|
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 |
1.03e-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: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 266 AWVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSkG 345
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 568955199 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 |
2.60e-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: 117.76 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 121 WAVRVEEKAKFDGIFESLLP-VNGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 199
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
.
gi 568955199 200 V 200
Cdd:smart00027 82 I 82
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
131-196 |
6.24e-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: 98.45 E-value: 6.24e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 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 |
6.58e-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: 95.36 E-value: 6.58e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 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 |
3.15e-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: 88.97 E-value: 3.15e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 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 |
3.73e-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: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 13 PGGNPLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQSGHEVTLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 568955199 93 SLSLTMPPPKF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
1.66e-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: 85.73 E-value: 1.66e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 19 YESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQS 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
363-543 |
7.63e-19 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 89.19 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 363 GTPIPDSSSTLASGEFtgvkELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQD 442
Cdd:COG4372 23 GILIAALSEQLRKALF----ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 443 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA--- 519
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlse 178
|
170 180
....*....|....*....|....*.
gi 568955199 520 --GRAQLETILRSLKCTQDDINQARS 543
Cdd:COG4372 179 aeAEQALDELLKEANRNAEKEEELAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-564 |
9.91e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 9.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|..
gi 568955199 543 SKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEE 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-561 |
1.23e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170 180
....*....|....*....|
gi 568955199 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 462 LELLAELLEEAALLEAALAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-561 |
2.46e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180
....*....|....*....|
gi 568955199 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 448 AEEEAELEEEEEALLELLAE 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-564 |
4.11e-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: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180
....*....|....*....|...
gi 568955199 542 RSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
390-564 |
7.00e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 469
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 470 DETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170
....*....|....*
gi 568955199 550 ESHLEAHRSLEQYDQ 564
Cdd:COG1196 393 RAAAELAAQLEELEE 407
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-611 |
1.14e-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: 81.64 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRAQLETILRSLKCTQDDINQ 540
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 541 ARSKLSQLQESHLEAHRSLEQYDQVPDGVSGtslpDLATLNEGILLAERgGFGAMDDPFKNKALLFSNNSQ 611
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAER----ELAQLQARLDSLER-LQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-561 |
1.32e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdqqkAKLRDML 461
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180
....*....|....*....|
gi 568955199 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR02168 858 AAEIEELEELIEELESELEA 877
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-561 |
1.42e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREKYSLEqdIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVR 465
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-------LEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 466 QKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170
....*....|....*.
gi 568955199 546 SQLQESHLEAHRSLEQ 561
Cdd:COG1196 368 LEAEAELAEAEEELEE 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-561 |
1.45e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180
....*....|....*....|
gi 568955199 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-567 |
4.60e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.72 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQ 453
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisrLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 KAKLRDMLSDVRQKcQDETQTI-SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:TIGR02168 318 LEELEAQLEELESK-LDELAEElAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190
....*....|....*....|....*....|....*
gi 568955199 533 CTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 567
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-561 |
6.44e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREK---YSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG1196 261 ELAELEAELEELRlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170
....*....|....*....
gi 568955199 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 |
7.55e-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: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrQK 467
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 468 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170
....*....|....*..
gi 568955199 548 LQEShlEAHRSLEQYDQ 564
Cdd:TIGR02168 433 AELK--ELQAELEELEE 447
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
405-564 |
1.94e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 75.71 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 405 IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcqdetqtISSLKTQIQS 484
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 485 QESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
383-565 |
3.57e-14 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 72.65 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVR-----QKCQDEtqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDD 537
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180
....*....|....*....|....*...
gi 568955199 538 INQARSKLsqlqESHLEAhRSLEQYDQV 565
Cdd:COG1579 161 LEAEREEL----AAKIPP-ELLALYERI 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-564 |
4.02e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL----NRLQQEETQL---EQSIQAGRAQLETILRSLKC 533
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALleaEAELAEAEEELEELAEELLE 390
|
170 180 190
....*....|....*....|....*....|.
gi 568955199 534 TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-550 |
4.71e-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: 74.80 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 454
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170
....*....|....*.
gi 568955199 535 QDDINQARSKLSQLQE 550
Cdd:COG4942 212 AAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-551 |
9.70e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 469
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 470 DETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
..
gi 568955199 550 ES 551
Cdd:TIGR02168 393 LQ 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-550 |
1.00e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 73.64 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 461
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 ----------------------------------SDVRQKC----QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL 503
Cdd:COG4942 111 ralyrlgrqpplalllspedfldavrrlqylkylAPARREQaeelRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568955199 504 NRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-564 |
1.41e-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: 74.71 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 467
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 468 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170
....*....|....*..
gi 568955199 548 LQESHLEAHRSLEQYDQ 564
Cdd:TIGR02168 829 LERRIAATERRLEDLEE 845
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-549 |
1.57e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.42 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 458
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 459 DMLSDVRQKcqdeTQTISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDD 537
Cdd:COG4717 160 ELEEELEEL----EAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170
....*....|....
gi 568955199 538 --INQARSKLSQLQ 549
Cdd:COG4717 236 leAAALEERLKEAR 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-591 |
1.80e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRdml 461
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLE--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 sDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG1196 404 -ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568955199 542 RSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGG 591
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
381-532 |
2.23e-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: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 458
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 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 |
2.34e-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: 73.90 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELNRLQQE----ETQLEQSIQagraQLETI 527
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEisntQTQLNQLKD----EQNKI 265
|
170 180
....*....|....*....|...
gi 568955199 528 LRSLKCTQDDINQARSKLSQLQE 550
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEK 288
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-561 |
3.10e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKTSEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 446
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 LDEMDQQKAKLRDMLSDVRQKC-QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLE 525
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 568955199 526 TILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
391-564 |
3.13e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 391 IAQLQREKYSLE-----------QDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LRDMLSdvRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRAQLETILRSLKCTQ 535
Cdd:COG4717 128 LPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*....
gi 568955199 536 DDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-564 |
3.17e-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: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 S-------DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRAQLETILRSL 531
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALL 892
|
170 180 190
....*....|....*....|....*....|....*..
gi 568955199 532 KC----TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:TIGR02168 893 RSeleeLSEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
382-594 |
4.35e-13 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 71.78 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQ--------------- 444
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSvsyldvllgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 445 --DRLDEMDQQKAKLRDMLSDVrqkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRA 522
Cdd:COG3883 117 flDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 523 QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGGFGA 594
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-530 |
6.53e-13 |
|
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: 72.79 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 463 DVRQKCQDETQTISSLktqiqsqesdlksqEDDLNRAKSELNRLQQEETQLEQSIQAGRAQlETILRS 530
Cdd:TIGR02169 466 KYEQELYDLKEEYDRV--------------EKELSKLQRELAEAEAQARASEERVRGGRAV-EEVLKA 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-561 |
1.34e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 dvRQKCQDETQTISSLKTQIQSQESDLKSQEddlnrakSELNRLQQEETQLEQSIQ---------------------AGR 521
Cdd:TIGR02169 790 --HSRIPEIQAELSKLEEEVSRIEARLREIE-------QKLNRLTLEKEYLEKEIQelqeqridlkeqiksiekeieNLN 860
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568955199 522 AQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-550 |
1.87e-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: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
....*....
gi 568955199 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 |
1.99e-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: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLKCTQDD---- 537
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEKlese 532
|
170
....*....|...
gi 568955199 538 INQARSKLSQLQE 550
Cdd:TIGR04523 533 KKEKESKISDLED 545
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
382-525 |
4.14e-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: 66.87 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 461
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 462 SDVRQKCQDEtqtISSLKTQIQSQESDLKSQEDDLNRAKSELN----RLQQEETQLEQSIQAGRAQLE 525
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAAKIP 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-565 |
1.12e-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: 68.54 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRET-------SSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealallrSELEELSEELRELESKRSELRREL 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLksQEDDL---NRAKSELNRLQQEETQLEQSIQA-GRAQLETI--- 527
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT--LEEAEaleNKIEDDEEEARRRLKRLENKIKElGPVNLAAIeey 995
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568955199 528 ------LRSLKCTQDDINQARSKLSQL-QESHLEAH-RSLEQYDQV 565
Cdd:TIGR02168 996 eelkerYDFLTAQKEDLTEAKETLEEAiEEIDREAReRFKDTFDQV 1041
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
373-561 |
1.31e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 373 LASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 452
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 453 QKAKLRDMLSdvRQKCQDETQTISSLKTQIQSQESDLKSQED--DLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrs 530
Cdd:COG4942 91 EIAELRAELE--AQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAAL--- 165
|
170 180 190
....*....|....*....|....*....|.
gi 568955199 531 lkctQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:COG4942 166 ----RAELEAERAELEALLAELEEERAALEA 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
378-519 |
1.56e-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: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 378 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 457 LRDMLSDVRQKCQDETQTISSLKTQIQSQ----ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
382-566 |
1.67e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 66.78 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 458
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 459 -------------------DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQA 519
Cdd:COG3883 103 syldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE-------LEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568955199 520 GRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVP 566
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-560 |
5.90e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKTSEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 457
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 458 RDMLSDVRQKCQDETQTISSLK---TQIQSQESDLKSQ----EDDLNRAKSELNRLQQEETQLEQSIQAGRAQ------- 523
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRedaDDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERfgdapvd 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568955199 524 ---LETILRSLKCTQDDINQA----RSKLSQLQESHLEAHRSLE 560
Cdd:PRK02224 407 lgnAEDFLEELREERDELREReaelEATLRTARERVEEAEALLE 450
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
390-555 |
1.26e-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: 64.76 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 390 EIAQLQREKYSLEQDIREKEEAIRQKTSevqELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 469
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELS---ELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 470 DETQTISSLKTQIQSQESDLKSQEDD---LNRAKSELNRLQQEETQLEQsIQAGRAQLETILRSLKCTQDDINQARSKLS 546
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 568955199 547 QLQESHLEA 555
Cdd:pfam05557 239 REEKYREEA 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-550 |
1.42e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRE-------TSSLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 456 KLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQ 535
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170
....*....|....*
gi 568955199 536 DDINQARSKLSQLQE 550
Cdd:TIGR02168 929 LRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-552 |
1.51e-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: 65.08 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 406 REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQ 485
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 486 ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH 552
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-570 |
3.05e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 396 REKYSLEQDIREKEEAIRQktsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMdQQKAKLRDMLSDVRQkCQDETQTI 475
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVAS-AEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 476 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170
....*....|....*
gi 568955199 556 HRSLEQYDQVPDGVS 570
Cdd:COG4913 754 RFAAALGDAVERELR 768
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-561 |
3.72e-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: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKTSEVQE-------LQNDLDRETSSLQELEAQKQDAQDRLDEMD 451
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISElkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ---SQESDLKSQ--EDDLNRAKSEL----NRLQQEETQLEQSIQagra 522
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELknqeKKLEEIQNQISQNNK---- 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 568955199 523 qletILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR04523 336 ----IISQLN---EQISQLKKELTNSESENSEKQRELEE 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
438-565 |
4.34e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 517
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568955199 518 QAGRAQLETILRSLkctQDDINQARSKLSQLQESHLEAHRSLEQYDQV 565
Cdd:COG4942 100 EAQKEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYL 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-550 |
5.09e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQdaqdRLDEMdQQKAKLRDM 460
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVK----ELKEL-KEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIqagrAQLETILRSLkctqddiNQ 540
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL----EELEERHELY-------EE 366
|
170
....*....|
gi 568955199 541 ARSKLSQLQE 550
Cdd:PRK03918 367 AKAKKEELER 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
385-561 |
5.11e-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: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKT------SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 456 KLRDMLSDVRQkcqdeTQTISSLKTQIQSQESDLKSQED-------DLNRAKSELN----RLQQEETQLEQSIQAGRAQL 524
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAalraQLQQEAQRILASLEAELEAL 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 568955199 525 ETILRSLkctQDDINQARSKLSQLQESHLEAhRSLEQ 561
Cdd:COG3206 326 QAREASL---QAQLAQLEARLAELPELEAEL-RRLER 358
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
376-458 |
6.77e-10 |
|
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: 59.94 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 376 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 455
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 568955199 456 KLR 458
Cdd:COG1579 160 ELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-582 |
8.56e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIR--QKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAK 456
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQsiQAGRAQLETILRSLkct 534
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAA--ALGDAVERELRENL--- 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955199 535 QDDINQARSKLSQLqESHLEahRSLEQYDQVPDGVSGTSLPDLATLNE 582
Cdd:COG4913 772 EERIDALRARLNRA-EEELE--RAMRAFNREWPAETADLDADLESLPE 816
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-561 |
9.56e-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: 62.35 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdml 461
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIqagrAQLETILRSLKCTQDDINQa 541
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD----SVKELIIKNLDNTRESLET- 468
|
170 180
....*....|....*....|
gi 568955199 542 rsKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQ 486
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
382-565 |
1.03e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 61.79 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKeeairqktsEVQELQNDLDRETSSLQELEAqkQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDK---------EIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 ---SDVRQKCQDETQTISSLKTQIQSQESDLKS-----------QEDDLNRAKS---ELNRLQQEETQLEQSIQAG---- 520
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEelervqqsytlNENELERVRGlekQLEELEKRYDEIVERLEEKevay 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955199 521 ---RAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 565
Cdd:pfam06160 360 selQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLE 407
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
382-554 |
2.16e-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: 58.85 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMLSDVRQKCQDETQT-ISSLKTQIQSQESDLKSQEDDL--NRAKSELNRLQQEETQLEQsiqagrAQLETILRSL 531
Cdd:pfam12795 130 QQIRNRLNGPAPPGEPLSEAqRWALQAELAALKAQIDMLEQELlsNNNRQDLLKARRDLLTLRI------QRLEQQLQAL 203
|
170 180
....*....|....*....|...
gi 568955199 532 kctQDDINQARSKLSQLQESHLE 554
Cdd:pfam12795 204 ---QELLNEKRLQEAEQAVAQTE 223
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
383-561 |
2.29e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.62 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKTSEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 450
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 ---DQQKAKLRDMLSDVRQKCQ-----------------DETQTISSLKTQIQSQESDLKSQEDDLNRAK---SEL-NRL 506
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKEQNKelkeeidrvkqsytlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaySELqEEL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 507 QQEETQLEQsIQAGRAQLETILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:PRK04778 386 EEILKQLEE-IEKEQEKLSEMLQGLR---KDELEAREKLERYRNKLHEIKRYLEK 436
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-588 |
4.12e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 60.35 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVRQKCQdetqtisslktQIQSQESDLKSQEDDLNRAKSELNRLQ-QEETQLE--QSIQAGRAQLETILRSLKCTQDDIN 539
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLReQSGEALAdsQEVTAAMQQLLEREREATVERDELA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955199 540 QARSKLSQlqeshlEAHRsLEQydqvPDGVSGTSLPDLATLNEGILLAE 588
Cdd:COG3096 651 ARKQALES------QIER-LSQ----PGGAEDPRLLALAERLGGVLLSE 688
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
389-561 |
7.98e-09 |
|
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: 58.75 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDiREKEEAIRQKT---SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 465
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 466 QKCQDETQTISSLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEETQLEQSiQAGRAQLETILRSLKCT----------- 534
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSLSKEfqelrnslaqr 204
|
170 180 190
....*....|....*....|....*....|....
gi 568955199 535 -------QDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam07888 205 dtqvlqlQDTITTLTQKLTTAHRKEAENEALLEE 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-555 |
1.03e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEI-AQLQR--------EKYsleqdiREKEEAIRQK-----TSEVQELQNDLDRETSSLQELEAQKQDAQDRLDE 449
Cdd:TIGR02168 191 LEDILNELeRQLKSlerqaekaERY------KELKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 450 MDQQKAKLRDmlsdvrqkcqdetqTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILR 529
Cdd:TIGR02168 265 LEEKLEELRL--------------EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180
....*....|....*....|....*.
gi 568955199 530 SLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESL 356
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-551 |
1.04e-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: 58.88 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNR---------LQQEETQLEQ---SIQAGRA 522
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQtqkSLKKKQE 585
|
170 180
....*....|....*....|....*....
gi 568955199 523 QLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
385-574 |
1.37e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.98 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 464
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 465 RQKCQDetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSK 544
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
170 180 190
....*....|....*....|....*....|
gi 568955199 545 LSQLQESHLEAHRSLEQYDQVPDGVSGTSL 574
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASL 293
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
392-552 |
1.74e-08 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 57.40 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 392 AQLQrekySLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 471
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 472 TQTISSLKTQIQSQESDLKSQEDDLNRaKSELNRLQ----QEETQLEQSIQA-----GRAQLETIlRSLKCTQDDINQAR 542
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETI-AELKQTREELAAQK 186
|
170
....*....|
gi 568955199 543 SKLSQLQESH 552
Cdd:PRK11637 187 AELEEKQSQQ 196
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
382-550 |
2.54e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.47 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLE---QDIREK-EEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ-Q 453
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRlaaEDFRQKyEDELNLRTSaenDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 KAKLRDMLSDVRQ----------KCQDETQTISSLKTQ---------------IQSQESDLKSQ----EDDLNRAKSELN 504
Cdd:pfam00038 141 EEEVRELQAQVSDtqvnvemdaaRKLDLTSALAEIRAQyeeiaaknreeaeewYQSKLEELQQAaarnGDALRSAKEEIT 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568955199 505 ----RLQQEETQLeQSIQAGRAQLETILRSLKCTQD-DINQARSKLSQLQE 550
Cdd:pfam00038 221 elrrTIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISELEA 270
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-564 |
2.85e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIREKEEAIR----QKTSEVQELQN------DLDRETSSLQ----ELEAQKQDAQDRLDE 449
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENlngkkeELEEELEELEaalrDLESRLGDLKKERDE 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 450 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSE------LNRLQQEETQLEQSIQAgraq 523
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA---- 969
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955199 524 LETIlrSLKCTQD-DINQARskLSQLQESH--LEAHRS-----LEQYDQ 564
Cdd:TIGR02169 970 LEPV--NMLAIQEyEEVLKR--LDELKEKRakLEEERKailerIEEYEK 1014
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
382-564 |
2.91e-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: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQR--EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----------- 448
Cdd:COG3206 182 EQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellq 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 449 -----EMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDD-LNRAKSELNRLQQEEtqleQSIQAGRA 522
Cdd:COG3206 262 spviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQARE----ASLQAQLA 337
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955199 523 QLETILRSLkctqddiNQARSKLSQLQEshlEAHRSLEQYDQ 564
Cdd:COG3206 338 QLEARLAEL-------PELEAELRRLER---EVEVARELYES 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
386-564 |
3.14e-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: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREKYsLEQDIREKEEAIRQKTS----EVQELQNDLD---------RETSSLQELEAQKQDAQDRLDEMDQ 452
Cdd:COG3206 148 ELAAAVANALAEAY-LEQNLELRREEARKALEfleeQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 453 QKAKLRDMLSDVRQKcqdetqtISSLKTQIQSQESDLKSQEDD--LNRAKSELNRLQQEETQLEQ-------SIQAGRAQ 523
Cdd:COG3206 227 QLAEARAELAEAEAR-------LAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQ 299
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955199 524 LETILRSLKC-TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG3206 300 IAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
389-523 |
3.35e-08 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 52.64 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDIREKEEAIrqktsevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 468
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 469 QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSelnRLQQEETQLEQSIQAGRAQ 523
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
369-535 |
4.09e-08 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 55.53 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 369 SSSTLASGEFTGVKELddisqEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE--------LEAQK 440
Cdd:pfam09787 32 EGSGVEGLDSSTALTL-----ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 441 QDAQDRLDEMDQQKAKLRDMLSDVRQ-------KCQDETQTISSLKTQIQSQeSDLKSQEDDL-NRAKSELNRLQQEETQ 512
Cdd:pfam09787 107 SARREAEAELERLQEELRYLEEELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELeNRLHQLTETLIQKQTM 185
|
170 180
....*....|....*....|....*..
gi 568955199 513 LEqSIQAGRA----QLETILRSLKCTQ 535
Cdd:pfam09787 186 LE-ALSTEKNslvlQLERMEQQIKELQ 211
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
392-567 |
4.24e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 392 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 446
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS 516
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568955199 517 IQagraQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 567
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPE 201
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-532 |
6.08e-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: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENLNGKKEELEEE 869
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 461 LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
385-562 |
8.38e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.53 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 464
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 465 RQKCQDETQTISSLKTQIQSQESDLKSqeddLNRAKSELNRL---QQ-------EETQLEQSIQAGRAQLETILRSLKcT 534
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERLewrQQtevlspeEEKELVEKIKELEKELEKAKKALE-K 158
|
170 180
....*....|....*....|....*...
gi 568955199 535 QDDINQARSKLSQLQESHLEAHRSLEQY 562
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKEL 186
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
382-591 |
8.77e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 456 KLRDMLSDVRQKC-----QDET--QTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 528
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 529 RSLKCTQDDINQARSKLSQLqESHLEAHRslEQYDQVPdgvsgTSLPDLATLNEgILLAERGG 591
Cdd:PRK02224 370 SELEEAREAVEDRREEIEEL-EEEIEELR--ERFGDAP-----VDLGNAEDFLE-ELREERDE 423
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-567 |
8.78e-08 |
|
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: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 458
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 459 DMLSDVRQKCQDETQTISSlKTQIQSQESDLKSQEDDLNRAKSE----LNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190
....*....|....*....|....*....|...
gi 568955199 535 QDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 567
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
389-588 |
8.99e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 468
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 469 QdetqtisslktQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLE-QSIQAGRAQLETILRSLKctqddinQARSKL 545
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLREQsgEEFEDsQDVTEYMQQLLERERELT-------VERDEL 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568955199 546 SQLQESHLEAHRSLEQYDqvpdgvsGTSLPDLATLNE---GILLAE 588
Cdd:PRK04863 651 AARKQALDEEIERLSQPG-------GSEDPRLNALAErfgGVLLSE 689
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-565 |
9.09e-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: 55.80 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQE----IAQLQREKYSLEQD---IREKEEAIRQKTSEVQEL----QNDLDRETSS-LQELEAQKQDAQDRLDE 449
Cdd:TIGR04523 253 TQLNQLKDEqnkiKKQLSEKQKELEQNnkkIKELEKQLNQLKSEISDLnnqkEQDWNKELKSeLKNQEKKLEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 450 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGR---AQLET 526
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEklnQQKDE 412
|
170 180 190
....*....|....*....|....*....|....*....
gi 568955199 527 ILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 565
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
368-558 |
1.14e-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: 55.60 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 368 DSSSTLAsGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE---AQKQ-- 441
Cdd:pfam10174 373 EEKSTLA-GEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEri 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 442 ----------DAQDRLDEMDQQKAKLRDM---LSDVRQKCQDETQTISSLKTQIQSQESD-------LKSQEDDLNRAKS 501
Cdd:pfam10174 452 ierlkeqrerEDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 502 ELNRLQ--------QEET------------QLEQSIQ-----AGRAQ--LETILRSLKCTQDDINQARSKLSQLQESHLE 554
Cdd:pfam10174 532 ECSKLEnqlkkahnAEEAvrtnpeindrirLLEQEVArykeeSGKAQaeVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
....
gi 568955199 555 AHRS 558
Cdd:pfam10174 612 QMKE 615
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-557 |
1.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 461
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETqleqsiQAGRAQLEtilrslkctqdDINQA 541
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET------ADLDADLE-----------SLPEY 817
|
170
....*....|....*.
gi 568955199 542 RSKLSQLQESHLEAHR 557
Cdd:COG4913 818 LALLDRLEEDGLPEYE 833
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
382-530 |
1.87e-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: 55.07 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEA----------IRQKTSEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMD 451
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdelkdYREKLEKLKREINELKRELDRLQEE---LQRLSEELADLN 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 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 |
2.83e-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: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 399 YSLEQDIR---------EKEEAIRQKTSEVQELQnDLDRETSSL----QELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 465
Cdd:COG2433 376 LSIEEALEeliekelpeEEPEAEREKEHEERELT-EEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568955199 466 QKCQDETQT---ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ 508
Cdd:COG2433 455 SEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-559 |
4.48e-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: 53.80 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREkysLEQdIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQkqDAQDRLDEMDQQKAKLRDMLS 462
Cdd:COG3096 837 ELAALRQRRSELERE---LAQ-HRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVRQKCQdetqTISSLKTQIQSQESDLKSQED---DLNRAKSELNRLQQEETQLEQSIQ---------------AGRAQL 524
Cdd:COG3096 911 FIQQHGK----ALAQLEPLVAVLQSDPEQFEQlqaDYLQAKEQQRRLKQQIFALSEVVQrrphfsyedavgllgENSDLN 986
|
170 180 190
....*....|....*....|....*....|....*
gi 568955199 525 ETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 559
Cdd:COG3096 987 EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL 1021
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
381-548 |
4.58e-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: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 451
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSiqagraqLETILRSL 531
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170
....*....|....*..
gi 568955199 532 KCTQDDINQARSKLSQL 548
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEI 664
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
382-548 |
4.71e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDI---REKEEAIRQKT----SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELkelAEKRDELNAQVkelrEEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMlsdvRQKCQDETQTISSLKTQIQS-----QESDL-KSQEDDL----NRAKSELNRLQQEETQ------LEQSIQ 518
Cdd:COG1340 95 DELRKE----LAELNKAGGSIDKLRKEIERlewrqQTEVLsPEEEKELvekiKELEKELEKAKKALEKneklkeLRAELK 170
|
170 180 190
....*....|....*....|....*....|
gi 568955199 519 AGRAQLETILRSLKCTQDDINQARSKLSQL 548
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQELHEEMIEL 200
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
382-564 |
5.37e-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: 53.53 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQeIAQLQREKysleQDIREKEEAIRQKTSEVQ----ELQNDLDR-------------------ET------SS 432
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 433 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI------------------QSQESDLKSQED 494
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 495 DLNR-----------AKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYD 563
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
.
gi 568955199 564 Q 564
Cdd:TIGR02169 392 E 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-550 |
6.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 394 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 458
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 459 ---------DMLSDVRQKC------QDETQTISSLKTQIQSQESDLKSQEDDLNRA--KSELNRLQQEETQLEQ---SIQ 518
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEeleELR 452
|
170 180 190
....*....|....*....|....*....|..
gi 568955199 519 AGRAQLETILRSLKcTQDDINQARSKLSQLQE 550
Cdd:COG4717 453 EELAELEAELEQLE-EDGELAELLQELEELKA 483
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
395-515 |
6.60e-07 |
|
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: 48.76 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 395 QREKYSLEQDIREKEEAIRQKtsevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQT 474
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568955199 475 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQ 515
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
377-612 |
7.14e-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: 52.65 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 377 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 452
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 453 QKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQEsdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRAQLETILRSLk 532
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRAKL- 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 533 ctQDDINQARSKLSQLQES--HLEAHRSLEQYDQVPDGVSGTSL-PDLATLNEGILLAERGGFGamDDPFKNKALLFSNN 609
Cdd:COG5185 509 --ERQLEGVRSKLDQVAESlkDFMRARGYAHILALENLIPASELiQASNAKTDGQAANLRTAVI--DELTQYLSTIESQQ 584
|
...
gi 568955199 610 SQE 612
Cdd:COG5185 585 ARE 587
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
383-564 |
7.42e-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: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 462
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVRQKCQD------ETQTISSLKTQIQSQESDLKSQE--DDLNRAKSELNRLQQEETQLEQsIQAGRAQLETILRSL--K 532
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHKELEEELEA-HEPRLKSLNELAEELleE 175
|
170 180 190
....*....|....*....|....*....|..
gi 568955199 533 CTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:cd00176 176 GHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-560 |
8.20e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQKCQDEtqtissLKTQIQSQES------DLKSQEDDLnraKSELNRLQQEETQLEQSiqagRAQLETILRSLKCT 534
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPfyneylELKDAEKEL---EREEKELKKLEEELDKA----FEELAETEKRLEEL 645
|
170 180 190
....*....|....*....|....*....|.
gi 568955199 535 QDDINQARSKLSQ-----LQESHLEAHRSLE 560
Cdd:PRK03918 646 RKELEELEKKYSEeeyeeLREEYLELSRELA 676
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
383-557 |
8.70e-07 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 52.00 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 446
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 ---LD-----------------EMDQQKAKLR---DMLSDVRQKcqdetqTISSLK---TQIQSQEsdlKSQEDDLNRAK 500
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQE------TIAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 501 SELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHR 557
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
382-514 |
8.88e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 452
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 453 QKAKLRDMlsdvRQKCQDETQTISSLkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 514
Cdd:PRK12704 129 KEEELEEL----IEEQLQELERISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-555 |
9.48e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAiRQKTSEVQELQNDLDRETssLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQ-------------------IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgra 522
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK--- 491
|
170 180 190
....*....|....*....|....*....|...
gi 568955199 523 qlETILRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:PRK03918 492 --ESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
389-542 |
9.62e-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: 52.65 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 449
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 450 MDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL------------NRAKSELNRLQQE-------E 510
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190
....*....|....*....|....*....|..
gi 568955199 511 TQLEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-477 |
1.04e-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: 51.69 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
90
....*....|....*.
gi 568955199 462 SDVRQKCQDETQTISS 477
Cdd:COG4942 230 ARLEAEAAAAAERTPA 245
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
382-545 |
1.06e-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: 52.34 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 444
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 445 DRLDEMDQQ--KAK---------LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE--- 510
Cdd:pfam05667 415 QRLVELAGQweKHRvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568955199 511 --TQ--LE--QSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
403-564 |
1.13e-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: 52.48 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 403 QDIREKEEAIRQktsEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 482
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 483 QSQESDLKSQEDDLN-----RAKSELNR------LQQEETQLEQSI------QAGRAQLETILRSLKCTQDDinQARSKL 545
Cdd:pfam01576 267 RELEAQISELQEDLEseraaRNKAEKQRrdlgeeLEALKTELEDTLdttaaqQELRSKREQEVTELKKALEE--ETRSHE 344
|
170 180
....*....|....*....|...
gi 568955199 546 SQLQE---SHLEAHRSL-EQYDQ 564
Cdd:pfam01576 345 AQLQEmrqKHTQALEELtEQLEQ 367
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
382-550 |
1.17e-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: 52.48 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKTSEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170
....*....|....*.
gi 568955199 535 QDDINQARSKLSQLQE 550
Cdd:pfam01576 179 SKLKNKHEAMISDLEE 194
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
381-552 |
1.21e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDdisQEIAQLQREKYSLEQDIREKEEAI---RQKTSE-VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:PHA02562 176 IRELN---QQIQTLDMKIDHIQQQIKTYNKNIeeqRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LRDMLSDVRQK-----------------------CQDETQTISS---LKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 510
Cdd:PHA02562 253 PSAALNKLNTAaakikskieqfqkvikmyekggvCPTCTQQISEgpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955199 511 TQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH 552
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-553 |
1.22e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQRekysLEQDIREKEEAIRQKTSEvQELQNDLDR-ETSSLQELEA---QKQDAQDRLDEMDQQKAK 456
Cdd:COG4717 336 PEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LRDMLSDVRQkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE----ET-----QLEQSIQAGRAQLETI 527
Cdd:COG4717 411 LEELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAEleqlEEdgelaELLQELEELKAELREL 488
|
170 180
....*....|....*....|....*....
gi 568955199 528 LR---SLKCTQDDINQARSKLSQLQESHL 553
Cdd:COG4717 489 AEewaALKLALELLEEAREEYREERLPPV 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-550 |
1.30e-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: 52.36 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM----------- 450
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimerfqmelk 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 ------DQQKAKLRDM-----LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:TIGR00606 803 dverkiAQQAAKLQGSdldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
|
170 180 190
....*....|....*....|....*....|....
gi 568955199 520 GRA---QLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:TIGR00606 883 RQQfeeQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
363-529 |
1.70e-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: 51.61 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 363 GTPIPDSSSTLAsgeftgvKEL--DDISQEIAQLQREKYSLeqdiREK-EEAIRQKTSEVQELqndLDRETSSLQELEAQ 439
Cdd:pfam05622 261 LSPSSDPGDNLA-------AEImpAEIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 440 KQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDEtqtiSSLKtqiqsqeSDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:pfam05622 327 NRLANQRILELQQQVEELQKALQEQGSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDS 395
|
170
....*....|....
gi 568955199 520 GRAQ----LETILR 529
Cdd:pfam05622 396 NLAQkideLQEALR 409
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
382-567 |
1.84e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180
....*....|....*....|....*.
gi 568955199 542 RSKLSQLQESHLEAHRSLEQYDQVPD 567
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELEL 265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
400-564 |
2.02e-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: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 400 SLEQDIREKEEAI--------------RQKTSEVQELQNDLdretsslQELEAQKQDAQDRLDE----MDQQKAKLRD-- 459
Cdd:TIGR02169 643 TLEGELFEKSGAMtggsraprggilfsRSEPAELQRLRERL-------EGLKRELSSLQSELRRienrLDELSQELSDas 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 460 -MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLkcTQDDI 538
Cdd:TIGR02169 716 rKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRI 793
|
170 180
....*....|....*....|....*.
gi 568955199 539 NQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQ 819
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
377-549 |
2.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 377 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKTSEVQELQNDLDRET-SSLQELEAQKQ---------- 441
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneyl 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 442 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESdlKSQEDDLNRAKSELNRLQQEETQLEQSIQ 518
Cdd:PRK03918 606 elkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|....
gi 568955199 519 AGRAQLETI---LRSLKCTQDDINQARSKLSQLQ 549
Cdd:PRK03918 684 ELEKRREEIkktLEKLKEELEEREKAKKELEKLE 717
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
414-555 |
2.44e-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: 49.61 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 414 QKTSEVQELQNDLdretSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQTISSLKTQIQ 483
Cdd:pfam12795 14 AKKKLLQDLQQAL----SLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLEELEQRLL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 484 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI---LRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:pfam12795 89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrnrLNGPAPPGEPLSEAQRWALQAELAALKA 163
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
384-540 |
2.57e-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: 50.62 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKTSEV-----QELQ 423
Cdd:pfam03148 139 LEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDNieraeKERA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 424 N------DLD--RETSSlQELEAQKQDA----QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLK- 490
Cdd:pfam03148 219 AsaqlreLIDsiLEQTA-NDLRAQADAVnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKl 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 491 SQ---EDDLNRAKSEL------NRLQQEETQLEQSIQAGRAQL---ETILRSLKCTQDDINQ 540
Cdd:pfam03148 298 AQtrlENRTYRPNVELcrdeaqYGLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-500 |
2.71e-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: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREkysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 463
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 568955199 464 VRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAK 500
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
400-555 |
2.97e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.05 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 400 SLEQDIREKEEAIRQktsEVQELQNDLDRETSSL-------QELEAQKQDAQDRLDEMdQQKAKL----------RDMLS 462
Cdd:COG1842 16 ALLDKAEDPEKMLDQ---AIRDMEEDLVEARQALaqvianqKRLERQLEELEAEAEKW-EEKARLalekgredlaREALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 463 DVrqkcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQlETILRSLkcTQDDINQAR 542
Cdd:COG1842 92 RK----AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEAL--SGIDSDDAT 164
|
170
....*....|....*
gi 568955199 543 SKLSQLQES--HLEA 555
Cdd:COG1842 165 SALERMEEKieEMEA 179
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
382-550 |
3.02e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 48.91 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQKCQDETQTISSLKTQIQ---SQESDLKSQED--------DLNRAKSELNRLQQEETQLEQSIQAgRAQLETIL- 528
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNllkARLKAAKAQEAvqtslgslSTSSATDSFERIEEKIEEREARADA-AAELASAVd 191
|
170 180
....*....|....*....|....
gi 568955199 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 ... |
381-509 |
3.14e-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: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREkeeaIRQKTSEVQEL-QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 459
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQ----LKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568955199 460 MLSDVRQKCQDetqtissLKTQIQSQESDLKS----QEDDLNRAKSELNRLQQE 509
Cdd:smart00787 240 KIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
381-603 |
3.19e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 457
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 458 RDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlqqeetqleQSIQAGRAQLETILRSLKCTQDD 537
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL-----------QEFKILKDKKDAKIRELEARVSD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 538 INQARSKLSQLQESHLEAHRSLEQ-YDQVPDGVSgTSLPDLATLNEGILLAERGgfgamddpFKNKA 603
Cdd:pfam15921 630 LELEKVKLVNAGSERLRAVKDIKQeRDQLLNEVK-TSRNELNSLSEDYEVLKRN--------FRNKS 687
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
391-542 |
3.21e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 391 IAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 451
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLN------------RAKSELNRLQQE-------ETQ 512
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgaeeRARARRDELHARlsanrsrRNQ 1078
|
170 180 190
....*....|....*....|....*....|
gi 568955199 513 LEQSIQAGRAQLETILRSLKCTQDDINQAR 542
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
451-531 |
3.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 530
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 568955199 531 L 531
Cdd:COG3883 95 L 95
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
382-497 |
3.78e-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: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110
....*....|....*....|....*....|....*....
gi 568955199 462 SDVRQKCQ---DETQTISSLKTQIQSQESDLKSQEDDLN 497
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDII 679
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
409-564 |
3.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 409 EEAIRqktsEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQTISSLKTQI 482
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 483 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRAQLETILRslkctqdDINQARSKLSQLQeshleahRSLEQ 561
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER-------EIERLERELEERE-------RRRAR 363
|
...
gi 568955199 562 YDQ 564
Cdd:COG4913 364 LEA 366
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
425-551 |
3.80e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 425 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL-NRAKSE- 502
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALy 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 503 ---------------------------LNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
402-526 |
3.85e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 49.85 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 402 EQDIREKEEAIRQKTSEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDET 472
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPNSPQVRQLR 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 473 QTISSLKTQIQSQESDL--KSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLET 526
Cdd:COG3524 256 RRIAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
385-547 |
4.00e-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: 50.52 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE----------LEAQKQDAQDRlDEMDQqk 454
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNrwrekvfalmVQLKAQDLEHR-DSVKQ-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 akLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam07111 336 --LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
170
....*....|...
gi 568955199 535 QDDINQARSKLSQ 547
Cdd:pfam07111 414 QIWLETTMTRVEQ 426
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
385-558 |
4.37e-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: 50.12 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 453
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 KAKLRDMLSDVRQK--CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSL 531
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSY 438
|
170 180
....*....|....*....|....*..
gi 568955199 532 kcTQDDINQARSKLsqlqeSHLEAHRS 558
Cdd:pfam05557 439 --SKEEVDSLRRKL-----ETLELERQ 458
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
289-362 |
4.49e-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: 4.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 289 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKEQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 362
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-565 |
5.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 435 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 514
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568955199 515 QSIQAGRAQLETIlrslkctQDDINQARSKLSQLQES--HLEAHRSLEQYDQV 565
Cdd:TIGR02169 751 QEIENVKSELKEL-------EARIEELEEDLHKLEEAlnDLEARLSHSRIPEI 796
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
392-529 |
6.94e-06 |
|
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: 46.57 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 392 AQLQREKYslEQDIREKEEAIRQKTSEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 471
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 472 TQTIsslktQIQSQESDLKSQEDD----LNRAKselnRLQQEetqlEQSIQAGRAQLETILR 529
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
433-561 |
8.56e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.48 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 433 LQELEAQKQDAQDRLDEMDQQKAKLRD---MLSDVRQKCQDETQTISSLKTQIQSQESDLKS-QEDDLNRAKSELNRLQQ 508
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKeleLLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568955199 509 EETQLEQSIqagrAQLETILRSLKctqDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:smart00787 219 EIMIKVKKL----EELEEELQELE---SKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-564 |
8.69e-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: 49.40 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIREKEeairqktSEVQELQNDL--------DRET------SSLQELEA-------QKQD 442
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALE-------SENAELQAELrtlqqakqDSEHkrkkleGQLQELQArlseserQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 443 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLksQEDdlNRAK----SELNRLQQEET----QLE 514
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL--QEE--TRQKlnlsTRLRQLEDERNslqeQLE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568955199 515 QSIQAGRA---QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:pfam01576 507 EEEEAKRNverQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
382-484 |
8.82e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 45.64 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKtseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKK---EQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|...
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQS 484
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLEE 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
390-550 |
8.88e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 390 EIAQLQREKYSLEQDIREKE--EAIRQKTSEVQELQNDLDRETSSL----QELEAQKQD-------AQDRLDEMdQQKAK 456
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEdhEKIQHLEEEYKKEINDKEKQVSLLliqiTEKENKMKDltflleeSRDKANQL-EEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LRDM-LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE-ETQLEQSIQAGRAQ----------- 523
Cdd:pfam05483 279 LQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEkEAQMEELNKAKAAHsfvvtefeatt 358
|
170 180 190
....*....|....*....|....*....|....*..
gi 568955199 524 --LETILRS----LKCTQDDIN----QARSKLSQLQE 550
Cdd:pfam05483 359 csLEELLRTeqqrLEKNEDQLKiitmELQKKSSELEE 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
382-547 |
9.14e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQ-------LQREKYSLEQDIREKEEAIRQ-------KTSEVQELQ---NDLDRETSSL-----QELEAQ 439
Cdd:pfam15921 569 QQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEfkilkdkKDAKIRELEarvSDLELEKVKLvnagsERLRAV 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 440 KQDAQDR---LDEMDQQKAKLRDMLSD-------VRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 509
Cdd:pfam15921 649 KDIKQERdqlLNEVKTSRNELNSLSEDyevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955199 510 ETQLEQSIQAGRAQLETILRSLKCTQDDINQA----------RSKLSQ 547
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkekhflkeeKNKLSQ 776
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
384-554 |
9.41e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 456
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LrDMLSDvRQKCQ----DETQTISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELNRLQQEETQLeQSIQ 518
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*..
gi 568955199 519 AGRAQLETILRSLKCTQDDINQARS-KLSQLQESHLE 554
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvALDNWRQVHEQ 725
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
382-547 |
9.48e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 451
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQKAKLRDMLSDVRqkcQDETQTISSLKTQIQSqESDLKSQEDDLNRAK-------SELNRLQQEETQLEQsiqagrAQL 524
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRKSlegntqlQDLLQKQRDYLTARI------QRL 239
|
170 180
....*....|....*....|...
gi 568955199 525 ETILRSLkctQDDINQARSKLSQ 547
Cdd:PRK11281 240 EHQLQLL---QEAINSKRLTLSE 259
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
416-552 |
1.02e-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: 48.09 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 416 TSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQtisslktqiqSQESDLKSQEDD 495
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 496 LNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQAR----SKLSQLQESH 552
Cdd:smart00787 220 IMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQL 280
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
382-613 |
1.24e-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: 48.81 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslqELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----EAEDMLACEQHALLRKLQPEQDLQDVR 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQtissLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEetQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:TIGR00618 632 LHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSIRVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 542 RSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERggfgAMDDPFKNKALLFSNNSQEL 613
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH----QARTVLKARTEAHFNNNEEV 770
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
381-550 |
1.29e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 453
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 -------------KAKLRDM---LSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSI 517
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190
....*....|....*....|....*....|...
gi 568955199 518 QAGRAQLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
381-509 |
1.34e-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: 47.88 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 460
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568955199 461 lsdvrqkcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 509
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
382-565 |
1.49e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqqkakLRDML 461
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE-------LREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKcqdetqtisslktqIQSQESDLKSQEDDLNRAKselnRLQQE------ETQLEQSIQAG--------RAQLETI 527
Cdd:PRK02224 422 DELRER--------------EAELEATLRTARERVEEAE----ALLEAgkcpecGQPVEGSPHVEtieedrerVEELEAE 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 568955199 528 LRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 565
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL 521
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
382-562 |
1.52e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ----QEETQLEQsiqagRAQLETILRSLKCTQDD 537
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 568955199 538 IN---QARSKLSQLQESHLEAHRSLEQY 562
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-550 |
1.61e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 361 ERGTPIPDSSStlasgeftgVKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKTSEVQELQNDLDRetsslqeLEAQK 440
Cdd:PRK02224 456 ECGQPVEGSPH---------VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 441 QDAQDRLDEMDQQKAKLRDMLSDVRQKCQDetqtissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAg 520
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES- 590
|
170 180 190
....*....|....*....|....*....|
gi 568955199 521 RAQLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREALAE 620
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
1.62e-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: 1.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568955199 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 ... |
383-570 |
2.20e-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: 48.25 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEairqktsEVQELQNDLDRETS-------SLQELEAQKQDAQDRLDEMDQQKA 455
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEE-------ELQAALARLEEETAqknnalkKIRELEAQISELQEDLESERAARN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 456 K--------------LRDMLSDVrqkcQDETQTISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEET--------Q 512
Cdd:pfam01576 289 KaekqrrdlgeeleaLKTELEDT----LDTTAAQQELRSKREQEVTELKkALEEETRSHEAQLQEMRQKHTqaleelteQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 513 LEQ-------------SIQAGRAQLETILRSLKCTQDDINQARSKL-SQLQESHLEAHRSLEQYDQVPDGVS 570
Cdd:pfam01576 365 LEQakrnkanlekakqALESENAELQAELRTLQQAKQDSEHKRKKLeGQLQELQARLSESERQRAELAEKLS 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-565 |
2.21e-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: 48.13 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 408 KEEAIRQ--KTSE----VQELQNDLDRETSSLQ----------ELEAQKQDAQ-----DRLDEMDQQKAKLRDMLSDVRQ 466
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELERQLKSLErqaekaerykELKAELRELElallvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 467 KCQDETQTISslKTQIQSQESDLKSQEDDlnrakSELNRLQQE--ETQ-----LEQSIQAGRAQLETILRSLKCTQDDIN 539
Cdd:TIGR02168 254 ELEELTAELQ--ELEEKLEELRLEVSELE-----EEIEELQKElyALAneisrLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180
....*....|....*....|....*.
gi 568955199 540 QARSKLSQLQEshlEAHRSLEQYDQV 565
Cdd:TIGR02168 327 ELESKLDELAE---ELAELEEKLEEL 349
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
400-550 |
2.24e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 400 SLEQDIREKEEAIRQK------TSEVQELQNDLDRETSSLQELEAQKQDAQDR-------LDEMDQQKAKLRDMLSDVRQ 466
Cdd:PRK10929 79 KLSAELRQQLNNERDEprsvppNMSTDALEQEILQVSSQLLEKSRQAQQEQDRareisdsLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 467 KCQDETQTISSLK----TQIQSQESDLKSQEDDLNRA------KSELNRLQQE-----ETQLEQSIQAGRAQLeTILRsl 531
Cdd:PRK10929 159 RLQTLGTPNTPLAqaqlTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQALRNQL-NSQR-- 235
|
170
....*....|....*....
gi 568955199 532 kctQDDINQARSKLSQLQE 550
Cdd:PRK10929 236 ---QREAERALESTELLAE 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-559 |
2.39e-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: 48.19 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 282 LKTDLDLDGYVSGQEVKEIFM-HSGLTQnllaHIWA-LADTRQ-TGKLSKEQFALA-MYF--IQQKVSKGIdppQVLSPD 355
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLsHEGVLQ----EIRSiLVDFEEaSGKKIYEHDSMStMHFrsLGSAISKIL---RELDTE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 356 MVPPSERGTPIPDSSSTLASGEFTGVKEL-----DDISQEIAQLQREKYSLEQ---DIREKEEAIRQKTSEVQEL---QN 424
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLlqqhqDRIEQLISEHEVEITGLTEkasSARSQANSIQSQLEIIQEQarnQN 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 425 --------DLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDD 495
Cdd:pfam15921 313 smymrqlsDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 496 LNRAKSELNRLQQEETQLEQSIQAGRAQ----------LETILRSLKC-TQDDINQARSKLSQLQEShLEAHRSL 559
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRElddrnmevqrLEALLKAMKSeCQGQMERQMAAIQGKNES-LEKVSSL 466
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
432-564 |
2.69e-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: 44.70 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 432 SLQELEAQKQ--DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSlktQIQSQESDLKsqedDLNRAKSELNRLQQE 509
Cdd:pfam07321 9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRLYA---EIQGKLVLLK----ELEKVKQQVALLREN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 510 ETQLEQSIQAGRAQLEtilrslkctqddinQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:pfam07321 82 EADLEKQVAEARQQLE--------------AEREALRQARQALAEARRAVEKFAE 122
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
382-550 |
2.78e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYS---LEQDIREKEEaiRQKTSEV-QELQNDLDRETSSL-QELEAQKQ--DAQDRLDEMDQQK 454
Cdd:COG1340 92 EELDELRKELAELNKAGGSidkLRKEIERLEW--RQQTEVLsPEEEKELVEKIKELeKELEKAKKalEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQSqesdLKSQEDDLNRaksELNRLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRK---EADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
170
....*....|....*.
gi 568955199 535 QDDINQARSKLSQLQE 550
Cdd:COG1340 243 RKELKKLRKKQRALKR 258
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
388-597 |
3.00e-05 |
|
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: 46.25 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 467
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 468 CQDETQT----------ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLkctQDD 537
Cdd:pfam06008 119 DLSRMLAeaqrmlgeirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDL---REL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 538 INQARSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEG--ILLAERGGFGAMDD 597
Cdd:pfam06008 196 LREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTArdSLDAANLLLQEIDD 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-560 |
3.58e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQdaqdRLDEMDQQKAKLRDML 461
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKS---------ELNRLQQEETQLEQSIQAGRAQLETILRSLK 532
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180
....*....|....*....|....*...
gi 568955199 533 CTQDDINQARSKLSQLQESHLEAHRSLE 560
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLE 355
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-550 |
3.76e-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: 47.35 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYS---------LEQDIREKEEAIRQKTSEVQELQ-----------------NDLDRETSSLQEL 436
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGsdldrtvqqVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktNELKSEKLQIGTN 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 437 EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQ----IQSQESDLKSQEDDLNRAKSELNRLQQEETQ 512
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
170 180 190
....*....|....*....|....*....|....*...
gi 568955199 513 LEQSIQAGRAqletilRSLKCTQDDINQARSKLSQLQE 550
Cdd:TIGR00606 960 IENKIQDGKD------DYLKQKETELNTVNAQLEECEK 991
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
386-513 |
3.79e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREKYSLE---------QDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQ-------HSLEKLDTAIDELEEIMDEFNEQSKK 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 457 LRDMLSDVRQkcqdETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 513
Cdd:PHA02562 339 LLELKNKIST----NKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
382-542 |
3.84e-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: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNdlDRETSSLQELEAQK--QDAQDRLDEMDQQKAKLRD 459
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAE--ERRQRLEEALDLQQffRDADDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 460 MLSDvrqkcqDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE-----TQLEQSIQAGRAQLETILRSLKCT 534
Cdd:cd00176 132 EDLG------KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdadEEIEEKLEELNERWEELLELAEER 205
|
....*...
gi 568955199 535 QDDINQAR 542
Cdd:cd00176 206 QKKLEEAL 213
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
382-550 |
3.90e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 461
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 sdvrqkcqdetQTISSLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQA 541
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*....
gi 568955199 542 RSKLSQLQE 550
Cdd:pfam15905 320 EQEHQKLQQ 328
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
383-565 |
3.94e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL----------------QELEAQKQDAQDR 446
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehalsirvlpKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 LDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNRLQ------------ 507
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassSLGSDLAAREDALNQSLKELMHQArtvlkarteahf 764
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 508 -------------QEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSklSQLQESHLEAHRSLEQYDQV 565
Cdd:TIGR00618 765 nnneevtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP--SDEDILNLQCETLVQEEEQF 833
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
389-561 |
4.02e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQRekySLEQDIREKEEAI---RQK-TSEVQELQNDLD---RETSSL----QELEAQKQDAQDRL-------DEM 450
Cdd:pfam01576 327 QEVTELKK---ALEEETRSHEAQLqemRQKhTQALEELTEQLEqakRNKANLekakQALESENAELQAELrtlqqakQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRS 530
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 568955199 531 -------LKCTQDDinqaRSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam01576 484 klnlstrLRQLEDE----RNSLQEQLEEEEEAKRNVER 517
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
480-550 |
4.16e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 4.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 480 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-560 |
4.66e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 361 ERGTPIPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK 440
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 441 QDAQDRLDEMDQ--------------QKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEdDLNRAKSELNRL 506
Cdd:PRK02224 436 RTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERL 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 507 QQEETQLEQSIQAGRAQLETilRSLKCTQ-----DDIN-QARSKLSQLQESHLEAHRSLE 560
Cdd:PRK02224 515 EERREDLEELIAERRETIEE--KRERAEElreraAELEaEAEEKREAAAEAEEEAEEARE 572
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-554 |
5.14e-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: 47.04 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 373 LASGEFTGVK-ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndLDRETSSLQELEAQKQDAQDRLDEMD 451
Cdd:pfam15921 353 LANSELTEARtERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL---WDRDTGNSITIDHLRRELDDRNMEVQ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQKAKLRDMLSDVRQKCQDETQTIS----SLKtQIQSQESDLKSQEDDLNRAKSELNrlqQEETQLEQS---IQAGRAQL 524
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQMAAIQgkneSLE-KVSSLTAQLESTKEMLRKVVEELT---AKKMTLESSertVSDLTASL 505
|
170 180 190
....*....|....*....|....*....|..
gi 568955199 525 ETILRSLKCTQDDINQARSKLS-QLQE-SHLE 554
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDlKLQElQHLK 537
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
379-655 |
5.36e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 379 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 458
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 459 D------MLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRA-KSELNRLQQEETQLEQSIQAGRAQLETILRSL 531
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 532 KCTQDDINQAR-----SKLSQLQESHLEAHRSL--------EQYDQVPDGVSGtslpDLATLNEGILLAER--GGFGAMD 596
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVrskkedlnEELTQIESRVST----LKATLEKLRAKLERqlEGVRSKL 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 597 DPFKNKALLFSNNSQELHPDPFQAEDPFKSdpFKGADPFKGDPFQSDPFSEQQTAATDP 655
Cdd:COG5185 520 DQVAESLKDFMRARGYAHILALENLIPASE--LIQASNAKTDGQAANLRTAVIDELTQY 576
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
385-561 |
5.65e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKySLEQDirekEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 464
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 465 RQKcQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL--NRLQQEETQLEQSIQAGRAQ-LETILRSLKCTQDDINQA 541
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAQAALYANSQRLQqIRNLLKGGKVGGKALRPS 192
|
170 180
....*....|....*....|
gi 568955199 542 RSKLSQLQESHLEAHRSLEQ 561
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR 212
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
382-563 |
5.84e-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: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------TSEVQELQNDLDRETSSLQEL 436
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 437 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 510
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 511 TQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESH--LEAHRSLEQYD 563
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIreLEAQISELQED 279
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-509 |
5.89e-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: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 370 SSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDR 446
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 447 LDEMdqqKAKLRDMLSDV------RQKCQDEtqtISSLKTQIQSQEsdlkSQEDDLNRAKselNRLQQE 509
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLealeegKKRLQRE---LEALTQQLEEKA----AAYDKLEKTK---NRLQQE 581
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
382-502 |
6.24e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKTSEVQELQNDLD-----------RETSSLQELEAQKQ-- 441
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 442 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDL------KSQEddLNRAKSE 502
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
392-525 |
6.56e-05 |
|
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: 42.96 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 392 AQLQREKysleQDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDVRQKC 468
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEEKEIEL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 469 QDETQTISSLKTQIQSqesdlksqeddlnrAKSELNRLQQeetQLEQSIQAGRAQLE 525
Cdd:pfam18595 74 RELERREERLQRQLEN--------------AQEKLERLRE---QAEEKREAAQARLE 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-526 |
6.60e-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: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREkysleqdIREKEEAIRQKTSEVQELQNDLDR----ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDmlsdv 464
Cdd:COG4913 338 DRLEQLERE-------IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEE----- 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 465 rqkcqdetqtissLKTQIQSQESDLKSQEDDLnraKSELNRLQQEETQLEQSIQAGRAQLET 526
Cdd:COG4913 406 -------------ALAEAEAALRDLRRELREL---EAEIASLERRKSNIPARLLALRDALAE 451
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
382-551 |
7.15e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIR---------EKE-EAIRQKTSEVQELQNDLDRetsSLQELEAQKQ---------- 441
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDrvkqsytlnESElESVRQLEKQLESLEKQYDE---ITERIAEQEIayselqeele 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 442 DAQDRLDEMDQQKAKLRDMLSDVRqkcQDET---QTISSLKTQIQS-----QESDL----KSQEDDLNRAKSELNRLqqe 509
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLR---KDELearEKLERYRNKLHEikrylEKSNLpglpEDYLEMFFEVSDEIEAL--- 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955199 510 ETQLEQsiqaGRAQLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:PRK04778 461 AEELEE----KPINMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
417-560 |
7.92e-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: 45.44 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 417 SEVQELQNDLDRETSSlQELEAQKQDAQDRLDEMD------QQKA-KLRDMLSDVRQKCQDETQTISSLKTQIQSQ--ES 487
Cdd:cd22656 94 AEILELIDDLADATDD-EELEEAKKTIKALLDDLLkeakkyQDKAaKVVDKLTDFENQTEKDQTALETLEKALKDLltDE 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 488 DLKSQEDDLNRAKSELNRLQQEET-QLEQSIQAGRAQLETI---LRSLKCTQDDINQARSKLSQLQESHLEAHRSLE 560
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYAaKLKAKIDELKALIADDeakLAAALRLIADLTAADTDLDNLLALIGPAIPALE 249
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
401-509 |
9.13e-05 |
|
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: 44.63 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 401 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLkt 480
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 568955199 481 qiqsqESDLKSQEDDLNRAKSELNRLQQE 509
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
300-571 |
9.23e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 300 IFMHSGLTQNL-------LAHIWALADTRQTGKLSKEQFALAMYFIQ--QKVSKGIDPPQVLSPDmvPPSERGTPIPDSS 370
Cdd:COG5022 726 VFFKAGVLAALedmrdakLDNIATRIQRAIRGRYLRRRYLQALKRIKkiQVIQHGFRLRRLVDYE--LKWRLFIKLQPLL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 371 STLASGEFTG--VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK--QDAQDR 446
Cdd:COG5022 804 SLLGSRKEYRsyLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQrvELAERQ 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 LDEMDQQKAKL------------------RDMLSDVRQKCQDETQTISSLKTQIQsqESDLKSQEDDLNRAKSELNRLQQ 508
Cdd:COG5022 884 LQELKIDVKSIsslklvnleleseiielkKSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHE 961
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 509 EETQLEQSIQagraQLETILRSLKCTQDDINQARSKLSQLQEShLEAHRSleQYDQVPDGVSG 571
Cdd:COG5022 962 VESKLKETSE----EYEDLLKKSTILVREGNKANSELKNFKKE-LAELSK--QYGALQESTKQ 1017
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
339-536 |
9.94e-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: 45.87 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 339 QQKVSKGIDPPQVLSPDMVPPSERgtpiPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLE---QDIREKEEAI--- 412
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSE----LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 413 -RQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR---DMLSDVRQKCqdeTQTISSLKTQIQSQESD 488
Cdd:pfam05483 445 lQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcDKLLLENKEL---TQEASDMTLELKKHQED 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568955199 489 LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQD 536
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD 569
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
401-549 |
1.02e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 401 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQTISSLKT 480
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 481 QIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQAGRAQLETILRSLkctqdDINQARSKLSQLQ 549
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQ-------IAALRRQLAALEAAL-----DASEKRDRESQAK 173
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
432-550 |
1.08e-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: 44.60 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 432 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQTISSLKTQIQS--QESDLKSQEDDL 496
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 497 NRAKSEL-NRLQQEETQLeQSIQAGRAQLETILRSLkctQDDINQARSKLSQLQE 550
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQNQLAQLNSQLIEL---QTRPERAQQQLSEARQ 127
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
381-550 |
1.14e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD-------- 451
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYdELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyek 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 --------QQKAKLRDMLSDVRQKCQDETQTISSLKTQIQsqesDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQ 523
Cdd:PHA02562 284 ggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAID----ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
170 180
....*....|....*....|....*..
gi 568955199 524 LETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:PHA02562 360 AKKVKAAIEELQAEFVDNAEELAKLQD 386
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
384-561 |
1.18e-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: 45.98 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKTSEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 455
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 456 KLRDMLSDVRQKCQDEtqtisslKTQIQSQESDLKSQEDDLNrAKSELnRLQQEETQLEqsIQAGRAQLETILRSLKCTQ 535
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQAT-ATPEL-LLQLENFDER--IERAREEQEAANAEVERLQ 491
|
170 180
....*....|....*....|....*.
gi 568955199 536 DDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEE 517
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
382-519 |
1.22e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQEL----QNDLDRET-SSLQELEAQKQDAQDRLDEMDQQKAK 456
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAlekgREDLAREAlERKAELEAQAEALEAQLAQLEEQVEK 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 457 LRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE----DDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:COG1842 117 LKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA 183
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
401-552 |
1.25e-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: 45.61 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 401 LEQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQ 473
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 474 TISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRAQLETILRSLKCTQDDINQARSK---LSQLQ 549
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKRELESEIKKLTHDIKLKEEQIRELEIKvqeLRKYK 559
|
...
gi 568955199 550 ESH 552
Cdd:pfam09726 560 ESE 562
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
393-551 |
1.26e-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: 45.50 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 393 QLQREKYSLEQdIREKEEAIRQKtsEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvRQKCQD 470
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKLE------LEKEKR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 471 ETQTISSLKTQIQSQESDLKSQ---EDDLNR--------------AKSELNRLQQEETQLEQSIQAGRAQLETILRSL-- 531
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQamiEEERKRkllekemeerqkaiYEEERRREAEEERRKQQEMEERRRIQEQMRKATee 564
|
170 180
....*....|....*....|
gi 568955199 532 KCTQDDINQARSKLSQLQES 551
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVES 584
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
380-475 |
1.32e-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: 42.57 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 380 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 458
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 568955199 459 DMLSDVRQKCQDETQTI 475
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
394-561 |
1.36e-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: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 394 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS---DVRQKCQD 470
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQateDAKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 471 ETQtisSLKTQIqsqESDLKSQEDDLNRAKSELNR-LQQEETQLE----QSIQA--GRAQLETILRSLKCTQDDINQARS 543
Cdd:pfam01576 721 NMQ---ALKAQF---ERDLQARDEQGEEKRRQLVKqVRELEAELEderkQRAQAvaAKKKLELDLKELEAQIDAANKGRE 794
|
170 180
....*....|....*....|..
gi 568955199 544 ----KLSQLQESHLEAHRSLEQ 561
Cdd:pfam01576 795 eavkQLKKLQAQMKDLQRELEE 816
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
403-550 |
1.59e-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: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 403 QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI 482
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 483 QSQESDLKSQE-DDLNRakselnRLQQEETQLEQSIQAGRaqLETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:cd16853 91 EYVQKNLTDEElADWKR------RQQIACIGGPPNICLDR--LENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
430-561 |
1.65e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.72 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 430 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELN-- 504
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPig 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 505 -RLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQ--------ARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam00529 137 gISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaenqaeVRSELSGAQLQIAEAEAELKL 202
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
444-550 |
1.70e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 444 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQ 523
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100
....*....|....*....|....*..
gi 568955199 524 LETILRSLKCTQDDINQARSKLSQLQE 550
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEA 158
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
383-512 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSL--EQDIREKEEAIRQKTsEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRdm 460
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkkEQDEASFERLAELRD-ELAELEEELE-------ALKARWEAEKELIEEIQELKEELE-- 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 461 lsdvrqkcqDETQTISSLKTQIQSQESDLKSQEDDLNRAKSE--------------LNRLQQEETQ 512
Cdd:COG0542 482 ---------QRYGKIPELEKELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGERE 538
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-565 |
1.81e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 460
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQkcqdETQTISSLKTQ---IQSQESDLKSQEDDLNRAKSELNRLQQEETQL--------------EQSIQAGRAQ 523
Cdd:PRK04863 910 KRFVQQ----HGNALAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALtevvqrrahfsyedAAEMLAKNSD 985
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568955199 524 LETILRSlkctqdDINQARSKLSQLQESHLEAHRSLEQYDQV 565
Cdd:PRK04863 986 LNEKLRQ------RLEQAEQERTRAREQLRQAQAQLAQYNQV 1021
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
366-564 |
1.89e-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: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 366 IPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQD 445
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 446 RLDEMDQQKAKLRDMLSDVR--QKCQDETQTISSLKTQIQSqesdlKSQEDDLNRAKSELNRLQQEETQLEQSIQagrAQ 523
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDVTimERFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVV---SK 844
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568955199 524 LETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
390-513 |
1.94e-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: 42.43 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 461
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 513
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
397-518 |
2.15e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 397 EKYSLEQDIREKEEAIRQKTSEVQELQNDldretsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTIS 476
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568955199 477 slktQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQ 518
Cdd:COG0542 472 ----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
379-549 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 379 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKTS-------EVQELQNDLDRETSSLQELEAQKQDAQDR- 446
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQI--QSQESDLKSQEDDLNRAKSELNRLQ--- 507
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQvlq 1051
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568955199 508 --QEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:TIGR00606 1052 mkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
385-516 |
2.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 459
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 460 MLSDVRQKCqdetqtiSSLKTQIQSQESDLKSQEddlNRAKSELNRLQQEETQLEQS 516
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA 1114
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
384-505 |
2.42e-04 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 42.68 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLeqdiREKEEAIRQKTsevQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 463
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568955199 464 VRqkCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNR 505
Cdd:pfam16043 81 VS--RDQFDETLEELNQMLQELLDKLEGQEDAWKKALETLSE 120
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
433-554 |
2.48e-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: 43.48 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 433 LQELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL---------------- 496
Cdd:pfam00261 3 MQQIKEELDEAEERLKE-------AMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLaealekleeaekaade 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 497 ---------NRAKSELNRLQQEETQLEQSIQ----AGRaQLETILRSLKCTQDDINQARSKLSQLQE--SHLE 554
Cdd:pfam00261 76 sergrkvleNRALKDEEKMEILEAQLKEAKEiaeeADR-KYEEVARKLVVVEGDLERAEERAELAESkiVELE 147
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
372-565 |
2.49e-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: 43.56 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 372 TLASGEFTGvKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLD 448
Cdd:pfam06008 66 TLAKAQQVN-AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 449 EMDQQKAKLRDMLSDVR---QKCQDETQTissLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQS---IQAGRA 522
Cdd:pfam06008 145 NAEAELKAAQDLLSRIQtwfQSPQEENKA---LANALRDSLAEYEAKLSDLR------ELLREAAAKTRDAnrlNLANQA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568955199 523 QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQV 565
Cdd:pfam06008 216 NLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
382-524 |
2.61e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAI-RQKTSEVQELQNDLdretsslqeleaQKQDAQDRLDEMDQQKAKLRdm 460
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEQIELKERRLaEEAEREEEEFERML------------RKQAEDEEIEQEEAEKRRMK-- 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955199 461 lsdvRQKCQDEtqtissLKTQIQSQEsdlKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQL 524
Cdd:pfam13868 288 ----RLEHRRE------LEKQIEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
382-561 |
2.68e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSeVQELQNDL-DRETSSLQELEAQKQDAQDRL---------DEMD 451
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIeEREQKRQEEYEEKLQEREQMDeiveriqeeDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 -QQKAKLRDMLSDVRQKCQDETQTISSLKtQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL---EQSIQAGRAQLETI 527
Cdd:pfam13868 118 aEEKLEKQRQLREEIDEFNEEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKA 196
|
170 180 190
....*....|....*....|....*....|....
gi 568955199 528 LRslkcTQDDINQARSKLsqLQESHLEAHRSLEQ 561
Cdd:pfam13868 197 QD----EKAERDELRAKL--YQEEQERKERQKER 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
384-557 |
2.88e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 450
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 DQQKAKLRDMLSDVRQKCqDETQT--------ISSL---KTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ---S 516
Cdd:PRK04863 389 EEEVDELKSQLADYQQAL-DVQQTraiqyqqaVQALeraKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsV 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568955199 517 IQAGRAQLETILRSLKCTQDDI------NQARSKLSQLQESHLEAHR 557
Cdd:PRK04863 468 AQAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAEQ 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-506 |
2.92e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 467
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110
....*....|....*....|....*....|....*....
gi 568955199 468 CQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 506
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
382-524 |
3.08e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 450
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 ---DQQKAKLRD-MLSDVRQKCQDETQTISSLKTQIQSQEsdlKSQEDDLNRAKSELNRL---QQEETQLEQSIQAGRAQ 523
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQEEAEKRRM 286
|
.
gi 568955199 524 L 524
Cdd:pfam13868 287 K 287
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
395-565 |
3.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 395 QREKYSLEQDIREKEEAIRQktsevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 472
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 473 -QTISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELNRLQQEETQLEQSIQA--GRAQLETI 527
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 528 LR-------SLKCTQD-------------DINQARSKLSQLQE--SHLEAHRSLEQYDQV 565
Cdd:PRK11281 342 LYqqqqalpSADLIEGladriadlrleqfEINQQRDALFQPDAyiDKLEAGHKSEVTDEV 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-561 |
3.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAI-------RQKTSEvqELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 454
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 AKLRDMLSDVRqkcqdetqTISSLKT---QIQSQESDLKS-QEDDLNRAKSELNRLQQEETQLEqsiqagrAQLETILRS 530
Cdd:PRK03918 483 RELEKVLKKES--------ELIKLKElaeQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLK-------GEIKSLKKE 547
|
170 180 190
....*....|....*....|....*....|....
gi 568955199 531 LKCTQDDINQAR---SKLSQLQESHLEAHRSLEQ 561
Cdd:PRK03918 548 LEKLEELKKKLAeleKKLDELEEELAELLKELEE 581
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
379-560 |
3.86e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 379 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKTSEVQELQNDLDRETSS-------------- 432
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 433 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL-------NR 505
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLaaserarRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 506 LQQEETQLEQSIQAGRAQletilRSLkcTQDDINQARSKLSQLQESHLEAHRSLE 560
Cdd:pfam01576 859 AQQERDELADEIASGASG-----KSA--LQDEKRRLEARIAQLEEELEEEQSNTE 906
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
338-560 |
3.97e-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: 44.04 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 338 IQQKVSkgidppqVLSPDMVPPSERGTPIPDSSSTLASgefTGVKELDDISQ-EIA-----------QLQREK-YSLEQD 404
Cdd:pfam10174 480 LKEKVS-------ALQPELTEKESSLIDLKEHASSLAS---SGLKKDSKLKSlEIAveqkkeecsklENQLKKaHNAEEA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 405 IREKEE---AIRQKTSEVQ-------ELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQKCQDETQT 474
Cdd:pfam10174 550 VRTNPEindRIRLLEQEVArykeesgKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQMKEQNKK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 475 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEEtqleqsiqagraQLETILRSLKCTQDDINQARSKLSQLQESHLE 554
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL------------QLEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
....*.
gi 568955199 555 AHRSLE 560
Cdd:pfam10174 688 KDGHLT 693
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
379-587 |
4.15e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 379 TGVKEldDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK---- 454
Cdd:TIGR00618 693 TYWKE--MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNneev 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 455 -------AKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNrakSELNRLQQEETQLEQSIQAGRAQLETI 527
Cdd:TIGR00618 771 taalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN---LQCETLVQEEEQFLSRLEEKSATLGEI 847
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 528 LRSLKCTQDDINQARSKLSQLQESHLEAHRsLEQYDQVPDGVSGTSLPDLA---TLNEGILLA 587
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDK-LNGINQIKIQFDGDALIKFLheiTLYANVRLA 909
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
382-549 |
4.16e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKE-----------EAIRQKTS---EVQELQNDLDRETSSLQE------------ 435
Cdd:pfam01576 384 SENAELQAELRTLQQAKQDSEHKRKKLEgqlqelqarlsESERQRAElaeKLSKLQSELESVSSLLNEaegkniklskdv 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 436 --LEAQKQDAQDRLDEMDQQK----AKLRDMLSD---VRQKCQDETQTISSLKTQIQS---QESDLKSQ----------- 492
Cdd:pfam01576 464 ssLESQLQDTQELLQEETRQKlnlsTRLRQLEDErnsLQEQLEEEEEAKRNVERQLSTlqaQLSDMKKKleedagtleal 543
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 493 EDDLNRAKSELNRLQQ---EETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQ 549
Cdd:pfam01576 544 EEGKKRLQRELEALTQqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
164-335 |
4.24e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 41.32 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 164 LGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEpvpsilppplippskrkktvfagavpvlpaspppkdslrstpshg 243
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSE--------------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 244 svSSLNSTGSLSP---KHSVKQPPVAWVVPVADKMrFDEIflktDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADT 320
Cdd:COG5126 42 --ADTDGDGRISReefVAGMESLFEATVEPFARAA-FDLL----DTDGDGKISADEFRRLLTALGVSEEEADELFARLDT 114
|
170
....*....|....*
gi 568955199 321 RQTGKLSKEQFALAM 335
Cdd:COG5126 115 DGDGKISFEEFVAAV 129
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
431-555 |
4.47e-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: 40.70 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 431 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISslkTQIQSQESDLKSqeddLNRAKSELNRLQQEE 510
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 511 TQLEQSIQAGRAQLETILRSLKCT----QDDINQARSKLSQLQE------SHLEA 555
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNEqnkllhDQLES 128
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
388-559 |
4.72e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 388 SQEIAQLQRekysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 464
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 465 ---RQKCQDETQTISSLKTQIQSQESDLKSQE-------DDLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLKCT 534
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQETRK 488
|
170 180 190
....*....|....*....|....*....|.
gi 568955199 535 QDDINQARSKLSQL------QESHLEAHRSL 559
Cdd:TIGR00618 489 KAVVLARLLELQEEpcplcgSCIHPNPARQD 519
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
388-515 |
4.75e-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: 43.05 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 388 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQD--------------RLDEMDQQ 453
Cdd:pfam14915 150 SQQLSKAESKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDkvnkyigkqesleeRLAQLQSE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 454 KAKLRDMLSDVRQK----------CQDETQTISSlKTQIQSQESDLKSQEddlnRAK---SELNRLQQEETQLEQ 515
Cdd:pfam14915 230 NMLLRQQLEDAQNKadakektvidIQDQFQDIVK-KLQAESEKQVLLLEE----RNKeliNECNHLKERLYQYEK 299
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-519 |
5.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL 447
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 448 DEMDQ-----QKAK-LRDMLSDVRQKCQDEtqTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 519
Cdd:PRK03918 355 EELEErhelyEEAKaKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
383-520 |
5.42e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEMDQQKAKL 457
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKEAKKEADEI 589
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 458 rdmlsdVRQKCQDETQTISSLKTQiqsqesDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAG 520
Cdd:PRK00409 590 ------IKELRQLQKGGYASVKAH------ELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
469-564 |
5.44e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.18 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 469 QDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL-RSLKCTQDDINQARSKLSQ 547
Cdd:TIGR04320 250 PNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALAN 329
|
90
....*....|....*..
gi 568955199 548 LQESHLEAHRSLEQYDQ 564
Cdd:TIGR04320 330 AEARLAKAKEALANLNA 346
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
367-550 |
5.51e-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: 43.15 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 367 PDSSSTLASGEFTGVKELDDISQEIAQLQRekySLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDR 446
Cdd:pfam04108 156 LSSPSESISLIPTLLKELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 LDEMDQQKAKLRDMLS---DVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAK-------SELNRLQQEETQLEQS 516
Cdd:pfam04108 230 LDEMENNYERLQKLLEqknSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKetiedylSELEDLREFYEGFPSA 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568955199 517 -----IQAGR-----AQLETILRSLkctqddinqaRSKLSQLQE 550
Cdd:pfam04108 310 ygsllLEVERrrewaEKMKKILRKL----------AEELDRLQE 343
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
383-530 |
6.00e-04 |
|
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: 43.09 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 458
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955199 459 dmlsdvrqkcqDETQTISslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRAQlETILRS 530
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSAS 175
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
385-515 |
6.35e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 40.74 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQdirEKEEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 461
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 462 sdvrqkCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL-NRLQQEETQLEQ 515
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
401-550 |
6.61e-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: 42.02 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 401 LEQDIREKEEAIRQKTSEVQELQNDLDRetsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKT 480
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTK----------KQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNA 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 481 qIQSQESDLKSQEDDlnrAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCT--QDDINQARSKLSQLQE 550
Cdd:cd21116 152 -LKNQLNSLAEQIDA---AIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAflQADLKAAKADWNQLYE 219
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
368-550 |
6.95e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 368 DSSSTLASGEfTGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL 447
Cdd:PRK02224 499 ERAEDLVEAE-DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 448 DEMDQQKA----------KLRDMLSDvRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL------NRL---QQ 508
Cdd:PRK02224 575 AELNSKLAelkeriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeARIeeaRE 653
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568955199 509 EETQLEQSIqagrAQLETILRSLKCTQDD----INQARSKLSQLQE 550
Cdd:PRK02224 654 DKERAEEYL----EQVEEKLDELREERDDlqaeIGAVENELEELEE 695
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
392-554 |
6.99e-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: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 392 AQLQREKYSLEQD-IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD 470
Cdd:pfam17097 121 ASLEDEVSQLEDDtLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECWELLNELERLRDQRITVEEQTSN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 471 ETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE--QSIQAGRAQL-ETILRSLKCTQDDINQARSK-LS 546
Cdd:pfam17097 201 EKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEkvDKSSINRTQNdEESIQNTVQLNLLIDMWKSKfII 280
|
....*...
gi 568955199 547 QLQESHLE 554
Cdd:pfam17097 281 HEKISNLE 288
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-561 |
7.03e-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: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-----------DLDRETSSLQELEAQKQ--------- 441
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 442 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE---DDLNRAKSELNRLQQEETQLEQ 515
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955199 516 SiqagrAQLETILR---SLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:TIGR00606 493 N-----SLTETLKKevkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
382-562 |
7.10e-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: 42.25 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEV---QEL------------QNDLDRETSSLQELEAQKQDaqdR 446
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEKEES---K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 447 LDEMDQQKAKLRDMLsdvrQKCQDETQT---------------ISSLKTQIQsqesDLK-SQEDDLNraksELNRLQQEE 510
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEELNFlstykdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 511 TQ-LEQSIQAGRAQLETIL--RSLKCTQDDInQARSKLSQLQESHLEAHRSLEQY 562
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQESL-LQKTRDNQVMLKEIEQFREFIDE 204
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
382-550 |
7.38e-04 |
|
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: 43.20 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLE--QDIREKEEAIRQKTSEVqeLQNDLDRetsSLQELEAQ--------KQDAQDRLDEMD 451
Cdd:pfam07111 162 EALSSLTSKAEGLEKSLNSLEtkRAGEAKQLAEAQKEAEL--LRKQLSK---TQEELEAQvtlveslrKYVGEQVPPEVH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQ-----KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS-IQAGRAQLE 525
Cdd:pfam07111 237 SQtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSlLNRWREKVF 316
|
170 180
....*....|....*....|....*....
gi 568955199 526 TILRSLKCT----QDDINQARSKLSQLQE 550
Cdd:pfam07111 317 ALMVQLKAQdlehRDSVKQLRGQVAELQE 345
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
392-459 |
7.56e-04 |
|
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: 40.80 E-value: 7.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 392 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 459
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
384-528 |
7.68e-04 |
|
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: 41.35 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 463
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 464 vrqkcqdETQTISSLktqiqsqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIL 528
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
382-532 |
8.29e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 42.14 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKTSEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 454
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 455 aKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDdLNRAKSELNRLQQEETQLEQSIQagraQLETILRSLK 532
Cdd:COG5325 144 -FLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEE-LEYQQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
394-532 |
8.51e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.09 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 394 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdreTSSLQELEAQKQDAQDRLDEmdqqkaklrdmlsdVRQkcQDETQ 473
Cdd:PRK07352 48 LEERREAILQALKEAEERLRQAAQALAEAQQKL---AQAQQEAERIRADAKARAEA--------------IRA--EIEKQ 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 474 TISSLKTQIQSQESDLKSQEDdlnRAKSELNR------LQQEETQLEQSIQAGrAQLETILRSLK 532
Cdd:PRK07352 109 AIEDMARLKQTAAADLSAEQE---RVIAQLRReaaelaIAKAESQLPGRLDED-AQQRLIDRSIA 169
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
385-552 |
8.75e-04 |
|
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: 42.12 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 385 DDISQEIAQLQREKYSLEQ----------------------DIREKEEAIRQKTSEVQELQNDLDRETSSL--------Q 434
Cdd:pfam09755 110 NDLSRKLTQLRQEKVELEQtleqeqeyqvnklmrkiekleaETLNKQTNLEQLRREKVELENTLEQEQEALvnrlwkrmD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 435 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDvRQKCQDETQTISSLKTQIQSQESDLKSQEDDlnrAKSELNRLQQEETQL- 513
Cdd:pfam09755 190 KLEAEKRLLQEKLDQPVSAPPSPRDSTSE-GDTAQNLTAHIQYLRKEVERLRRQLATAQQE---HTEKMAQYAQEERHIr 265
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568955199 514 EQSIQAGRA-QLETILRSLKCTQddINQARSKLSQLQESH 552
Cdd:pfam09755 266 EENLRLQRKlQLEMERREALCRH--LSESESSLEMDEERY 303
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-553 |
9.96e-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: 42.73 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQktsevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 458
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGR-----LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 459 DMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIQAGRaQLETILRS 530
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielkkeiLEKKQEELKFVIKELQ-QLEGSSDR 472
|
170 180
....*....|....*....|...
gi 568955199 531 LKCTQDDINQARSKLSQLQESHL 553
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKNSL 495
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
384-561 |
1.01e-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: 40.71 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQrekyslEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 463
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 464 VRQKCQDETQTI-SSLKTQIQSQESDLKSQEDDL-NRAKSELNRLQqeeTQLEQSIQAGRAQLETILRSLKCTQDDI--- 538
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAPYaee 147
|
170 180
....*....|....*....|....*
gi 568955199 539 --NQARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam01442 148 vqAQLSQRLQELREKLEPQAEDLRE 172
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
387-492 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 387 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 462
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 568955199 463 DVRQKCQDETQTISSLKTQIQSQESDLKSQ 492
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
403-542 |
1.28e-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: 39.99 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 403 QDIREKEEaiRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqtissLKTQI 482
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 483 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRAQLETILRSLKCTQ---DDINQAR 542
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEKLKE--KKQKEYRAEEAKREQkemDELATQR 138
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
438-564 |
1.28e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdETQtISSLKTQ---------IQSQESDLksqedDLNRAKSELNRLQQ 508
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGEL------ERQ-LEPLERQaekaeryreLKEELKEL-----EAELLLLKLRELEA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 509 EETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
401-546 |
1.39e-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: 40.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 401 LEQDIREKEEAIRQKTSEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQTISSLKT 480
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955199 481 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC--TQDDINQARSKLS 546
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLS 158
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
373-561 |
1.40e-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: 42.26 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 373 LASGEFTGVKELD-DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEaqkqdaqdRLDEMD 451
Cdd:TIGR00618 181 LALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT--------QKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 452 QQKAKLRDMLSDVRQKCQdetqtisslktQIQSQESDLKSQEDDLNRAKSELnRLQQEETQLEQSiqagRAQLETILRSL 531
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIE-----------ELRAQEAVLEETQERINRARKAA-PLAAHIKAVTQI----EQQAQRIHTEL 316
|
170 180 190
....*....|....*....|....*....|..
gi 568955199 532 KCTQDDINQARSKLSQL--QESHLEAHRSLEQ 561
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHvkQQSSIEEQRRLLQ 348
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
339-570 |
1.43e-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: 41.94 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 339 QQKVSKGIDppQVLSPDMVPPSERGTPIPDSSSTLAS--GEFTGVKELDDISQEIAQLQR-EKYSLEQDIREKEEAIRQK 415
Cdd:pfam05667 245 RTKLLKRIA--EQLRSAALAGTEATSGASRSAQDLAEllSSFSGSSTTDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 416 TSEVQELQNDLDRETSSLQEleaqkqdaqdRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE-- 493
Cdd:pfam05667 323 VETEEELQQQREEELEELQE----------QLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKkt 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 494 -DDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI-------LRSLKCTQDD-INQARSKLSQLQESHL----------- 553
Cdd:pfam05667 393 lDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHrvplieeYRALKEAKSNkEDESQRKLEEIKELREkikevaeeakq 472
|
250 260
....*....|....*....|
gi 568955199 554 --EAHRSL-EQYDQVPDGVS 570
Cdd:pfam05667 473 keELYKQLvAEYERLPKDVS 492
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
382-447 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRL 447
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
438-561 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 438 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 517
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568955199 518 QAGRAQletilRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:COG1579 83 GNVRNN-----KEYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
408-556 |
1.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 408 KEEAIRQKTSEVQELQNDLDREtsslqeleaqkqdAQDRLDEMDQQKAKLRdmlsdvrQKcqdetqtisslKTQIQSQES 487
Cdd:PRK12704 55 KKEALLEAKEEIHKLRNEFEKE-------------LRERRNELQKLEKRLL-------QK-----------EENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 488 DLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSL-KCTQDD-----INQARSKL-----SQLQESHLEAH 556
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEEakeilLEKVEEEArheaaVLIKEIEEEAK 183
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
381-470 |
1.58e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 39.28 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLD------------RETSSLQELEAQKQDAQDRLD 448
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALE----ELEKLPDDTPiykivgnllvkvDKTKVEKELKERKELLELRSR 88
|
90 100
....*....|....*....|..
gi 568955199 449 EMDQQKAKLRDMLSDVRQKCQD 470
Cdd:PRK09343 89 TLEKQEKKLREKLKELQAKINE 110
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
382-513 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQrekysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 454
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 455 AKLRDMLSDVRQKCQDETQTISSLKTQIQ--SQESDLKSQEDDLNRAKSELNRLQQEETQL 513
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
384-469 |
1.74e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.17 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIRE----KEEAIRQKTSEVQELQNDLD-RETSSLQELEAQKqdaQDRLDEMDQQKAKLR 458
Cdd:smart00502 9 LTKLRKKAAELEDALKQLISIIQEveenAADVEAQIKAAFDELRNALNkRKKQLLEDLEEQK---ENKLKVLEQQLESLT 85
|
90
....*....|.
gi 568955199 459 DMLSDVRQKCQ 469
Cdd:smart00502 86 QKQEKLSHAIN 96
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
454-562 |
1.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 KAKLRDMLSDVRQKCQD---ETQTISSLK-TQIQSQESDLKSQ-EDDLNRAKSEL----NRLQQEETQLE---QSIQAGR 521
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEakkEAEAIKKEAlLEAKEEIHKLRNEfEKELRERRNELqkleKRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568955199 522 AQLETILRSLKCTQDDINQARSKLSQLQESHLEAhrsLEQY 562
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERI 147
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
477-547 |
1.76e-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: 1.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 477 SLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQ 547
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
387-541 |
1.78e-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: 39.82 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 387 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSlqeleaqkqdaqDRLDEMDQQKAKLRDMLSDVRQ 466
Cdd:pfam16789 23 VKDKKRALEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------------DKILQMKRYIKVVKERLKQEEK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 467 KCQDEtqtisslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkcTQDDINQA 541
Cdd:pfam16789 91 KVQDQ-------KEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEER------EQDEIGSA 152
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
390-552 |
1.87e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.41 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 390 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDL-DRE-------TSSLQELEAQKQDAQDRLDEmdqqkaKLRDML 461
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVeERElkaeaehRQRVVELSREVEEAKRAFEE------KLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKS-ELNRLQQEetqLEQSIQAGRAQLETiLRSLKctQDDINQ 540
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVED-LRKEK--KKLAEE 194
|
170
....*....|..
gi 568955199 541 ARSKLSQLQESH 552
Cdd:pfam15665 195 YEQKLSKAQAFY 206
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
454-564 |
1.93e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 41.76 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 KAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC 533
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQ 81
|
90 100 110
....*....|....*....|....*....|.
gi 568955199 534 TQDDINQARSKLSQLQESHLEAHRSLEQYDQ 564
Cdd:COG5283 82 LSAAQRRLRSSLEQTNRQLERQQQRLARLGA 112
|
|
| 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 568955199 403 QDIREKEEAIRQKTSEVQELQND-----LDR---ETSS-LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV--------- 464
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADavnfaLRKrieETEDaKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKeaplklaqt 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955199 465 ----RQK------CQDETQtiSSLK---TQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQ 518
Cdd:pfam03148 301 rlenRTYrpnvelCRDEAQ--YGLVdevKELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
387-559 |
2.02e-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: 41.22 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 387 ISQEIAQLQREKYSLEQDIREKEEAIRQktsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 463
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVLNELKKDFKQ---LLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 464 --VRQKCQdetQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ-------------QEETQLEQSIQA--------- 519
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMASllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 520 ------------GRA-----------QLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSL 559
Cdd:pfam04108 192 dqcvtavkltegGRAemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
382-551 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQrEKYSL----EQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEM 450
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAyselqeeLEEILEQLEEIEEEQEEF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 451 DQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSqeSDL----KSQEDDLNRAKSELNRLQQeetQLEQSiqagRAQLET 526
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEV----PLNMDE 454
|
170 180
....*....|....*....|....*
gi 568955199 527 ILRSLKCTQDDINQARSKLSQLQES 551
Cdd:pfam06160 455 VNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
352-561 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 352 LSPDMVPPSErgtPIPDSSSTLASGEFTGVKELDDISQEI-AQLQRekySLEQDI--REKEEAIRQKtsEVQELqndLDR 428
Cdd:pfam10168 471 LLIDAVPPSP---PLLCSKEDVTVDEPLRGLQEDSFEDHIkSILQR---SVSNPIlsADKLSSPSPQ--ECLQL---LSR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 429 ETSSLQELEAQKQDA-----QDRLDEMDQQKAK-LRDMlsdvrQKCQDETQTISSLKTQIQSQESDLK-SQEDDLNRAKS 501
Cdd:pfam10168 540 ATQVFREEYLKKHDLareeiQKRVKLLKLQKEQqLQEL-----QSLEEERKSLSERAEKLAEKYEEIKdKQEKLMRRCKK 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 502 ELNRLQqeeTQLEQSIQAGRA---QLETILRSLKCTQDDINQARSKLSQlQESHLEAHRSLEQ 561
Cdd:pfam10168 615 VLQRLN---SQLPVLSDAEREmkkELETINEQLKHLANAIKQAKKKMNY-QRYQIAKSQSIRK 673
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
400-460 |
2.25e-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: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 400 SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 460
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
408-515 |
2.26e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.25 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 408 KEEAIRQKTSEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqtisslk 479
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 568955199 480 tqiQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQ 515
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLER 142
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
417-551 |
2.45e-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: 40.09 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 417 SEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDL 496
Cdd:cd21116 73 SYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568955199 497 NRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQES 551
Cdd:cd21116 143 QAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESS 197
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
409-583 |
2.48e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 409 EEAIRQKTSEVQELQNdLDRETSSLQELEAQKQDAQD-RLDEMDQQKAKLRDMLSDVRqkcqDETQtisslktqiqsqeS 487
Cdd:pfam12128 247 QQEFNTLESAELRLSH-LHFGYKSDETLIASRQEERQeTSAELNQLLRTLDDQWKEKR----DELN-------------G 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 488 DLKSQEDDLNRAKSELNRLqqeETQLEQSIQAGraqletiLRSLKCTQDDINQARSKLSQLQESH---LEAHRSLEQ-YD 563
Cdd:pfam12128 309 ELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAADQEQLPSWQSELENLEERLkalTGKHQDVTAkYN 378
|
170 180
....*....|....*....|
gi 568955199 564 QVPDGVSGTSLPDLATLNEG 583
Cdd:pfam12128 379 RRRSKIKEQNNRDIAGIKDK 398
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
383-558 |
2.59e-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: 41.31 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKTSEVQELQNDLDRETSSLQ------- 434
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 435 ELEAQKQDAQDRLDEMDQQ-KAKLRdmlsdvrqkcqdetQTISSLKTQIQSQESDLKsQEddlNRAKSELNRL-QQEETQ 512
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFK--------------SSIAALEAKIAQLEEQLE-QE---SRERQAANKLvRRTEKK 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568955199 513 LEQSIqagrAQLETILRSLKCTQDDINQARSKLS----QLQESHLEAHRS 558
Cdd:pfam01576 1004 LKEVL----LQVEDERRHADQYKDQAEKGNSRMKqlkrQLEEAEEEASRA 1049
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
389-540 |
2.61e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDIrekeEAIRQKTSEVQELQnDLDRETSSLQE--LEAQKQDAQDRLDEMDQQKAKLrdmlsdvrq 466
Cdd:pfam12128 768 DVIAKLKREIRTLERKI----ERIAVRRQEVLRYF-DWYQETWLQRRprLATQLSNIERAISELQQQLARL--------- 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 467 kcqdetqtISSLKTQIQSQESDLKSQEDDLNRAKSELN------------RLQQEETQLEQSIQAGRAQLETILRSLKCT 534
Cdd:pfam12128 834 --------IADTKLRRAKLEMERKASEKQQVRLSENLRglrcemsklatlKEDANSEQAQGSIGERLAQLEDLKLKRDYL 905
|
....*.
gi 568955199 535 QDDINQ 540
Cdd:pfam12128 906 SESVKK 911
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
382-452 |
2.61e-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: 2.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 382 KELDDISQEIAQLQREKysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 452
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
384-561 |
2.64e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 455
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 456 KLRDMLSDVRQKCQDETQTISSLKTQIQSQ-------ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETI- 527
Cdd:COG0497 223 KLREALQEALEALSGGEGGALDLLGQALRAlerlaeyDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVe 302
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955199 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 |
2.70e-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: 2.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 404 DIREKEEAIRQKTSEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 466
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
476-556 |
2.90e-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: 40.87 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 476 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEA 555
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLAT 322
|
.
gi 568955199 556 H 556
Cdd:TIGR04320 323 A 323
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
383-526 |
3.08e-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: 40.90 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQ-REKYSLEQDIREKEEAIRQ------------KTSEVQELQNDLDRETSSLQ---------ELEAQK 440
Cdd:pfam09731 295 EIDQLSKKLAELKkREEKHIERALEKQKEELDKlaeelsarleevRAADEAQLRLEFEREREEIResyeeklrtELERQA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 441 QDAQDRL-DEMDQQKAKL-RDMLSDVRQKCQDE----TQTISSLKTQIQSQE---SDLKSQEDDLNRAKselnrlqqeet 511
Cdd:pfam09731 375 EAHEEHLkDVLVEQEIELqREFLQDIKEKVEEEragrLLKLNELLANLKGLEkatSSHSEVEDENRKAQ----------- 443
|
170
....*....|....*
gi 568955199 512 QLEQSIQAGRAQLET 526
Cdd:pfam09731 444 QLWLAVEALRSTLED 458
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
381-556 |
3.12e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 40.76 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 453
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 454 KAKLRDMLSDVRQKCQdetQTISSLKTQIQSQESDLK----SQEDDLNRAKSELNRLQQEETQLEQS-IQAGRAQLETIL 528
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
170 180
....*....|....*....|....*....
gi 568955199 529 RSL-KCTQDDINQARSKLSQLQESHLEAH 556
Cdd:pfam03999 298 DKLfYSTEQRKRFIPFFEELYTEDLLELH 326
|
|
| ClyA_MakA-like |
cd22655 |
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
416-527 |
3.12e-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: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 416 TSEVQELQNDL-DRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQE 493
Cdd:cd22655 77 TSQILNIFKALpTAPDDAQvEQIIALLQALQKPVQEIISNIAAYQGKLKAWGDKMQAAHDNLTTGAAQIQAAETDLQADI 156
|
90 100 110
....*....|....*....|....*....|....*.
gi 568955199 494 DDLNRAKSELNR-LQQEETQLEQS-IQAGRAQLETI 527
Cdd:cd22655 157 DKINNAIANLNAeIAKDNKAIAAAqIAIGVGIFELV 192
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
358-532 |
3.65e-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: 40.81 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 358 PPSERGtpIPDSSSTLASGEFTGVKELDDISQEIAQLQREKYSLEQD--------------IREKEEAIRQKTSEVQELQ 423
Cdd:pfam05911 659 LSSDPE--IPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVElasctenlestksqLQESEQLIAELRSELASLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 424 N-------DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDl 496
Cdd:pfam05911 737 EsnslaetQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDA- 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568955199 497 nrakselnrlQQEETQLEQ--SIQAGRAQL----ETIL---RSLK 532
Cdd:pfam05911 816 ----------DQEDKKLQQekEITAASEKLaecqETILnlgKQLK 850
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
382-507 |
3.94e-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: 39.96 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQR---EKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQdaqdrldEMDQQKAKLR 458
Cdd:pfam02841 183 QSKEAVEEAILQTDQaltAKEKAIEAERAKAEAAEAEQELLREKQKEEE------QMMEAQER-------SYQEHVKQLI 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568955199 459 DMLSDVRQKCQDETQTISSLKTQIQ---SQESdLKSQEDDLNRaksELNRLQ 507
Cdd:pfam02841 250 EKMEAEREQLLAEQERMLEHKLQEQeelLKEG-FKTEAESLQK---EIQDLK 297
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
484-552 |
4.37e-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: 4.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955199 484 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLETIlrslkctQDDI-------NQARSKLSQLQESH 552
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL-------NDELialqienNLLEEKLRKLQEEN 69
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-614 |
4.71e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 382 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 461
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 462 SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLEtiLRSLKCTQdDINQA 541
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE--LKKEILEK-KQEEL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 542 RSKLSQLQESHLEAHRSLEQYDQVPDGVSGTSLPDLATLNEGILLAERGGFGAMDDPFKNKALLFSNNSQELH 614
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
389-525 |
4.82e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDrldEMDQQKAKLRDmlSDVRQKC 468
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQL---QAAQERARQQQ--EEFRRKL 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 469 QdetqtisslktQIQSqesdlKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRAQLE 525
Cdd:pfam15709 433 Q-----------ELQR-----KKQQEEAERAEAEKQRQKELEMQLaeEQKRLMEMAEEE 475
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
384-515 |
4.88e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 37.93 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKysleqdirekeeairqktsevqelqndldretsslQELEAQKQDAQDRLDEMDQQKAKLRDML-- 461
Cdd:pfam05103 27 LDQVAEDYEALIREN-----------------------------------AELKEKIEELEEKLAHYKNLEETLQNTLil 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 462 -----SDVRQKCQDETQTISSlKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQLEQ 515
Cdd:pfam05103 72 aqetaEEVKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
387-523 |
4.90e-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: 40.54 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 387 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ 466
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ-------AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955199 467 KCQDETQTISSL---KTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL---EQSIQAGRAQ 523
Cdd:pfam01576 560 QLEEKAAAYDKLektKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMlaeEKAISARYAE 622
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
423-552 |
5.04e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 423 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKcQDETQ------------TISSLKTQIQSQESDLk 490
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL-YRELRksllanrfsfgpALDELEKQLENLEEEF- 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 491 SQEDDLN------RAKSELNRLQQEETQLEQSIQagraQLETILRSLKCT-QDDINQARSKLSQLQESH 552
Cdd:PRK04778 182 SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAGYRELVEEG 246
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
409-549 |
5.13e-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: 40.43 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 409 EEAIRQKTSEVQELQNDLDRETSSLQELEAQkqdaqdrLDEMDQQKAKLRDMLSDVRQ-KCQDETQtissLKTQIQSQEs 487
Cdd:pfam05911 687 KEEFEQLKSEKENLEVELASCTENLESTKSQ-------LQESEQLIAELRSELASLKEsNSLAETQ----LKCMAESYE- 754
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955199 488 DLKSQEDDLnraKSELNRLQQEETQLEQSIQAGRaqletilrslKCTQDDInqARSKLSQLQ 549
Cdd:pfam05911 755 DLETRLTEL---EAELNELRQKFEALEVELEEEK----------NCHEELE--AKCLELQEQ 801
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
389-557 |
5.34e-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: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDIREKEEAIRQKT---SEVQELQNDLDretSSLQELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDV 464
Cdd:cd07651 22 EELRSFYKERASIEEEYAKRLEKLSRKSlggSEEGGLKNSLD---TLRLETESMAKSHLKFAKQIRQDlEEKLAAFASSY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 465 RQKCQDETQTISSLKTQIQSQESDL-KSQ---EDDLNRAKS-----------ELNRLQQEETQLEQSIQAGRAQLETILR 529
Cdd:cd07651 99 TQKRKKIQSHMEKLLKKKQDQEKYLeKARekyEADCSKINSytlqsqltwgkELEKNNAKLNKAQSSINSSRRDYQNAVK 178
|
170 180
....*....|....*....|....*....
gi 568955199 530 SLKCTQDDINQA-RSKLSQLQesHLEAHR 557
Cdd:cd07651 179 ALRELNEIWNREwKAALDDFQ--DLEEER 205
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
416-561 |
5.67e-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: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 416 TSEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetQTISSLKtqiQSQE-SD----LK 490
Cdd:pfam15272 3 TSEYLELLDKLDKNNRALHLL---NKDVRERDEHYQLQETSYKKKYLQTRN------ELINELK---QSKKlYDnyykLY 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955199 491 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRAQLEtilRSLKCTQDDINQarsklSQLQESHLEAHRSLEQ 561
Cdd:pfam15272 71 SKYQQLKKISNESLDLQSTITNLESQLVDQAIDKD---REIHNLNEKILS-----LELRNQELETKREIDK 133
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
381-562 |
5.83e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDD---ISQEIAQLQREKYSLEQDIREKEEAIRQKTSE-VQELQNDLDRET-------SSLQELE----AQKQDAQD 445
Cdd:pfam10174 76 IQALQDelrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAkelfllrKTLEEMElrieTQKQTLGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 446 RldemDQQKAKLRDML------SDVRQKCQDETQTISSLKTQIQSQESDLKSQEDDLNRAKSEL---NRLQQEETQ---L 513
Cdd:pfam10174 156 R----DESIKKLLEMLqskglpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaL 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568955199 514 EQSIQAGRAQLETILRSLKCTQDDINQARSKLSQLQESHLEAHRSLEQY 562
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
383-457 |
5.87e-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: 39.84 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 383 ELDDISQEIAQLQREKYSLEQDIREKEEAI---------RQKTSEVqEL-----QNDLDRETSSLQE----LEAQKQDAQ 444
Cdd:pfam03148 266 QLKKTLQEIAELEKNIEALEKAIRDKEAPLklaqtrlenRTYRPNV-ELcrdeaQYGLVDEVKELEEtieaLKQKLAEAE 344
|
90
....*....|...
gi 568955199 445 DRLDEMDQQKAKL 457
Cdd:pfam03148 345 ASLQALERTRLRL 357
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
406-521 |
5.93e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.67 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 406 REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD---ML----SDVRQKCQDETQTISSL 478
Cdd:pfam19220 272 RDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEEraeMLtkalAAKDAALERAEERIASL 351
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568955199 479 KTQIQSQESDLKSQEDDL---NRA-KSELNRLQQEETQLEQSIQAGR 521
Cdd:pfam19220 352 SDRIAELTKRFEVERAALeqaNRRlKEELQRERAERALAQGALEIAR 398
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
386-515 |
6.25e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.67 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREKY-SLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 464
Cdd:pfam12718 10 ENAQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVE-------KLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568955199 465 RQKCQDETQTISSLKTQIQS-QESDLKSQEddLNRAKSEL-NRLQQEETQLEQ 515
Cdd:pfam12718 83 QLLEEELEESDKRLKETTEKlRETDVKAEH--LERKVQALeQERDEWEKKYEE 133
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
386-567 |
6.95e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 386 DISQEIAQLQREKYSLEQ------DIREK-----------EEAIRQKTSEVQELQN---DLDRETSSLQELEAQKQDAQD 445
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQykekacEIRDQitskeaqlessREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 446 RLDEMDQQKAKLRDMLSDVRQKCQDEtqtissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS-----IQAG 520
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEktellVEQG 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568955199 521 RAQLetilrslkctQDDINQARSKLSQLQESHLEAHRSLEQYDQVPD 567
Cdd:TIGR00606 351 RLQL----------QADRHQEHIRARDSLIQSLATRLELDGFERGPF 387
|
|
| DUF5082 |
pfam16888 |
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized. |
389-506 |
7.80e-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: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 389 QEIAQLQREKYSLEQDIREKEEAiRQKTSEVQElqndldretsslqELEAQKQDAQDRLDEMD----QQKAKLRDMLSDV 464
Cdd:pfam16888 10 AQIAQLRSEIAALEEKIERLKEA-KTKLDAEKE-------------SLHDKKTKLQGPLNSSEswngSNENNYDGIRSNL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568955199 465 RQKCQ---DET-QTISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 506
Cdd:pfam16888 76 ETSYQnyvDELdELIDAIEEEITRLENQINEAQGVIDTLQSQLNSL 121
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
384-461 |
8.11e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.13 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 384 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQDRLD---EMDQQKAKLRD 459
Cdd:pfam00038 226 IQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETrQEMARQLREYQELLNvklALDIEIATYRK 305
|
..
gi 568955199 460 ML 461
Cdd:pfam00038 306 LL 307
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
381-561 |
8.21e-03 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 38.92 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 381 VKELDDISQEIAQLQRekySLeQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 460
Cdd:pfam16591 65 VRLLQEQLQLIQAYRK---SF-NELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTPEADSRRAAQYQAISELKRQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 461 LSDVRQ---------KCQDETQTISSLKTQIQSQESdLKSQEDDLNRAkselnRLQqeetQLEQSIQAGRAQLETilrsL 531
Cdd:pfam16591 141 VQMARYqvrgytftpNEDSEQAAYQQLDAALASLDQ-LRQALAGDPGA-----ALQ----QLTSALQGYRDALDT----F 206
|
170 180 190
....*....|....*....|....*....|
gi 568955199 532 KCTQDDINQARSKLSQLQESHLEAHRSLEQ 561
Cdd:pfam16591 207 KAAVAAIEQARQEMTSQGDEIVRISDELYQ 236
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
395-555 |
8.95e-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: 39.63 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 395 QREKYSLEQDIREKEEAI---RQKTSEVQELQNDLDRETSSLQELEAQ-------------KQDAQDRLDEMDQQK--AK 456
Cdd:pfam05701 218 EQDKLNWEKELKQAEEELqrlNQQLLSAKDLKSKLETASALLLDLKAElaaymesklkeeaDGEGNEKKTSTSIQAalAS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 457 LRDMLSDVR---QKCQDETQTISSLKTQIQSqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRAQLETILRSLKC 533
Cdd:pfam05701 298 AKKELEEVKaniEKAKDEVNCLRVAAASLRS----------ELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIAL 367
|
170 180
....*....|....*....|....*.
gi 568955199 534 TQDDINQARSKLS----QLQESHLEA 555
Cdd:pfam05701 368 VQAKEKEAREKMVelpkQLQQAAQEA 393
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
410-525 |
9.62e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 36.86 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 410 EAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQTISSLKTQIQSQ 485
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLisiiQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKENK 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568955199 486 ESDLKSQeddlnrakseLNRLQQEETQLEQSIQAGRAQLE 525
Cdd:smart00502 74 LKVLEQQ----------LESLTQKQEKLSHAINFTEEALN 103
|
|
| MIP-T3_C |
pfam17749 |
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ... |
407-545 |
9.73e-03 |
|
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.
Pssm-ID: 465481 [Multi-domain] Cd Length: 154 Bit Score: 37.43 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 407 EKEEAIRQKTSEVQELQNDLDRE------TSSLQELEAQKqdaqdrldEMDQQKAKLrdmlSDVRQKCQDETQTISSLKT 480
Cdd:pfam17749 4 DAQGGLVKKILETKKEYEKGGAEaepgesDRSLQESSAKK--------GRTVSASDI----NQLRESIQTLTKSANPLGK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955199 481 QIQSQESDLKSQEDDLNRAKSELNR----LQQEETQLEQSIQAGRAQLETILRSLKCTQDDINQARSKL 545
Cdd:pfam17749 72 LLDFIQDDIDSMQRELQMWRSEYRQnaqaLQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQI 140
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
424-550 |
9.97e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 37.59 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955199 424 NDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQTISSLKTQIQSQES-DLKSQEDDLNRAKSE 502
Cdd:cd12923 1 DDVEKLAKKLKEINKEYLDKSREYDELYEKYNKLSQEIQLKRQALEAFEEAVKMFEEQLRTQEKfQKEAQPHEKQRLMEN 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568955199 503 LNRLQQEETQLEQSiqagRAQLETILR----SLKCTQDDINQARSKLSQLQE 550
Cdd:cd12923 81 NELLKSRLKELEES----KEQLEEDLRkqvaYNRELEREMNSLKPELMQLRK 128
|
|
| |
