|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
121-214 |
5.48e-40 |
|
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: 142.42 E-value: 5.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 121 WAVRVEEKAKFDGIFESLLP-INGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 199
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 1953011268 200 VPSVLPPSLIPPSKR 214
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
269-364 |
9.26e-37 |
|
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: 133.17 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 269 WVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSkGI 348
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80
|
90
....*....|....*.
gi 1953011268 349 DPPQVLSPDMVPPSER 364
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
131-196 |
4.50e-25 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 98.83 E-value: 4.50e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 131 FDGIFESLLPIN-GLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 196
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 ... |
127-214 |
5.14e-25 |
|
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: 100.14 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 127 EKAKFDGIFESLLPINGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPSVL 204
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDEL 87
|
90
....*....|
gi 1953011268 205 PPSLIPPSKR 214
Cdd:pfam12763 88 PDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
279-345 |
5.38e-24 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 95.75 E-value: 5.38e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 279 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVS 345
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
1.07e-20 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 86.50 E-value: 1.07e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 19 YESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQS 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
2.72e-20 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 86.18 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 13 PTGNPLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQSGHEVTLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 1953011268 93 NLNLNMPPPKF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-568 |
3.17e-20 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 93.43 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 381 TGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkVQLETIIKSLKSTQDEI 540
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQALDELLKEA 192
|
170 180
....*....|....*....|....*...
gi 1953011268 541 NQARSKLSQLQESHQEAHRTLEQYDEAL 568
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEEL 220
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-591 |
4.96e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 455
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS 535
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 536 TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-571 |
5.27e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR 544
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|....*..
gi 1953011268 545 SKLSQLQESHQEAHRTLEQYDEALDGA 571
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-591 |
2.71e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011268 544 RSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-591 |
4.06e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQD-------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 536
Cdd:COG1196 368 LEAEAELAEaeeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 537 QDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-584 |
1.49e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 392 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 471
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 472 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQ 551
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190
....*....|....*....|....*....|...
gi 1953011268 552 ESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 584
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-571 |
2.15e-17 |
|
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: 87.42 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE-------ETQLEQSIQAGKVQLETIIKSLKSTQ 537
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190
....*....|....*....|....*....|....
gi 1953011268 538 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 571
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-600 |
2.24e-17 |
|
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: 87.42 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV-----QLETIIKSLKSTQ 537
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQ 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 538 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG------ASLTNLADLSEGVS--LAERGGFGAMDDP 600
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQArldsleRLQENLEGFSEGVKalLKNQSGLSGILGV 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-571 |
6.86e-17 |
|
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: 85.88 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 390 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrQK 469
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 470 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQ 549
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170 180
....*....|....*....|..
gi 1953011268 550 LQEshQEAHRTLEQYDEALDGA 571
Cdd:TIGR02168 433 AEL--KELQAELEELEEELEEL 452
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-614 |
2.66e-16 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 81.49 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 407 IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 486
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 487 QESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEahRTLEQYDE 566
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011268 567 ALDGAHGASLTNLADLSEGVSLAERGGFGAMDDPFKNKALLFSNNAQE 614
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-584 |
3.28e-16 |
|
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: 83.57 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 390 SQEIAQLqrekyslEQDIREKEEAIRQKSNEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 469
Cdd:TIGR02168 676 RREIEEL-------EEKIEELEEKIAELEKALAELR-------KELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 470 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEIN-------Q 542
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaN 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011268 543 ARSKLSQLQESHQEAHRTLEQYDEALDGA--HGASLT-NLADLSE 584
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELseDIESLAaEIEELEE 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-576 |
5.76e-16 |
|
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: 80.58 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 456
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlQQEETQLEQSIQAGKVQLETIIKSLKST 536
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011268 537 QDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASL 576
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-571 |
1.03e-15 |
|
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: 79.81 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 463
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 sDVRQK------------CQDETQMISSLKTqIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIK 531
Cdd:COG4942 111 -RALYRlgrqpplalllsPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011268 532 SLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 571
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
385-573 |
1.32e-15 |
|
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: 76.89 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVR-----QKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 539
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 540 INQARSKL-SQLQEshqeahRTLEQYDEALDGAHG 573
Cdd:COG1579 161 LEAEREELaAKIPP------ELLALYERIRKRKNG 189
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-584 |
3.26e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELT----RLQQEETQL---EQSIQAGKVQLETIIKSLKS 535
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALleaEAELAEAEEELEELAEELLE 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011268 536 TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 584
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-591 |
4.67e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQkqdaQDRLDE----------- 451
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER----LEELEEelaeleeelee 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 452 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIK 531
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 532 SLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-556 |
5.68e-15 |
|
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: 79.29 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSL 533
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
170 180
....*....|....*....|...
gi 1953011268 534 KSTQDEINQARSKLSQLQESHQE 556
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQ 292
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-563 |
1.17e-14 |
|
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: 78.57 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 375 LGSGEFTGVKE-LDDISQEIAQLQR--------------EKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELE 439
Cdd:TIGR02169 284 LGEEEQLRVKEkIGELEAEIASLERsiaekereledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI-------QSQESDLKSQEDDLNRAKSELTRLQQEE 512
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 513 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-568 |
1.24e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.89 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 393 IAQLQREKYSLE-----------QDIREKEEAIRQKSNEV---QELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDM--LSDVRQKCQDETQMISSLKTQIQsqesDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV-QLETIIKSLKS 535
Cdd:COG4717 128 LPLYqeLEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1953011268 536 TQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 568
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-552 |
1.72e-14 |
|
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: 77.37 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKSTQD----E 539
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEklesE 532
|
170
....*....|...
gi 1953011268 540 INQARSKLSQLQE 552
Cdd:TIGR04523 533 KKEKESKISDLED 545
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-588 |
2.13e-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: 77.79 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 S-------DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA-------GKVQLETI 529
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALL 892
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 530 IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSL 588
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-571 |
3.43e-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: 77.02 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:TIGR02168 326 EELESKLDE-------LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 544 RS-------KLSQLQESHQEAHRTLEQYDEALDGA 571
Cdd:TIGR02168 399 NNeierleaRLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-563 |
1.10e-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: 75.10 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD-----AQDRLDEMDQQKAK 458
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDMLSDVR----------QKCQDETQMISSLKTQIQSQESDLKSQEDDlNRAKSELTRLQQEEtqLEQSIQAGKVQLET 528
Cdd:TIGR02169 803 LEEEVSRIEarlreieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKS-IEKEIENLNGKKEE--LEEELEELEAALRD 879
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 529 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-525 |
1.28e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.42 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKS--NEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 461 DMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 525
Cdd:COG4717 174 ELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-568 |
1.48e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.42 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDetqmISSLKTQIQSQESDLK-SQEDDLNRAKSELTRLQQEETQLEQsiqagkvqletiikSLKSTQDE 539
Cdd:COG4717 160 ELEEELEELEAE----LAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEE--------------ELEEAQEE 221
|
170 180
....*....|....*....|....*....
gi 1953011268 540 INQARSKLSQLQEShQEAHRTLEQYDEAL 568
Cdd:COG4717 222 LEELEEELEQLENE-LEAAALEERLKEAR 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-596 |
1.65e-13 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 72.94 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 460
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 ---------DMLSDVRQKCQDETQMISSLKTQIQSQESD---LKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 528
Cdd:COG3883 103 syldvllgsESFSDFLDRLSALSKIADADADLLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 529 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGFGA 596
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-591 |
2.17e-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: 74.32 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 392 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 471
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 472 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQ 551
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011268 552 ESHQEAHRTLEQYD---EALDGAHGASLTNLADLSEGVSLAER 591
Cdd:TIGR02168 393 LQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEEAEL 435
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-556 |
2.51e-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: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|...
gi 1953011268 544 RSKLSQLQESHQE 556
Cdd:TIGR04523 495 EKELKKLNEEKKE 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-591 |
7.25e-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: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQK-SNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQ 542
Cdd:TIGR02169 331 IDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 543 ARSKLSQLQESHQEAHRTLEQYDEALDGA---HGASLTNLADLSEGVSLAER 591
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEDKALEIKKQEW 455
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-592 |
1.12e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKSNEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 459
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 RDMLSDVRqkcqdetqmisslkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 539
Cdd:PRK02224 327 RDRLEECR--------------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 540 INQARSKLSQLQESHQEAHRTLEQYDEALDGAHG------ASLTNLAD-LSEGVSLAERG 592
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREreaeleATLRTARErVEEAEALLEAG 452
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
383-542 |
1.16e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.59 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMI-SSLKTQI---QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 536
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....*.
gi 1953011268 537 QDEINQ 542
Cdd:COG3206 378 RLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-558 |
1.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD-- 461
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEEle 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 462 -MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 540
Cdd:COG1196 407 eAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
170
....*....|....*...
gi 1953011268 541 NQARSKLSQLQESHQEAH 558
Cdd:COG1196 487 AEAAARLLLLLEAEADYE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-563 |
2.95e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.71 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKSNEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 448
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 LDEMDQQKAKLRDMLSDVRQKC-QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLE 527
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953011268 528 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
387-563 |
3.39e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 70.05 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKSN------EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 457
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNGlvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 458 KLRDMLSDVRQkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE----ETQLEQSIQAGKVQLETIIKSL 533
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQiaalRAQLQQEAQRILASLEAELEAL 325
|
170 180 190
....*....|....*....|....*....|....
gi 1953011268 534 KST----QDEINQARSKLSQLQESHQEAHRtLEQ 563
Cdd:COG3206 326 QAReaslQAQLAQLEARLAELPELEAELRR-LER 358
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
384-533 |
4.41e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 66.49 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 463
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSEltrLQQEETQLEQSIQAGKVQLETIIKSL 533
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-521 |
6.58e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 380 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 459 LRDMLSDVRQKCQDETQMISSLKTQIQSQ----ESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 521
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-568 |
8.01e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 398 REKYSLEQDIREKEEAIRQksnEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDmLSDVRQKCQDetqmI 477
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEEL-------AEAEERLEALEAELDALQERREALQR-LAEYSWDEID----V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 478 SSLKTQIQSQESDLksqeDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 557
Cdd:COG4913 664 ASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170
....*....|.
gi 1953011268 558 HRTLEQYDEAL 568
Cdd:COG4913 740 EDLARLELRAL 750
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
392-584 |
1.55e-11 |
|
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: 67.84 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 392 EIAQLQREKYSLEQDIREKEEAIRqksNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 471
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLK---NELSELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 472 DETQMISSLKTQIQSQESDLKSQEDD---LNRAKSELTRLQQEETQLEQSIQAGKvQLETIIKSLKSTQDEINQARSKLS 548
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELERLREHNK-HLNENIENKLLLKEEVEDLKRKLE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011268 549 QlQESHQEAHRTLE----------QYDEALDGAHGASLTNLADLSE 584
Cdd:pfam05557 239 R-EEKYREEAATLElekekleqelQSWVKLAQDTGLNLRSPEDLSR 283
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
385-512 |
2.16e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1953011268 465 DVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE 512
Cdd:TIGR02169 466 KYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
391-591 |
2.42e-11 |
|
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: 66.84 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQDiREKEEAIRQKS---NEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 468 QKCQDETQMISSLKTQIQSQESDLKSQEDdlnRAKSELTRLQQEETQLEQSiqagKVQLETIIKSLKSTQDEINQARSKL 547
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL----QAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011268 548 SQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
384-563 |
2.48e-11 |
|
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: 64.63 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDML-------SDVRQKCQDETQM-ISSLKTQIQSQESDLKS--QEDDLNRAKSELTRLQQEetQLEQSIQAgkvqL 526
Cdd:pfam12795 130 QQIRNRLngpappgEPLSEAQRWALQAeLAALKAQIDMLEQELLSnnNRQDLLKARRDLLTLRIQ--RLEQQLQA----L 203
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011268 527 ETIIKSLKSTQDEinQARSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam12795 204 QELLNEKRLQEAE--QAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-563 |
3.12e-11 |
|
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: 66.97 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKyslEQDI-REKEEAIRQKSNEVQELQNDLDRETSSLQEL-------EAQKQDAQDRLDEMDQQ 455
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLneqisqlKKELTNSESENSEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ---------- 525
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknnseikd 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011268 526 -------LETIIKSLKSTQDEINQarsKLSQLQESHQEAHRTLEQ 563
Cdd:TIGR04523 445 ltnqdsvKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-584 |
3.88e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQeIAQLQREKysleQDIREKEEAIRQKSNEVQ----ELQNDLDR-------------------ET------SS 434
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI------------------QSQESDLKSQED 496
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 497 DLNR-----------AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYD 565
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260
....*....|....*....|..
gi 1953011268 566 EALDGA---HGASLTNLADLSE 584
Cdd:TIGR02169 392 EKLEKLkreINELKRELDRLQE 413
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-567 |
5.95e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLD------RETSSLQE-------LEAQKQDAQDRL 449
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEkaeeyikLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 450 DEMDQQKAKLRDMLSDVRQKCQD------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE-QSIQAG 522
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKL 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011268 523 KVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 567
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
392-539 |
8.41e-11 |
|
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: 64.01 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 392 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQ-------KCQDETQMISSLKTQIQSQeSDLKSQEDDLNRAKSELTR-LQQEETQLEqSIQAGK----VQLETIIK 531
Cdd:pfam09787 128 EELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELENRLHQLTEtLIQKQTMLE-ALSTEKnslvLQLERMEQ 205
|
....*...
gi 1953011268 532 SLKSTQDE 539
Cdd:pfam09787 206 QIKELQGE 213
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-566 |
1.30e-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: 65.04 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELTRLQQEETQleQSIQAGKVQLETIIKSLKST 536
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKK 583
|
170 180 190
....*....|....*....|....*....|
gi 1953011268 537 QDEINQarsKLSQLQESHQEAHRTLEQYDE 566
Cdd:TIGR04523 584 QEEKQE---LIDQKEKEKKDLIKEIEEKEK 610
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-556 |
1.33e-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: 65.04 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLE---QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQ--EDDLNRAKSELT----RLQQEETQLEQSIQAGKvQLETIIK 531
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELKnqekKLEEIQNQISQNNKIIS-QLNEQIS 345
|
170 180
....*....|....*....|....*.
gi 1953011268 532 SLKSTQDEINQARSKLS-QLQESHQE 556
Cdd:TIGR04523 346 QLKKELTNSESENSEKQrELEEKQNE 371
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-556 |
1.50e-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: 64.66 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQ---KSNEVQELQNDLDRETSSLQELEAQ-----KQDAQDRL----DE 451
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNkelkSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 452 MDQQKAKLRDMLSDVRQKcqdeTQMISSLKTQIqsqeSDLKSQEDDLNRAKSELTR-LQQEETQLE----------QSIQ 520
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQN----NKIISQLNEQI----SQLKKELTNSESENSEKQReLEEKQNEIEklkkenqsykQEIK 387
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011268 521 agkvQLETIIKSLKST---QDEINQAR-SKLSQLQESHQE 556
Cdd:TIGR04523 388 ----NLESQINDLESKiqnQEKLNQQKdEQIKKLQQEKEL 423
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
394-582 |
1.66e-10 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 63.94 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQrekySLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 473
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 474 TQMISSLKTQIQSQESDLKSQEDDLNRaKSELTRLQ----QEETQLEQSIQA-----GKVQLETIIKsLKSTQDEINQAR 544
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETIAE-LKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953011268 545 SKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADL 582
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGL 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
423-582 |
2.25e-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: 61.48 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 423 ELQnDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 502
Cdd:COG1579 11 DLQ-ELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 503 S--ELTRLQQEETQLEQSIQagkvQLEtiikslkstqDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLA 580
Cdd:COG1579 87 NnkEYEALQKEIESLKRRIS----DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
..
gi 1953011268 581 DL 582
Cdd:COG1579 153 EL 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
386-566 |
3.71e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLEQDIREKEEAIR----QKSNEVQELQN------DLDRETSSLQ----ELEAQKQDAQDRLDE 451
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENlngkkeELEEELEELEaalrDLESRLGDLKKERDE 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 452 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSE------LTRLQQEETQLEQSIQAgkvq 525
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA---- 969
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011268 526 LETI----IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDE 566
Cdd:TIGR02169 970 LEPVnmlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
378-460 |
4.01e-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: 60.71 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 378 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 457
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 1953011268 458 KLR 460
Cdd:COG1579 160 ELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
393-563 |
4.91e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 393 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQnDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDVRQk 469
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDvasAEREIAELEAELERLDASSDDLAA- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 470 cqdetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQ 549
Cdd:COG4913 690 ----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170
....*....|....
gi 1953011268 550 LQESHQEAHRTLEQ 563
Cdd:COG4913 760 GDAVERELRENLEE 773
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
384-572 |
5.56e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.47 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelaekrdELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQDETQM---ISSLKTQIQSQESDLKsQEDDLNRAKSEL-TRLQQEETQLEQsiqagKVQLETIIKS 532
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLrkeIERLEWRQQTEVLSPE-EEKELVEKIKELeKELEKAKKALEK-----NEKLKELRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1953011268 533 LKSTQDEINQARSKLSQLQESHQEAH-------RTLEQYDEALDGAH 572
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHeemielyKEADELRKEADELH 215
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
384-569 |
7.00e-10 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 61.09 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIR------EKEEAIRQKS-NEVQELQNDLDRETSSLQELEAQKQDAQDRLD------ 450
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRLAAEdfrqkyEDELNLRTSAeNDLVGLRKDLDEATLARVDLEAKIESLKEELAflkknh 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 451 --EMDQQKAKLRD-----------------MLSDVRQkcQDEtQMISSLKTQI----QSQESDLKSQ----EDDLNRAKS 503
Cdd:pfam00038 141 eeEVRELQAQVSDtqvnvemdaarkldltsALAEIRA--QYE-EIAAKNREEAeewyQSKLEELQQAaarnGDALRSAKE 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 504 ELT----RLQQEETQLeQSIQAGKVQLETIIKSLKSTQD-EINQARSKLS----QLQESHQEAHRTLEQYDEALD 569
Cdd:pfam00038 218 EITelrrTIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQELLN 291
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-571 |
7.59e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 457
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 458 KLRDMLSDVRQKC-----QDET--QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 530
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 571
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-578 |
8.32e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqLETIIKSLKSTQDEINQA 543
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA----SEERVRGGRAVEEVLKAS 519
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953011268 544 RS----KLSQLQeshqeahRTLEQYDEALDGAHGASLTN 578
Cdd:TIGR02169 520 IQgvhgTVAQLG-------SVGERYATAIEVAAGNRLNN 551
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
385-568 |
9.96e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 61.78 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKSNEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 452
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 453 ---DQQKAKLRDMLSDVR---QKCQDETQMISslktqiQS---QESDLKSQ---EDDLNRAKSELTRLQQEETQLEQSIQ 520
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKeqnKELKEEIDRVK------QSytlNESELESVrqlEKQLESLEKQYDEITERIAEQEIAYS 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011268 521 AGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 568
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
383-557 |
1.48e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 453
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 454 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSiqagkvqLETIIKSL 533
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170 180
....*....|....*....|....
gi 1953011268 534 KSTQDEINQARSKLSQLQESHQEA 557
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKES 671
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-557 |
3.20e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKysleQDIREKEEAIRQKSNEVQELQN------DLDRETSSLQELEAQKQD---AQDRLDEMDQ 454
Cdd:COG4913 617 AELAELEEELAEAEERL----EALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERldaSSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 455 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE--ETQLEQSIQAGKVQ--LETII 530
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERelRENLE 772
|
170 180
....*....|....*....|....*..
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQESHQEA 557
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
384-566 |
3.42e-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: 60.25 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEeaIRQKSNEVQELQNDLDRetsslQELEaqkqDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALLEN-----LELD----EAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 ---SDVRQKCQDETQMISSLKTQIQSQESDLKSqeddlnraksELTRLQQ------EETQLEQSIQAgkvQLETIIKSLK 534
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKE----------ELERVQQsytlneNELERVRGLEK---QLEELEKRYD 346
|
170 180 190
....*....|....*....|....*....|..
gi 1953011268 535 STQDEINQARSKLSQLQESHQEAHRTLEQYDE 566
Cdd:pfam06160 347 EIVERLEEKEVAYSELQEELEEILEQLEEIEE 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-591 |
3.93e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 411 EEAIRqksnEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQMISSLKTQI 484
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 485 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqletiikslkSTQDEINQARSKLSQLQESHQEAHRTLEQY 564
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180
....*....|....*....|....*..
gi 1953011268 565 DEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAA 391
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
385-572 |
5.60e-09 |
|
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: 57.07 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQksneVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVRQKCQD------ETQMISSLKTQIQSQESDLKSQE--DDLNRAKSELTRLQqeetQLEQSIQAGKVQLETIIKSLKS- 535
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHK----ELEEELEAHEPRLKSLNELAEEl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011268 536 ----TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 572
Cdd:cd00176 173 leegHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-571 |
6.00e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDEtqmissLKTQIQSQES------DLKSQEDDLnraKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST 536
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPfyneylELKDAEKEL---EREEKELKKLEEELDKAFE----ELAETEKRLEEL 645
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 537 QDEINQARSKLSqlQESHQEAHRTLEQYDEALDGA 571
Cdd:PRK03918 646 RKELEELEKKYS--EEEYEELREEYLELSRELAGL 678
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-542 |
8.10e-09 |
|
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: 59.30 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDETQMISSLKTQIQSQESD---------------------------------------------------- 490
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealenkieddeeearrrlkrlenkikelgpvnlaaieeyeelkeryd 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1953011268 491 -LKSQEDDLNRAKseltrlqqeeTQLEQSIQagkvQLETIIKS-LKSTQDEINQ 542
Cdd:TIGR02168 1004 fLTAQKEDLTEAK----------ETLEEAIE----EIDREARErFKDTFDQVNE 1043
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-569 |
1.42e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMdqqKAKLRDM 462
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENL---NGKKEEL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQdE 539
Cdd:TIGR02169 867 EEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-E 945
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011268 540 INQARSKLSQLQESHQEAHRTL-----------EQYDEALD 569
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIralepvnmlaiQEYEEVLK 986
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
405-571 |
1.86e-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: 58.26 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 405 QDIREKEEAIRQksnEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 484
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 485 QSQESDLKSQEDDLN-----RAKSELTR------LQQEETQLEQSI------QAGKVQLETIIKSLKSTQDEinQARSKL 547
Cdd:pfam01576 267 RELEAQISELQEDLEseraaRNKAEKQRrdlgeeLEALKTELEDTLdttaaqQELRSKREQEVTELKKALEE--ETRSHE 344
|
170 180
....*....|....*....|....
gi 1953011268 548 SQLQESHQEAHRTLEQYDEALDGA 571
Cdd:pfam01576 345 AQLQEMRQKHTQALEELTEQLEQA 368
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
438-569 |
2.00e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 438 LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD--ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL 515
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 516 EQSIQAGKVQLETIIKS--LKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:COG3206 246 RAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
384-594 |
2.12e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQK 456
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEElqkerqdLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQ-----ESDLKSQEDDLNRA--KSELTRLQQEETQLEQSIQAGKVQLETI 529
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALseaeaEQALDELLKEANRNaeKEEELAEAEKLIESLPRELAEELLEAKD 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 530 IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGF 594
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
391-525 |
2.24e-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: 53.41 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQDIREKEEAIrqksnevQELQNDLDRETSSLQEleaqkqdAQDRLD-EMdQQKAKLRDMLSDVRQK 469
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYErEL-VLHAEDIKALQALREE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 470 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSeltRLQQEETQLEQSIQAGKVQ 525
Cdd:pfam07926 66 LNELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
384-529 |
3.08e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.10 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKSNEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 454
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 455 QKAKLRDMLSDVRQKCQDetqmISSLkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI 529
Cdd:PRK12704 129 KEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAI 198
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
396-567 |
3.24e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 396 LQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 460
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 ---------DMLSDVRQKC------QDETQMISSLKTQIQSQESDLKSQEDDLNRAkseltRLQQEETQLEQSIQAGKVQ 525
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011268 526 LETIIKSLKSTQDEINQARS--KLSQLQESHQEAHRTLEQYDEA 567
Cdd:COG4717 448 LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
440-584 |
3.43e-08 |
|
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: 56.31 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSI 519
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 520 QAGKVQL------------------------------------------ETIIKSLKSTQDEINQARSKLSQLQESHQEA 557
Cdd:COG4942 100 EAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180
....*....|....*....|....*..
gi 1953011268 558 HRTLEQYDEALDGAHGASLTNLADLSE 584
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEK 206
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
394-553 |
3.53e-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: 57.06 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 448
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS 518
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 519 IQagkvQLETIIKSLKSTQDEINQARSKLsQLQES 553
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEI-QSQEQ 184
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
387-559 |
3.72e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.83 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 466
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 467 RQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSK 546
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERKVEGLGEE 259
|
170
....*....|....*..
gi 1953011268 547 LS----QLQESHQEAHR 559
Cdd:pfam07888 260 LSsmaaQRDRTQAELHQ 276
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-552 |
3.81e-08 |
|
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: 57.36 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIrEKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLdemDQQKAKLRDM 462
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDI-EEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI---AQQAAKLQGS 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 -----LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE---QSIQAGKVQLETIIKSLK 534
Cdd:TIGR00606 819 dldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlQRRQQFEEQLVELSTEVQ 898
|
170
....*....|....*...
gi 1953011268 535 STQDEINQARSKLSQLQE 552
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLET 916
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-551 |
4.23e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 379 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKSNEVQELQNDLDRET-SSLQELEAQKQ---------- 443
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneyl 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 444 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQEETQLEQSIQ 520
Cdd:PRK03918 606 elkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|....
gi 1953011268 521 AGKVQLETIIKS---LKSTQDEINQARSKLSQLQ 551
Cdd:PRK03918 684 ELEKRREEIKKTlekLKEELEEREKAKKELEKLE 717
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
379-575 |
5.45e-08 |
|
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: 56.50 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 379 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 454
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 455 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQEsdlksqeddlnrAKSELTRLQQEETQLEQSIQAGKVQLETII---- 530
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRakle 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGAS 575
Cdd:COG5185 510 RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-545 |
5.88e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQEL--------------------------------------- 424
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsyldvllgsesfsdfldrlsalskiada 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 425 QNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS 503
Cdd:COG3883 131 DADLLEELKADKaELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953011268 504 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARS 545
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
385-559 |
7.12e-08 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 55.47 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKSNEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 448
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 ---LD-----------------EMDQQKAKLR---DMLSDVRQKCqdetqmISSLK---TQIQSQEsdlKSQEDDLNRAK 502
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQET------IAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 503 SELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHR 559
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-557 |
7.20e-08 |
|
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: 56.28 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAqkqdaqdRLDEMDQQKAKLRDML 463
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA-------RVSDLELEKVKLVNAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtRLQQEEtqLEQSIQAGKVQLetiikslKSTQDEINQA 543
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF-RNKSEE--METTTNKLKMQL-------KSAQSELEQT 711
|
170
....*....|....
gi 1953011268 544 RSKLSQLQESHQEA 557
Cdd:pfam15921 712 RNTLKSMEGSDGHA 725
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-569 |
7.71e-08 |
|
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: 56.28 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 459
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 RDMLSDVRQKCQDETQMISSL----------KTQIQSQESD----------LKSQED-DLNRAKSELTRLQQEETQLeqs 518
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHgrtagamqveKAQLEKEINDrrlelqefkiLKDKKDaKIRELEARVSDLELEKVKL--- 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 519 IQAGKVQLETiIKSLKSTQD----EINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:pfam15921 638 VNAGSERLRA-VKDIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-590 |
7.83e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQksneVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKstqdEINQAR 544
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVER 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011268 545 SKLSQLQESHQEAHRTLEQYdealDGAHGASLTNLADLSEGVSLAE 590
Cdd:COG3096 647 DELAARKQALESQIERLSQP----GGAEDPRLLALAERLGGVLLSE 688
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
387-563 |
7.89e-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: 55.90 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 455
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 KAKLRDMLSDVRQK--CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETiiKSL 533
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL--ADP 436
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953011268 534 KSTQDEINQARSKLSQLQESHQE------------AHRTLEQ 563
Cdd:pfam05557 437 SYSKEEVDSLRRKLETLELERQRlreqknelemelERRCLQG 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
384-572 |
8.06e-08 |
|
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: 56.13 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDiREKEEAIRQKSNEVQELQndldRETSSLQELEAQKQDAQDRLDeMDQQKAKL---R 460
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQLR----ARIEELRAQEAVLEETQERIN-RARKAAPLaahI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ------SIQAGKVQLETIIK 531
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSkmrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatSIREISCQQHTLTQ 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011268 532 SLKSTQ-------DEINQARSKLSQLQ-ESHQEAHRTLEQYDEALDGAH 572
Cdd:TIGR00618 380 HIHTLQqqkttltQKLQSLCKELDILQrEQATIDTRTSAFRDLQGQLAH 428
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-584 |
8.38e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQ-------LQREKYSLEQDIREK---------EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQ----- 443
Cdd:COG3096 793 ERDELAEQYAKasfdvqkLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeq 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 444 -----------------DAQDRLDEMDQQKAKLRDMLSDVRQKCqdetQMISSLKTQIQSQESDLKSQED---DLNRAKS 503
Cdd:COG3096 873 lqllnkllpqanlladeTLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLVAVLQSDPEQFEQlqaDYLQAKE 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 504 ELTRLQQEETQLEQSIQ-------AGKVQL--------ETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLeqydEAL 568
Cdd:COG3096 949 QQRRLKQQIFALSEVVQrrphfsyEDAVGLlgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL----ASL 1024
|
250
....*....|....*.
gi 1953011268 569 DGAHGASLTNLADLSE 584
Cdd:COG3096 1025 KSSRDAKQQTLQELEQ 1040
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
391-591 |
8.60e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQDiREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 451
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 452 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL------------NRAKSELTRLQQE-------E 512
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 513 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES-----------------------HQEAHRTLEQYDEALD 569
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGwcavlrlardndverrlhrrelaYLSADELRSMSDKALG 1155
|
250 260
....*....|....*....|....*..
gi 1953011268 570 GAHGA-----SLTNLADLSEGVSLAER 591
Cdd:COG3096 1156 ALRLAvadneHLRDALRLSEDPRRPER 1182
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
455-563 |
8.62e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 455 QKAKLRdmLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE----ETQLEQS---IQAGKVQLE 527
Cdd:COG4372 9 GKARLS--LFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseLEQLEEELE 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 1953011268 528 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
414-566 |
9.25e-08 |
|
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: 52.02 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 414 IRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDemdqqkaklrdmlsDVRQKCQDETQMISSlktQIQSQESDLKs 493
Cdd:pfam07321 5 LRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQ--------------DYRAWRPQEEQRLYA---EIQGKLVLLK- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 494 qedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR---SKLSQLQESHQEAHRTLEQYDE 566
Cdd:pfam07321 67 ---ELEKVKQQVALLRENEADLEKQVAEARQQLEAEREALRQARQALAEARravEKFAELVRLVQAEELRQQERQE 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
375-559 |
1.17e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 375 LGSGEFTGVKELDDISQEIAQLQRekysLEQDIREKEEAIRQKSNEvQELQNDLDR-ETSSLQELEA---QKQDAQDRLD 450
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELKE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 451 EMDQQKAKLRDMLSDVRQKCQDETQmiSSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS--IQAGKVQLET 528
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEE 480
|
170 180 190
....*....|....*....|....*....|....
gi 1953011268 529 IIKSLKSTQDE---INQARSKLSQLQESHQEAHR 559
Cdd:COG4717 481 LKAELRELAEEwaaLKLALELLEEAREEYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-569 |
1.28e-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: 55.46 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 402 SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELeaqkqdaQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLK 481
Cdd:TIGR02169 643 TLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRL-------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 482 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQEShqEAHRTL 561
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRI 793
|
....*...
gi 1953011268 562 EQYDEALD 569
Cdd:TIGR02169 794 PEIQAELS 801
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-583 |
1.31e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 536
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1953011268 537 QDEINQARSKLSQLQE---SHQEAHRTLEQYDEALDGAHGASLTNLADLS 583
Cdd:pfam01576 179 SKLKNKHEAMISDLEErlkKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
427-593 |
1.67e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 427 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL-NRAKS-- 503
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 504 ----------------------------------------ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1953011268 544 RSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGG 593
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
386-572 |
1.99e-07 |
|
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: 54.84 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKSNEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 457
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 458 KLRDMLSDVRQKCQDEtqmisslKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqLETIIKSLKSTQ 537
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREE----QEAANAEVERLQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 538 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 572
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
384-547 |
2.00e-07 |
|
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: 54.65 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 446
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 447 DRLDEMDQQ--KAK---------LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE--- 512
Cdd:pfam05667 415 QRLVELAGQweKHRvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011268 513 --TQ--LE--QSIQAGKVQLETIIKSLKSTQDEINQARSKL 547
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 ... |
387-577 |
2.10e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 460
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQEDDLNRAKSE----LTRLQQEETQLEQSIQAGKVQLETIIKSLKST 536
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011268 537 QDEINQARSKLSQLQESHQEAHRTLEQY--------DEALDGAHGASLT 577
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAqqerdelaDEIASGASGKSAL 880
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
386-563 |
2.47e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLEQDIREKEEairqksnEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQKAK 458
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALES-------ENAELQAELRTLQQAKQDsehkrkkLEGQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDMLSdvrqKCQDETQMISSLktqiqsqesdlksqeddLNRAKSELTRLQQEETQLEQSIQAGKVQL--ETIIK----- 531
Cdd:pfam01576 431 LAEKLS----KLQSELESVSSL-----------------LNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQKlnlst 489
|
170 180 190
....*....|....*....|....*....|..
gi 1953011268 532 SLKSTQDEinqaRSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam01576 490 RLRQLEDE----RNSLQEQLEEEEEAKRNVER 517
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
373-551 |
3.50e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 373 SCLgSGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELE---AQKQ----- 443
Cdd:pfam10174 376 STL-AGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEriier 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 444 -------DAQDRLDEMDQQKAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESD-------LKSQEDDLNRAKSELT 506
Cdd:pfam10174 455 lkeqrerEDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKEECS 534
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 507 RLQ--------QEET------------QLEQSIQ-----AGKVQ--LETIIKSLKSTQDEINQARSKLSQLQ 551
Cdd:pfam10174 535 KLEnqlkkahnAEEAvrtnpeindrirLLEQEVArykeeSGKAQaeVERLLGILREVENEKNDKDKKIAELE 606
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-566 |
3.54e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKS--NEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 462 MLSDVRQKCQDETQMIsSLKTQIQSQESDLK-----------SQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETII 530
Cdd:PRK03918 544 LKKELEKLEELKKKLA-ELEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDAEK----ELEREE 618
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ----YDE 566
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEElekkYSE 658
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-580 |
4.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 463
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQleqsiqagkvqletiikSLKSTQDEINQA 543
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA-----------------DLDADLESLPEY 817
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011268 544 RSKLSQLQESHQEAHRtlEQYDEALDGAHGASLTNLA 580
Cdd:COG4913 818 LALLDRLEEDGLPEYE--ERFKELLNENSIEFVADLL 852
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
383-556 |
4.86e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDdisQEIAQLQREKYSLEQDIREKEEAI---RQKSNE-VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:PHA02562 176 IRELN---QQIQTLDMKIDHIQQQIKTYNKNIeeqRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDMLSDVRQK--------------------------C----QDETQMISSLKT---QIQSQESDLKSQEDDLNRAKSEL 505
Cdd:PHA02562 253 PSAALNKLNTAaakikskieqfqkvikmyekggvcptCtqqiSEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 506 TRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA-------RSKLSQLQESHQE 556
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvdnAEELAKLQDELDK 390
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
354-571 |
4.94e-07 |
|
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: 53.43 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 354 LSPDMVPPSERGTpipDGSSCLGSGEFTGVKELDDISQEIAQLQREkyslEQDIREKEEAIRQKSNEVQE----LQNDLD 429
Cdd:TIGR00618 522 NPGPLTRRMQRGE---QTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCDNRSKEdipnLQNITV 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 430 R---ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmissLKTQIQSQESDLKSQEDdlnRAKSELT 506
Cdd:TIGR00618 595 RlqdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSI 667
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 507 RLQQEetQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 571
Cdd:TIGR00618 668 RVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
384-559 |
5.70e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 453
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 454 QQKAKLRDMLSDVRqkcQDETQMISSLKTQIQSqESDLKSQEDDLNR----AKSELTRL---QQEETQLEQSiqagkvQL 526
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRksleGNTQLQDLlqkQRDYLTARIQ------RL 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011268 527 ETIIKSLkstQDEINQARSKLSQLQ----ESHQEAHR 559
Cdd:PRK11281 240 EHQLQLL---QEAINSKRLTLSEKTvqeaQSQDEAAR 273
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
391-590 |
5.75e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 471 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQqeetqlEQS--IQAGKVQLETIIKSLKSTQDEINQARSKLS 548
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLR------EQSgeEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011268 549 QLQEShqeahrtLEQYDEALDGAHGASLTNLADLSE---GVSLAE 590
Cdd:PRK04863 652 ARKQA-------LDEEIERLSQPGGSEDPRLNALAErfgGVLLSE 689
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-556 |
6.01e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIaqlqREKYSLEQDIREKEEAIRQKSNEVQELQ---NDLDRETSSLQ----ELEAQKQDAQDRLDEMDQQK 456
Cdd:PRK03918 200 KELEEVLREI----NEISSELPELREELEKLEKEVKELEELKeeiEELEKELESLEgskrKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVR--QKCQDETQMISSLKTQIqsqesdlksqEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLK 534
Cdd:PRK03918 276 EELEEKVKELKelKEKAEEYIKLSEFYEEY----------LDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLE 341
|
170 180
....*....|....*....|..
gi 1953011268 535 STQDEINQARSKLSQLQESHQE 556
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHEL 363
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
394-531 |
6.53e-07 |
|
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: 49.65 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQREKYslEQDIREKEEAIRQKSNEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 473
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 474 TQMIsslktQIQSQESDLKSQEDD----LNRAKseltRLQQEetqlEQSIQAGKVQLETIIK 531
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-568 |
7.83e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQ---DRLDEMDQQKAKLR 460
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISSLKTQI---QSQESDLKSQEDD----------LNRAKSELTRLQQEETQLEQSIQAgkvqLE 527
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLSRLEEEING----IE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011268 528 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 568
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-582 |
8.53e-07 |
|
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: 52.92 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 455
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 -------------KAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlQQEETQLEQSI 519
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 520 QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHrtLEQYDEALDGAHGASLTNLADL 582
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLK--EDANSEQAQGSIGERLAQLEDL 898
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
402-591 |
9.76e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.59 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 402 SLEQDIREKEEAIRQksnEVQELQNDLDRETSSL-------QELEAQKQDAQDRLDEMdQQKAKL----------RDMLS 464
Cdd:COG1842 16 ALLDKAEDPEKMLDQ---AIRDMEEDLVEARQALaqvianqKRLERQLEELEAEAEKW-EEKARLalekgredlaREALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DvRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQlETIIKSLKSTQDEinQAR 544
Cdd:COG1842 92 R-KAELEAQ---AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEALSGIDSD--DAT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011268 545 SKLSQLQESHQEahrtLEQYDEALDG-AHGASLTN-LADLSEGVSLAER 591
Cdd:COG1842 165 SALERMEEKIEE----MEARAEAAAElAAGDSLDDeLAELEADSEVEDE 209
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
391-569 |
1.05e-06 |
|
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: 52.66 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRE-TSSLQELEAQKQDA------QDRLDEMDQQKAKLR 460
Cdd:TIGR00618 462 QESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISSLKTQIQsqesdlksqeddlnrakseltRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 540
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQ---------------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
170 180 190
....*....|....*....|....*....|
gi 1953011268 541 N-QARSKLSQLQESHQEahrtLEQYDEALD 569
Cdd:TIGR00618 601 EkLSEAEDMLACEQHAL----LRKLQPEQD 626
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-572 |
1.34e-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: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 382 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ---NDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDMLSDVRQKCQDETQMISSLKTQ----IQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVqletiiKSLK 534
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD------DYLK 973
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953011268 535 STQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 572
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-574 |
1.40e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------SNEVQELQND---LDRETSSL 435
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDillLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 436 QEleaQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ 509
Cdd:pfam01576 151 SK---ERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 510 QEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGA 574
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
411-584 |
1.58e-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: 49.99 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 411 EEAIRQKSNEVQ--ELQNDLDRETSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQMIS 478
Cdd:pfam12795 3 DELEKAKLDEAAkkKLLQDLQQALSLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 479 SLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI---IKSLKSTQDEINQARSKLSQLQESHQ 555
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrnrLNGPAPPGEPLSEAQRWALQAELAAL 161
|
170 180
....*....|....*....|....*....
gi 1953011268 556 EAhrTLEQYDEALdgahgASLTNLADLSE 584
Cdd:pfam12795 162 KA--QIDMLEQEL-----LSNNNRQDLLK 183
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
385-569 |
1.60e-06 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 51.11 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL---QELE--------AQKQDAQD---RLD 450
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAewkLELErvlpqlkvTIKADAKDwraHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 451 EMDQQKAKLRDMLSDVRQKcqdetqmisslktqiqsqesdLKSQEDDLNRAkseLTRLQQEETQLEQsiqagkvQLETII 530
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:pfam10498 275 QEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELE 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-553 |
1.61e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 410 KEEAIRQ--KSNE----VQELQNDLDRetsSLQELEAQKQDAQ------------------DRLDEMDQQKAKLRDMLSD 465
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELER---QLKSLERQAEKAErykelkaelrelelallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 466 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARS 545
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
....*...
gi 1953011268 546 KLSQLQES 553
Cdd:TIGR02168 331 KLDELAEE 338
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
397-510 |
1.63e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 397 QREKYSLEQDIREKEEAIRQKSNEVQELqndldretsslqelEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDE--- 473
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERL--------------EAEVEELEAELEEKDERIERLERELSEARSEERREirk 463
|
90 100 110
....*....|....*....|....*....|....*..
gi 1953011268 474 TQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ 510
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-567 |
1.70e-06 |
|
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: 51.89 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLdreTSSLQELEAQKQDAQDRLDE-MDQQKAKLR 460
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCqtlLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDALNQSLKElMHQARTVLK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMIsslktQIQSQESDLKSQEDDLNRAKSELT-RLQQEETQLEQSI----QAGKVQLETIIKSLKS 535
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAAL-----QTGAELSHLAAEIQFFNRLREEDThLLKTLEAEIGQEIpsdeDILNLQCETLVQEEEQ 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011268 536 TQDEINQARSKL--------------SQLQESHQEAHRTLEQYDEA 567
Cdd:TIGR00618 833 FLSRLEEKSATLgeithqllkyeecsKQLAQLTQEQAKIIQLSDKL 878
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
482-569 |
1.71e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 482 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 561
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
....*...
gi 1953011268 562 EQYDEALD 569
Cdd:COG4372 104 ESLQEEAE 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
386-502 |
1.74e-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: 50.92 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREkysLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 465
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 1953011268 466 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 502
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
381-587 |
1.84e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.50 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 381 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmDQQKAKLR 460
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTE-NLEAIKEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DM-------LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRA-KSELTRLQQEETQLEQSIQAGKVQLETIIKS 532
Cdd:COG5185 363 IEnivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKL 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 533 LKSTQDEINQAR-----SKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVS 587
Cdd:COG5185 443 LNELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-569 |
2.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVR-------------------QKCQDETQMISSLKtQIQSQESDLKSQEDDLNR 500
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGELErqleplerqaekaeryrelKEELKELEAELLLL-KLRELEAELEELEAELEE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 501 AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-575 |
2.60e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQ-------------------KC----------------QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSeltrL 508
Cdd:PRK02224 429 AELEAtlrtarerveeaealleagKCpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED----L 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 509 QQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGAS 575
Cdd:PRK02224 505 VEAEDRIERLEE----RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
383-511 |
2.62e-06 |
|
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: 50.19 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 462
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1953011268 463 lsdvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE 511
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-569 |
3.00e-06 |
|
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: 51.12 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL----------------QELEAQKQDAQDR 448
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehalsirvlpKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 521
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011268 522 GKVQLETI-IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:TIGR00618 765 NNNEEVTAaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
384-564 |
3.17e-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: 50.88 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ----QEETQLEQsiqagKVQLETIIKSLKSTQDE 539
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 1953011268 540 IN---QARSKLSQLQESHQEAHRTLEQY 564
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
397-517 |
3.24e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 46.84 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 397 QREKYSLEQDIREKEEAIRQKsnevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQM 476
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953011268 477 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE--ETQLEQ 517
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
393-563 |
3.42e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 393 IAQLQREKYSLEQDiREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 453
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 454 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN----RAKSEL-TRLQQEETQLEQSIQAGKVQLET 528
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAeERARARRDELHARLSANRSRRNQ 1078
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011268 529 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
383-511 |
3.72e-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: 49.63 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQrekySLEQDIREKEEAIRQKSNEVQEL--------QNDLDRETSSLQELEAQKQDAQDRLDEMDQ 454
Cdd:smart00787 157 KEDYKLLMKELELLN----SIKPKLRDRKDALEEELRQLKQLedeledcdPTELDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 455 QKAKLRDMLSDVRQKCQDetqmissLKTQIQSQESDLKS----QEDDLNRAKSELTRLQQE 511
Cdd:smart00787 233 ELQELESKIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
435-567 |
3.86e-06 |
|
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: 48.87 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 435 LQELEAQKQDAQDRLDEMDQQKAKLRDmlsdVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAkseLTRLQQEETQ 514
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEK----RAEKAEAE---VAALNRRIQLLEEELERTEERLAEA---LEKLEEAEKA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 515 LEQSIQAGKVqLETiikslKSTQDEiNQARSKLSQLQESHQEAHRTLEQYDEA 567
Cdd:pfam00261 73 ADESERGRKV-LEN-----RALKDE-EKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
382-542 |
3.92e-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: 49.85 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 382 GVKEL-----DDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKSNEV 421
Cdd:pfam03148 130 GIQELlqrtlEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 422 -----QELQN--DLdRET--SSLQ----ELEAQKQDA----QDRLDEMDQQKAKLRDMLsdvrQKCQDEtqmISSLKTQI 484
Cdd:pfam03148 210 ieraeKERAAsaQL-RELidSILEqtanDLRAQADAVnfalRKRIEETEDAKNKLEWQL----KKTLQE---IAELEKNI 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 485 QSQESDLKSQEDDL--------NRAK---SELTR------LQQEETQLEQSIQAGKVQL---ETIIKSLKSTQDEINQ 542
Cdd:pfam03148 282 EALEKAIRDKEAPLklaqtrleNRTYrpnVELCRdeaqygLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
384-488 |
4.08e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 46.41 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKKE---QELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|....*
gi 1953011268 464 SDVRQKcqdetqmISSLKTQIQSQE 488
Cdd:pfam13863 83 KKLTAQ-------IEELKSEISKLE 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
384-567 |
4.38e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQeIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRET-SSLQELEAQKQDA----------------- 445
Cdd:pfam02463 156 LEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKeQAKKALEYYQLKEkleleeeyllyldylkl 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 446 -QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV 524
Cdd:pfam02463 235 nEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011268 525 QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 567
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
482-552 |
4.46e-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: 4.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 482 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQE 552
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-567 |
4.66e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEaqkqdaqDRLDEMDQQKAKlrdml 463
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-------DELNKDDFELKK----- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 sdvrqkcqdetqmiSSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:TIGR04523 557 --------------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
170 180
....*....|....*....|....*..
gi 1953011268 544 R---SKLSQLQESHQEAHRTLEQYDEA 567
Cdd:TIGR04523 623 KkenEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-571 |
4.89e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKSNEVQELQNDLDRetsslqeLEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERREDLEELIAERRETIEEKRER 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKvQLETIIKSLKSTQDEINQ 542
Cdd:PRK02224 539 AEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953011268 543 ARSKLSQLQESHQEAHRTLE-------QYDEALDGA 571
Cdd:PRK02224 611 LREKREALAELNDERRERLAekrerkrELEAEFDEA 646
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
386-521 |
5.33e-06 |
|
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: 47.68 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLeqdiREKEEAIrqkSNEVQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 465
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSEL---SERLQQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 466 VRQKCQDET-----QMISSLKTQIQSQESDLK-----SQEDDLNRA-KSELTRLQQeetQLEQSIQA 521
Cdd:pfam16043 81 VSRDQFDETleelnQMLQELLDKLEGQEDAWKkaletLSEELDTKLdRLELDPLKE---LLERRIKA 144
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
381-566 |
6.48e-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: 49.79 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 381 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKSNEVQELQNDLDRETSS-------------- 434
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCqDETQMiSSLKTQIQSQESD--LKSQEDDLNRAKSELT------ 506
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQREL-EEARA-SRDEILAQSKESEkkLKNLEAELLQLQEDLAaserar 856
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 507 -RLQQEETQLEQSIQAGKvqletiiKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDE 566
Cdd:pfam01576 857 rQAQQERDELADEIASGA-------SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLND 910
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
403-556 |
6.78e-06 |
|
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: 49.85 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 403 LEQDIReKEEAIRQKSNEV-QELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET 474
Cdd:pfam09726 400 LEQDIK-KLKAELQASRQTeQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQ 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 475 QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQ-LEQSIQagkvQLETIIKSL----KSTQDEINQARSK--- 546
Cdd:pfam09726 479 EARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKR----ELESEIKKLthdiKLKEEQIRELEIKvqe 554
|
170
....*....|
gi 1953011268 547 LSQLQESHQE 556
Cdd:pfam09726 555 LRKYKESEKD 564
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
435-553 |
7.42e-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: 49.73 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 435 LQELEAQKQDAQDRLDEMDQ----QKAKLRDMLSDVRQKCQdETQMISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQ 510
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElhekQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES--QSQEDLRNQLQNTVHELEA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953011268 511 EETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 553
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEA 199
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
384-548 |
7.75e-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: 47.75 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKcqdetqmISSLKTQIQsqesDLKSQEDDLnrakseLTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEIN- 541
Cdd:pfam04012 113 VEQLRKQ-------LAALETKIQ----QLKAKKNLL------KARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIEe 175
|
....*...
gi 1953011268 542 -QARSKLS 548
Cdd:pfam04012 176 rEARADAA 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-568 |
8.22e-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: 49.79 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEE---------------------AIRQKSNEVQELQNDLDRETSSL-------- 435
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEelqaalarleeetaqknnalkKIRELEAQISELQEDLESERAARnkaekqrr 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 436 ---QELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSEL 505
Cdd:pfam01576 296 dlgEELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKANL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 506 trlqqEETQleQSIQAGKVQLETIIKSLKSTQDEINQARSKL-SQLQE---SHQEAHRTLEQYDEAL 568
Cdd:pfam01576 376 -----EKAK--QALESENAELQAELRTLQQAKQDSEHKRKKLeGQLQElqaRLSESERQRAELAEKL 435
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
420-555 |
8.80e-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: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 420 EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmisslktqiqSQESDLKSQEDDLN 499
Cdd:smart00787 152 NLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQEIM 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 500 RAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR----SKLSQLQESHQ 555
Cdd:smart00787 222 IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLK 281
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
384-552 |
8.97e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.65 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 463
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 sdvrqkcqdetQMISSLKTQIQSQESDLKSQEDDLNrakselTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*....
gi 1953011268 544 RSKLSQLQE 552
Cdd:pfam15905 320 EQEHQKLQQ 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-566 |
8.98e-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: 49.66 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQdirEKEEAIRQKSNevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 460
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQ---EKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCQDETQMISSLKTQIQSQESdlksqeddlnRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 540
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKER----------LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
170 180
....*....|....*....|....*....
gi 1953011268 541 NQARSKLSQLQESHQE---AHRTLEQYDE 566
Cdd:TIGR00606 464 QQLEGSSDRILELDQElrkAERELSKAEK 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-568 |
9.52e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL 449
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 450 DEMdQQKAKLrdmLSDVRQKcqdETQMiSSLKTQIQSQE-SDLKSQEDDLNRAKSELTRlqqEETQLEQSIQagkvQLET 528
Cdd:PRK03918 355 EEL-EERHEL---YEEAKAK---KEEL-ERLKKRLTGLTpEKLEKELEELEKAKEEIEE---EISKITARIG----ELKK 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011268 529 IIKSLKSTQDEINQARSKL----SQLQESHQEahRTLEQYDEAL 568
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKCpvcgRELTEEHRK--ELLEEYTAEL 461
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
395-556 |
1.09e-05 |
|
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: 48.97 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 395 QLQREKYSLEQdIREKEEAIRQKsnEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvRQKCQD 472
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKLE------LEKEKR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 473 ETQMISSLKTQIQSQESDLKSQ---EDDLNR--------------AKSELTRLQQEETQLEQSIQAGKVQLETIIKSL-- 533
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQamiEEERKRkllekemeerqkaiYEEERRREAEEERRKQQEMEERRRIQEQMRKATee 564
|
170 180
....*....|....*....|...
gi 1953011268 534 KSTQDEINQARSKLSQLQESHQE 556
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEKA 587
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
291-364 |
1.12e-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: 44.67 E-value: 1.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 291 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 364
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-566 |
1.16e-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: 49.20 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ-LALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DV---RQKCQDETQMISSLKTQIQSQES---------------DLKSQEDDLNRAKSELTRLQQ---EETQLEQSIQAGK 523
Cdd:TIGR00618 712 HIeeyDREFNEIENASSSLGSDLAAREDalnqslkelmhqartVLKARTEAHFNNNEEVTAALQtgaELSHLAAEIQFFN 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 524 VQLETIIKSLKSTQDEINQAR-------------------SKLSQLQESHQEAH---RTLEQYDE 566
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIpsdedilnlqcetlvqeeeQFLSRLEEKSATLGeitHQLLKYEE 856
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
395-552 |
1.24e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 395 QLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDaqdrLDEMDQQKAKLRDMLSDV--RQKCQD 472
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD----FEEASGKKIYEHDSMSTMhfRSLGSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 473 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTR-----LQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKL 547
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
....*
gi 1953011268 548 SQLQE 552
Cdd:pfam15921 302 EIIQE 306
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
385-592 |
1.28e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEET---------QLEQSIQAGKVQ-LETIIKSL 533
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlRRELDDRNMEVQrLEALLKAM 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 534 KS-TQDEI----------NQARSKLSQLQ---ESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERG 592
Cdd:pfam15921 439 KSeCQGQMerqmaaiqgkNESLEKVSSLTaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
393-562 |
1.33e-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: 48.95 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 393 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqqkakLRDMLSDvRQKCQD 472
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE-------LKKILAE-DEKLLD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 473 ETQMISSLKTQIQSQESD----LKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETiiKSLKSTQDEINQARSKLS 548
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK--EKLKNIELTAHCDKLLLE 500
|
170
....*....|....
gi 1953011268 549 QLQESHQEAHRTLE 562
Cdd:pfam05483 501 NKELTQEASDMTLE 514
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
384-557 |
1.35e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKSNEVQ------ELQNDLDRETSSL-QELEAQKQ--DAQDRLDE 451
Cdd:COG1340 85 EKLNELREELDELRKELAELNKaggSIDKLRKEIERLEWRQQtevlspEEEKELVEKIKELeKELEKAKKalEKNEKLKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 452 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqesdLKSQEDDLNR----AKSELTRLQQEETQLEQSIQAGKVQLE 527
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRKeadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
170 180 190
....*....|....*....|....*....|..
gi 1953011268 528 TIIKSLKSTQDEINQARSKLSQ--LQESHQEA 557
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEI 272
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-563 |
1.38e-05 |
|
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: 47.99 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKsNEVQELQNDL-DRETSSLQELEAQKQDAQ------DRLDEMDQQK 456
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERK-RYRQELEEQIeEREQKRQEEYEEKLQEREqmdeivERIQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLsdvRQKCQDETQMISSLKTQIQSQEsDLKSQEDDL-----NRAKSELTRLQQEEtQLEQSIQAGKVQ--LETI 529
Cdd:pfam13868 118 AEEKLEK---QRQLREEIDEFNEEQAEWKELE-KEEEREEDErileyLKEKAEREEEREAE-REEIEEEKEREIarLRAQ 192
|
170 180 190
....*....|....*....|....*....|....
gi 1953011268 530 IKSLKSTQDEINQARSKLsqLQESHQEAHRTLEQ 563
Cdd:pfam13868 193 QEKAQDEKAERDELRAKL--YQEEQERKERQKER 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
453-590 |
1.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 453 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLE----- 527
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 528 --------------------------------------TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|.
gi 1953011268 570 GAHGASLTNLADLSEGVSLAE 590
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAE 195
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
435-563 |
1.49e-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: 47.70 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 435 LQELEAQKQDAQDRLDEMDQQKAKLRD---MLSDVRQKCQDETQmisSLKTQIQSqesdLKSQEDDLNRAK-SELTRLQQ 510
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKeleLLNSIKPKLRDRKD---ALEEELRQ----LKQLEDELEDCDpTELDRAKE 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 511 EETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
1.52e-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: 44.67 E-value: 1.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1953011268 32 GRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLV 80
Cdd:pfam12763 24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
433-552 |
1.55e-05 |
|
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: 44.94 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 433 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISslkTQIQSQESDLKSqeddLNRAKSELTRLQQEE 512
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1953011268 513 TQLEQSIQAGKVQLETIIKSLKST----QDEINQARSKLSQLQE 552
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNE 117
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
390-557 |
1.58e-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: 47.41 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 390 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV-RQ 468
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALpSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 469 KCQDETQMISSLKTQIQSQesDLKSQ----EDDLNRAKSELTRLQqeetQLEQSIQAgkvQLETIiksLKSTQDEINQAR 544
Cdd:pfam06008 119 DLSRMLAEAQRMLGEIRSR--DFGTQlqnaEAELKAAQDLLSRIQ----TWFQSPQE---ENKAL---ANALRDSLAEYE 186
|
170
....*....|...
gi 1953011268 545 SKLSQLQESHQEA 557
Cdd:pfam06008 187 AKLSDLRELLREA 199
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-573 |
1.68e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 381 TGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA--- 457
Cdd:PRK02224 509 DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 458 -------KLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL---------TRLQQEETQLEQSIQA 521
Cdd:PRK02224 586 eriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeariEEAREDKERAEEYLEQ 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 522 GKVQLETIIKSLKSTQDEINQARSKLSQLqESHQEAHRTLEQYDEALDGAHG 573
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEEL-EELRERREALENRVEALEALYD 715
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
372-511 |
1.72e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 372 SSCLGSGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDR 448
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 449 LDEMdqqKAKLRDMLSDVRQKCQDETQMISSLKTQIQsQESDLKSQEDDLNRAKselTRLQQE 511
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLEALEEGKKRLQRELEALTQ-QLEEKAAAYDKLEKTK---NRLQQE 581
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
395-569 |
1.78e-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: 46.67 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 395 QLQREKYSLEQDIREKEEAIRQKSNEvqelqndldretSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlSDVRQKCQDET 474
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG------------DDLESVEALLKKHEALEAELAAHEERV----EALNELGEQLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 475 QMISSLKTQIQSQESDLKSQEDDLN-RAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 553
Cdd:cd00176 68 EEGHPDAEEIQERLEELNQRWEELReLAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK 147
|
170
....*....|....*.
gi 1953011268 554 HQEAHRTLEQYDEALD 569
Cdd:cd00176 148 HKELEEELEAHEPRLK 163
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-568 |
1.98e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQLETIIKSlkstqDEIN 541
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIrdEKKGLGRTIELKKEILE-----KKQE 454
|
170 180
....*....|....*....|....*..
gi 1953011268 542 QARSKLSQLQESHQEAHRTLEQyDEAL 568
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILEL-DQEL 480
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
405-552 |
2.01e-05 |
|
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: 46.14 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 405 QDIREKEEAIRQKSNEVQELQNDLDRETSSLqeleaqKQDAQDRLDEMDQQKAklrdmlsdVRQKCQDETQMISSLKTQI 484
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTL------KSQGDMQDLNGNNQSV--------TRQKMQQLEQMLTALDQMR 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 485 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQ--AGKV-----QLETIIKSLKSTQDEINQARSKLSQLQE 552
Cdd:cd16853 77 RQIVSELAGLLSAMEYVQKNLTDEELADWKRRQQIAciGGPPnicldRLENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
388-562 |
2.11e-05 |
|
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: 47.76 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREKYSLeqdiREK-EEAIRQKSNEVQELqndLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:pfam05622 279 EIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 467 RQKCQDEtqmiSSLKtqiqsqeSDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ-LETIIKSLKSTQDEINQARS 545
Cdd:pfam05622 352 GSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEE 420
|
170
....*....|....*..
gi 1953011268 546 KLSQLQESHQEAHRTLE 562
Cdd:pfam05622 421 RYKKYVEKAKSVIKTLD 437
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
396-563 |
2.11e-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: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 396 LQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ-KCQDET 474
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 475 QMiSSLKTQIqsqESDLKSQEDD-------LNRAKSEL-TRLQQEETQLEQSIqAGKVQLETIIKSLKSTQDEINQARS- 545
Cdd:pfam01576 721 NM-QALKAQF---ERDLQARDEQgeekrrqLVKQVRELeAELEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGREe 795
|
170 180
....*....|....*....|.
gi 1953011268 546 ---KLSQLQESHQEAHRTLEQ 563
Cdd:pfam01576 796 avkQLKKLQAQMKDLQRELEE 816
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-569 |
2.34e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQ---DETQMISSLKTQIQSQESDLKSQEDDLNraksELTRLQQEEtqleqsiqaGKVQLETIIKSLKSTQDEI 540
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDII----ELMKDWLKE---------LSLHYKKYITRMIRIKDLP 707
|
170 180
....*....|....*....|....*....
gi 1953011268 541 nqarsKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:TIGR04523 708 -----KLEEKYKEIEKELKKLDEFSKELE 731
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-517 |
2.44e-05 |
|
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: 47.22 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 452
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 453 ---DQQKAKLRD-MLSDVRQKCQDETQMISSLKTQIQSQEsDLKSQEDDLNRA-KSELTRLQQEETQLEQ 517
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE-RRLAEEAEREEEeFERMLRKQAEDEEIEQ 278
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
404-528 |
2.49e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 404 EQDIREKEEAIRQKSNEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSD----VRQKc 470
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPnspqVRQL- 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 471 qdETQmISSLKTQIQSQESDL--KSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 528
Cdd:COG3524 255 --RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
382-477 |
2.71e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.50 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 382 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 460
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 1953011268 461 DMLSDVRQKCQDETQMI 477
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
410-557 |
2.79e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 45.65 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 410 KEEAIRQKSNEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqmisslk 481
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 482 tqiQSQESDLKSQEDDLNRAKSELTRLQQEETQ-LEQSIQAGKVQLETIIksLKSTQDEINQARSKLsqLQESHQEA 557
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLERISGLTSEEAKEIL--LDEVEEELRHEAAVM--IKEIEEEA 178
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
340-562 |
2.85e-05 |
|
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: 47.89 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 340 IQQKVSkgidppqVLSPDMVPPSERGTPIPDGSSCLGSgefTGVKELDDISQ-EIA-----------QLQREK-YSLEQD 406
Cdd:pfam10174 480 LKEKVS-------ALQPELTEKESSLIDLKEHASSLAS---SGLKKDSKLKSlEIAveqkkeecsklENQLKKaHNAEEA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 407 IREKEE---AIRQKSNEVQ-------ELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQKCQDETQM 476
Cdd:pfam10174 550 VRTNPEindRIRLLEQEVArykeesgKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQMKEQNKK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 477 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEetqleqsiqagkVQLETIIKSLKSTQDEINQARSKLSQLQESHQE 556
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ------------LQLEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
....*.
gi 1953011268 557 AHRTLE 562
Cdd:pfam10174 688 KDGHLT 693
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
381-568 |
3.05e-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: 47.73 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 381 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKS-------NEVQELQNDLDRETSSLQELEAQKQDAQDR- 448
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKEtsnkkaqDKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI--QSQESDLKSQEDDLNRAKSEL-----TR 507
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMgqmqvLQ 1051
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 508 LQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEahrtlEQYDEAL 568
Cdd:TIGR00606 1052 MKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAE-----EKYREMM 1107
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
394-556 |
3.61e-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: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQREKYSLEQDIREKEEAirqkSNEVQELQNDLDRETSSLQE--------------LEAQKQDAQDRLDEMDQQKAKL 459
Cdd:pfam01576 412 GQLQELQARLSESERQRAEL----AEKLSKLQSELESVSSLLNEaegkniklskdvssLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 RdmlSDVRQKCQDETQMISSLKTQIQSQESdLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 539
Cdd:pfam01576 488 S---TRLRQLEDERNSLQEQLEEEEEAKRN-VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
170
....*....|....*..
gi 1953011268 540 INQARSKLSQLQESHQE 556
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
493-593 |
4.00e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 493 SQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 572
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100
....*....|....*....|.
gi 1953011268 573 GASLTNLADLSEGVSLAERGG 593
Cdd:COG4942 97 AELEAQKEELAELLRALYRLG 117
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-563 |
4.21e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 452
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 453 DQQKAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ---SI 519
Cdd:PRK04863 389 EEEVDELKSQLADYQQaldvqqtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsVA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 520 QAGKVQLETIIKSLKSTQDEI------NQARSKLSQLQESHQEA---------HRTLEQ 563
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAeqlqqlrmrLSELEQ 527
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
383-538 |
4.39e-05 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 46.92 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 455
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 KAKLRDMLSDVRQKCQdetQMISSLKTQIQSQESDLK----SQEDDLNRAKSELTRLQQEETQLEQS-IQAGKVQLETII 530
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
....*....
gi 1953011268 531 -KSLKSTQD 538
Cdd:pfam03999 298 dKLFYSTEQ 306
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
382-556 |
4.40e-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: 47.02 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 382 GVKELD-DISQEIAQLQREKYSLEQDIRE----KEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:pfam05483 64 GLKDSDfENSEGLSRLYSKLYKEAEKIKKwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQ--DETQMISSLKT---QIQSQES-----DLKSQEDDLNRAKSELtRLQQEETQLEQSIQAgKVQL 526
Cdd:pfam05483 144 KDLIKENNATRHLCNllKETCARSAEKTkkyEYEREETrqvymDLNNNIEKMILAFEEL-RVQAENARLEMHFKL-KEDH 221
|
170 180 190
....*....|....*....|....*....|..
gi 1953011268 527 ETIIKSLKSTQDEINQARSKLSQL--QESHQE 556
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLliQITEKE 253
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
403-550 |
4.54e-05 |
|
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: 45.48 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 403 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVRQKCQDETQMISSLKT 482
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 483 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET--IIKSLKSTQDEINQARSKLSQL 550
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAafLQADLKAAKADWNQLYEQAKSL 224
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
394-527 |
4.84e-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: 43.34 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQREKysleQDIREKEEAIRQ---KSNEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDvRQKC 470
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEE-KEIE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 471 QDETQMisslktqiqsQESDLKSQeddLNRAKSELTRLQQeetQLEQSIQAGKVQLE 527
Cdd:pfam18595 73 LRELER----------REERLQRQ---LENAQEKLERLRE---QAEEKREAAQARLE 113
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
384-521 |
5.25e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.90 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLqREKysLEQDIREKEEAIRQKSN---EVQELQNDLDRETSSLQELEAQKQDAQDRLD-------EMD 453
Cdd:pfam13851 47 KLMSEIQQENKRL-TEP--LQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELKDLKWEHEVLEQrfekverERD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 454 QQKAKLRDMLSDVRQKCQDETQMissLKTQIQSQESDLKSQEDDLN----RAKSELTRLQQEETQLEQSIQA 521
Cdd:pfam13851 124 ELYDKFEAAIQDVQQKTGLKNLL---LEKKLQALGETLEKKEAQLNevlaAANLDPDALQAVTEKLEDVLES 192
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
386-562 |
5.27e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQrekyslEQDIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 465
Cdd:PRK02224 189 LDQLKAQIEEKE------EKDLHERLNGLESELAELDE---EIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 466 VRQKCQDETQMIS---SLKTQIQSQESDLKSQEDDLN--RAKSELTRLQQEETQLeqsiqagkvQLETIIKSLKSTQDEI 540
Cdd:PRK02224 260 IEDLRETIAETERereELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEA---------RREELEDRDEELRDRL 330
|
170 180
....*....|....*....|....*
gi 1953011268 541 NQARSKLSQLQ---ESHQEAHRTLE 562
Cdd:PRK02224 331 EECRVAAQAHNeeaESLREDADDLE 355
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
390-561 |
5.55e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 390 SQEIAQLQRekysLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 466
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 467 ---RQKCQDETQMISSLKTQIQSQESDLKSQE-------DDLNRAKSELTRLQQ---EETQLEQsiqagkvQLETIIKSL 533
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQslkEREQQLQ-------TKEQIHLQE 485
|
170 180 190
....*....|....*....|....*....|....
gi 1953011268 534 KSTQDEINQARSKLSQL------QESHQEAHRTL 561
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEpcplcgSCIHPNPARQD 519
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
486-556 |
5.68e-05 |
|
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: 42.55 E-value: 5.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 486 SQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQE 556
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
397-574 |
5.88e-05 |
|
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: 46.56 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 397 QREKYSLEQDIREKEEAIRQKSNEV---QELQNDLDRETSSLQELEAQ-------------KQDAQDRLDEMDQQK--AK 458
Cdd:pfam05701 218 EQDKLNWEKELKQAEEELQRLNQQLlsaKDLKSKLETASALLLDLKAElaaymesklkeeaDGEGNEKKTSTSIQAalAS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDMLSDVR---QKCQDETQMISSLKTQIQSqesdlksqedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS 535
Cdd:pfam05701 298 AKKELEEVKaniEKAKDEVNCLRVAAASLRS----------ELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIAL 367
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011268 536 TQDEINQARSKLS----QLQESHQEAhrtleqyDEALDGAHGA 574
Cdd:pfam05701 368 VQAKEKEAREKMVelpkQLQQAAQEA-------EEAKSLAQAA 403
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
432-565 |
6.32e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.88 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 432 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK------ 502
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapig 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 503 --------SELTRLQQEETQLEQSI-QAGKVQLE---TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYD 565
Cdd:pfam00529 137 gisreslvTAGALVAQAQANLLATVaQLDQIYVQitqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
387-517 |
7.35e-05 |
|
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: 43.44 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQdirEKEEAIRQKSN---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 463
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 464 sdvrqkCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL-TRLQQEETQLEQ 517
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
403-511 |
7.67e-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: 45.02 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 403 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLkt 482
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 1953011268 483 qiqsqESDLKSQEDDLNRAKSELTRLQQE 511
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
403-573 |
7.76e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 403 LEQDIREKEEAIRQKSNEVQELqnDLDRetsSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrqKC-QDETQMISSLK 481
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGS--DLDR---TVQQVNQEKQEKQHELDTVVSKIELNR--------KLiQDQQEQIQHLK 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 482 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 561
Cdd:TIGR00606 864 SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV 943
|
170
....*....|..
gi 1953011268 562 EQYDEALDGAHG 573
Cdd:TIGR00606 944 NDIKEKVKNIHG 955
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
384-504 |
7.99e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKSNEVQELQNDLD-----------RETSSLQELEAQKQ-- 443
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 444 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDL------KSQEddLNRAKSE 504
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
420-614 |
8.21e-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: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 420 EVQELQNDLDRETSSlQELEAQKQDAQDRLDEMdQQKAKlrdmlsDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN 499
Cdd:cd22656 95 EILELIDDLADATDD-EELEEAKKTIKALLDDL-LKEAK------KYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 500 RA--KSELTRLQQEETQLEQSIQAgkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH---GA 574
Cdd:cd22656 167 DLltDEGGAIARKEIKDLQKELEK---LNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLaliGP 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011268 575 SLTNLADLsegvslaeRGGFGAMDDPFKNKALLFSNNAQE 614
Cdd:cd22656 244 AIPALEKL--------QGAWQAIATDLDSLKDLLEDDISK 275
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
387-555 |
9.06e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKySLEQDirekEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 467 RQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQqeeTQLEQ---SIQAGKVQLETIIKSLKSTQDEINQA 543
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ---TQPERaqaALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170
....*....|..
gi 1953011268 544 RSKLSQLQESHQ 555
Cdd:PRK11281 190 RPSQRVLLQAEQ 201
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-584 |
9.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 422 QELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLSDVRQkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA 501
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 502 KSELTRLQQEETQLEQS---IQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTn 578
Cdd:PRK03918 237 KEEIEELEKELESLEGSkrkLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR- 315
|
....*.
gi 1953011268 579 LADLSE 584
Cdd:PRK03918 316 LSRLEE 321
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
385-520 |
9.36e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLeqdIREKEEAirqksnevqelqndldretsslqeleaqkqdAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG0542 412 ELDELERRLEQLEIEKEAL---KKEQDEA-------------------------------SFERLAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 465 DVRQKCQDETQMISslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQ 520
Cdd:COG0542 458 ALKARWEAEKELIE----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
477-569 |
9.49e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 45.49 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 477 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKS-LKSTQDEINQARSKLSQLQESHQ 555
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQaLQTAQNNLATAQAALANAEARLA 335
|
90
....*....|....
gi 1953011268 556 EAHRTLEQYDEALD 569
Cdd:TIGR04320 336 KAKEALANLNADLA 349
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
421-564 |
1.08e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 44.35 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 421 VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdETQMISSL---KTQ----IQSQESDLKS 493
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKH----ENDNLSSMlnrKERrlkdLEDQLSELKN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 494 QEDDLNRAKSELT----RLQQEETQLEQSIQAGKVQLETIIKSLK----STQDEINQARSKLSQLQeshQEAHRTLEQY 564
Cdd:pfam17078 81 SYEELTESNKQLKkrleNSSASETTLEAELERLQIQYDALVDSQNeykdHYQQEINTLQESLEDLK---LENEKQLENY 156
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
479-562 |
1.08e-04 |
|
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: 43.07 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 479 SLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQL--QESHQE 556
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIktQFAHEV 135
|
....*.
gi 1953011268 557 AHRTLE 562
Cdd:pfam11559 136 KKRDRE 141
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
383-570 |
1.15e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD---AQDRLD--EMDQQKA 457
Cdd:COG1340 49 NAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIErlEWRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 458 KL-----RDMLSDVRQKCQ--DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 530
Cdd:COG1340 129 VLspeeeKELVEKIKELEKelEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDG 570
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
388-515 |
1.16e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREKYSLE---------QDIREKEEAIrqksnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI-------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953011268 459 LRDMLSDvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA-------KSELTRLQQEETQL 515
Cdd:PHA02562 339 LLELKNK-----------ISTNKQSLITLVDKAKKVKAAIEELqaefvdnAEELAKLQDELDKI 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-489 |
1.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREkysleqdIREKEEAIRQKSNEVQELQNDLDR----ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:COG4913 338 DRLEQLERE-------IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100
....*....|....*....|...
gi 1953011268 467 RQKCQDETQMISSLKTQIQSQES 489
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLER 433
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
434-563 |
1.29e-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: 44.21 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 434 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQMISSLKTQIQS--QESDLKSQEDDL 498
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 499 NRAKSEL-TRLQQEETQLeQSIQAgkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQN---QLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNG 138
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-572 |
1.33e-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: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKSNEVQELQNDLDRETSSLQ------- 436
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 437 ELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDVRQKcqdetqmISSLKTQIQsQESDLKSQEDDLNRA-----KSELTRLQQ 510
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFKSSIAALEAK-------IAQLEEQLE-QESRERQAANKLVRRtekklKEVLLQVED 1013
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 511 EETQLEQSiqagKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 572
Cdd:pfam01576 1014 ERRHADQY----KDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
397-581 |
1.33e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 397 QREKYSLEQDIREKEEAIRQksnevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 474
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 475 -QMISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELTRLQQEETQLEQSIQA--GKVQLETI 529
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 530 IK-------SLKSTQD-------------EINQARSKLSQLQESHQeahrTLEQYD-EALDGAHGASLTNLAD 581
Cdd:PRK11281 342 LYqqqqalpSADLIEGladriadlrleqfEINQQRDALFQPDAYID----KLEAGHkSEVTDEVRDALLQLLD 410
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
400-557 |
1.34e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 400 KYSLEQDIREKEEAIRQKsneVQELQNDLDrETSSLQELEAQkqdaqdrlDEMDQQKaklRDMLSDVRQKcqdetqmiss 479
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLR---NEFEKELRER---------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 480 lKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLqeSHQEA 557
Cdd:PRK12704 81 -RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEA 155
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
426-568 |
1.36e-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: 44.82 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 426 NDLDRETSSLQE----LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMIS-SLKTQIQSqesdLKSQEDDL-- 498
Cdd:pfam09755 24 EQLQKRIESLQQenrvLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISnTLLKKIQA----LKKEKETLam 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 499 ----------NRAKSELTRLQQEETQLEQSI-QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 567
Cdd:pfam09755 100 nyeqeeefltNDLSRKLTQLRQEKVELEQTLeQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEA 179
|
.
gi 1953011268 568 L 568
Cdd:pfam09755 180 L 180
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-563 |
1.41e-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: 45.81 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-----------DLDRETSSLQELEAQKQ--------- 443
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 444 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE---DDLNRAKSELTRLQQEETQLEQ 517
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011268 518 SIQAGKVQLEtiIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:TIGR00606 493 NSLTETLKKE--VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
384-546 |
1.46e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIR----------QKSNEvqelqnDLDRET-SSLQELEAQKQDAQDRLDEM 452
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlalEKGRE------DLAREAlERKAELEAQAEALEAQLAQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 453 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE----DDLNRAKSELTRLQQEETQLEQSIQAgkvqLET 528
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA----AAE 186
|
170
....*....|....*...
gi 1953011268 529 IIKSlKSTQDEINQARSK 546
Cdd:COG1842 187 LAAG-DSLDDELAELEAD 203
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
403-605 |
1.54e-04 |
|
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: 43.90 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 403 LEQDIREKEEAIRQKSNEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQMISSLKT 482
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 483 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--TQDEINQARSKLSQlqeshQEAHRT 560
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLST-----SSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 561 LEQYD------EALDGAHgASLTNLADLSEGVSLAERGGFGAMDDPFKNKA 605
Cdd:pfam04012 166 FERIEekieerEARADAA-AELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
388-557 |
1.54e-04 |
|
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: 42.68 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREKY-SLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAklrdmlsdv 466
Cdd:pfam12718 10 ENAQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVE-------KLEEQLKEAKEKAEESEKLKT--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 467 rqkcQDEtqmisSLKTQIQSQESDLKSQEDDLnraKSELTRLQQEETQLEQSiqagkvqlETIIKSLkstQDEINQARSK 546
Cdd:pfam12718 74 ----NNE-----NLTRKIQLLEEELEESDKRL---KETTEKLRETDVKAEHL--------ERKVQAL---EQERDEWEKK 130
|
170
....*....|.
gi 1953011268 547 LSQLQESHQEA 557
Cdd:pfam12718 131 YEELEEKYKEA 141
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
436-563 |
1.54e-04 |
|
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: 42.17 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 436 QELEAQKQDAQDRLDEMDQQKAKLRDMlsdvRQKCQDETQMIsslktqiqsqESDLKSQEDDLNRAKseltRLQQEETQL 515
Cdd:pfam13863 13 LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKF----------DKFLKENDAKRRRAL----KKAEEETKL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1953011268 516 eqsiqagKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam13863 75 -------KKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
440-592 |
1.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 440 AQKQDAQDRLDEMdQQKAKL---RDMLSDVR---QKCQDETQ-MISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQE- 511
Cdd:PRK02224 146 ATPSDRQDMIDDL-LQLGKLeeyRERASDARlgvERVLSDQRgSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEi 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 512 ---ETQLEQSIQAgKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSL 588
Cdd:PRK02224 223 eryEEQREQARET-RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE 301
|
....
gi 1953011268 589 AERG 592
Cdd:PRK02224 302 AGLD 305
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
385-486 |
1.61e-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: 42.24 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQ-----------KSNEVQELQ---NDLDRETSSLQELEAQKQDAQDRLD 450
Cdd:pfam07926 9 EIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqnyerelvlHAEDIKALQalrEELNELKAEIAELKAEAESAKAELE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1953011268 451 EM----DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 486
Cdd:pfam07926 89 ESeeswEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
425-584 |
1.61e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 425 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD-------------ETqmISSLKTQIQSQESDL 491
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrksllanrfsfgPA--LDELEKQLENLEEEF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 492 kSQEDDLN------RAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST-QDEINQARSKLSQLQES-----HQEAHR 559
Cdd:PRK04778 182 -SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAGYRELVEEgyhldHLDIEK 256
|
170 180
....*....|....*....|....*
gi 1953011268 560 TLEQYDEALDgahgaslTNLADLSE 584
Cdd:PRK04778 257 EIQDLKEQID-------ENLALLEE 274
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
385-590 |
1.66e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE---LEAQKQDAQDRLDEMDQQKAKL-- 459
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSMELEKNNYYke 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 --------------------RDMLSDVRQkCQDETQMISSLKTQIQSQE------SDL----------KSQEDDLNRAKS 503
Cdd:PRK01156 278 leerhmkiindpvyknrnyiNDYFKYKND-IENKKQILSNIDAEINKYHaiikklSVLqkdyndyikkKSRYDDLNNQIL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 504 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQ----ARSKLSQLQESHQEAHRTLEQYD---EALDGAHGASL 576
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEilkiQEIDPDAIKKELNEINVKLQDISskvSSLNQRIRALR 436
|
250
....*....|....
gi 1953011268 577 TNLADLSEGVSLAE 590
Cdd:PRK01156 437 ENLDELSRNMEMLN 450
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
386-556 |
1.66e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 458
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LrDMLSDvRQKCQ----DETQMISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELTRLQQEETQLeQSIQ 520
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011268 521 AGKVQLETIIKSLKSTQDEINQARS-KLSQLQESHQE 556
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvALDNWRQVHEQ 725
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
401-543 |
1.67e-04 |
|
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: 42.90 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 401 YSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQqkakLRDMLSD--VRQKCQDETQMI 477
Cdd:pfam16789 3 YPLEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVrKHKKAKMQQ----LRDEMDRgtTSDKILQMKRYI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953011268 478 SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--------TQDEINQA 543
Cdd:pfam16789 79 KVVKERLKQEEKKVQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKeeedqeerEQDEIGSA 152
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
388-569 |
1.86e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQ-------------KCQDETQMISSLK---TQIQSQESDLKSQEDDL-----NRAK---SELTRLQQEETQLEQS 518
Cdd:PRK04863 910 KRFVQQhgnalaqlepivsVLQSDPEQFEQLKqdyQQAQQTQRDAKQQAFALtevvqRRAHfsyEDAAEMLAKNSDLNEK 989
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 519 IQAGKVQLE----TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:PRK04863 990 LRQRLEQAEqertRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQ 1044
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
387-518 |
1.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 461
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 462 MLSDVRQKCqdetqmiSSLKTQIQSQESDLKSQEddlNRAKSELTRLQQEETQLEQS 518
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA 1114
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
386-552 |
2.06e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKysleQDIREKEEAIRQKSNEV----QELQNDL--DRET--SSLQELEAQKQDAQDRLDEMDQ--- 454
Cdd:PRK04778 114 LDLIEEDIEQILEEL----QELLESEEKNREEVEQLkdlyRELRKSLlaNRFSfgPALDELEKQLENLEEEFSQFVElte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 455 ----QKA-----KLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlqqEETQLEQSIQAGKVQ 525
Cdd:PRK04778 190 sgdyVEAreildQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHL-----DHLDIEKEIQDLKEQ 264
|
170 180
....*....|....*....|....*..
gi 1953011268 526 LETIIKSLKSTqdEINQARSKLSQLQE 552
Cdd:PRK04778 265 IDENLALLEEL--DLDEAEEKNEEIQE 289
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
407-567 |
2.10e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 407 IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRldemdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQS 486
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR----------KQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 487 QESDLKSQEDDLNRAKSELTRLQQEETQLEQSI---QAGKV------QLETIIKSLKSTQDEINQARSKLSQLQESHQEA 557
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyEKGGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170
....*....|
gi 1953011268 558 HRTLEQYDEA 567
Cdd:PHA02562 326 EEIMDEFNEQ 335
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
412-569 |
2.18e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 412 EAIRQKSNEVQELQNDLDretSSLQELEAQKQDAQDRLD----EMDQQKAKLRDMLSDVrqkcQDETQMISSLKTQI--- 484
Cdd:PRK01156 583 ETNRSRSNEIKKQLNDLE---SRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEI----QENKILIEKLRGKIdny 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 485 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV---QLETIIKSLKSTQDEINQARSKLSQLQESHQE---AH 558
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAnraRLESTIEILRTRINELSDRINDINETLESMKKikkAI 735
|
170
....*....|.
gi 1953011268 559 RTLEQYDEALD 569
Cdd:PRK01156 736 GDLKRLREAFD 746
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
385-584 |
2.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ------NDLDRET--SSLQELEAQKQDAQD--------- 447
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlNLLADETlaDRVEEIREQLDEAEEakrfvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 448 -RLDEMDQQKAKLRdmlsdvrqkcQDETQmISSLK---TQIQSQESDLKSQEDDL-----NRAK---SELTRLQQEETQL 515
Cdd:PRK04863 918 nALAQLEPIVSVLQ----------SDPEQ-FEQLKqdyQQAQQTQRDAKQQAFALtevvqRRAHfsyEDAAEMLAKNSDL 986
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 516 EQSIQAGKVQLEtiikslkstqdeinQARSKLSQLQESHQEAHRtleQYDE---ALDGAHGASLTNLADLSE 584
Cdd:PRK04863 987 NEKLRQRLEQAE--------------QERTRAREQLRQAQAQLA---QYNQvlaSLKSSYDAKRQMLQELKQ 1041
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
389-561 |
2.28e-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: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 389 ISQEIAQLQREKYSLEQ------DIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQ---------DRLDEMD 453
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQlegssdRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADldrklrkldQEMEQLN 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 454 QQKAKLRDMLSDVRQKcQDETQMISSLKTQIQSQ--------------ESDLKSQEDDLNRAKSELTRLQQEETQLEQSI 519
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDK-MDKDEQIRKIKSRHSDEltsllgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011268 520 QAGKVQLETIIKSLKSTQDEINQA------RSKLSQLQESHQEAHRTL 561
Cdd:TIGR00606 608 NHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEKSSKQR 655
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-573 |
2.34e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 460
Cdd:pfam01576 833 KKLKNLEAELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQsnt 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVRQKCqdeTQMISSLKTQIQSQESDLKSQED---DLNRAKSEL-TRLQQEETQ-----------LEQSIQAGKVQ 525
Cdd:pfam01576 906 ELLNDRLRKS---TLQVEQLTTELAAERSTSQKSESarqQLERQNKELkAKLQEMEGTvkskfkssiaaLEAKIAQLEEQ 982
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011268 526 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG 573
Cdd:pfam01576 983 LEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNS 1030
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
410-569 |
2.35e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 410 KEEAIRQkSNEVQELQND---LDRETS-SLQELEAQKQDAQDRLDEMDQQKAKLRDMLSdvRQKCQDETQMISSLKTQIQ 485
Cdd:TIGR01612 1103 KEENIKY-ADEINKIKDDiknLDQKIDhHIKALEEIKKKSENYIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIENIV 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 486 SQESDLKSQEDDLNRAKSELTRLQQEETQLEQ--------SIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 557
Cdd:TIGR01612 1180 TKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEvkginlsyGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKS 1259
|
170
....*....|..
gi 1953011268 558 HRTLEQYDEALD 569
Cdd:TIGR01612 1260 PEIENEMGIEMD 1271
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
478-584 |
2.46e-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: 44.33 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 478 SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESH-QE 556
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNlAT 322
|
90 100
....*....|....*....|....*....
gi 1953011268 557 AHRTLEQYDEALDGAhGASLTNL-ADLSE 584
Cdd:TIGR04320 323 AQAALANAEARLAKA-KEALANLnADLAK 350
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
385-553 |
2.54e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqksnEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEmdqqkAKl 459
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKE-----AK- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 rdmlsdvrqkcQDETQMISSLKTQIQSQESDLKSQE-----DDLNRAKSELTRLQQEETQLEQSIQAG-KVQLET----- 528
Cdd:PRK00409 584 -----------KEADEIIKELRQLQKGGYASVKAHEliearKRLNKANEKKEKKKKKQKEKQEELKVGdEVKYLSlgqkg 652
|
170 180 190
....*....|....*....|....*....|
gi 1953011268 529 IIKSLKSTQDEINQA-----RSKLSQLQES 553
Cdd:PRK00409 653 EVLSIPDDKEAIVQAgimkmKVPLSDLEKI 682
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
384-449 |
2.77e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.79 E-value: 2.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslQELEAQKQDAQDRL 449
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
389-561 |
2.87e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 389 ISQEIAQLQREKYSLEQDIrekEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 465
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVL---NELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 466 --VRQKCQdetQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ-------------QEETQLEQSI----------- 519
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMasllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 520 ----QAGKV-----------------QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 561
Cdd:pfam04108 192 dqcvTAVKLteggraemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
388-591 |
2.89e-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: 44.65 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREKYSLEQ------DIREK-----------EEAIRQKSNEVQELQN---DLDRETSSLQELEAQKQDAQD 447
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQykekacEIRDQitskeaqlessREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 448 RLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLK-TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQL 526
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 527 ETIIKSLKSTQDEI--NQARSKLSQLQE---SHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:TIGR00606 357 DRHQEHIRARDSLIqsLATRLELDGFERgpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
387-559 |
3.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQDIREK-EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDaqdrldEMDQQKAKLRDMLSd 465
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEYLALLDRLEED------GLPEYEERFKELLN- 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 466 vrqkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAkseLTRLQ-QEETQLEqsIQAGKVQLETIikslKSTQDEINQAR 544
Cdd:COG4913 842 -----ENSIEFVADLLSKLRRAIREIKERIDPLNDS---LKRIPfGPGRYLR--LEARPRPDPEV----REFRQELRAVT 907
|
170
....*....|....*
gi 1953011268 545 SKLSQLQESHQEAHR 559
Cdd:COG4913 908 SGASLFDEELSEARF 922
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
389-494 |
3.42e-04 |
|
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: 43.81 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 389 ISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 464
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 1953011268 465 DVRQKCQDETQMISSLKTQIQSQESDLKSQ 494
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
384-568 |
3.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSleqdIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRL----DEMDQQKaKL 459
Cdd:PRK04863 279 NERRVHLEEALELRRELYT----SRRQLAAEQYRLVEMAR---ELAELNEAESDLEQDYQAASDHLnlvqTALRQQE-KI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 RDMLSDVRQKCQ--DETQMISSLKTQIQSQ-ESDLKSQEDDLNRAKSELTRLQQ----EET---QLEQSIQA-GKVQ--- 525
Cdd:PRK04863 351 ERYQADLEELEErlEEQNEVVEEADEQQEEnEARAEAAEEEVDELKSQLADYQQaldvQQTraiQYQQAVQAlERAKqlc 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 526 ---------LETIIKSLKSTQDEINQARSKLSQLQESHQEAHrtlEQYDEAL 568
Cdd:PRK04863 431 glpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH---SQFEQAY 479
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
456-589 |
3.55e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.07 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQL--------- 526
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrq 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 527 -----ETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALdGAHGASLTNLADLSEGVSLA 589
Cdd:COG5283 82 lsaaqRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLA-GAGAAAAAIGAALAASVKPA 148
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
386-568 |
3.59e-04 |
|
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: 42.25 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQrekyslEQDIREKEEAIRQKSNEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 465
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 466 VRQKCQDETQMI-SSLKTQIQSQESDLKSQEDDL-NRAKSELTRLQqeeTQLEQSIQAGKVQLETIIKSLKSTQDEinQA 543
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAP--YA 145
|
170 180
....*....|....*....|....*
gi 1953011268 544 RSKLSQLQESHQEAHRTLEQYDEAL 568
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDL 170
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
385-568 |
3.81e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 43.48 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREkysleqdIREKEEAIRQKSNEVQELQNDlDRETSSLQELEAQKQ-------DA-QDRLDEMDQQK 456
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETE-SSCSTPLRRNESFSSlhgcvqlDAlQEKLRGLEEEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQD----ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL-------EQSIQAGKVQ 525
Cdd:pfam04849 181 LKLRSEASHLKTETDTyeekEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLlaqivdlQHKCKELGIE 260
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011268 526 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 568
Cdd:pfam04849 261 NEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEEL 303
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
385-559 |
4.02e-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: 43.86 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 460
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 dmlsdvrqkcqDETQMISslKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQlETIIKSL---KS 535
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSASKeieKT 181
|
170 180
....*....|....*....|....*....
gi 1953011268 536 TQD---EINQARSKLSQLQESHQEA--HR 559
Cdd:pfam05701 182 VEEltiELIATKESLESAHAAHLEAeeHR 210
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
475-562 |
4.03e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 475 QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ----SIQAGKVQLETIIKSLKSTQDEINQARSKLSQL 550
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90
....*....|..
gi 1953011268 551 QESHQEAHRTLE 562
Cdd:PRK00409 600 GYASVKAHELIE 611
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
394-461 |
4.26e-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: 41.58 E-value: 4.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 394 AQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
384-552 |
4.30e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldreTSSLQELEAQKQDAQDR-------LDEMDQQK 456
Cdd:PRK10929 72 QVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQV-----SSQLLEKSRQAQQEQDRareisdsLSQLPQQQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSDVRQKCQ----DETQMISSLKTQIQSQESDLKSQEDDLNRA------KSELTRLQQE-----ETQLEQSIQA 521
Cdd:PRK10929 147 TEARRQLNEIERRLQtlgtPNTPLAQAQLTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQA 226
|
170 180 190
....*....|....*....|....*....|.
gi 1953011268 522 GKVQLETiikslkSTQDEINQARSKLSQLQE 552
Cdd:PRK10929 227 LRNQLNS------QRQREAERALESTELLAE 251
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
384-567 |
4.38e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.78 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLR 460
Cdd:pfam06008 75 AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQNAEAELKAAQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 DMLSDVR---QKCQDETQmisSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvQLETIIKSLKSTQ 537
Cdd:pfam06008 155 DLLSRIQtwfQSPQEENK---ALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA---NLREFQRKKEEVS 228
|
170 180 190
....*....|....*....|....*....|
gi 1953011268 538 DEINQARSKLSQLQESHQEAHRTLEQYDEA 567
Cdd:pfam06008 229 EQKNQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
407-520 |
4.51e-04 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 40.71 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 407 IREK-EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQMISSLKTQIQ 485
Cdd:smart00502 1 QREAlEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKE 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1953011268 486 SQESDLKSQeddlnrakseLTRLQQEETQLEQSIQ 520
Cdd:smart00502 72 NKLKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| Flagellar_rod |
pfam05149 |
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod ... |
397-512 |
5.20e-04 |
|
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod component proteins. The eukaryotic flagellum represents one of the most complex macromolecular structures found in any organizm and contains more than 250 proteins. In addition to its locomotive role, the flagellum is probably involved in nutrient uptake since receptors for host low-density lipoproteins are localized on the flagellar membrane as well as on the flagellar pocket membrane.
Pssm-ID: 368306 [Multi-domain] Cd Length: 287 Bit Score: 42.73 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 397 QREKYSLEQdiREKEEAIRQKSNEVQELQNDLDRETSSLQEL-EAQKQDAQDRLDEM-----------------DQQKAK 458
Cdd:pfam05149 38 QRKRFKTQR--RESDKFLQQNVEQQQKLWREIEELERELQKLaEERREEVEDRIEAVereaqrrtdhesflnfaDQHKQR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1953011268 459 LRDMLSDVrQKCQDETQMISSLktqIQSQESDLKSQEDDLNRAKSELTRLQQEE 512
Cdd:pfam05149 116 LRRTLENC-DGALDCARSLEEY---VQEGCDHLPAKQDKLRNALNELLDAVRKE 165
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
416-567 |
5.28e-04 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 43.34 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 416 QKSNEVQELQNDLDRETSSLQELEAQKQD-AQDRLDEMDQQK---------------AKLRD-MLSDVRQKCQDET-QMI 477
Cdd:COG3853 25 PEVPEQAAGMVDPEEAEVDLSKLSAEADAfVEALAAQIDLSDvnailqygakaqrklAAFSNrMLDRVKTKDLGEVgDSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 478 SSLKTQIQsqESDLKSQEDD---------LNRAKSELTRLQQEEtqleQSIQAgkvQLETIIKSLKSTQDEINQARSKLS 548
Cdd:COG3853 105 SELRRTLE--DLDPSELDDLkkkgllgklFPKGGNKLEKYFAKY----QSAQT---QIDKISVALEKGQDELLKDNAMLD 175
|
170
....*....|....*....
gi 1953011268 549 QLQESHQEAHRTLEQYDEA 567
Cdd:COG3853 176 QLYEKNWEYFKELNQYIAA 194
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
384-535 |
5.71e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 42.52 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKSNEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 456
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 aKLRDMLSDVR--QKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELTRLQQEETQLEQSIQagkvQLETIIKSLK 534
Cdd:COG5325 144 -FLRNKNNDQHplEEEEDEESLSSLGSQQTLQQQGLSNEELEY---QQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
.
gi 1953011268 535 S 535
Cdd:COG5325 216 S 216
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-591 |
5.75e-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: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 460
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQDEESDLERLKEEIEKSSKQRAMLAgat 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 461 -------DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQ----EDDLNRAKSELTRLQQeetqlEQSIQAGKVQLETI 529
Cdd:TIGR00606 663 avysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlaPDKLKSTESELKKKEK-----RRDEMLGLAPGRQS 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 530 IKSLKstQDEINQARSKLSQLQESHQEAHRTLEQyDEALDGAHGASLTNLADLSEGVSLAER 591
Cdd:TIGR00606 738 IIDLK--EKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMER 796
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
462-564 |
6.22e-04 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 42.89 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 462 MLSDVRQKCQDET-QMISSLKTQIQSQESDLKSQEDDL------NRAKSELTRLQQEEtqleQSIQAgkvQLETIIKSLK 534
Cdd:pfam05816 33 MLDNVRTKDLGEVgDLLNELRRTLKDFDPDELGEEKKLgflplfKKAGNKIEKYFAKY----QTAGA---QIDKIVVELE 105
|
90 100 110
....*....|....*....|....*....|
gi 1953011268 535 STQDEINQARSKLSQLQESHQEAHRTLEQY 564
Cdd:pfam05816 106 KGQDELLKDNAMLDQMYEKNLEYFKELEKY 135
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
392-557 |
6.28e-04 |
|
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: 41.95 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 392 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRetsslQELEAQKQDAQdRLDEMDQQ--------KAKLRDML 463
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE-----RELKAEAEHRQ-RVVELSREveeakrafEEKLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS-ELTRLQQEetqLEQSIQAGKVQLETIIKSLKSTQDEINQ 542
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVEDLRKEKKKLAEEYEQ 197
|
170
....*....|....*
gi 1953011268 543 arsKLSQLQESHQEA 557
Cdd:pfam15665 198 ---KLSKAQAFYERE 209
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
446-563 |
6.35e-04 |
|
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: 42.96 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 446 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQeddLNRAKSELTRLQQEETQLEQSiqagkvq 525
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR---VAELKEELRQSREKHEELEEK------- 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 1953011268 526 letiIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam07888 103 ----YKELSASSEELSEEKDALLAQRAAHEARIRELEE 136
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
405-567 |
6.86e-04 |
|
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: 43.14 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 405 QDIREKEEAIRQKSNE-------VQELQNDLDRETSSLQELEAQKQDAQD-------RLDEMDQQKAKLRDML------- 463
Cdd:pfam05622 3 SEAQEEKDELAQRCHEldqqvslLQEEKNSLQQENKKLQERLDQLESGDDsgtpggkKYLLLQKQLEQLQEENfrletar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDetqmissLKTQIQsqesDLKSQEDDLNRAKSELTRLQQEETQLEQSiqAGKV-QLETIIKSLKSTQDEINQ 542
Cdd:pfam05622 83 DDYRIKCEE-------LEKEVL----ELQHRNEELTSLAEEAQALKDEMDILRES--SDKVkKLEATVETYKKKLEDLGD 149
|
170 180
....*....|....*....|....*.
gi 1953011268 543 ARSKLSQLQESHQE-AHRTLEQYDEA 567
Cdd:pfam05622 150 LRRQVKLLEERNAEyMQRTLQLEEEL 175
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
392-515 |
7.08e-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: 40.89 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 392 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 463
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL 515
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
446-591 |
7.46e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 446 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKtqiqsqesdlksqeDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 525
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 526 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG---ASLTNLADLSE--GVSLAER 591
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKrdrESQAKIADLGRrlNVALAQR 188
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
386-517 |
7.78e-04 |
|
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: 40.24 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdretsslqeLEAQKqdaqdrldemdqqkaklrdMLSD 465
Cdd:pfam05103 27 LDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTL---------ILAQE-------------------TAEE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1953011268 466 VRQKCQDETQMISSlKTQIQSQESdLKSQEDDLNRAKSELTRLQQEETQLEQ 517
Cdd:pfam05103 79 VKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
393-566 |
8.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 393 IAQLQREKYSLEQDIrEKEEAI----RQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK---AKLRDMLSD 465
Cdd:PRK03918 171 IKEIKRRIERLEKFI-KRTENIeeliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKeeiEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 466 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS---------ELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 536
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190
....*....|....*....|....*....|
gi 1953011268 537 QDEINQARSKLSQLQESHQEAHRTLEQYDE 566
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEE 359
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
424-569 |
8.16e-04 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.83 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 424 LQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKS 503
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRAL-------KAELESLEVYNRQLERLVASQEQEIASLER 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 504 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARskLSQLQESHQEAHRTL-EQYD---EALD 569
Cdd:pfam11932 84 QIEEIERTERELVPLMLKMLDRLEQFVALDLPFLLEERQAR--LARLRELMDDADVSLaEKYRrilEAYQ 151
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
384-564 |
8.24e-04 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 42.50 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREkysLEQDI----REKE---EAIRQKSNEV---QELQNDLDRETssLQELEAQKQDAQDRldeMD 453
Cdd:pfam05816 95 AQIDKIVVELEKGQDE---LLKDNamldQMYEknlEYFKELEKYIaagELKLEELDAEL--LPELEAKAAASGDP---ED 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 454 QQKAK-LRDMLSDVRQKCQD-ETQM-------------------------------ISSLKTQ------IQSQESDLKSQ 494
Cdd:pfam05816 167 AQALRdLRQALFRLEQRIHDlELQRavsiqtapqirlvqnnnqeliekiqsaitttIPLWKNQlvvalaLKRQKLALEAQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 495 E------DDLNRAKSELTRLQQEETQlEQSiQAGKVQLETIIK---SLKSTQDEINQ----ARSKLSQLQESHQEAHRTL 561
Cdd:pfam05816 247 KavndttNELLLKNAEMLKTQSIETA-KEA-ERGIVDIETLKKtnqTLIATIDETLQiqeeGREKRREAEAELEQLEEEL 324
|
...
gi 1953011268 562 EQY 564
Cdd:pfam05816 325 KQK 327
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
384-569 |
8.36e-04 |
|
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: 42.92 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQrEKYSLEQDireKEEAIRQKSNEVQELQNDLDRET----------SSLQ----ELEAQKQDAQDRL 449
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLNEN---ELERVRGLEKQLEELEKRYDEIVerleekevaySELQeeleEILEQLEEIEEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 450 DEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqeSDL----KSQEDDLNRAKSELTRLQQeetQLEQS---IQAG 522
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEVplnMDEV 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 523 KVQLETIIKSL----KSTQDEINQA-------------RSKLSQLQESHQEAHRTLE--QYDEALD 569
Cdd:pfam06160 456 NRLLDEAQDDVdtlyEKTEELIDNAtlaeqliqyanryRSSNPEVAEALTEAELLFRnyDYEKALE 521
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
386-584 |
8.46e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 457
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 458 KLRDMLSDVRQKCQDETQ----MISSLKTQIQSQES---DLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI- 529
Cdd:COG0497 223 KLREALQEALEALSGGEGgaldLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVe 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 530 -----IKSLK----STQDEI----NQARSKLSQLQESHQEahrtLEQYDEALDGAHgASLTNLAD-LSE 584
Cdd:COG0497 303 erlalLRRLArkygVTVEELlayaEELRAELAELENSDER----LEELEAELAEAE-AELLEAAEkLSA 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-547 |
9.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVRQkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSElTRLQQEETQLEQSIQA-GKV---------QLETIIKSLK 534
Cdd:COG1196 725 ALEE--QLEAEREELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEAlGPVnllaieeyeELEERYDFLS 801
|
170
....*....|...
gi 1953011268 535 STQDEINQARSKL 547
Cdd:COG1196 802 EQREDLEEARETL 814
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
384-552 |
9.39e-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: 42.37 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQRekySLEQDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam04108 171 KELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQKLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 S---DVRQKCQDETQMISSLKTQIqsqeSDLKSQEDDL-NRAKSELTRLQQEETQLEQSIQAgKVQLETIIKSL------ 533
Cdd:pfam04108 245 EqknSLIDELLSALQLIAEIQSRL----PEYLAALKEFeERWEEEKETIEDYLSELEDLREF-YEGFPSAYGSLllever 319
|
170 180
....*....|....*....|....
gi 1953011268 534 -KSTQDE----INQARSKLSQLQE 552
Cdd:pfam04108 320 rREWAEKmkkiLRKLAEELDRLQE 343
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
383-472 |
9.74e-04 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 39.67 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSN---------EVQELQNDLDREtSSLQELEAQKQDAQDRLDEMD 453
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKlpddtpiykIVGNLLVKVDKT-KVEKELKERKELLELRSRTLE 91
|
90
....*....|....*....
gi 1953011268 454 QQKAKLRDMLSDVRQKCQD 472
Cdd:PRK09343 92 KQEKKLREKLKELQAKINE 110
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
384-599 |
9.92e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR--ETSSLQELEAQKQDAQDRLDEMDQQKA--KL 459
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNAEKEEELAEaeKL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 RDMLSDVRQKCQDETQMISSLKTQIQSqESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 539
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 540 INQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGFGAMDD 599
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
387-585 |
1.02e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKysLEQDIREKE--EAIRQKSNEVQELQNDLDRETSSLQEL--------EAQKQDAqDRLDEMDQQK 456
Cdd:pfam12128 209 DGVVPPKSRLNRQQ--VEHWIRDIQaiAGIMKIRPEFTKLQQEFNTLESAELRLshlhfgykSDETLIA-SRQEERQETS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 457 AKLRDMLSdvrqkcQDETQmissLKTQIQSQESDLKSQEDDLNRAKSELTRLqqeETQLEQSIQAGkvqletiIKSLKST 536
Cdd:pfam12128 286 AELNQLLR------TLDDQ----WKEKRDELNGELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAAD 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1953011268 537 QDEINQARSKLSQLQESHQ---EAHRTLEQYDEALDGAHGASL-TNLADLSEG 585
Cdd:pfam12128 346 QEQLPSWQSELENLEERLKaltGKHQDVTAKYNRRRSKIKEQNnRDIAGIKDK 398
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
456-567 |
1.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 456 KAKLRDMLSDVRQKCQDETQMISSLK----TQIQSQESDLKSQ-EDDLNRAKSELT----RLQQEETQLE---QSIQAGK 523
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKkealLEAKEEIHKLRNEfEKELRERRNELQklekRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1953011268 524 VQLETIIKSLKSTQDEINQARSKLSQLQESHQEAhrtLEQY-----DEA 567
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERIsgltaEEA 155
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
388-571 |
1.17e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 42.51 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREK-------YSLEQDIREKEEAIRQKSNEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:pfam15450 24 DLQAEVVSLRGHKercehatLSLLRELLQVRAHVQLQDSELKQLRQEVQQAARApeKEALEFPGPQNQNQMQALDKRLVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 459 LRDMLSDVRQK--CQDE-------------TQMISSLKTQIQSQESD----LKSQEDDLNRAKSELTRLQQEETQL--EQ 517
Cdd:pfam15450 104 VREALTQIRRKqaLQDSerkgaeqeanlrlTKLTGKLKQEEQGREAAcsalQKSQEEASQKVDHEVARMQAQVTKLgeEM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 518 S-------------IQAGKVQLETIIKSLKSTQ--------DEINQARSKLSQLQESH---------QEAHRTLEQYdEA 567
Cdd:pfam15450 184 SlrflkreaklcsfLQKSFLALEKRMKASESTRlkaesslrEELEGRWQKLQELTEERlralqgqreQEEGHLLEQC-RG 262
|
....
gi 1953011268 568 LDGA 571
Cdd:pfam15450 263 LDAA 266
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
387-568 |
1.17e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.91 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:pfam14988 25 NQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 467 RQKcqdetqmissLKTQIQSQESDLKSQEDDLN------RAKSELTRLQQEETqleqsiQAGKVQLETIIKSLKSTQDEI 540
Cdd:pfam14988 105 DRE----------AHLQFLKEKALLEKQLQELRilelgeRATRELKRKAQALK------LAAKQALSEFCRSIKRENRQL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953011268 541 NQARSKL-----------SQLQESHQEAHRTlEQYDEAL 568
Cdd:pfam14988 169 QKELLQLiqetqaleaikSKLENRKQRLKEE-QWYLEAL 206
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
396-549 |
1.19e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 42.40 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 396 LQREKYSLEQDIREkeeaiRQKSNEVQelqndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetq 475
Cdd:PRK06975 344 LNRKVDRLDQELVQ-----RQQANDAQ------------TAELRVKTEQAQASVHQLDSQFAQLDGKLADAQSAQQ---- 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 476 misslktQIQSQESDLKSQEDDLNRAKSE-LTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQD-EINQARSKLSQ 549
Cdd:PRK06975 403 -------ALEQQYQDLSRNRDDWMIAEVEqMLSSASQQLQLTGNVQLALIALQNADARLATSDSpQAVAVRKAIAQ 471
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
164-337 |
1.23e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 164 LGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEPVPsvlppslippskrkktvfpgavpvlpaspppkdslrstpshg 243
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADT------------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 244 svsslNSTGSLSPKHSIK-QTQPTVSWVVPVADKMrFDEIflktDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADT 322
Cdd:COG5126 45 -----DGDGRISREEFVAgMESLFEATVEPFARAA-FDLL----DTDGDGKISADEFRRLLTALGVSEEEADELFARLDT 114
|
170
....*....|....*
gi 1953011268 323 RQTGKLSKDQFALAM 337
Cdd:COG5126 115 DGDGKISFEEFVAAV 129
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
394-563 |
1.24e-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: 42.65 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQREKYSLEQDIREKEEAIRQKSNEVQElqndldRETSSLQELEAQKQDAQD---RLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLE------KELKHLREALQQTQQSHAyltQKREAQEEQLKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 471 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELtRLQQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSKLSQL 550
Cdd:TIGR00618 270 E-----------ELRAQEAVLEETQERINRARKAA-PLAAHIKAVTQIEQ----QAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170
....*....|....*
gi 1953011268 551 --QESHQEAHRTLEQ 563
Cdd:TIGR00618 334 vkQQSSIEEQRRLLQ 348
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
388-518 |
1.25e-03 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 40.76 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 388 DISQEIAQLQREKYSLEQDIREKEEAiRQKSNEVQELQNDLDRETSSLQELEAQKQ-----DAQDRLDEMDQQKAklrdm 462
Cdd:pfam03280 76 SAEEKQQRLAALRAQLPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQRA----- 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 463 lsdvrqkcqdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS 518
Cdd:pfam03280 150 --------------------AWQQRLDDYLAERQQINAAGLSEQERQAAIAQLRQQ 185
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
385-593 |
1.31e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 465 DVRqKCQDETQMISSLktqiqsqESDLKSQEDDLNRAKSELTRLQQ--EETQLEQSIQAGKV-QLETII----------- 530
Cdd:pfam10174 549 AVR-TNPEINDRIRLL-------EQEVARYKEESGKAQAEVERLLGilREVENEKNDKDKKIaELESLTlrqmkeqnkkv 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 531 KSLKSTQDEinQARSKLSQLQESHQE--------AHRTLEQYDEALD------GAHGASLTnladlSEGVSLAERGG 593
Cdd:pfam10174 621 ANIKHGQQE--MKKKGAQLLEEARRRednladnsQQLQLEELMGALEktrqelDATKARLS-----STQQSLAEKDG 690
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
386-552 |
1.32e-03 |
|
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: 41.59 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:cd22656 123 LDDLLKEAKKYQ-------DKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLNEEY 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDEtqmissLKTQIQSQESDLKSQE---DDLNRAKSELTRLQQeetQLEQSIQA-GKVQ---------LETII 530
Cdd:cd22656 196 AAKLKAKIDE------LKALIADDEAKLAAALrliADLTAADTDLDNLLA---LIGPAIPAlEKLQgawqaiatdLDSLK 266
|
170 180
....*....|....*....|..
gi 1953011268 531 KSLKSTQDEINQARSKLSQLQE 552
Cdd:cd22656 267 DLLEDDISKIPAAILAKLELEK 288
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
412-531 |
1.42e-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: 39.87 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 412 EAIRQKSNEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetqmisslktQIQSQESD 490
Cdd:pfam03938 8 QKILEESPEGKAAQAQLEKKFKKRQaELEAKQKELQKLYEELQKDGALLEEEREEKEQ--------------ELQKKEQE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1953011268 491 LKSQEDDLNRAkseltrLQQEETQLEQSIQAgkvQLETIIK 531
Cdd:pfam03938 74 LQQLQQKAQQE------LQKKQQELLQPIQD---KINKAIK 105
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
384-563 |
1.55e-03 |
|
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: 41.09 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEV---QEL------------QNDLDRETSSLQELEAQkqdAQDR 448
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEK---EESK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 LDEMDQQKAKLRDMLsdvrQKCQDE-----TQM----------ISSLKTQIQsqesDLK-SQEDDLNraksELTRLQQEE 512
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEElnflsTYKdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 513 TQ-LEQSIQAGKVQLETII--KSLKSTQD--------------EINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQEsllqktrdnqvmlkEIEQFREFIDELEEEIPKLKAEVQQ 218
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
376-590 |
1.68e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 376 GSGEFTGVKELDDisqeiaqLQREKYSLEQDIrekeEAIRQKSNEVQELQND---LDRETS----SLQELEAQKQDAQDR 448
Cdd:PLN02939 218 GLCVHSLSKELDV-------LKEENMLLKDDI----QFLKAELIEVAETEERvfkLEKERSlldaSLRELESKFIVAQED 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 449 LDEMDQQKAklrDMLSDVRQKCQDetqMISSLKTQIQsQESDLKSQEDDLnRAKSEltrlqqeetQLEQSIQAGKVQlet 528
Cdd:PLN02939 287 VSKLSPLQY---DCWWEKVENLQD---LLDRATNQVE-KAALVLDQNQDL-RDKVD---------KLEASLKEANVS--- 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953011268 529 iikSLKSTQDEINQARSKL--SQLQESHQEAHRTLEQYDEALDGAHGaSLTNLADLSEGVSLAE 590
Cdd:PLN02939 347 ---KFSSYKVELLQQKLKLleERLQASDHEIHSYIQLYQESIKEFQD-TLSKLKEESKKRSLEH 406
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
405-517 |
1.68e-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: 39.61 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 405 QDIREKEEaiRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqmissLKTQI 484
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110
....*....|....*....|....*....|...
gi 1953011268 485 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ 517
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEK 110
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
383-564 |
1.85e-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: 41.73 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 383 VKELDD---ISQEIAQLQREKYSLEQDIREKEEAIRQKSNE-VQELQNDLDRET-------SSLQELE----AQKQDAQD 447
Cdd:pfam10174 76 IQALQDelrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAkelfllrKTLEEMElrieTQKQTLGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 448 RldemDQQKAKLRDML------SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTR---LQQEETQ---L 515
Cdd:pfam10174 156 R----DESIKKLLEMLqskglpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRrnqLQPDPAKtkaL 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011268 516 EQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQY 564
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
403-521 |
1.88e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 403 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKT 482
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 1953011268 483 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 521
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAA 155
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
379-529 |
1.97e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 379 EFTGVKELDdisQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQEL------------QNDLDRETSSLQ---ELEAQKQ 443
Cdd:TIGR00618 709 LETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMHQartvlkarteahFNNNEEVTAALQtgaELSHLAA 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 444 DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE-ETQLEQSIQAG 522
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKyEECSKQLAQLT 865
|
....*..
gi 1953011268 523 KVQLETI 529
Cdd:TIGR00618 866 QEQAKII 872
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
412-552 |
2.04e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 412 EAIRQKSNEVQELqndldreTSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlKTQIQSQESDL 491
Cdd:TIGR00606 169 KALKQKFDEIFSA-------TRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIV 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 492 KSQEDDLNRAKSELTRLQQEETQLeqsiqagkVQLETIIKSLKSTQDEINQARSKLSQLQE 552
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKI--------MKLDNEIKALKSRKKQMEKDNSELELKME 293
|
|
| COG5074 |
COG5074 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
401-556 |
2.12e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 41.03 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 401 YSLEQDIREKEEAIRQKSNEVQELQNdldRETSSLQEL-EAQKQDAQDRLDEMDQQKAKLR-----DMLSDVRQKCQDET 474
Cdd:COG5074 21 VTFMNKILSINKNLSVYEKEINQIDN---LHKDLLTEVfEEQSRKLRRSLDNFSSQTTDLQrnlkkDIKSAERDGIHLAN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 475 QMISS------LKTQIQS-QESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKL 547
Cdd:COG5074 98 KQAQAenvrqkFLKLIQDyRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRGEAKTAL 177
|
....*....
gi 1953011268 548 SQLQESHQE 556
Cdd:COG5074 178 AEVQARHQE 186
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
376-542 |
2.17e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.58 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 376 GSGEFTGVKELDDISQE-------IAQLQREKYSLEQDIREKEEAIRQKSNEV------QELQNDLDRETSSLQELEAQK 442
Cdd:pfam13166 299 ISSLLAQLPAVSDLASLlsafeldVEDIESEAEVLNSQLDGLRRALEAKRKDPfksielDSVDAKIESINDLVASINELI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 443 QDAQDRLDEMDQQKAKLRDMLsdvrqkcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQag 522
Cdd:pfam13166 379 AKHNEITDNFEEEKNKAKKKL---------RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIK-- 447
|
170 180
....*....|....*....|
gi 1953011268 523 kvQLETIIKSLKSTQDEINQ 542
Cdd:pfam13166 448 --ELEAQLRDHKPGADEINK 465
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
382-458 |
2.33e-03 |
|
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: 39.30 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 382 GVKELDDISQEIAQL---QREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA----QDRLDEMDQ 454
Cdd:pfam07321 64 LLKELEKVKQQVALLrenEADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEelrqQERQEEQEL 143
|
....
gi 1953011268 455 QKAK 458
Cdd:pfam07321 144 EEFA 147
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
406-468 |
2.34e-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: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 406 DIREKEEAIRQKSNEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 468
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
386-530 |
2.43e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 39.81 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 465
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 466 vrqkcqdETQMISSLktqiqsqesdlksqedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 530
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
394-576 |
2.80e-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: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 394 AQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:pfam01576 524 AQLSDMKKKLEEDagtLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 471 QDETQMISSLKTqIQSQESDLKSQEDDLNRAKS----ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA--- 543
Cdd:pfam01576 604 KKFDQMLAEEKA-ISARYAEERDRAEAEAREKEtralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhe 682
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953011268 544 --RSKlsQLQESHQEAHRT-LEQYDEALDGAHGASL 576
Cdd:pfam01576 683 leRSK--RALEQQVEEMKTqLEELEDELQATEDAKL 716
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
384-515 |
2.80e-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: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 456
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDLNRAKSELTRLQQEETQL 515
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
501-569 |
2.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011268 501 AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 569
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
384-564 |
3.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQ----------REKYSLEQDIREKEEAIRQKSNEV-----------QELQNDLDRETSSLQELEAQK 442
Cdd:PRK01156 346 SRYDDLNNQILELEgyemdynsylKSIESLKKKIEEYSKNIERMSAFIseilkiqeidpDAIKKELNEINVKLQDISSKV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 443 QDAQDRLDEMDQQKAKLR---DMLSDvRQKCQDETQMISSLKTQ--IQSQESDLKSQEDDLNRAKSELTRLQQEETQL-- 515
Cdd:PRK01156 426 SSLNQRIRALRENLDELSrnmEMLNG-QSVCPVCGTTLGEEKSNhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLkk 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 516 -EQSIQAGKV-QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQY 564
Cdd:PRK01156 505 rKEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
384-563 |
3.04e-03 |
|
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: 40.01 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQkaklrdmL 463
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNR-------RIQLLEEELERTEERLAEALEK-------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK----------SELTR-LQQEETQLEQSIQAGK------VQL 526
Cdd:pfam00261 67 EEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKeiaeeadrkyEEVARkLVVVEGDLERAEERAElaeskiVEL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011268 527 E----TIIKSLKSTqdEINQArsKLSQLQESHQEAHRTLEQ 563
Cdd:pfam00261 147 EeelkVVGNNLKSL--EASEE--KASEREDKYEEQIRFLTE 183
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
384-454 |
3.05e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011268 384 KELDDISQEIAQLQREKysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 454
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
393-520 |
3.12e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 393 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEmdqqkaklrdmlsdvRQK--- 469
Cdd:pfam03148 253 IEETEDAKNKLEWQLKKTLQEIAELEKNIEALEK-------AIRDKEAPLKLAQTRLEN---------------RTYrpn 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 470 ---CQDETQ--MISSLKtQIQSQESDLKSQeddLNRAKSELTRLQQEETQLEQSIQ 520
Cdd:pfam03148 311 velCRDEAQygLVDEVK-ELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
418-553 |
3.68e-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: 39.70 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 418 SNEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDD 497
Cdd:cd21116 72 QSYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATK 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 498 LNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 553
Cdd:cd21116 142 AQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESS 197
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
422-551 |
3.93e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 40.43 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 422 QELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLrdmlsdvrQKCQDETQMISSLKTQIQSQESdLKS 493
Cdd:pfam15070 196 QHVKKELAKKLGQLQEelgelketLELKSQEAQSLQEQRDQYLAHL--------QQYVAAYQQLASEKEELHKQYL-LQT 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 494 QEDDlnrakseltRLQQEETQleqsiqaGKVQLETIIKSLKSTQDEINQARSKLSQLQ 551
Cdd:pfam15070 267 QLMD---------RLQHEEVQ-------GKVAAEMARQELQETQERLEALTQQNQQLQ 308
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
387-528 |
4.13e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 40.20 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 387 DDISQEIAQLQREKYSLEQ----------------------DIREKEEAIRQKSNEVQELQNDLDRETSSL--------Q 436
Cdd:pfam09755 110 NDLSRKLTQLRQEKVELEQtleqeqeyqvnklmrkiekleaETLNKQTNLEQLRREKVELENTLEQEQEALvnrlwkrmD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 437 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELTRLQQEETQL- 515
Cdd:pfam09755 190 KLEAEKRLLQEKLDQPVSAPPSPRDSTSE-GDTAQNLTAHIQYLRKEVERLRRQLATAQQE---HTEKMAQYAQEERHIr 265
|
170
....*....|....
gi 1953011268 516 EQSIQ-AGKVQLET 528
Cdd:pfam09755 266 EENLRlQRKLQLEM 279
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
391-529 |
4.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV- 466
Cdd:PRK12705 43 QKEAEEKLEAALLEAKellLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELe 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 467 --RQKCQDETQMISSLkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI 529
Cdd:PRK12705 123 elEKQLDNELYRVAGL-TPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAM 186
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
385-472 |
4.23e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.22 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAI---------RQK---------------SNEVQELQNdldretsSLQELEA 440
Cdd:pfam03148 266 QLKKTLQEIAELEKNIEALEKAIRDKEAPLklaqtrlenRTYrpnvelcrdeaqyglVDEVKELEE-------TIEALKQ 338
|
90 100 110
....*....|....*....|....*....|....*....
gi 1953011268 441 QKQDAQDRLDEMDQQKAKLRDMLSDV-------RQKCQD 472
Cdd:pfam03148 339 KLAEAEASLQALERTRLRLEEDIAVKanslfidREKCMG 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-469 |
4.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQReKYSlEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKL---- 459
Cdd:PRK03918 640 KRLEELRKELEELEK-KYS-EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekle 717
|
90
....*....|..
gi 1953011268 460 --RDMLSDVRQK 469
Cdd:PRK03918 718 kaLERVEELREK 729
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
402-462 |
4.79e-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: 4.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 402 SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 462
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
384-569 |
5.23e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIrQKSNEVQELQNDLDREtsSLQELEAQKQDAQDRLDE----MDQQKAKL 459
Cdd:PTZ00440 1031 KLIKEKGKEIEEKVDQYISLLEKMKTKLSSF-HFNIDIKKYKNPKIKE--EIKLLEEKVEALLKKIDEnknkLIEIKNKS 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 RDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ-EETQLE----------QSIQAGKVQLET 528
Cdd:PTZ00440 1108 HEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvNEIEIEyerilidhivEQINNEAKKSKT 1187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011268 529 IIKSLKSTQDEINQARSKLSQLQESHqeaHRTLE---QYDEALD 569
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSKERNDH---LTTFEynaYYDKATA 1228
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
341-546 |
5.39e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 39.62 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 341 QQKVSKGIDPPQVLSPDM---VPPSERGTPIP-DGSSCLGSGEFTgvkeLDDISQEIAQLQREKYSLeqdireKEEAirq 416
Cdd:pfam04849 121 RHELSKKDDLLQIYSNDAeesETESSCSTPLRrNESFSSLHGCVQ----LDALQEKLRGLEEENLKL------RSEA--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 417 ksnevqelqNDLDRETSSLQELEAQ-KQDAQDRLDEMDQQKAklrdMLSDVRQKCQDET----QMISSLKTQIQSQESDL 491
Cdd:pfam04849 188 ---------SHLKTETDTYEEKEQQlMSDCVEQLSEANQQMA----ELSEELARKMEENlrqqEEITSLLAQIVDLQHKC 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011268 492 KSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSK 546
Cdd:pfam04849 255 KELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| PI3K_P85_iSH2 |
pfam16454 |
Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain; This domain is found ... |
446-563 |
5.42e-03 |
|
Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain; This domain is found between the two SH2 domains in phosphatidylinositol 3-kinase regulatory subunit P85. It forms a complex with the adaptor-binding domain of phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha.
Pssm-ID: 465121 [Multi-domain] Cd Length: 161 Bit Score: 38.40 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 446 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDlnrAKSELTRLQQE--ETQLEQSIQA 521
Cdd:pfam16454 2 QEDEVVKEDDIEAVGKKLIEIHKQYLEKSREYDRLYEEYNktSQEIQMKRQALE---AFNEAIKMFEEqiKLQERFSKEA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1953011268 522 GKVQLETIIKS---LKSTQDEINQARSKLSQLQESHQEAHRTLEQ 563
Cdd:pfam16454 79 QPHEIERLLENyelLKSRLKELHDSKEQLEEDLKTQKEYNRELER 123
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
391-559 |
5.93e-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: 39.93 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 391 QEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQndldretsslQELEAQKQDAQdrlDEMDQQKAKLRDmlSDVRQKC 470
Cdd:pfam15709 368 LERAEKMREELELEQQRRFEEIRLRKQRLEEERQR----------QEEEERKQRLQ---LQAAQERARQQQ--EEFRRKL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 471 QdetqmisslktQIQSqesdlKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQlETIIKSLKSTQDEINQARSKLS 548
Cdd:pfam15709 433 Q-----------ELQR-----KKQQEEAERAEAEKQRQKELEMQLaeEQKRLMEMAE-EERLEYQRQKQEAEEKARLEAE 495
|
170
....*....|.
gi 1953011268 549 QLQESHQEAHR 559
Cdd:pfam15709 496 ERRQKEEEAAR 506
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-591 |
6.07e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQndlDREtsslQELEAQKQDAQDRLDEMD---QQKAKL-- 459
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELS---ARE----SDLEQDYQAASDHLNLVQtalRQQEKIer 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 460 -RDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ----EET---QLEQSIQA-GKVQ----- 525
Cdd:COG3096 352 yQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQaldvQQTraiQYQQAVQAlEKARalcgl 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 526 -------LETIIKSLKSTQDEINQARSKLSQlQESHQEAHRTleQYDEAL------------DGAHGASLTNLADLSEGV 586
Cdd:COG3096 432 pdltpenAEDYLAAFRAKEQQATEEVLELEQ-KLSVADAARR--QFEKAYelvckiageverSQAWQTARELLRRYRSQQ 508
|
....*
gi 1953011268 587 SLAER 591
Cdd:COG3096 509 ALAQR 513
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
382-469 |
6.28e-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: 37.94 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 382 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQQKAKLR 460
Cdd:pfam03938 3 GYVDMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQ 82
|
....*....
gi 1953011268 461 DMLSDVRQK 469
Cdd:pfam03938 83 QELQKKQQE 91
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
402-561 |
6.59e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 39.22 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 402 SLEQDIREKEEAIRQKSNEVQELQ----------NDLDRETSSLQ----ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:pfam14932 71 ALEESLEEIREATEDLEAELQELQktkqlkinrlNKLQAQASSLSqglrALVAEEEEAAKQLEELQEELAALNAKTNNVL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 468 QKCQDETQMISSLKTQIQ-----SQeSDLK---SQEDdlnRAKSELTRLQQEetQLEQSIQA-------GKVQLETIIKS 532
Cdd:pfam14932 151 QSLQSEVKELASFFSASEppvflSQ-LPLEpylLQEE---QFTKYLTLYTKK--QFFQGISElvefsneERFQLLDLSDC 224
|
170 180 190
....*....|....*....|....*....|.
gi 1953011268 533 --LKSTQDEINQARSKLSQLQESHQEAHRTL 561
Cdd:pfam14932 225 seRDSDEVDVEHRRSELARLQSAYICAQLQL 255
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
142-189 |
8.99e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 37.46 E-value: 8.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1953011268 142 NGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMH 189
Cdd:COG5126 83 DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
435-549 |
9.10e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 36.79 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR------QKCQDETQMISSLKT-QIQSQESDLKsqeDDLNRAKSEL-T 506
Cdd:COG1382 9 VQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEkaleelEKLPDDAEVYKSVGNlLVKTDKEEVI---KELEEKKETLeL 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953011268 507 RLQQEETQlEQSIQagkvqletiiKSLKSTQDEINQARSKLSQ 549
Cdd:COG1382 86 RLKTLEKQ-EERLQ----------KQLEELQEKLQEALSGAGG 117
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
384-519 |
9.41e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.47 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 384 KELDDISQEIAQ----LQREKYSLE---QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:PRK00106 90 QEFKSERQELKQiesrLTERATSLDrkdENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAE 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011268 457 AklRDMLsdvrqKCQDETQMISSLKTQIQSQESDLKSQEDDLnrAKSELTRLQQE---ETQLEQSI 519
Cdd:PRK00106 170 A--REII-----LAETENKLTHEIATRIREAEREVKDRSDKM--AKDLLAQAMQRlagEYVTEQTI 226
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
390-512 |
9.58e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 38.81 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 390 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQD--------------RLDEMDQQ 455
Cdd:pfam14915 150 SQQLSKAESKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDkvnkyigkqesleeRLAQLQSE 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011268 456 KAKLRDMLSDVRQKCQDETQMIsslkTQIQSQESDLKSQEddlnRAKSELTRLQQEE 512
Cdd:pfam14915 230 NMLLRQQLEDAQNKADAKEKTV----IDIQDQFQDIVKKL----QAESEKQVLLLEE 278
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
402-601 |
9.83e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 39.59 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 402 SLEQDIREKEEAIRQ-KSNEVQELQNDLDRETSSLQELEAQKQD---------AQDRLDEMDQQKAKLRD---------M 462
Cdd:pfam13779 555 DLQRMLDRIEELARSgRRAEAQQMLSQLQQMLENLQAGQPQQQQqqgqsemqqAMDELGDLLREQQQLLDetfrqlqqqG 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011268 463 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDdlnrAKSELTRLQQEETQLEQsiqagkvQLETIIKSLKSTQDEinQ 542
Cdd:pfam13779 635 GQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQG----GAEALGDLAERQQALRR-------RLEELQDELKELGGK--E 701
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011268 543 ARSKLSQLQESHQEAHRTLEQ--YDEALDGAHGAsltnLADLSEGV-SLAE----------------RGGFGAMDDPF 601
Cdd:pfam13779 702 PGQALGDAGRAMRDAEEALGQgdLAGAVDAQGRA----LEALRKGAqQLAEamqqqqgqgqqpgqggQGGRQAGQDPL 775
|
|
| |
