK 73
|
90 100 110
....*....|....*....|....*....|...
gi 568955195 486 ESDLKSQeddlnrakseLNRLQQEETQLEQSIQ 518
Cdd:smart00502 74 LKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
387-523 |
9.31e-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: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955195 387 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ 466
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ-------AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955195 467 KCQDETQTISSL---KTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL---EQSIQAGRAQ 523
Cdd:pfam01576 560 QLEEKAAAYDKLektKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMlaeEKAISARYAE 622
|
|
| |
