|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
115-210 |
1.50e-36 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 132.40 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 115 WVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSkGI 194
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80
|
90
....*....|....*.
gi 1239950982 195 DPPQVLSPDMVPPSER 210
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
1-60 |
1.68e-26 |
|
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: 103.90 E-value: 1.68e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 1 MNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEPVPSVLPPSLIPPSKR 60
Cdd:smart00027 37 LKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
125-191 |
8.39e-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: 94.98 E-value: 8.39e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 125 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVS 191
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
231-417 |
2.04e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR 390
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|....*..
gi 1239950982 391 SKLSQLQESHQEAHRTLEQYDEALDGA 417
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-437 |
3.07e-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: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 301
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS 381
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 382 TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-414 |
3.08e-18 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 87.26 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 227 TGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 306
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkVQLETIIKSLKSTQDEI 386
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQALDELLKEA 192
|
170 180
....*....|....*....|....*...
gi 1239950982 387 NQARSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEEL 220
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-437 |
1.09e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 389
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239950982 390 RSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-437 |
1.83e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQD-------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 382
Cdd:COG1196 368 LEAEAELAEaeeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 383 QDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
238-430 |
5.59e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 238 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 317
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 318 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQ 397
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190
....*....|....*....|....*....|...
gi 1239950982 398 ESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 430
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-417 |
9.58e-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: 85.11 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE-------ETQLEQSIQAGKVQLETIIKSLKSTQ 383
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190
....*....|....*....|....*....|....
gi 1239950982 384 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 417
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-446 |
1.03e-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: 85.11 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV-----QLETIIKSLKSTQ 383
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQ 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 384 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG------ASLTNLADLSEGVS--LAERGGFGAMDDP 446
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQArldsleRLQENLEGFSEGVKalLKNQSGLSGILGV 524
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
1-42 |
1.49e-16 |
|
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: 74.56 E-value: 1.49e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1239950982 1 MNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 42
Cdd:cd00052 26 GKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
236-417 |
3.15e-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: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 236 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrQK 315
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 316 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQ 395
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170 180
....*....|....*....|..
gi 1239950982 396 LQEshQEAHRTLEQYDEALDGA 417
Cdd:TIGR02168 433 AEL--KELQAELEELEEELEEL 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-422 |
1.72e-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: 79.04 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 302
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlQQEETQLEQSIQAGKVQLETIIKSLKST 382
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239950982 383 QDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASL 422
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
236-430 |
2.03e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.87 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 236 SQEIAQLqrekyslEQDIREKEEAIRQKSNEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 315
Cdd:TIGR02168 676 RREIEEL-------EEKIEELEEKIAELEKALAELR-------KELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 316 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEIN-------Q 388
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaN 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239950982 389 ARSKLSQLQESHQEAHRTLEQYDEALDG--AHGASLT-NLADLSE 430
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEElsEDIESLAaEIEELEE 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-417 |
3.02e-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: 78.27 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 309
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 S-----------DVRQKCQDETQMISSLKTqIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKS 378
Cdd:COG4942 111 RalyrlgrqpplALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239950982 379 LKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 417
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
2-60 |
4.47e-15 |
|
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: 71.64 E-value: 4.47e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 2 NSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPSVLPPSLIPPSKR 60
Cdd:pfam12763 37 NSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDELPDWLVPGSKA 97
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
231-419 |
9.12e-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: 74.58 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVR-----QKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 385
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 386 INQARSKL-SQLQEshqeahRTLEQYDEALDGAHG 419
Cdd:COG1579 161 LEAEREELaAKIPP------ELLALYERIRKRKNG 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-460 |
1.39e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 76.09 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 253 IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 332
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 333 QESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEahRTLEQYDE 412
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239950982 413 ALDGAHGASLTNLADLSEGVSLAERGGFGAMDDPFKNKALLFSNNAQE 460
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
229-430 |
1.40e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELT----RLQQEETQL---EQSIQAGKVQLETIIKSLKS 381
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALleaEAELAEAEEELEELAEELLE 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239950982 382 TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 430
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
229-437 |
2.00e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQkqdaQDRLDE----------- 297
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER----LEELEEelaeleeelee 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 298 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIK 377
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 378 SLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-402 |
2.03e-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: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSL 379
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
170 180
....*....|....*....|...
gi 1239950982 380 KSTQDEINQARSKLSQLQESHQE 402
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQ 292
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-398 |
6.00e-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: 75.83 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKSTQD----E 385
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEklesE 532
|
170
....*....|...
gi 1239950982 386 INQARSKLSQLQE 398
Cdd:TIGR04523 533 KKEKESKISDLED 545
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-409 |
6.95e-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: 75.87 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 221 LGSGEFTGVKE-LDDISQEIAQLQR--------------EKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELE 285
Cdd:TIGR02169 284 LGEEEQLRVKEkIGELEAEIASLERsiaekereledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 286 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI-------QSQESDLKSQEDDLNRAKSELTRLQQEE 358
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 359 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
239-414 |
7.92e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.19 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 239 IAQLQREKYSLE-----------QDIREKEEAIRQKSNEV---QELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 304
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDM--LSDVRQKCQDETQMISSLKTQIQsqesDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV-QLETIIKSLKS 381
Cdd:COG4717 128 LPLYqeLEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1239950982 382 TQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-434 |
8.14e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 S-------DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA-------GKVQLETI 375
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALL 892
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 376 IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSL 434
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-417 |
1.29e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 389
Cdd:TIGR02168 326 EELESKLDE-------LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 390 RS-------KLSQLQESHQEAHRTLEQYDEALDGA 417
Cdd:TIGR02168 399 NNeierleaRLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
229-371 |
5.34e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKS--NEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 306
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 307 DMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 371
Cdd:COG4717 174 ELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-409 |
6.45e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD-----AQDRLDEMDQQKAK 304
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDMLSDVR----------QKCQDETQMISSLKTQIQSQESDLKSQEDDlNRAKSELTRLQQEEtqLEQSIQAGKVQLET 374
Cdd:TIGR02169 803 LEEEVSRIEarlreieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKS-IEKEIENLNGKKEE--LEEELEELEAALRD 879
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 375 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-402 |
6.73e-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: 72.36 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 389
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|...
gi 1239950982 390 RSKLSQLQESHQE 402
Cdd:TIGR04523 495 EKELKKLNEEKKE 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
238-437 |
7.30e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 238 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 317
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 318 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQ 397
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239950982 398 ESHQEAHRTLEQYD---EALDGAHGASLTNLADLSEGVSLAER 437
Cdd:TIGR02168 393 LQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEEAEL 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
229-414 |
8.43e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 8.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 306
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDetqmISSLKTQIQSQESDLK-SQEDDLNRAKSELTRLQQEETQLEQsiqagkvqletiikSLKSTQDE 385
Cdd:COG4717 160 ELEEELEELEAE----LAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEE--------------ELEEAQEE 221
|
170 180
....*....|....*....|....*....
gi 1239950982 386 INQARSKLSQLQEShQEAHRTLEQYDEAL 414
Cdd:COG4717 222 LEELEEELEQLENE-LEAAALEERLKEAR 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-442 |
1.54e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.86 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 306
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 ---------DMLSDVRQKCQDETQMISSLKTQIQSQESD---LKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 374
Cdd:COG3883 103 syldvllgsESFSDFLDRLSALSKIADADADLLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 375 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGFGA 442
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
229-388 |
1.60e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.20 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 306
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMI-SSLKTQI---QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 382
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....*.
gi 1239950982 383 QDEINQ 388
Cdd:COG3206 378 RLAEAL 383
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-437 |
3.18e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQK-SNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQ 388
Cdd:TIGR02169 331 IDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 389 ARSKLSQLQESHQEAHRTLEQYDEALDGA---HGASLTNLADLSEGVSLAER 437
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEDKALEIKKQEW 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-404 |
5.11e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD-- 307
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEEle 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 308 -MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 386
Cdd:COG1196 407 eAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
170
....*....|....*...
gi 1239950982 387 NQARSKLSQLQESHQEAH 404
Cdd:COG1196 487 AEAAARLLLLLEAEADYE 504
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
233-409 |
5.48e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 69.28 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKSN------EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 303
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNGlvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 304 KLRDMLSDVRQkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE----ETQLEQSIQAGKVQLETIIKSL 379
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQiaalRAQLQQEAQRILASLEAELEAL 325
|
170 180 190
....*....|....*....|....*....|....
gi 1239950982 380 KST----QDEINQARSKLSQLQESHQEAHRtLEQ 409
Cdd:COG3206 326 QAReaslQAQLAQLEARLAELPELEAELRR-LER 358
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
231-438 |
1.14e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKSNEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 305
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 306 RDMLSDVRqkcqdetqmisslkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 385
Cdd:PRK02224 327 RDRLEECR--------------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 386 INQARSKLSQLQESHQEAHRTLEQYDEALDGAHG------ASLTNLAD-LSEGVSLAERG 438
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREreaeleATLRTARErVEEAEALLEAG 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-409 |
1.20e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKSNEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 294
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 LDEMDQQKAKLRDMLSDVRQKC-QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLE 373
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239950982 374 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
230-379 |
1.91e-11 |
|
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: 64.56 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 309
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSEltrLQQEETQLEQSIQAGKVQLETIIKSL 379
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-367 |
2.06e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 226 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 304
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 305 LRDMLSDVRQKCQDETQMISSLKTQIQSQ----ESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 367
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-414 |
3.32e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 244 REKYSLEQDIREKEEAIRQksnEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDmLSDVRQKCQDetqmI 323
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEEL-------AEAEERLEALEAELDALQERREALQR-LAEYSWDEID----V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 324 SSLKTQIQSQESDLksqeDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 403
Cdd:COG4913 664 ASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170
....*....|.
gi 1239950982 404 HRTLEQYDEAL 414
Cdd:COG4913 740 EDLARLELRAL 750
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-358 |
8.07e-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: 65.86 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1239950982 311 DVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE 358
Cdd:TIGR02169 466 KYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
238-403 |
9.53e-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: 65.15 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 238 EIAQLQREKYSLEQDIREKEEAIRqksNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 317
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLK---NELSELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 318 DETQMISSLKTQIQSQESDLKSQEDD---LNRAKSELTRLQQEETQLEQSIQAGKvQLETIIKSLKSTQDEINQARSKLS 394
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELERLREHNK-HLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 1239950982 395 QLQESHQEA 403
Cdd:pfam05557 239 REEKYREEA 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-409 |
1.37e-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: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKyslEQDI-REKEEAIRQKSNEVQELQNDLDRETSSLQEL-------EAQKQDAQDRLDEMDQQ 301
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLneqisqlKKELTNSESENSEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ---------- 371
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknnseikd 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239950982 372 -------LETIIKSLKSTQDEINQarsKLSQLQESHQEAHRTLEQ 409
Cdd:TIGR04523 445 ltnqdsvKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQ 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-413 |
1.87e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLD------RETSSLQE-------LEAQKQDAQDRL 295
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEkaeeyikLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 296 DEMDQQKAKLRDMLSDVRQKCQD------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE-QSIQAG 368
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKL 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239950982 369 KVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 413
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
237-437 |
2.40e-10 |
|
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: 63.76 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREKYSLEQDiREKEEAIRQKS---NEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 313
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 314 QKCQDETQMISSLKTQIQSQESDLKSQEDdlnRAKSELTRLQQEETQLEQSiqagKVQLETIIKSLKSTQDEINQARSKL 393
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL----QAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239950982 394 SQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-430 |
3.59e-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: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQeIAQLQREKysleQDIREKEEAIRQKSNEVQ----ELQNDLDR-------------------ET------SS 280
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 281 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI------------------QSQESDLKSQED 342
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 343 DLNR-----------AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYD 411
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260
....*....|....*....|..
gi 1239950982 412 EALDGA---HGASLTNLADLSE 430
Cdd:TIGR02169 392 EKLEKLkreINELKRELDRLQE 413
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
238-385 |
3.97e-10 |
|
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: 61.70 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 238 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQ-------KCQDETQMISSLKTQIQSQeSDLKSQEDDLNRAKSELTR-LQQEETQLEqSIQAGK----VQLETIIK 377
Cdd:pfam09787 128 EELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELENRLHQLTEtLIQKQTMLE-ALSTEKnslvLQLERMEQ 205
|
....*...
gi 1239950982 378 SLKSTQDE 385
Cdd:pfam09787 206 QIKELQGE 213
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-412 |
4.10e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELTRLQQEETQleQSIQAGKVQLETIIKSLKST 382
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKK 583
|
170 180 190
....*....|....*....|....*....|
gi 1239950982 383 QDEINQarsKLSQLQESHQEAHRTLEQYDE 412
Cdd:TIGR04523 584 QEEKQE---LIDQKEKEKKDLIKEIEEKEK 610
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-402 |
5.25e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLE---QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 306
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQ--EDDLNRAKSELT----RLQQEETQLEQSIQAGKvQLETIIK 377
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELKnqekKLEEIQNQISQNNKIIS-QLNEQIS 345
|
170 180
....*....|....*....|....*.
gi 1239950982 378 SLKSTQDEINQARSKLS-QLQESHQE 402
Cdd:TIGR04523 346 QLKKELTNSESENSEKQrELEEKQNE 371
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
240-428 |
6.69e-10 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 62.02 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 240 AQLQrekySLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 319
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 320 TQMISSLKTQIQSQESDLKSQEDDLNRaKSELTRLQ----QEETQLEQSIQA-----GKVQLETIIKsLKSTQDEINQAR 390
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETIAE-LKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239950982 391 SKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADL 428
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGL 224
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
230-409 |
7.71e-10 |
|
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: 60.01 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 302
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDML-------SDVRQKCQDETQM-ISSLKTQIQSQESDLKS--QEDDLNRAKSELTRLQQEetQLEQSIQAgkvqL 372
Cdd:pfam12795 130 QQIRNRLngpappgEPLSEAQRWALQAeLAALKAQIDMLEQELLSnnNRQDLLKARRDLLTLRIQ--RLEQQLQA----L 203
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239950982 373 ETIIKSLKSTQDEinQARSKLSQLQESHQEAHRTLEQ 409
Cdd:pfam12795 204 QELLNEKRLQEAE--QAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-402 |
8.71e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQ---KSNEVQELQNDLDRETSSLQELEAQ-----KQDAQDRL----DE 297
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNkelkSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 298 MDQQKAKLRDMLSDVRQKcqdeTQMISSLKTQIqsqeSDLKSQEDDLNRAKSELTR-LQQEETQLE----------QSIQ 366
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQN----NKIISQLNEQI----SQLKKELTNSESENSEKQReLEEKQNEIEklkkenqsykQEIK 387
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239950982 367 agkvQLETIIKSLKST---QDEINQAR-SKLSQLQESHQE 402
Cdd:TIGR04523 388 ----NLESQINDLESKiqnQEKLNQQKdEQIKKLQQEKEL 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
269-428 |
1.07e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 269 ELQnDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 348
Cdd:COG1579 11 DLQ-ELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 349 S--ELTRLQQEETQLEQSIQagkvQLEtiikslkstqDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLA 426
Cdd:COG1579 87 NnkEYEALQKEIESLKRRIS----DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
..
gi 1239950982 427 DL 428
Cdd:COG1579 153 EL 154
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
224-306 |
1.21e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.17 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 224 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 303
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 1239950982 304 KLR 306
Cdd:COG1579 160 ELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-409 |
1.58e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 239 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQnDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDVRQk 315
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDvasAEREIAELEAELERLDASSDDLAA- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 316 cqdetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQ 395
Cdd:COG4913 690 ----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170
....*....|....
gi 1239950982 396 LQESHQEAHRTLEQ 409
Cdd:COG4913 760 GDAVERELRENLEE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-412 |
1.73e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL-------DEMDQQK 302
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkerDELEAQL 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSE------LTRLQQEETQLEQSIQAgkvqLETI- 375
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA----LEPVn 974
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239950982 376 ---IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDE 412
Cdd:TIGR02169 975 mlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
231-414 |
2.80e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.23 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKSNEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 298
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 299 ---DQQKAKLRDMLSDVR---QKCQDETQMISslktqiQS---QESDLKSQ---EDDLNRAKSELTRLQQEETQLEQSIQ 366
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKeqnKELKEEIDRVK------QSytlNESELESVrqlEKQLESLEKQYDEITERIAEQEIAYS 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239950982 367 AGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-424 |
3.12e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqLETIIKSLKSTQDEINQA 389
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA----SEERVRGGRAVEEVLKAS 519
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239950982 390 RS----KLSQLQeshqeahRTLEQYDEALDGAHGASLTN 424
Cdd:TIGR02169 520 IQgvhgTVAQLG-------SVGERYATAIEVAAGNRLNN 551
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
230-417 |
4.31e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 303
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 304 KLRDMLSDVRQKC-----QDET--QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 376
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 417
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-403 |
4.63e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 299
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 300 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSiqagkvqLETIIKSL 379
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170 180
....*....|....*....|....
gi 1239950982 380 KSTQDEINQARSKLSQLQESHQEA 403
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKES 671
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
230-418 |
5.83e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 302
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelaekrdELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQDETQM---ISSLKTQIQSQESDLKsQEDDLNRAKSEL-TRLQQEETQLEQsiqagKVQLETIIKS 378
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLrkeIERLEWRQQTEVLSPE-EEKELVEKIKELeKELEKAKKALEK-----NEKLKELRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239950982 379 LKSTQDEINQARSKLSQLQESHQEAH-------RTLEQYDEALDGAH 418
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHeemielyKEADELRKEADELH 215
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
230-415 |
7.68e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 58.01 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIR------EKEEAIRQKS-NEVQELQNDLDRETSSLQELEAQKQDAQDRLD------ 296
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRLAAEdfrqkyEDELNLRTSAeNDLVGLRKDLDEATLARVDLEAKIESLKEELAflkknh 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 297 --EMDQQKAKLRD-----------------MLSDVRQkcQDEtQMISSLKTQI----QSQESDLKSQ----EDDLNRAKS 349
Cdd:pfam00038 141 eeEVRELQAQVSDtqvnvemdaarkldltsALAEIRA--QYE-EIAAKNREEAeewyQSKLEELQQAaarnGDALRSAKE 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 350 ELT----RLQQEETQLeQSIQAGKVQLETIIKSLKSTQD-EINQARSKLS----QLQESHQEAHRTLEQYDEALD 415
Cdd:pfam00038 218 EITelrrTIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQELLN 291
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-403 |
1.07e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKysleQDIREKEEAIRQKSNEVQELQN------DLDRETSSLQELEAQKQD---AQDRLDEMDQ 300
Cdd:COG4913 617 AELAELEEELAEAEERL----EALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERldaSSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 301 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE--ETQLEQSIQAGKVQ--LETII 376
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERelRENLE 772
|
170 180
....*....|....*....|....*..
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQESHQEA 403
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
230-412 |
1.14e-08 |
|
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: 58.33 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEeaIRQKSNEVQELQNDLDRetsslQELEaqkqDAQDRLDEMDQQKAKLRDML 309
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALLEN-----LELD----EAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 ---SDVRQKCQDETQMISSLKTQIQSQESDLKSqeddlnraksELTRLQQ------EETQLEQSIQAgkvQLETIIKSLK 380
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKE----------ELERVQQsytlneNELERVRGLEK---QLEELEKRYD 346
|
170 180 190
....*....|....*....|....*....|..
gi 1239950982 381 STQDEINQARSKLSQLQESHQEAHRTLEQYDE 412
Cdd:pfam06160 347 EIVERLEEKEVAYSELQEELEEILEQLEEIEE 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-437 |
1.40e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 257 EEAIRqksnEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQMISSLKTQI 330
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 331 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqletiikslkSTQDEINQARSKLSQLQESHQEAHRTLEQY 410
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180
....*....|....*....|....*..
gi 1239950982 411 DEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAA 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-417 |
1.94e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQDEtqmissLKTQIQSQES------DLKSQEDDLnraKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST 382
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPfyneylELKDAEKEL---EREEKELKKLEEELDKAFE----ELAETEKRLEEL 645
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 383 QDEINQARSKLSqlQESHQEAHRTLEQYDEALDGA 417
Cdd:PRK03918 646 RKELEELEKKYS--EEEYEELREEYLELSRELAGL 678
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
284-415 |
2.63e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 284 LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD--ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL 361
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 362 EQSIQAGKVQLETIIKS--LKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:COG3206 246 RAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
230-375 |
2.87e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.10 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKSNEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 300
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 301 QKAKLRDMLSDVRQKCQDetqmISSLkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI 375
Cdd:PRK12704 129 KEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAI 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-388 |
4.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQDETQMISSLKTQIQSQESD---------------------------------------------------- 336
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealenkieddeeearrrlkrlenkikelgpvnlaaieeyeelkeryd 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239950982 337 -LKSQEDDLNRAKseltrlqqeeTQLEQSIQagkvQLETIIKS-LKSTQDEINQ 388
Cdd:TIGR02168 1004 fLTAQKEDLTEAK----------ETLEEAIE----EIDREARErFKDTFDQVNE 1043
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
231-418 |
5.42e-08 |
|
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: 53.99 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQksneVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVRQKCQD------ETQMISSLKTQIQSQESDLKSQedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--- 381
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEElle 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239950982 382 --TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 418
Cdd:cd00176 175 egHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-415 |
6.42e-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: 56.23 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMdqqKAKLRDM 308
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENL---NGKKEEL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQdE 385
Cdd:TIGR02169 867 EEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-E 945
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239950982 386 INQARSKLSQLQESHQEAHRTL-----------EQYDEALD 415
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIralepvnmlaiQEYEEVLK 986
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-430 |
7.39e-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: 55.16 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 286 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSI 365
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 366 QAGKVQL------------------------------------------ETIIKSLKSTQDEINQARSKLSQLQESHQEA 403
Cdd:COG4942 100 EAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180
....*....|....*....|....*..
gi 1239950982 404 HRTLEQYDEALDGAHGASLTNLADLSE 430
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEK 206
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
225-397 |
1.21e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 225 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKSNEVQELQNDLDRET-SSLQELEAQKQ---------- 289
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneyl 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 290 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQEETQLEQSIQ 366
Cdd:PRK03918 606 elkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|....
gi 1239950982 367 AGKVQLETIIKS---LKSTQDEINQARSKLSQLQ 397
Cdd:PRK03918 684 ELEKRREEIKKTlekLKEELEEREKAKKELEKLE 717
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
237-371 |
1.55e-07 |
|
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: 50.72 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREKYSLEQDIREKEEAIrqksnevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 316
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 317 QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSeltRLQQEETQLEQSIQAGKVQ 371
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-398 |
1.57e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIrEKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR 306
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDI-EEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQaaKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE---QSIQAGKVQLETIIKSLKSTQ 383
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlQRRQQFEEQLVELSTEVQSLI 901
|
170
....*....|....*
gi 1239950982 384 DEINQARSKLSQLQE 398
Cdd:TIGR00606 902 REIKDAKEQDSPLET 916
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
242-413 |
1.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 242 LQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 306
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 ---------DMLSDVRQKC------QDETQMISSLKTQIQSQESDLKSQEDDLNRAkseltRLQQEETQLEQSIQAGKVQ 371
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239950982 372 LETIIKSLKSTQDEINQARS--KLSQLQESHQEAHRTLEQYDEA 413
Cdd:COG4717 448 LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
240-399 |
2.32e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 240 AQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 294
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS 364
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 365 IQagkvQLETIIKSLKSTQDEINQARSKLsQLQES 399
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEI-QSQEQ 184
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
231-436 |
2.34e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQksneVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKstqdEINQAR 390
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVER 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239950982 391 SKLSQLQESHQEAHRTLEQYdealDGAHGASLTNLADLSEGVSLAE 436
Cdd:COG3096 647 DELAARKQALESQIERLSQP----GGAEDPRLLALAERLGGVLLSE 688
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
251-417 |
2.49e-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: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 251 QDIREKEEAIRQksnEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 330
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 331 QSQESDLKSQEDDLN-----RAKSELTR------LQQEETQLEQSI------QAGKVQLETIIKSLKSTQDEinQARSKL 393
Cdd:pfam01576 267 RELEAQISELQEDLEseraaRNKAEKQRrdlgeeLEALKTELEDTLdttaaqQELRSKREQEVTELKKALEE--ETRSHE 344
|
170 180
....*....|....*....|....
gi 1239950982 394 SQLQESHQEAHRTLEQYDEALDGA 417
Cdd:pfam01576 345 AQLQEMRQKHTQALEELTEQLEQA 368
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
233-405 |
3.00e-07 |
|
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: 53.75 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 312
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 313 RQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSK 392
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERKVEGLGEE 259
|
170
....*....|....*..
gi 1239950982 393 LS----QLQESHQEAHR 405
Cdd:pfam07888 260 LSsmaaQRDRTQAELHQ 276
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
225-421 |
3.07e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.81 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 225 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 300
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 301 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQEsdlksqeddlnrAKSELTRLQQEETQLEQSIQAGKVQLETII---- 376
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRakle 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGAS 421
Cdd:COG5185 510 RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
231-405 |
3.42e-07 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 53.54 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKSNEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 294
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 ---LD-----------------EMDQQKAKLR---DMLSDVRQKCqdetqmISSLK---TQIQSQEsdlKSQEDDLNRAK 348
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQET------IAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 349 SELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHR 405
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
230-403 |
3.44e-07 |
|
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: 53.97 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAqkqdaqdRLDEMDQQKAKLRDML 309
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA-------RVSDLELEKVKLVNAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtRLQQEEtqLEQSIQAGKVQLetiikslKSTQDEINQA 389
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF-RNKSEE--METTTNKLKMQL-------KSAQSELEQT 711
|
170
....*....|....
gi 1239950982 390 RSKLSQLQESHQEA 403
Cdd:pfam15921 712 RNTLKSMEGSDGHA 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-415 |
3.61e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 248 SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELeaqkqdaQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLK 327
Cdd:TIGR02169 643 TLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRL-------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 328 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQEShqEAHRTL 407
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRI 793
|
....*...
gi 1239950982 408 EQYDEALD 415
Cdd:TIGR02169 794 PEIQAELS 801
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
237-437 |
3.67e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREKYSLEQDiREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 297
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 298 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL------------NRAKSELTRLQQE-------E 358
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 359 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES-----------------------HQEAHRTLEQYDEALD 415
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGwcavlrlardndverrlhrrelaYLSADELRSMSDKALG 1155
|
250 260
....*....|....*....|....*..
gi 1239950982 416 GAHGA-----SLTNLADLSEGVSLAER 437
Cdd:COG3096 1156 ALRLAvadneHLRDALRLSEDPRRPER 1182
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
233-402 |
3.72e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.59 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 301
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 KAKLRDMLSDVRQK--CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETiiKSL 379
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL--ADP 436
|
170 180
....*....|....*....|...
gi 1239950982 380 KSTQDEINQARSKLSQLQESHQE 402
Cdd:pfam05557 437 SYSKEEVDSLRRKLETLELERQR 459
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
231-430 |
3.79e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQ-------LQREKYSLEQDIREK---------EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQ----- 289
Cdd:COG3096 793 ERDELAEQYAKasfdvqkLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeq 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 290 -----------------DAQDRLDEMDQQKAKLRDMLSDVRQKCqdetQMISSLKTQIQSQESDLKSQED---DLNRAKS 349
Cdd:COG3096 873 lqllnkllpqanlladeTLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLVAVLQSDPEQFEQlqaDYLQAKE 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 350 ELTRLQQEETQLEQSIQ-------AGKVQL--------ETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLeqydEAL 414
Cdd:COG3096 949 QQRRLKQQIFALSEVVQrrphfsyEDAVGLlgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL----ASL 1024
|
250
....*....|....*.
gi 1239950982 415 DGAHGASLTNLADLSE 430
Cdd:COG3096 1025 KSSRDAKQQTLQELEQ 1040
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-391 |
3.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQEL--------------------------------------- 270
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsyldvllgsesfsdfldrlsalskiada 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 271 QNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS 349
Cdd:COG3883 131 DADLLEELKADKaELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239950982 350 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARS 391
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
229-415 |
5.40e-07 |
|
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: 53.58 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 305
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 306 RDMLSDVRQKCQDETQMI--------------SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE----QSIQA 367
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNA 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 368 GKVQLETiIKSLKSTQD----EINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:pfam15921 641 GSERLRA-VKDIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
230-440 |
5.58e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQK 302
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEElqkerqdLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQ-----ESDLKSQEDDLNRA--KSELTRLQQEETQLEQSIQAGKVQLETI 375
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALseaeaEQALDELLKEANRNaeKEEELAEAEKLIESLPRELAEELLEAKD 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 376 IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGF 440
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
221-405 |
5.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 221 LGSGEFTGVKELDDISQEIAQLQRekysLEQDIREKEEAIRQKSNEvQELQNDLDR-ETSSLQELEA---QKQDAQDRLD 296
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELKE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 297 EMDQQKAKLRDMLSDVRQKCQDETQmiSSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS--IQAGKVQLET 374
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEE 480
|
170 180 190
....*....|....*....|....*....|....
gi 1239950982 375 IIKSLKSTQDE---INQARSKLSQLQESHQEAHR 405
Cdd:COG4717 481 LKAELRELAEEwaaLKLALELLEEAREEYREERL 514
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
230-405 |
5.65e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 299
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 300 QQKAKLRDMLSDVRqkcQDETQMISSLKTQIQSqESDLKSQEDDLNR----AKSELTRL---QQEETQLEQSiqagkvQL 372
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRksleGNTQLQDLlqkQRDYLTARIQ------RL 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239950982 373 ETIIKSLkstQDEINQARSKLSQLQ----ESHQEAHR 405
Cdd:PRK11281 240 EHQLQLL---QEAINSKRLTLSEKTvqeaQSQDEAAR 273
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
230-418 |
6.16e-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: 53.05 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDiREKEEAIRQKSNEVQELQndldRETSSLQELEAQKQDAQDRLDeMDQQKAKL---R 306
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQLR----ARIEELRAQEAVLEETQERIN-RARKAAPLaahI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ------SIQAGKVQLETIIK 377
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSkmrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatSIREISCQQHTLTQ 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239950982 378 SLKSTQ-------DEINQARSKLSQLQ-ESHQEAHRTLEQYDEALDGAH 418
Cdd:TIGR00618 380 HIHTLQqqkttltQKLQSLCKELDILQrEQATIDTRTSAFRDLQGQLAH 428
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
230-393 |
6.42e-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: 52.72 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 292
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 293 DRLDEMDQQKAK-----------LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE--- 358
Cdd:pfam05667 415 QRLVELAGQWEKhrvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239950982 359 --TQ--LE--QSIQAGKVQLETIIKSLKSTQDEINQARSKL 393
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-418 |
7.70e-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: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKSNEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 303
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 304 KLRDMLSDVRQKCQDEtqmisslKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqLETIIKSLKSTQ 383
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREE----QEAANAEVERLQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 384 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 418
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
229-402 |
9.69e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDdisQEIAQLQREKYSLEQDIREKEEAI---RQKSNE-VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 304
Cdd:PHA02562 176 IRELN---QQIQTLDMKIDHIQQQIKTYNKNIeeqRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDMLSDVRQK--------------------------C----QDETQMISSLKT---QIQSQESDLKSQEDDLNRAKSEL 351
Cdd:PHA02562 253 PSAALNKLNTAaakikskieqfqkvikmyekggvcptCtqqiSEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 352 TRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA-------RSKLSQLQESHQE 402
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvdnAEELAKLQDELDK 390
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
230-429 |
1.03e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 302
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 382
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239950982 383 QDEINQARSKLSQLQE---SHQEAHRTLEQYDEALDGAHGASLTNLADLS 429
Cdd:pfam01576 179 SKLKNKHEAMISDLEErlkKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-412 |
1.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKS--NEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 307
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 308 MLSDVRQKCQDETQMIsSLKTQIQSQESDLK-----------SQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETII 376
Cdd:PRK03918 544 LKKELEKLEELKKKLA-ELEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDAEK----ELEREE 618
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ----YDE 412
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEElekkYSE 658
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-437 |
1.12e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 273 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL-NRAKSE- 350
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 351 ---------------------------LTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 403
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....
gi 1239950982 404 HRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-426 |
1.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 309
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQleqsiqagkvqletiikSLKSTQDEINQA 389
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA-----------------DLDADLESLPEY 817
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239950982 390 RSKLSQLQESHQEAHRtlEQYDEALDGAHGASLTNLA 426
Cdd:COG4913 818 LALLDRLEEDGLPEYE--ERFKELLNENSIEFVADLL 852
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
260-412 |
1.49e-06 |
|
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: 48.55 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 260 IRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDemdqqkaklrdmlsDVRQKCQDETQMISSlktQIQSQESDLKs 339
Cdd:pfam07321 5 LRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQ--------------DYRAWRPQEEQRLYA---EIQGKLVLLK- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 340 qedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR---SKLSQLQESHQEAHRTLEQYDE 412
Cdd:pfam07321 67 ---ELEKVKQQVALLRENEADLEKQVAEARQQLEAEREALRQARQALAEARravEKFAELVRLVQAEELRQQERQE 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-402 |
1.76e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIaqlqREKYSLEQDIREKEEAIRQKSNEVQELQ---NDLDRETSSLQ----ELEAQKQDAQDRLDEMDQQK 302
Cdd:PRK03918 200 KELEEVLREI----NEISSELPELREELEKLEKEVKELEELKeeiEELEKELESLEgskrKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVR--QKCQDETQMISSLKTQIqsqesdlksqEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLK 380
Cdd:PRK03918 276 EELEEKVKELKelKEKAEEYIKLSEFYEEY----------LDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLE 341
|
170 180
....*....|....*....|..
gi 1239950982 381 STQDEINQARSKLSQLQESHQE 402
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHEL 363
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
243-356 |
1.97e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 243 QREKYSLEQDIREKEEAIRQKSNEVQELqndldretsslqelEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDE--- 319
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERL--------------EAEVEELEAELEEKDERIERLERELSEARSEERREirk 463
|
90 100 110
....*....|....*....|....*....|....*..
gi 1239950982 320 TQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ 356
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-414 |
1.98e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQ---DRLDEMDQQKAKLR 306
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSLKTQI---QSQESDLKSQEDD----------LNRAKSELTRLQQEETQLEQSIQAgkvqLE 373
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLSRLEEEING----IE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239950982 374 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
237-436 |
2.07e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 316
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 317 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQqeetqlEQS--IQAGKVQLETIIKSLKSTQDEINQARSKLS 394
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLR------EQSgeEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239950982 395 QLQEShqeahrtLEQYDEALDGAHGASLTNLADLSE---GVSLAE 436
Cdd:PRK04863 652 ARKQA-------LDEEIERLSQPGGSEDPRLNALAErfgGVLLSE 689
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-409 |
2.23e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 296 DEMDQQKAKLRDMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE----ETQLEQS---IQAG 368
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseLEQL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1239950982 369 KVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
233-423 |
2.30e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 306
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQEDDLNRAKSE----LTRLQQEETQLEQSIQAGKVQLETIIKSLKST 382
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239950982 383 QDEINQARSKLSQLQESHQEAHRTLEQY--------DEALDGAHGASLT 423
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAqqerdelaDEIASGASGKSAL 880
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-348 |
3.14e-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: 50.15 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREkysLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 311
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 1239950982 312 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 348
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
231-415 |
3.21e-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: 49.95 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL---QELE--------AQKQDAQD---RLD 296
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAewkLELErvlpqlkvTIKADAKDwraHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 297 EMDQQKAKLRDMLSDVRQKcqdetqmisslktqiqsqesdLKSQEDDLNRAkseLTRLQQEETQLEQsiqagkvQLETII 376
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:pfam10498 275 QEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELE 313
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
229-428 |
3.35e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 301
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 -------------KAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlQQEETQLEQSI 365
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 366 QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHrtLEQYDEALDGAHGASLTNLADL 428
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLK--EDANSEQAQGSIGERLAQLEDL 898
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
200-417 |
3.44e-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: 50.74 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 200 LSPDMVPPSERGTpipDGSSCLGSGEFTGVKELDDISQEIAQLQREkyslEQDIREKEEAIRQKSNEVQE----LQNDLD 275
Cdd:TIGR00618 522 NPGPLTRRMQRGE---QTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCDNRSKEdipnLQNITV 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 276 R---ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmissLKTQIQSQESDLKSQEDdlnRAKSELT 352
Cdd:TIGR00618 595 RlqdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSI 667
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 353 RLQQEetQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 417
Cdd:TIGR00618 668 RVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
219-397 |
3.64e-06 |
|
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: 50.59 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 219 SCLgSGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELE---AQKQ----- 289
Cdd:pfam10174 376 STL-AGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEriier 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 290 -------DAQDRLDEMDQQKAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESD-------LKSQEDDLNRAKSELT 352
Cdd:pfam10174 455 lkeqrerEDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKEECS 534
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 353 RLQ--------QEET------------QLEQSIQ-----AGKVQ--LETIIKSLKSTQDEINQARSKLSQLQ 397
Cdd:pfam10174 535 KLEnqlkkahnAEEAvrtnpeindrirLLEQEVArykeeSGKAQaeVERLLGILREVENEKNDKDKKIAELE 606
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-409 |
3.76e-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: 50.56 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLEQDIREKEEairqksnEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQKAK 304
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALES-------ENAELQAELRTLQQAKQDsehkrkkLEGQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDMLSdvrqKCQDETQMISSLktqiqsqesdlksqeddLNRAKSELTRLQQEETQLEQSIQAGKVQL--ETIIK-SLKS 381
Cdd:pfam01576 431 LAEKLS----KLQSELESVSSL-----------------LNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQKlNLST 489
|
170 180
....*....|....*....|....*...
gi 1239950982 382 TQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:pfam01576 490 RLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
228-418 |
4.56e-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: 50.43 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 228 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ---NDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 304
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDMLSDVRQKCQDETQMISSLKTQ----IQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVqletiiKSLK 380
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD------DYLK 973
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239950982 381 STQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 418
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-399 |
5.10e-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: 50.06 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 256 KEEAIRQ--KSNE----VQELQNDLDRetsSLQELEAQKQDAQ------------------DRLDEMDQQKAKLRDMLSD 311
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELER---QLKSLERQAEKAErykelkaelrelelallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 312 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARS 391
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
....*...
gi 1239950982 392 KLSQLQES 399
Cdd:TIGR02168 331 KLDELAEE 338
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-415 |
5.80e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 286 AQKQDAQDRLDEMDQQKAKLRDMLSDVR-------------------QKCQDETQMISSLKtQIQSQESDLKSQEDDLNR 346
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGELErqleplerqaekaeryrelKEELKELEAELLLL-KLRELEAELEELEAELEE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 347 AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
237-415 |
7.21e-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: 49.58 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRE-TSSLQELEAQKQDA------QDRLDEMDQQKAKLR 306
Cdd:TIGR00618 462 QESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSLKTQIQsqesdlksqeddlnrakseltRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 386
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQ---------------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
170 180 190
....*....|....*....|....*....|
gi 1239950982 387 N-QARSKLSQLQESHQEahrtLEQYDEALD 415
Cdd:TIGR00618 601 EkLSEAEDMLACEQHAL----LRKLQPEQD 626
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
232-388 |
7.79e-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: 49.08 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKSNEV-----QELQ 271
Cdd:pfam03148 139 LEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDNieraeKERA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 272 N--DLdRET--SSLQ----ELEAQKQDA----QDRLDEMDQQKAKLRDMLsdvrQKCQDEtqmISSLKTQIQSQESDLKS 339
Cdd:pfam03148 219 AsaQL-RELidSILEqtanDLRAQADAVnfalRKRIEETEDAKNKLEWQL----KKTLQE---IAELEKNIEALEKAIRD 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 340 QEDDL--------NRAK---SELTR------LQQEETQLEQSIQAGKVQL---ETIIKSLKSTQDEINQ 388
Cdd:pfam03148 291 KEAPLklaqtrleNRTYrpnVELCRdeaqygLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
229-357 |
8.33e-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: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQrekySLEQDIREKEEAIRQKSNEVQEL--------QNDLDRETSSLQELEAQKQDAQDRLDEMDQ 300
Cdd:smart00787 157 KEDYKLLMKELELLN----SIKPKLRDRKDALEEELRQLKQLedeledcdPTELDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 301 QKAKLRDMLSDVRQKCQDetqmissLKTQIQSQESDLKS----QEDDLNRAKSELTRLQQE 357
Cdd:smart00787 233 ELQELESKIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
239-409 |
1.07e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 239 IAQLQREKYSLEQDiREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 299
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 300 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN----RAKSEL-TRLQQEETQLEQSIQAGKVQLET 374
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAeERARARRDELHARLSANRSRRNQ 1078
|
170 180 190
....*....|....*....|....*....|....*
gi 1239950982 375 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
231-413 |
1.09e-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: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLdreTSSLQELEAQKQDAQDRLDE-MDQQKAKLR 306
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCqtlLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDALNQSLKElMHQARTVLK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMIsslktQIQSQESDLKSQEDDLNRAKSELT-RLQQEETQLEQSI----QAGKVQLETIIKSLKS 381
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAAL-----QTGAELSHLAAEIQFFNRLREEDThLLKTLEAEIGQEIpsdeDILNLQCETLVQEEEQ 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239950982 382 TQDEINQARSKL--------------SQLQESHQEAHRTLEQYDEA 413
Cdd:TIGR00618 833 FLSRLEEKSATLgeithqllkyeecsKQLAQLTQEQAKIIQLSDKL 878
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
227-433 |
1.15e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.80 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 227 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 306
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 D------MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRA-KSELTRLQQEETQLEQSIQAGKVQLETIIKSL 379
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 380 KSTQDEINQAR-----SKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVS 433
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE 502
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
229-357 |
1.23e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 308
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1239950982 309 lsdvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE 357
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-413 |
1.25e-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: 48.86 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEaqkqdaqDRLDEMDQQKAKlrdml 309
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-------DELNKDDFELKK----- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 sdvrqkcqdetqmiSSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 389
Cdd:TIGR04523 557 --------------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
170 180
....*....|....*....|....*..
gi 1239950982 390 R---SKLSQLQESHQEAHRTLEQYDEA 413
Cdd:TIGR04523 623 KkenEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
230-421 |
1.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQ-------------------KC----------------QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSeltrL 354
Cdd:PRK02224 429 AELEAtlrtarerveeaealleagKCpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED----L 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 355 QQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGAS 421
Cdd:PRK02224 505 VEAEDRIERLEE----RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
231-415 |
1.33e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL----------------QELEAQKQDAQDR 294
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehalsirvlpKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 367
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239950982 368 GKVQLETI-IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:TIGR00618 765 NNNEEVTAaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
249-402 |
1.36e-05 |
|
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: 48.70 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQ 321
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 322 MISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQ-LEQSIQagkvQLETIIKSL----KSTQDEINQARSK---L 393
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKR----ELESEIKKLthdiKLKEEQIRELEIKvqeL 555
|
....*....
gi 1239950982 394 SQLQESHQE 402
Cdd:pfam09726 556 RKYKESEKD 564
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
328-415 |
1.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 328 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 407
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
....*...
gi 1239950982 408 EQYDEALD 415
Cdd:COG4372 104 ESLQEEAE 111
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
249-437 |
1.42e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIrqksnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMdQQKAKL----------RDMLSDvRQKCQD 318
Cdd:COG1842 28 LDQAIRDMEEDL-------VEARQALAQVIANQKRLERQLEELEAEAEKW-EEKARLalekgredlaREALER-KAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 319 EtqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQlETIIKSLKSTQDEinQARSKLSQLQE 398
Cdd:COG1842 99 Q---AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEALSGIDSD--DATSALERMEE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239950982 399 SHQEahrtLEQYDEALDG-AHGASLTN-LADLSEGVSLAER 437
Cdd:COG1842 173 KIEE----MEARAEAAAElAAGDSLDDeLAELEADSEVEDE 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
328-398 |
1.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 328 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQE 398
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
137-210 |
1.51e-05 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 44.29 E-value: 1.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 137 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 210
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
230-413 |
1.64e-05 |
|
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: 48.43 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQeIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRET-SSLQELEAQKQDA----------------- 291
Cdd:pfam02463 156 LEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKeQAKKALEYYQLKEkleleeeyllyldylkl 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 292 -QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV 370
Cdd:pfam02463 235 nEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239950982 371 QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 413
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
266-401 |
1.69e-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: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 266 EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmisslktqiqSQESDLKSQEDDLN 345
Cdd:smart00787 152 NLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQEIM 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 346 RAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR----SKLSQLQESHQ 401
Cdd:smart00787 222 IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLK 281
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
230-334 |
1.93e-05 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 44.48 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKKE---QELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|....*
gi 1239950982 310 SDVRQKcqdetqmISSLKTQIQSQE 334
Cdd:pfam13863 83 KKLTAQ-------IEELKSEISKLE 100
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
230-410 |
1.94e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ----QEETQLEQsiqagKVQLETIIKSLKSTQDE 385
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 1239950982 386 IN---QARSKLSQLQESHQEAHRTLEQY 410
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
230-420 |
2.03e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------SNEVQELQNDLDRETSSLQEL 284
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 285 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE 358
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 359 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGA 420
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
257-430 |
2.32e-05 |
|
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: 46.53 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 257 EEAIRQKSNEVQ--ELQNDLDRETSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQMIS 324
Cdd:pfam12795 3 DELEKAKLDEAAkkKLLQDLQQALSLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 325 SLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI---IKSLKSTQDEINQARSKLSQLQESHQ 401
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrnrLNGPAPPGEPLSEAQRWALQAELAAL 161
|
170 180
....*....|....*....|....*....
gi 1239950982 402 EAhrTLEQYDEALdgahgASLTNLADLSE 430
Cdd:pfam12795 162 KA--QIDMLEQEL-----LSNNNRQDLLK 183
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
281-399 |
2.53e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 281 LQELEAQKQDAQDRLDEMDQ----QKAKLRDMLSDVRQKCQdETQMISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQ 356
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElhekQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES--QSQEDLRNQLQNTVHELEA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1239950982 357 EETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 399
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEA 199
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
232-367 |
2.54e-05 |
|
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: 45.37 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLeqdiREKEEAIrqkSNEVQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 311
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSEL---SERLQQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 312 VRQKCQDET-----QMISSLKTQIQSQESDLKSQEDDLNRA------KSELTRLQQeetQLEQSIQA 367
Cdd:pfam16043 81 VSRDQFDETleelnQMLQELLDKLEGQEDAWKKALETLSEEldtkldRLELDPLKE---LLERRIKA 144
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
229-417 |
2.54e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKSNEVQELQNDLDRetsslqeLEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERREDLEELIAERRETIEEKRER 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKvQLETIIKSLKSTQDEINQ 388
Cdd:PRK02224 539 AEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239950982 389 ARSKLSQLQESHQEAHRTLE-------QYDEALDGA 417
Cdd:PRK02224 611 LREKREALAELNDERRERLAekrerkrELEAEFDEA 646
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
281-409 |
3.18e-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: 46.55 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 281 LQELEAQKQDAQDRLDEMDQQKAKLRD---MLSDVRQKCQDETQmisSLKTQIQSqesdLKSQEDDLNRAK-SELTRLQQ 356
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKeleLLNSIKPKLRDRKD---ALEEELRQ----LKQLEDELEDCDpTELDRAKE 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 357 EETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
281-413 |
3.48e-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: 45.79 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 281 LQELEAQKQDAQDRLDEMDQQKAKLRDmlsdVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAkseLTRLQQEETQ 360
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEK----RAEKAEAE---VAALNRRIQLLEEELERTEERLAEA---LEKLEEAEKA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 361 LEQSIQAGKVqLETiikslKSTQDEiNQARSKLSQLQESHQEAHRTLEQYDEA 413
Cdd:pfam00261 73 ADESERGRKV-LEN-----RALKDE-EKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-414 |
3.54e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL 295
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 296 DEMdQQKAKLrdmlsdvrqkcqdeTQMISSLKTQIQSQESDLKSQE-DDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 374
Cdd:PRK03918 355 EEL-EERHEL--------------YEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239950982 375 IIKSLKSTQDEINQARSKL----SQLQESHQEahRTLEQYDEAL 414
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKCpvcgRELTEEHRK--ELLEEYTAEL 461
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
243-363 |
3.91e-05 |
|
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: 43.75 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 243 QREKYSLEQDIREKEEAIRQKsnevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQM 322
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1239950982 323 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE--ETQLEQ 363
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-412 |
4.19e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQdirEKEEAIRQKSNevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 306
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQ---EKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQDETQMISSLKTQIQSQESdlksqeddlnRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 386
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKER----------LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
170 180
....*....|....*....|....*....
gi 1239950982 387 NQARSKLSQLQESHQE---AHRTLEQYDE 412
Cdd:TIGR00606 464 QQLEGSSDRILELDQElrkAERELSKAEK 492
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
250-374 |
4.34e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 250 EQDIREKEEAIRQKSNEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSD----VRQKc 316
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPnspqVRQL- 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 317 qdETQmISSLKTQIQSQESDL--KSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 374
Cdd:COG3524 255 --RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
241-398 |
4.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 241 QLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDaqdrLDEMDQQKAKLRDMLSDV--RQKCQD 318
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD----FEEASGKKIYEHDSMSTMhfRSLGSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 319 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTR-----LQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKL 393
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
....*
gi 1239950982 394 SQLQE 398
Cdd:pfam15921 302 EIIQE 306
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
230-398 |
4.50e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.34 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 309
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 sdvrqkcqdetQMISSLKTQIQSQESDLKSQEDDLNrakselTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 389
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*....
gi 1239950982 390 RSKLSQLQE 398
Cdd:pfam15905 320 EQEHQKLQQ 328
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
236-403 |
5.30e-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: 45.48 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 236 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 315
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 316 CQDETQ----------MISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEqsiqagkvqletiikslKSTQDE 385
Cdd:pfam06008 119 DLSRMLaeaqrmlgeiRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA-----------------NALRDS 181
|
170
....*....|....*...
gi 1239950982 386 INQARSKLSQLQESHQEA 403
Cdd:pfam06008 182 LAEYEAKLSDLRELLREA 199
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
240-377 |
5.74e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.88 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 240 AQLQREKYslEQDIREKEEAIRQKSNEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 319
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 320 TQMIsslktQIQSQESDLKSQEDD----LNRAKseltRLQQEetqlEQSIQAGKVQLETIIK 377
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
251-398 |
6.02e-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: 44.60 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 251 QDIREKEEAIRQKSNEVQELQNDLDRETSSLqeleaqKQDAQDRLDEMDQQKAklrdmlsdVRQKCQDETQMISSLKTQI 330
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTL------KSQGDMQDLNGNNQSV--------TRQKMQQLEQMLTALDQMR 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 331 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQ--AGKV-----QLETIIKSLKSTQDEINQARSKLSQLQE 398
Cdd:cd16853 77 RQIVSELAGLLSAMEYVQKNLTDEELADWKRRQQIAciGGPPnicldRLENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-439 |
6.12e-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: 45.91 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 339 SQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 418
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100
....*....|....*....|.
gi 1239950982 419 GASLTNLADLSEGVSLAERGG 439
Cdd:COG4942 97 AELEAQKEELAELLRALYRLG 117
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-345 |
6.12e-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: 46.55 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110
....*....|....*....|....*....|....*....
gi 1239950982 310 SDVRQKCQ---DETQMISSLKTQIQSQESDLKSQEDDLN 345
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDII 679
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
231-438 |
6.84e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEET---------QLEQSIQAGKVQ-LETIIKSL 379
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlRRELDDRNMEVQrLEALLKAM 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 380 KS-TQDEI----------NQARSKLSQLQ---ESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERG 438
Cdd:pfam15921 439 KSeCQGQMerqmaaiqgkNESLEKVSSLTaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
239-408 |
6.99e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 239 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqqkakLRDMLSDvRQKCQD 318
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE-------LKKILAE-DEKLLD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 319 ETQMISSLKTQIQSQESD----LKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETiiKSLKSTQDEINQARSKLS 394
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK--EKLKNIELTAHCDKLLLE 500
|
170
....*....|....
gi 1239950982 395 QLQESHQEAHRTLE 408
Cdd:pfam05483 501 NKELTQEASDMTLE 514
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
249-396 |
7.08e-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: 44.71 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVRQKCQDETQMISSLKT 328
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 329 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET--IIKSLKSTQDEINQARSKLSQL 396
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAafLQADLKAAKADWNQLYEQAKSL 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-414 |
7.21e-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: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQLETIIKSlkstqDEIN 387
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIrdEKKGLGRTIELKKEILE-----KKQE 454
|
170 180
....*....|....*....|....*..
gi 1239950982 388 QARSKLSQLQESHQEAHRTLEQyDEAL 414
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILEL-DQEL 480
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
279-398 |
7.25e-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: 43.01 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 279 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISslkTQIQSQESDLKSqeddLNRAKSELTRLQQEE 358
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1239950982 359 TQLEQSIQAGKVQLETIIKSLKST----QDEINQARSKLSQLQE 398
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNE 117
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
230-394 |
7.27e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 44.67 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 308
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKcqdetqmISSLKTQIQsqesDLKSQEDDLnrakseLTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEIN- 387
Cdd:pfam04012 113 VEQLRKQ-------LAALETKIQ----QLKAKKNLL------KARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIEe 175
|
....*...
gi 1239950982 388 -QARSKLS 394
Cdd:pfam04012 176 rEARADAA 183
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
295-427 |
7.40e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 LDEMDQQKAKLRDmLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK--SELTRLQQEETQLEQSIQAGKVQL 372
Cdd:COG4717 70 LKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 373 EtiikSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLAD 427
Cdd:COG4717 149 E----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
299-436 |
7.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 299 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLE----- 373
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 374 --------------------------------------TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|.
gi 1239950982 416 GAHGASLTNLADLSEGVSLAE 436
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAE 195
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
241-402 |
7.65e-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: 46.27 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 241 QLQREKYSLEQdIREKEEAIRQKsnEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKL-RDMLSDVRQKCQ 317
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKLeLEKEKRDRKRAE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 318 DETQMI-----SSLKTQIQSQESDLKSQEDDLNR-----AKSELTRLQQEETQLEQSIQAGKVQLETIIKSL--KSTQDE 385
Cdd:pfam17380 491 EQRRKIlekelEERKQAMIEEERKRKLLEKEMEErqkaiYEEERRREAEEERRKQQEMEERRRIQEQMRKATeeRSRLEA 570
|
170
....*....|....*..
gi 1239950982 386 INQARSKLSQLQESHQE 402
Cdd:pfam17380 571 MEREREMMRQIVESEKA 587
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
231-412 |
7.69e-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: 46.50 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ-LALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DV---RQKCQDETQMISSLKTQIQSQES---------------DLKSQEDDLNRAKSELTRLQQ---EETQLEQSIQAGK 369
Cdd:TIGR00618 712 HIeeyDREFNEIENASSSLGSDLAAREDalnqslkelmhqartVLKARTEAHFNNNEEVTAALQtgaELSHLAAEIQFFN 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 370 VQLETIIKSLKSTQDEINQAR-------------------SKLSQLQESHQEAH---RTLEQYDE 412
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIpsdedilnlqcetlvqeeeQFLSRLEEKSATLGeitHQLLKYEE 856
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
227-412 |
7.85e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 227 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKSNEVQELQNDLDRETSS-------------- 280
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 281 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQ 360
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 361 LEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDE 412
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLND 910
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
227-419 |
7.89e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 227 TGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA--- 303
Cdd:PRK02224 509 DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 304 -------KLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL---------TRLQQEETQLEQSIQA 367
Cdd:PRK02224 586 eriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeariEEAREDKERAEEYLEQ 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 368 GKVQLETIIKSLKSTQDEINQARSKLSQLqESHQEAHRTLEQYDEALDGAHG 419
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEEL-EELRERREALENRVEALEALYD 715
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
228-323 |
8.03e-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: 43.34 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 228 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 306
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 1239950982 307 DMLSDVRQKCQDETQMI 323
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
241-415 |
8.21e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.36 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 241 QLQREKYSLEQDIREKEEAIRQKSNEvqelqndldretSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlSDVRQKCQDET 320
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG------------DDLESVEALLKKHEALEAELAAHEERV----EALNELGEQLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 321 QMISSLKTQIQSQESDLKSQEDDLNRAKSE-LTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 399
Cdd:cd00176 68 EEGHPDAEEIQERLEELNQRWEELRELAEErRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK 147
|
170
....*....|....*.
gi 1239950982 400 HQEAHRTLEQYDEALD 415
Cdd:cd00176 148 HKELEEELEAHEPRLK 163
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
233-401 |
8.93e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKySLEQDirekEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 312
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 313 RQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQqeeTQLEQ---SIQAGKVQLETIIKSLKSTQDEINQA 389
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ---TQPERaqaALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170
....*....|..
gi 1239950982 390 RSKLSQLQESHQ 401
Cdd:PRK11281 190 RPSQRVLLQAEQ 201
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
234-371 |
9.14e-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: 45.84 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 234 DISQEIAQLQREKYSLeqdiREK-EEAIRQKSNEVQELqndLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 312
Cdd:pfam05622 279 EIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQ 351
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 313 RQKCQDEtqmiSSLKtqiqsqeSDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 371
Cdd:pfam05622 352 GSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQ 399
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
332-402 |
1.08e-04 |
|
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: 41.78 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 332 SQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQE 402
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
278-411 |
1.09e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.11 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 278 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK------ 348
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapig 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 349 --------SELTRLQQEETQLEQSI----QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYD 411
Cdd:pfam00529 137 gisreslvTAGALVAQAQANLLATVaqldQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
218-357 |
1.09e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 218 SSCLGSGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDR 294
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 295 LDEMdqqKAKLRDMLSDVRQKCQDETQMISSLKTQIQsQESDLKSQEDDLNRAKselTRLQQE 357
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLEALEEGKKRLQRELEALTQ-QLEEKAAAYDKLEKTK---NRLQQE 581
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
230-403 |
1.10e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKSNEVQ------ELQNDLDRETSSL-QELEAQKQ--DAQDRLDE 297
Cdd:COG1340 85 EKLNELREELDELRKELAELNKaggSIDKLRKEIERLEWRQQtevlspEEEKELVEKIKELeKELEKAKKalEKNEKLKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 298 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqesdLKSQEDDLNR----AKSELTRLQQEETQLEQSIQAGKVQLE 373
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRKeadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
170 180 190
....*....|....*....|....*....|..
gi 1239950982 374 TIIKSLKSTQDEINQARSKLSQ--LQESHQEA 403
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEI 272
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
231-366 |
1.11e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLeqdIREKEEAirqksnevqelqndldretsslqeleaqkqdAQDRLDEMDQQKAKLRDMLS 310
Cdd:COG0542 412 ELDELERRLEQLEIEKEAL---KKEQDEA-------------------------------SFERLAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 311 DVRQKCQDETQMISslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQ 366
Cdd:COG0542 458 ALKARWEAEKELIE----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
229-384 |
1.19e-04 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 45.38 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 301
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 KAKLRDMLSDVRQKCQdetQMISSLKTQIQSQESDLK----SQEDDLNRAKSELTRLQQEETQLEQS-IQAGKVQLETII 376
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
....*....
gi 1239950982 377 -KSLKSTQD 384
Cdd:pfam03999 298 dKLFYSTEQ 306
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
246-403 |
1.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 246 KYSLEQDIREKEEAIRQKsneVQELQNDLDrETSSLQELEAQkqdaqdrlDEMDQQKaklRDMLSDVRQKcqdetqmiss 325
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLR---NEFEKELRER---------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 326 lKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLqeSHQEA 403
Cdd:PRK12704 81 -RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEA 155
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
243-427 |
1.29e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 243 QREKYSLEQDIREKEEAIRQksnevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 320
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 321 -QMISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELTRLQQEETQLEQSIQA--GKVQLETI 375
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 376 IK-------SLKSTQD-------------EINQARSKLSQLQESHQeahrTLEQYD-EALDGAHGASLTNLAD 427
Cdd:PRK11281 342 LYqqqqalpSADLIEGladriadlrleqfEINQQRDALFQPDAYID----KLEAGHkSEVTDEVRDALLQLLD 410
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
236-408 |
1.35e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 236 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQK 315
Cdd:pfam10174 543 AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQ 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 316 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEetqleqsiqagkVQLETIIKSLKSTQDEINQARSKLSQ 395
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ------------LQLEELMGALEKTRQELDATKARLSS 680
|
170
....*....|...
gi 1239950982 396 LQESHQEAHRTLE 408
Cdd:pfam10174 681 TQQSLAEKDGHLT 693
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
266-460 |
1.37e-04 |
|
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: 44.67 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 266 EVQELQNDLDRETSSlQELEAQKQDAQDRLDEMdQQKAKlrdmlsDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN 345
Cdd:cd22656 95 EILELIDDLADATDD-EELEEAKKTIKALLDDL-LKEAK------KYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 346 RA--KSELTRLQQEETQLEQSIQAgkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH---GA 420
Cdd:cd22656 167 DLltDEGGAIARKEIKDLQKELEK---LNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLaliGP 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239950982 421 SLTNLADLsegvslaeRGGFGAMDDPFKNKALLFSNNAQE 460
Cdd:cd22656 244 AIPALEKL--------QGAWQAIATDLDSLKDLLEDDISK 275
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
323-415 |
1.38e-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: 44.72 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 323 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKS-LKSTQDEINQARSKLSQLQESHQ 401
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQaLQTAQNNLATAQAALANAEARLA 335
|
90
....*....|....
gi 1239950982 402 EAHRTLEQYDEALD 415
Cdd:TIGR04320 336 KAKEALANLNADLA 349
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
231-414 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEE---------------------AIRQKSNEVQELQNDLDRETSSL-------- 281
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEelqaalarleeetaqknnalkKIRELEAQISELQEDLESERAARnkaekqrr 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 282 ---QELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSEL 351
Cdd:pfam01576 296 dlgEELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKANL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 352 trlqqEETQleQSIQAGKVQLETIIKSLKSTQDEINQARSKL-SQLQE---SHQEAHRTLEQYDEAL 414
Cdd:pfam01576 376 -----EKAK--QALESENAELQAELRTLQQAKQDSEHKRKKLeGQLQElqaRLSESERQRAELAEKL 435
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
232-409 |
1.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 298
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 299 DQQKAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ---SI 365
Cdd:PRK04863 389 EEEVDELKSQLADYQQaldvqqtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsVA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 366 QAGKVQLETIIKSLKSTQDEI------NQARSKLSQLQESHQEA---------HRTLEQ 409
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAeqlqqlrmrLSELEQ 527
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
256-403 |
1.45e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 256 KEEAIRQKSNEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqmisslk 327
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 328 tqiQSQESDLKSQEDDLNRAKSELTRLQQEETQ-LEQSIQAGKVQLETIIksLKSTQDEINQARSKLsqLQESHQEA 403
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLERISGLTSEEAKEIL--LDEVEEELRHEAAVM--IKEIEEEA 178
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
230-367 |
1.51e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLqREKysLEQDIREKEEAIRQKSN---EVQELQNDLDRETSSLQELEAQKQDAQDRLD-------EMD 299
Cdd:pfam13851 47 KLMSEIQQENKRL-TEP--LQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELKDLKWEHEVLEQrfekverERD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 300 QQKAKLRDMLSDVRQKCQDETQMissLKTQIQSQESDLKSQEDDLN----RAKSELTRLQQEETQLEQSIQA 367
Cdd:pfam13851 124 ELYDKFEAAIQDVQQKTGLKNLL---LEKKLQALGETLEKKEAQLNevlaAANLDPDALQAVTEKLEDVLES 192
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
227-414 |
1.51e-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: 45.42 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 227 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKS-------NEVQELQNDLDRETSSLQELEAQKQDAQDR- 294
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKEtsnkkaqDKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI--QSQESDLKSQEDDLNRAKSEL-----TR 353
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMgqmqvLQ 1051
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 354 LQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEahrtlEQYDEAL 414
Cdd:TIGR00606 1052 MKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAE-----EKYREMM 1107
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
234-361 |
1.90e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 234 DISQEIAQLQREKYSLE---------QDIREKEEAIrqksnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 304
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI-------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239950982 305 LRDMLSDvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA-------KSELTRLQQEETQL 361
Cdd:PHA02562 339 LLELKNK-----------ISTNKQSLITLVDKAKKVKAAIEELqaefvdnAEELAKLQDELDKI 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
230-350 |
2.06e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKSNEVQELQNDLD-----------RETSSLQELEAQKQ-- 289
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 290 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDL------KSQEddLNRAKSE 350
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
242-409 |
2.18e-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: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 242 LQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ-KCQDET 320
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 321 QMiSSLKTQIqsqESDLKSQEDD-------LNRAKSEL-TRLQQEETQLEQSIqAGKVQLETIIKSLKSTQDEINQARS- 391
Cdd:pfam01576 721 NM-QALKAQF---ERDLQARDEQgeekrrqLVKQVRELeAELEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGREe 795
|
170 180
....*....|....*....|.
gi 1239950982 392 ---KLSQLQESHQEAHRTLEQ 409
Cdd:pfam01576 796 avkQLKKLQAQMKDLQRELEE 816
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-415 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 256 KEEAIRQkSNEVQELQND---LDRETS-SLQELEAQKQDAQDRLDEMDQQKAKLRDMLSdvRQKCQDETQMISSLKTQIQ 331
Cdd:TIGR01612 1103 KEENIKY-ADEINKIKDDiknLDQKIDhHIKALEEIKKKSENYIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIENIV 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 332 SQESDLKSQEDDLNRAKSELTRLQQEETQLEQ--------SIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 403
Cdd:TIGR01612 1180 TKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEvkginlsyGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKS 1259
|
170
....*....|..
gi 1239950982 404 HRTLEQYDEALD 415
Cdd:TIGR01612 1260 PEIENEMGIEMD 1271
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-430 |
2.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 268 QELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLSDVRQkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA 347
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 348 KSELTRLQQEETQLEQS---IQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTn 424
Cdd:PRK03918 237 KEEIEELEKELESLEGSkrkLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR- 315
|
....*.
gi 1239950982 425 LADLSE 430
Cdd:PRK03918 316 LSRLEE 321
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
325-408 |
2.32e-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: 42.30 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 325 SLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQL--QESHQE 402
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIktQFAHEV 135
|
....*.
gi 1239950982 403 AHRTLE 408
Cdd:pfam11559 136 KKRDRE 141
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
267-410 |
2.53e-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: 43.19 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 267 VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdETQMISSL---KTQ----IQSQESDLKS 339
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKH----ENDNLSSMlnrKERrlkdLEDQLSELKN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 340 QEDDLNRAKSELT----RLQQEETQLEQSIQAGKVQLETIIKSLK----STQDEINQARSKLSQLQeshQEAHRTLEQY 410
Cdd:pfam17078 81 SYEELTESNKQLKkrleNSSASETTLEAELERLQIQYDALVDSQNeykdHYQQEINTLQESLEDLK---LENEKQLENY 156
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
249-419 |
2.53e-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: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELqnDLDRetsSLQELEAQKQDAQDRLDEMDQQKAKLRDMLsdvrqkcQDETQMISSLKT 328
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGS--DLDR---TVQQVNQEKQEKQHELDTVVSKIELNRKLI-------QDQQEQIQHLKS 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 329 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLE 408
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
170
....*....|.
gi 1239950982 409 QYDEALDGAHG 419
Cdd:TIGR00606 945 DIKEKVKNIHG 955
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
240-402 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 240 AQLQREKYSLEQDIREKEEAirqkSNEVQELQNDLDRETSSLQE--------------LEAQKQDAQDRLDEMDQQKAKL 305
Cdd:pfam01576 412 GQLQELQARLSESERQRAEL----AEKLSKLQSELESVSSLLNEaegkniklskdvssLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 306 RdmlSDVRQKCQDETQMISSLKTQIQSQESdLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 385
Cdd:pfam01576 488 S---TRLRQLEDERNSLQEQLEEEEEAKRN-VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
170
....*....|....*..
gi 1239950982 386 INQARSKLSQLQESHQE 402
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQ 580
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-408 |
2.56e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQrekyslEQDIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 311
Cdd:PRK02224 189 LDQLKAQIEEKE------EKDLHERLNGLESELAELDE---EIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 312 VRQKCQDETQMIS---SLKTQIQSQESDLKSQEDDLN--RAKSELTRLQQEETQLeqsiqagkvQLETIIKSLKSTQDEI 386
Cdd:PRK02224 260 IEDLRETIAETERereELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEA---------RREELEDRDEELRDRL 330
|
170 180
....*....|....*....|....*
gi 1239950982 387 NQARSKLSQLQ---ESHQEAHRTLE 408
Cdd:PRK02224 331 EECRVAAQAHNeeaESLREDADDLE 355
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
243-420 |
2.65e-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: 44.25 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 243 QREKYSLEQDIREKEEAIRQKSNEV---QELQNDLDRETSSLQELEAQ-------------KQDAQDRLDEMDQQK--AK 304
Cdd:pfam05701 218 EQDKLNWEKELKQAEEELQRLNQQLlsaKDLKSKLETASALLLDLKAElaaymesklkeeaDGEGNEKKTSTSIQAalAS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDMLSDVR---QKCQDETQMISSLKTQIQSqesdlksqedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS 381
Cdd:pfam05701 298 AKKELEEVKaniEKAKDEVNCLRVAAASLRS----------ELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIAL 367
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239950982 382 TQDEINQARSKLS----QLQESHQEAhrtleqyDEALDGAHGA 420
Cdd:pfam05701 368 VQAKEKEAREKMVelpkQLQQAAQEA-------EEAKSLAQAA 403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-335 |
2.77e-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: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREkysleqdIREKEEAIRQKSNEVQELQNDLDR----ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 312
Cdd:COG4913 338 DRLEQLERE-------IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100
....*....|....*....|...
gi 1239950982 313 RQKCQDETQMISSLKTQIQSQES 335
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLER 433
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
253-413 |
2.84e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 253 IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRldemdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQS 332
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR----------KQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 333 QESDLKSQEDDLNRAKSELTRLQQEETQLEQSI---QAGKV------QLETIIKSLKSTQDEINQARSKLSQLQESHQEA 403
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyEKGGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170
....*....|
gi 1239950982 404 HRTLEQYDEA 413
Cdd:PHA02562 326 EEIMDEFNEQ 335
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
236-407 |
3.10e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 236 SQEIAQLQRekysLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 312
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 313 ---RQKCQDETQMISSLKTQIQSQESDLKSQE-------DDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST 382
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQETRK 488
|
170 180 190
....*....|....*....|....*....|.
gi 1239950982 383 QDEINQARSKLSQL------QESHQEAHRTL 407
Cdd:TIGR00618 489 KAVVLARLLELQEEpcplcgSCIHPNPARQD 519
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
249-357 |
3.15e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLkt 328
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 1239950982 329 qiqsqESDLKSQEDDLNRAKSELTRLQQE 357
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
228-396 |
3.22e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 228 GVKELD-DISQEIAQLQREKYSLEQDIRE----KEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 302
Cdd:pfam05483 64 GLKDSDfENSEGLSRLYSKLYKEAEKIKKwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQ--DETQMISSLKT---QIQSQES-----DLKSQEDDLNRAKSELtRLQQEETQLEQSIQAgKVQL 372
Cdd:pfam05483 144 KDLIKENNATRHLCNllKETCARSAEKTkkyEYEREETrqvymDLNNNIEKMILAFEEL-RVQAENARLEMHFKL-KEDH 221
|
170 180
....*....|....*....|....
gi 1239950982 373 ETIIKSLKSTQDEINQARSKLSQL 396
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLL 245
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
231-399 |
3.50e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqksnEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEmdqqkAKl 305
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKE-----AK- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 306 rdmlsdvrqkcQDETQMISSLKTQIQSQESDLKSQE-----DDLNRAKSELTRLQQEETQLEQSIQAG-KVQLET----- 374
Cdd:PRK00409 584 -----------KEADEIIKELRQLQKGGYASVKAHEliearKRLNKANEKKEKKKKKQKEKQEELKVGdEVKYLSlgqkg 652
|
170 180 190
....*....|....*....|....*....|
gi 1239950982 375 IIKSLKSTQDEINQA-----RSKLSQLQES 399
Cdd:PRK00409 653 EVLSIPDDKEAIVQAgimkmKVPLSDLEKI 682
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
324-430 |
3.70e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.56 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 324 SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESH-QE 402
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNlAT 322
|
90 100
....*....|....*....|....*....
gi 1239950982 403 AHRTLEQYDEALDGAhGASLTNL-ADLSE 430
Cdd:TIGR04320 323 AQAALANAEARLAKA-KEALANLnADLAK 350
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
271-430 |
3.88e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 271 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD-------------ETqmISSLKTQIQSQESDL 337
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrksllanrfsfgPA--LDELEKQLENLEEEF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 338 kSQEDDLN------RAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST-QDEINQARSKLSQLQES-----HQEAHR 405
Cdd:PRK04778 182 -SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAGYRELVEEgyhldHLDIEK 256
|
170 180
....*....|....*....|....*
gi 1239950982 406 TLEQYDEALDgahgaslTNLADLSE 430
Cdd:PRK04778 257 EIQDLKEQID-------ENLALLEE 274
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
233-363 |
4.08e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQdirEKEEAIRQKSN---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 309
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 310 sdvrqkCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL-TRLQQEETQLEQ 363
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
230-398 |
4.32e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldreTSSLQELEAQKQDAQDR-------LDEMDQQK 302
Cdd:PRK10929 72 QVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQV-----SSQLLEKSRQAQQEQDRareisdsLSQLPQQQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQ----DETQMISSLKTQIQSQESDLKSQEDDLNRA------KSELTRLQQE-----ETQLEQSIQA 367
Cdd:PRK10929 147 TEARRQLNEIERRLQtlgtPNTPLAQAQLTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQA 226
|
170 180 190
....*....|....*....|....*....|.
gi 1239950982 368 GKVQLETiikslkSTQDEINQARSKLSQLQE 398
Cdd:PRK10929 227 LRNQLNS------QRQREAERALESTELLAE 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
233-364 |
4.58e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 307
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 308 MLSDVRQKCqdetqmiSSLKTQIQSQESDLKSQEddlNRAKSELTRLQQEETQLEQS 364
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA 1114
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
321-408 |
4.60e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 321 QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ----SIQAGKVQLETIIKSLKSTQDEINQARSKLSQL 396
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90
....*....|..
gi 1239950982 397 QESHQEAHRTLE 408
Cdd:PRK00409 600 GYASVKAHELIE 611
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
302-435 |
4.64e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 43.69 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQL--------- 372
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrq 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 373 -----ETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALdGAHGASLTNLADLSEGVSLA 435
Cdd:COG5283 82 lsaaqRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLA-GAGAAAAAIGAALAASVKPA 148
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
232-398 |
4.89e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKysleQDIREKEEAIRQKSNEV----QELQNDL--DRET--SSLQELEAQKQDAQDRLDEMDQ--- 300
Cdd:PRK04778 114 LDLIEEDIEQILEEL----QELLESEEKNREEVEQLkdlyRELRKSLlaNRFSfgPALDELEKQLENLEEEFSQFVElte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 301 ----QKA-----KLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlqqEETQLEQSIQAGKVQ 371
Cdd:PRK04778 190 sgdyVEAreildQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHL-----DHLDIEKEIQDLKEQ 264
|
170 180
....*....|....*....|....*..
gi 1239950982 372 LETIIKSLKSTqdEINQARSKLSQLQE 398
Cdd:PRK04778 265 IDENLALLEEL--DLDEAEEKNEEIQE 289
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
231-436 |
5.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE---LEAQKQDAQDRLDEMDQQKAKL-- 305
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSMELEKNNYYke 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 306 --------------------RDMLSDVRQkCQDETQMISSLKTQIQSQE------SDL----------KSQEDDLNRAKS 349
Cdd:PRK01156 278 leerhmkiindpvyknrnyiNDYFKYKND-IENKKQILSNIDAEINKYHaiikklSVLqkdyndyikkKSRYDDLNNQIL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 350 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQ----ARSKLSQLQESHQEAHRTLEQYD---EALDGAHGASL 422
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEilkiQEIDPDAIKKELNEINVKLQDISskvSSLNQRIRALR 436
|
250
....*....|....
gi 1239950982 423 TNLADLSEGVSLAE 436
Cdd:PRK01156 437 ENLDELSRNMEMLN 450
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
230-363 |
5.08e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 298
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 299 ---DQQKAKLRD-MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ 363
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQ 278
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
240-373 |
5.35e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 40.26 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 240 AQLQREKysleQDIREKEEAIRQ---KSNEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDvRQKC 316
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEE-KEIE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 317 QDETQMisslktqiqsQESDLKSQeddLNRAKSELTRLQQeetQLEQSIQAGKVQLE 373
Cdd:pfam18595 73 LRELER----------REERLQRQ---LENAQEKLERLRE---QAEEKREAAQARLE 113
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
229-416 |
5.43e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD---AQDRLD--EMDQQKA 303
Cdd:COG1340 49 NAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIErlEWRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 304 KL-----RDMLSDVRQKCQ--DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 376
Cdd:COG1340 129 VLspeeeKELVEKIKELEKelEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDG 416
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
258-399 |
5.48e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 258 EAIRQKSNEVQELQNDLDretSSLQELEAQKQDAQDRLD----EMDQQKAKLRDMLSDVrqkcQDETQMISSLKTQI--- 330
Cdd:PRK01156 583 ETNRSRSNEIKKQLNDLE---SRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEI----QENKILIEKLRGKIdny 655
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 331 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV---QLETIIKSLKSTQDEINQARSKLSQLQES 399
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAnraRLESTIEILRTRINELSDRINDINETLES 727
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-409 |
5.58e-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: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-----------DLDRETSSLQELEAQKQ--------- 289
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 290 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE---DDLNRAKSELTRLQQEETQLEQ 363
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239950982 364 SIQAGKVQLEtiIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:TIGR00606 493 NSLTETLKKE--VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
230-409 |
5.64e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKsNEVQELQNDL-DRETSSLQELEAQKQDAQDRL---------DEMD 299
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERK-RYRQELEEQIeEREQKRQEEYEEKLQEREQMDeiveriqeeDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 300 -QQKAKLRDMLSDVRQKCQDETQMISSLKtQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE--QSIQAgkvQLETII 376
Cdd:pfam13868 118 aEEKLEKQRQLREEIDEFNEEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIA---RLRAQQ 193
|
170 180 190
....*....|....*....|....*....|...
gi 1239950982 377 KSLKSTQDEINQARSKLsqLQESHQEAHRTLEQ 409
Cdd:pfam13868 194 EKAQDEKAERDELRAKL--YQEEQERKERQKER 224
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
342-414 |
6.05e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 42.51 E-value: 6.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239950982 342 DDLNRaksELTRLQQEETQLEQSI-QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:pfam09755 110 NDLSR---KLTQLRQEKVELEQTLeQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEAL 180
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
234-415 |
6.32e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 234 DISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 308
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQ-------------KCQDETQMISSLK---TQIQSQESDLKSQEDDL-----NRAK---SELTRLQQEETQLEQS 364
Cdd:PRK04863 910 KRFVQQhgnalaqlepivsVLQSDPEQFEQLKqdyQQAQQTQRDAKQQAFALtevvqRRAHfsyEDAAEMLAKNSDLNEK 989
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 365 IQAGKVQLE----TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:PRK04863 990 LRQRLEQAEqertRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQ 1044
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
232-402 |
6.33e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 304
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LrDMLSDvRQKCQ----DETQMISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELTRLQQEETQLeQSIQ 366
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239950982 367 AGKVQLETIIKSLKSTQDEINQARS-KLSQLQESHQE 402
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvALDNWRQVHEQ 725
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
235-407 |
6.62e-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: 42.76 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 235 ISQEIAQLQREKYSLEQDIrekEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 311
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVL---NELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 312 --VRQKCQdetQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ-------------QEETQLEQSI----------- 365
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMasllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 366 ----QAGKV-----------------QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 407
Cdd:pfam04108 192 dqcvTAVKLteggraemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
235-340 |
7.06e-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: 42.66 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 235 ISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 310
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 1239950982 311 DVRQKCQDETQMISSLKTQIQSQESDLKSQ 340
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
231-332 |
7.72e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQ-----------KSNEVQELQ---NDLDRETSSLQELEAQKQDAQDRLD 296
Cdd:pfam07926 9 EIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqnyerelvlHAEDIKALQalrEELNELKAEIAELKAEAESAKAELE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1239950982 297 EM----DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 332
Cdd:pfam07926 89 ESeeswEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
230-295 |
8.01e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 8.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslQELEAQKQDAQDRL 295
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
230-367 |
8.12e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIR----------QKSNEvqelqnDLDRET-SSLQELEAQKQDAQDRLDEM 298
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlalEKGRE------DLAREAlERKAELEAQAEALEAQLAQL 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 299 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE----DDLNRAKSELTRLQQEETQLEQSIQA 367
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
286-438 |
8.51e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 286 AQKQDAQDRLDEMdQQKAKL---RDMLSDVR---QKCQDETQ-MISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQE- 357
Cdd:PRK02224 146 ATPSDRQDMIDDL-LQLGKLeeyRERASDARlgvERVLSDQRgSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEi 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 358 ---ETQLEQSIQAgKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSL 434
Cdd:PRK02224 223 eryEEQREQARET-RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE 301
|
....
gi 1239950982 435 AERG 438
Cdd:PRK02224 302 AGLD 305
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
231-430 |
9.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ------NDLDRET--SSLQELEAQKQDAQD--------- 293
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlNLLADETlaDRVEEIREQLDEAEEakrfvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 294 -RLDEMDQQKAKLRdmlsdvrqkcQDETQmISSLK---TQIQSQESDLKSQEDDL-----NRAK---SELTRLQQEETQL 361
Cdd:PRK04863 918 nALAQLEPIVSVLQ----------SDPEQ-FEQLKqdyQQAQQTQRDAKQQAFALtevvqRRAHfsyEDAAEMLAKNSDL 986
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 362 EQSIQAGKVQLEtiikslkstqdeinQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 430
Cdd:PRK04863 987 NEKLRQRLEQAE--------------QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
230-438 |
9.49e-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: 42.85 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-------QDAQDRLDEMD--- 299
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAlslaralEEALEAKEELErtn 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 300 -QQKAKLRDMLS---DV--------RQKCQDETQMiSSLKTQIQSQESDLKSQEDdlnrAKseltrlqqeeTQLEQSIQA 367
Cdd:pfam01576 660 kQLRAEMEDLVSskdDVgknvheleRSKRALEQQV-EEMKTQLEELEDELQATED----AK----------LRLEVNMQA 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 368 GKVQLETIIkslkSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASL-TNLADLSEGVSLAERG 438
Cdd:pfam01576 725 LKAQFERDL----QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLeLDLKELEAQIDAANKG 792
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
282-409 |
9.49e-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: 39.47 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 282 QELEAQKQDAQDRLDEMDQQKAKLRDMlsdvRQKCQDETQMIsslktqiqsqESDLKSQEDDLNRAKseltRLQQEETQL 361
Cdd:pfam13863 13 LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKF----------DKFLKENDAKRRRAL----KKAEEETKL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1239950982 362 eqsiqagKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:pfam13863 75 -------KKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
235-407 |
1.03e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 235 ISQEIAQLQREKYSLEQ------DIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQ---------DRLDEMD 299
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQlegssdRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADldrklrkldQEMEQLN 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 300 QQKAKLRDMLSDVRQKcQDETQMISSLKTQIQSQ--------------ESDLKSQEDDLNRAKSELTRLQQEETQLEQSI 365
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDK-MDKDEQIRKIKSRHSDEltsllgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239950982 366 QAGKVQLETIIKSLKSTQDEINQA------RSKLSQLQESHQEAHRTL 407
Cdd:TIGR00606 608 NHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEKSSKQR 655
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
247-389 |
1.04e-03 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 40.59 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 247 YSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQqkakLRDMLSD--VRQKCQDETQMI 323
Cdd:pfam16789 3 YPLEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVrKHKKAKMQQ----LRDEMDRgtTSDKILQMKRYI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239950982 324 SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--------TQDEINQA 389
Cdd:pfam16789 79 KVVKERLKQEEKKVQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKeeedqeerEQDEIGSA 152
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
308-410 |
1.05e-03 |
|
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: 42.12 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 308 MLSDVRQKCQDET-QMISSLKTQIQSQESDLKSQEDDL------NRAKSELTRLQQEEtqleQSIQAgkvQLETIIKSLK 380
Cdd:pfam05816 33 MLDNVRTKDLGEVgDLLNELRRTLKDFDPDELGEEKKLgflplfKKAGNKIEKYFAKY----QTAGA---QIDKIVVELE 105
|
90 100 110
....*....|....*....|....*....|
gi 1239950982 381 STQDEINQARSKLSQLQESHQEAHRTLEQY 410
Cdd:pfam05816 106 KGQDELLKDNAMLDQMYEKNLEYFKELEKY 135
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
302-413 |
1.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 302 KAKLRDMLSDVRQKCQDETQMISSLK----TQIQSQESDLKSQ-EDDLNRAKSELT----RLQQEETQLE---QSIQAGK 369
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKkealLEAKEEIHKLRNEfEKELRERRNELQklekRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1239950982 370 VQLETIIKSLKSTQDEINQARSKLSQLQESHQEAhrtLEQY-----DEA 413
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERIsgltaEEA 155
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
233-405 |
1.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREK-EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDaqdrldEMDQQKAKLRDMLSd 311
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEYLALLDRLEED------GLPEYEERFKELLN- 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 312 vrqkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAkseLTRLQ-QEETQLEqsIQAGKVQLETIikslKSTQDEINQAR 390
Cdd:COG4913 842 -----ENSIEFVADLLSKLRRAIREIKERIDPLNDS---LKRIPfGPGRYLR--LEARPRPDPEV----REFRQELRAVT 907
|
170
....*....|....*
gi 1239950982 391 SKLSQLQESHQEAHR 405
Cdd:COG4913 908 SGASLFDEELSEARF 922
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
253-366 |
1.10e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.56 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 253 IREK-EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQMISSLKTQIQ 331
Cdd:smart00502 1 QREAlEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKE 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1239950982 332 SQESDLKSQeddlnrakseLTRLQQEETQLEQSIQ 366
Cdd:smart00502 72 NKLKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
234-437 |
1.23e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 234 DISQEIAQLQREKYSLEQ------DIREK-----------EEAIRQKSNEVQELQN---DLDRETSSLQELEAQKQDAQD 293
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQykekacEIRDQitskeaqlessREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 294 RLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLK-TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQL 372
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 373 ETIIKSLKSTQDEI--NQARSKLSQLQE---SHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:TIGR00606 357 DRHQEHIRARDSLIqsLATRLELDGFERgpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
231-414 |
1.25e-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: 41.55 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREkysleqdIREKEEAIRQKSNEVQELQNDlDRETSSLQELEAQKQ-------DA-QDRLDEMDQQK 302
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETE-SSCSTPLRRNESFSSlhgcvqlDAlQEKLRGLEEEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 AKLRDMLSDVRQKCQD----ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL-------EQSIQAGKVQ 371
Cdd:pfam04849 181 LKLRSEASHLKTETDTyeekEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLlaqivdlQHKCKELGIE 260
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239950982 372 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:pfam04849 261 NEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEEL 303
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
230-414 |
1.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSleqdIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRLDEMD---QQKAKLR 306
Cdd:PRK04863 279 NERRVHLEEALELRRELYT----SRRQLAAEQYRLVEMAR---ELAELNEAESDLEQDYQAASDHLNLVQtalRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCQ--DETQMISSLKTQIQSQ-ESDLKSQEDDLNRAKSELTRLQQ----EET---QLEQSIQA-GKVQ---- 371
Cdd:PRK04863 352 RYQADLEELEErlEEQNEVVEEADEQQEEnEARAEAAEEEVDELKSQLADYQQaldvQQTraiQYQQAVQAlERAKqlcg 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 372 --------LETIIKSLKSTQDEINQARSKLSQLQESHQEAHrtlEQYDEAL 414
Cdd:PRK04863 432 lpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH---SQFEQAY 479
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
292-437 |
1.46e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 292 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKtqiqsqesdlksqeDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 371
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 372 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG---ASLTNLADLSE--GVSLAER 437
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKrdrESQAKIADLGRrlNVALAQR 188
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
280-409 |
1.51e-03 |
|
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: 41.13 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 280 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQMISSLKTQIQS--QESDLKSQEDDL 344
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 345 NRAKSEL-TRLQQEETQLeQSIQAgkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQN---QLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNG 138
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
262-413 |
1.52e-03 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 41.80 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 262 QKSNEVQELQNDLDRETSSLQELEAQKQD-AQDRLDEMDQQK---------------AKLRD-MLSDVRQKCQDET-QMI 323
Cdd:COG3853 25 PEVPEQAAGMVDPEEAEVDLSKLSAEADAfVEALAAQIDLSDvnailqygakaqrklAAFSNrMLDRVKTKDLGEVgDSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 324 SSLKTQIQsqESDLKSQEDD---------LNRAKSELTRLQQEEtqleQSIQAgkvQLETIIKSLKSTQDEINQARSKLS 394
Cdd:COG3853 105 SELRRTLE--DLDPSELDDLkkkgllgklFPKGGNKLEKYFAKY----QSAQT---QIDKISVALEKGQDELLKDNAMLD 175
|
170
....*....|....*....
gi 1239950982 395 QLQESHQEAHRTLEQYDEA 413
Cdd:COG3853 176 QLYEKNWEYFKELNQYIAA 194
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
230-413 |
1.55e-03 |
|
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: 41.24 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLR 306
Cdd:pfam06008 75 AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQNAEAELKAAQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVR---QKCQDETQmisSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvQLETIIKSLKSTQ 383
Cdd:pfam06008 155 DLLSRIQtwfQSPQEENK---ALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA---NLREFQRKKEEVS 228
|
170 180 190
....*....|....*....|....*....|
gi 1239950982 384 DEINQARSKLSQLQESHQEAHRTLEQYDEA 413
Cdd:pfam06008 229 EQKNQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
249-451 |
1.58e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQMISSLKT 328
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 329 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--TQDEINQARSKLSQlqeshQEAHRT 406
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLST-----SSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 407 LEQYD------EALDGAHgASLTNLADLSEGVSLAERGGFGAMDDPFKNKA 451
Cdd:pfam04012 166 FERIEekieerEARADAA-AELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
270-415 |
1.63e-03 |
|
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: 40.68 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 270 LQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKS 349
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRAL-------KAELESLEVYNRQLERLVASQEQEIASLER 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 350 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARskLSQLQESHQEAHRTL-EQYD---EALD 415
Cdd:pfam11932 84 QIEEIERTERELVPLMLKMLDRLEQFVALDLPFLLEERQAR--LARLRELMDDADVSLaEKYRrilEAYQ 151
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
232-430 |
1.72e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 303
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 304 KLRDMLSDVRQKCQDETQ----MISSLKTQIQSQES---DLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI- 375
Cdd:COG0497 223 KLREALQEALEALSGGEGgaldLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVe 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 376 -----IKSLK----STQDEI----NQARSKLSQLQESHQEahrtLEQYDEALDGAHgASLTNLAD-LSE 430
Cdd:COG0497 303 erlalLRRLArkygVTVEELlayaEELRAELAELENSDER----LEELEAELAEAE-AELLEAAEkLSA 366
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
229-318 |
1.83e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 38.90 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 229 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSN---------EVQELQNDLDREtSSLQELEAQKQDAQDRLDEMD 299
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKlpddtpiykIVGNLLVKVDKT-KVEKELKERKELLELRSRTLE 91
|
90
....*....|....*....
gi 1239950982 300 QQKAKLRDMLSDVRQKCQD 318
Cdd:PRK09343 92 KQEKKLREKLKELQAKINE 110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
239-412 |
1.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 239 IAQLQREKYSLEQDIrEKEEAI----RQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK---AKLRDMLSD 311
Cdd:PRK03918 171 IKEIKRRIERLEKFI-KRTENIeeliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKeeiEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 312 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS---------ELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 382
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190
....*....|....*....|....*....|
gi 1239950982 383 QDEINQARSKLSQLQESHQEAHRTLEQYDE 412
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEE 359
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
231-418 |
1.92e-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: 41.70 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKSNEVQELQNDLDRETSSLQ------- 282
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 283 ELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDVRQKcqdetqmISSLKTQIQsQESDLKSQEDDLNRA-----KSELTRLQQ 356
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFKSSIAALEAK-------IAQLEEQLE-QESRERQAANKLVRRtekklKEVLLQVED 1013
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 357 EETQLEQSiqagKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 418
Cdd:pfam01576 1014 ERRHADQY----KDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
242-395 |
1.95e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.63 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 242 LQREKYSLEQDIREkeeaiRQKSNEVQelqndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetq 321
Cdd:PRK06975 344 LNRKVDRLDQELVQ-----RQQANDAQ------------TAELRVKTEQAQASVHQLDSQFAQLDGKLADAQSAQQ---- 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 322 misslktQIQSQESDLKSQEDDLNRAKSE-LTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQD-EINQARSKLSQ 395
Cdd:PRK06975 403 -------ALEQQYQDLSRNRDDWMIAEVEqMLSSASQQLQLTGNVQLALIALQNADARLATSDSpQAVAVRKAIAQ 471
|
|
| Flagellar_rod |
pfam05149 |
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod ... |
243-358 |
1.97e-03 |
|
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: 40.81 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 243 QREKYSLEQdiREKEEAIRQKSNEVQELQNDLDRETSSLQEL-EAQKQDAQDRLDEM-----------------DQQKAK 304
Cdd:pfam05149 38 QRKRFKTQR--RESDKFLQQNVEQQQKLWREIEELERELQKLaEERREEVEDRIEAVereaqrrtdhesflnfaDQHKQR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1239950982 305 LRDMLSDVrQKCQDETQMISSLktqIQSQESDLKSQEDDLNRAKSELTRLQQEE 358
Cdd:pfam05149 116 LRRTLENC-DGALDCARSLEEY---VQEGCDHLPAKQDKLRNALNELLDAVRKE 165
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
234-403 |
1.99e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.21 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 234 DISQEIAQLQREKY-SLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAklrdmlsdv 312
Cdd:pfam12718 10 ENAQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVE-------KLEEQLKEAKEKAEESEKLKT--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 313 rqkcQDEtqmisSLKTQIQSQESDLKSQEDDLnraKSELTRLQQEETQLEQSiqagkvqlETIIKSLkstQDEINQARSK 392
Cdd:pfam12718 74 ----NNE-----NLTRKIQLLEEELEESDKRL---KETTEKLRETDVKAEHL--------ERKVQAL---EQERDEWEKK 130
|
170
....*....|.
gi 1239950982 393 LSQLQESHQEA 403
Cdd:pfam12718 131 YEELEEKYKEA 141
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
230-398 |
2.00e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.22 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQRekySLEQDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:pfam04108 171 KELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQKLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 S---DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK-------SELTRLQQEETQLEQSIQAGKVQLETIIKSL 379
Cdd:pfam04108 245 EqknSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKetiedylSELEDLREFYEGFPSAYGSLLLEVERRREWA 324
|
170
....*....|....*....
gi 1239950982 380 KSTQDEINQARSKLSQLQE 398
Cdd:pfam04108 325 EKMKKILRKLAEELDRLQE 343
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
231-404 |
2.03e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 306
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 dmlsdvrqkcqDETQMISslKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQlETIIKSlKSTQD 384
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSAS-KEIEK 180
|
170 180
....*....|....*....|
gi 1239950982 385 EINQARSKLSQLQESHQEAH 404
Cdd:pfam05701 181 TVEELTIELIATKESLESAH 200
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
230-381 |
2.11e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 40.98 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKSNEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 302
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 303 aKLRDMLSDVR--QKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELTRLQQEETQLEQSIQagkvQLETIIKSLK 380
Cdd:COG5325 144 -FLRNKNNDQHplEEEEDEESLSSLGSQQTLQQQGLSNEELEY---QQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
.
gi 1239950982 381 S 381
Cdd:COG5325 216 S 216
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
232-398 |
2.13e-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: 40.82 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLRDML 309
Cdd:cd22656 123 LDDLLKEAKKYQ-------DKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLNEEY 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDEtqmissLKTQIQSQESDLKSQE---DDLNRAKSELTRLQQeetQLEQSIQA-GKVQ---------LETII 376
Cdd:cd22656 196 AAKLKAKIDE------LKALIADDEAKLAAALrliADLTAADTDLDNLLA---LIGPAIPAlEKLQgawqaiatdLDSLK 266
|
170 180
....*....|....*....|..
gi 1239950982 377 KSLKSTQDEINQARSKLSQLQE 398
Cdd:cd22656 267 DLLEDDISKIPAAILAKLELEK 288
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
230-419 |
2.16e-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: 41.70 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 306
Cdd:pfam01576 833 KKLKNLEAELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQsnt 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 DMLSDVRQKCqdeTQMISSLKTQIQSQESDLKSQED---DLNRAKSEL-TRLQQEETQ-----------LEQSIQAGKVQ 371
Cdd:pfam01576 906 ELLNDRLRKS---TLQVEQLTTELAAERSTSQKSESarqQLERQNKELkAKLQEMEGTvkskfkssiaaLEAKIAQLEEQ 982
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239950982 372 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG 419
Cdd:pfam01576 983 LEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNS 1030
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
240-307 |
2.22e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 39.26 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 240 AQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 307
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
231-393 |
2.29e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVRQkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSElTRLQQEETQLEQSIQA-GKV---------QLETIIKSLK 380
Cdd:COG1196 725 ALEE--QLEAEREELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEAlGPVnllaieeyeELEERYDFLS 801
|
170
....*....|...
gi 1239950982 381 STQDEINQARSKL 393
Cdd:COG1196 802 EQREDLEEARETL 814
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
238-361 |
2.35e-03 |
|
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: 39.35 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 238 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 309
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL 361
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-437 |
2.53e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 306
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQDEESDLERLKEEIEKSSKQRAMLAgat 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 307 -------DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQ----EDDLNRAKSELTRLQQeetqlEQSIQAGKVQLETI 375
Cdd:TIGR00606 663 avysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlaPDKLKSTESELKKKEK-----RRDEMLGLAPGRQS 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 376 IKSLKstQDEINQARSKLSQLQESHQEAHRTLEQyDEALDGAHGASLTNLADLSEGVSLAER 437
Cdd:TIGR00606 738 IIDLK--EKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMER 796
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
292-409 |
2.53e-03 |
|
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: 41.03 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 292 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQeddLNRAKSELTRLQQEETQLEQSiqagkvq 371
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR---VAELKEELRQSREKHEELEEK------- 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 1239950982 372 letiIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:pfam07888 103 ----YKELSASSEELSEEKDALLAQRAAHEARIRELEE 136
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
252-314 |
2.71e-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: 2.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 252 DIREKEEAIRQKSNEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 314
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
233-410 |
2.71e-03 |
|
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: 40.58 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKsneVQELQNDLdretssLQELEAQKQDAQDRldeMDQQKAK-LRDM 308
Cdd:pfam05816 109 DELLKDNAMLDQMYEKNLEYFKELEKYIaagELK---LEELDAEL------LPELEAKAAASGDP---EDAQALRdLRQA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 309 LSDVRQKCQD-ETQM-------------------------------ISSLKTQ------IQSQESDLKSQE------DDL 344
Cdd:pfam05816 177 LFRLEQRIHDlELQRavsiqtapqirlvqnnnqeliekiqsaitttIPLWKNQlvvalaLKRQKLALEAQKavndttNEL 256
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 345 NRAKSELTRLQQEETQlEQSiQAGKVQLETIIK---SLKSTQDEINQ----ARSKLSQLQESHQEAHRTLEQY 410
Cdd:pfam05816 257 LLKNAEMLKTQSIETA-KEA-ERGIVDIETLKKtnqTLIATIDETLQiqeeGREKRREAEAELEQLEEELKQK 327
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
232-363 |
2.74e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 38.70 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdretsslqeLEAQKqdaqdrldemdqqkaklrdMLSD 311
Cdd:pfam05103 27 LDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTL---------ILAQE-------------------TAEE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1239950982 312 VRQKCQDETQMISSlKTQIQSQESdLKSQEDDLNRAKSELTRLQQEETQLEQ 363
Cdd:pfam05103 79 VKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
230-415 |
2.97e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQrEKYSL----EQDIREKEEAIRQKSNEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEM 298
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAyselqeeLEEILEQLEEIEEEQEEF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 299 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqeSDL----KSQEDDLNRAKSELTRLQQeetQLEQS---IQAGKVQ 371
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEVplnMDEVNRL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239950982 372 LETIIKSL----KSTQDEINQA-------------RSKLSQLQESHQEAHRTLE--QYDEALD 415
Cdd:pfam06160 459 LDEAQDDVdtlyEKTEELIDNAtlaeqliqyanryRSSNPEVAEALTEAELLFRnyDYEKALE 521
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
232-414 |
3.03e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.17 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQrekyslEQDIREKEEAIRQKSNEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 311
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 312 VRQKCQDETQMI-SSLKTQIQSQESDLKSQEDDL-NRAKSELTRLQqeeTQLEQSIQAGKVQLETIIKSLKSTQDEinQA 389
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAP--YA 145
|
170 180
....*....|....*....|....*
gi 1239950982 390 RSKLSQLQESHQEAHRTLEQYDEAL 414
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDL 170
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
249-367 |
3.04e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKT 328
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 1239950982 329 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 367
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAA 155
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
222-436 |
3.30e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 222 GSGEFTGVKELDDisqeiaqLQREKYSLEQDIrekeEAIRQKSNEVQELQND---LDRETS----SLQELEAQKQDAQDR 294
Cdd:PLN02939 218 GLCVHSLSKELDV-------LKEENMLLKDDI----QFLKAELIEVAETEERvfkLEKERSlldaSLRELESKFIVAQED 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 LDEMDQQKAklrDMLSDVRQKCQDetqMISSLKTQIQsQESDLKSQEDDLnRAKSEltrlqqeetQLEQSIQAGKVQlet 374
Cdd:PLN02939 287 VSKLSPLQY---DCWWEKVENLQD---LLDRATNQVE-KAALVLDQNQDL-RDKVD---------KLEASLKEANVS--- 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239950982 375 iikSLKSTQDEINQARSKL--SQLQESHQEAHRTLEQYDEALDGAHGaSLTNLADLSEGVSLAE 436
Cdd:PLN02939 347 ---KFSSYKVELLQQKLKLleERLQASDHEIHSYIQLYQESIKEFQD-TLSKLKEESKKRSLEH 406
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
230-300 |
3.32e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 230 KELDDISQEIAQLQREKysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 300
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
249-431 |
3.54e-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: 40.98 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 249 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSdvrqkcqdetqmisslkt 328
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN------------------ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 329 qiqsqeSDLKSQEDDLNRAKSELTRLqqeETQLEQSIQAGkvqletiIKSLKSTQDEINQARSKLSQLQESHQ---EAHR 405
Cdd:pfam12128 308 ------GELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAADQEQLPSWQSELENLEERLKaltGKHQ 371
|
170 180
....*....|....*....|....*..
gi 1239950982 406 TLEQYDEALDGAHGASL-TNLADLSEG 431
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNnRDIAGIKDK 398
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
251-413 |
3.91e-03 |
|
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: 40.44 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 251 QDIREKEEAIRQKSNE-------VQELQNDLDRETSSLQELEAQKQDAQD-------RLDEMDQQKAKLRDML------- 309
Cdd:pfam05622 3 SEAQEEKDELAQRCHEldqqvslLQEEKNSLQQENKKLQERLDQLESGDDsgtpggkKYLLLQKQLEQLQEENfrletar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDetqmissLKTQIQsqesDLKSQEDDLNRAKSELTRLQQEETQLEQSiqAGKV-QLETIIKSLKSTQDEINQ 388
Cdd:pfam05622 83 DDYRIKCEE-------LEKEVL----ELQHRNEELTSLAEEAQALKDEMDILRES--SDKVkKLEATVETYKKKLEDLGD 149
|
170 180
....*....|....*....|....*.
gi 1239950982 389 ARSKLSQLQESHQE-AHRTLEQYDEA 413
Cdd:pfam05622 150 LRRQVKLLEERNAEyMQRTLQLEEEL 175
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
222-388 |
4.10e-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: 40.43 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 222 GSGEFTGVKELDDISQE-------IAQLQREKYSLEQDIREKEEAIRQKSNEV------QELQNDLDRETSSLQELEAQK 288
Cdd:pfam13166 299 ISSLLAQLPAVSDLASLlsafeldVEDIESEAEVLNSQLDGLRRALEAKRKDPfksielDSVDAKIESINDLVASINELI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 289 QDAQDRLDEMDQQKAKLRDMLsdvrqkcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQag 368
Cdd:pfam13166 379 AKHNEITDNFEEEKNKAKKKL---------RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIK-- 447
|
170 180
....*....|....*....|
gi 1239950982 369 kvQLETIIKSLKSTQDEINQ 388
Cdd:pfam13166 448 --ELEAQLRDHKPGADEINK 465
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
124-183 |
4.28e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.23 E-value: 4.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 124 RFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAM 183
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
239-366 |
4.41e-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: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 239 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEmdqqkaklrdmlsdvRQK--- 315
Cdd:pfam03148 253 IEETEDAKNKLEWQLKKTLQEIAELEKNIEALEK-------AIRDKEAPLKLAQTRLEN---------------RTYrpn 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 316 ---CQDETQ--MISSLKtQIQSQESDLKSQeddLNRAKSELTRLQQEETQLEQSIQ 366
Cdd:pfam03148 311 velCRDEAQygLVDEVK-ELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
238-403 |
4.56e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 39.26 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 238 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRetsslQELEAQKQDAQdRLDEMDQQ--------KAKLRDML 309
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE-----RELKAEAEHRQ-RVVELSREveeakrafEEKLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 310 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS-ELTRLQQEetqLEQSIQAGKVQLETIIKSLKSTQDEINQ 388
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVEDLRKEKKKLAEEYEQ 197
|
170
....*....|....*
gi 1239950982 389 arsKLSQLQESHQEA 403
Cdd:pfam15665 198 ---KLSKAQAFYERE 209
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
230-361 |
4.64e-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: 39.32 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 302
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 303 AKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDLNRAKSELTRLQQEETQL 361
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
232-376 |
4.87e-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: 38.66 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 232 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 311
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 312 vrqkcqdETQMISSLktqiqsqesdlksqedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 376
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
258-377 |
5.20e-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: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 258 EAIRQKSNEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetqmisslktQIQSQESD 336
Cdd:pfam03938 8 QKILEESPEGKAAQAQLEKKFKKRQaELEAKQKELQKLYEELQKDGALLEEEREEKEQ--------------ELQKKEQE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1239950982 337 LKSQEDDLNRAkseltrLQQEETQLEQSIQAgkvQLETIIK 377
Cdd:pfam03938 74 LQQLQQKAQQE------LQKKQQELLQPIQD---KINKAIK 105
|
|
| COG5074 |
COG5074 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
247-402 |
5.30e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 39.48 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 247 YSLEQDIREKEEAIRQKSNEVQELQNdldRETSSLQEL-EAQKQDAQDRLDEMDQQKAKLR-----DMLSDVRQKCQDET 320
Cdd:COG5074 21 VTFMNKILSINKNLSVYEKEINQIDN---LHKDLLTEVfEEQSRKLRRSLDNFSSQTTDLQrnlkkDIKSAERDGIHLAN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 321 QMISS------LKTQIQS-QESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKL 393
Cdd:COG5074 98 KQAQAenvrqkFLKLIQDyRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRGEAKTAL 177
|
....*....
gi 1239950982 394 SQLQESHQE 402
Cdd:COG5074 178 AEVQARHQE 186
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
240-409 |
5.50e-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: 40.34 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 240 AQLQREKYSLEQDIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQde 319
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLE---KELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 320 tqmisslktQIQSQESDLKSQEDDLNRAKSELtRLQQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSKLSQL--Q 397
Cdd:TIGR00618 271 ---------ELRAQEAVLEETQERINRARKAA-PLAAHIKAVTQIEQ----QAQRIHTELQSKMRSRAKLLMKRAAHvkQ 336
|
170
....*....|..
gi 1239950982 398 ESHQEAHRTLEQ 409
Cdd:TIGR00618 337 QSSIEEQRRLLQ 348
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
264-399 |
5.56e-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: 38.93 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 264 SNEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDD 343
Cdd:cd21116 72 QSYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATK 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239950982 344 LNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 399
Cdd:cd21116 142 AQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESS 197
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
237-375 |
5.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 237 QEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV- 312
Cdd:PRK12705 43 QKEAEEKLEAALLEAKellLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELe 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 313 --RQKCQDETQMISSLkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI 375
Cdd:PRK12705 123 elEKQLDNELYRVAGL-TPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAM 186
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
231-305 |
5.77e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 39.84 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAI---------RQK---------------SNEVQELQNdldretsSLQELEA 286
Cdd:pfam03148 266 QLKKTLQEIAELEKNIEALEKAIRDKEAPLklaqtrlenRTYrpnvelcrdeaqyglVDEVKELEE-------TIEALKQ 338
|
90
....*....|....*....
gi 1239950982 287 QKQDAQDRLDEMDQQKAKL 305
Cdd:pfam03148 339 KLAEAEASLQALERTRLRL 357
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
230-409 |
6.31e-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: 39.17 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEV---QEL------------QNDLDRETSSLQELEAQKQDaqdR 294
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEKEES---K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 295 LDEMDQQKAKLRDMLsdvrQKCQDE-----TQM----------ISSLKTQIQsqesDLK-SQEDDLNraksELTRLQQEE 358
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEElnflsTYKdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239950982 359 TQ-LEQSIQAGKVQLETII--KSLKSTQD--------------EINQARSKLSQLQESHQEAHRTLEQ 409
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQEsllqktrdnqvmlkEIEQFREFIDELEEEIPKLKAEVQQ 218
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
251-363 |
6.57e-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: 37.68 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 251 QDIREKEEaiRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqmissLKTQI 330
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110
....*....|....*....|....*....|...
gi 1239950982 331 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ 363
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEK 110
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
258-398 |
6.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 258 EAIRQKSNEVQELqndldreTSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlKTQIQSQESDL 337
Cdd:TIGR00606 169 KALKQKFDEIFSA-------TRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIV 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 338 KSQEDDLNRAKSELTRLQQEETQLeqsiqagkVQLETIIKSLKSTQDEINQARSKLSQLQE 398
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKI--------MKLDNEIKALKSRKKQMEKDNSELELKME 293
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
347-415 |
7.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239950982 347 AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 415
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
230-410 |
7.81e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQ----------REKYSLEQDIREKEEAIRQKSNEV-----------QELQNDLDRETSSLQELEAQK 288
Cdd:PRK01156 346 SRYDDLNNQILELEgyemdynsylKSIESLKKKIEEYSKNIERMSAFIseilkiqeidpDAIKKELNEINVKLQDISSKV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 289 QDAQDRLDEMDQQKAKLR---DMLSDvRQKCQDETQMISSLKTQ--IQSQESDLKSQEDDLNRAKSELTRLQQEETQL-- 361
Cdd:PRK01156 426 SSLNQRIRALRENLDELSrnmEMLNG-QSVCPVCGTTLGEEKSNhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLkk 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239950982 362 -EQSIQAGKV-QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQY 410
Cdd:PRK01156 505 rKEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
225-375 |
7.93e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 225 EFTGVKELDdisQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ------------NDLDRETSSLQ---ELEAQKQ 289
Cdd:TIGR00618 709 LETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMHQArtvlkarteahfNNNEEVTAALQtgaELSHLAA 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 290 DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE-ETQLEQSIQAG 368
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKyEECSKQLAQLT 865
|
....*..
gi 1239950982 369 KVQLETI 375
Cdd:TIGR00618 866 QEQAKII 872
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
234-417 |
8.12e-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: 39.43 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 234 DISQEIAQLQREK-------YSLEQDIREKEEAIRQKSNEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAK 304
Cdd:pfam15450 24 DLQAEVVSLRGHKercehatLSLLRELLQVRAHVQLQDSELKQLRQEVQQAARApeKEALEFPGPQNQNQMQALDKRLVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 305 LRDMLSDVRQK--CQDE-------------TQMISSLKTQIQSQESD----LKSQEDDLNRAKSELTRLQQEETQL--EQ 363
Cdd:pfam15450 104 VREALTQIRRKqaLQDSerkgaeqeanlrlTKLTGKLKQEEQGREAAcsalQKSQEEASQKVDHEVARMQAQVTKLgeEM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 364 S-------------IQAGKVQLETIIKSLKSTQ--------DEINQARSKLSQLQESH---------QEAHRTLEQYdEA 413
Cdd:pfam15450 184 SlrflkreaklcsfLQKSFLALEKRMKASESTRlkaesslrEELEGRWQKLQELTEERlralqgqreQEEGHLLEQC-RG 262
|
....
gi 1239950982 414 LDGA 417
Cdd:pfam15450 263 LDAA 266
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-315 |
8.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQReKYSlEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKL---- 305
Cdd:PRK03918 640 KRLEELRKELEELEK-KYS-EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekle 717
|
90
....*....|..
gi 1239950982 306 --RDMLSDVRQK 315
Cdd:PRK03918 718 kaLERVEELREK 729
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
233-414 |
8.36e-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: 38.21 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 233 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 312
Cdd:pfam14988 25 NQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 313 RQKcqdetqmissLKTQIQSQESDLKSQEDDLN------RAKSELTRLQQEETqleqsiQAGKVQLETIIKSLKSTQDEI 386
Cdd:pfam14988 105 DRE----------AHLQFLKEKALLEKQLQELRilelgeRATRELKRKAQALK------LAAKQALSEFCRSIKRENRQL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239950982 387 NQARSKL-----------SQLQESHQEAHRTlEQYDEAL 414
Cdd:pfam14988 169 QKELLQLiqetqaleaikSKLENRKQRLKEE-QWYLEAL 206
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
230-415 |
8.44e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 39.81 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 230 KELDDISQEIAQLQREKYSLEQDIREKEEAIrQKSNEVQELQNDLDREtsSLQELEAQKQDAQDRLDE----MDQQKAKL 305
Cdd:PTZ00440 1031 KLIKEKGKEIEEKVDQYISLLEKMKTKLSSF-HFNIDIKKYKNPKIKE--EIKLLEEKVEALLKKIDEnknkLIEIKNKS 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 306 RDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ-EETQLE----------QSIQAGKVQLET 374
Cdd:PTZ00440 1108 HEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvNEIEIEyerilidhivEQINNEAKKSKT 1187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239950982 375 IIKSLKSTQDEINQARSKLSQLQESHqeaHRTLE---QYDEALD 415
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSKERNDH---LTTFEynaYYDKATA 1228
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
231-439 |
8.85e-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: 39.42 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 231 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 310
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950982 311 DVRqKCQDETQMISSLktqiqsqESDLKSQEDDLNRAKSELTRLQQ--EETQLEQSIQAGKV-QLETII----------- 376
Cdd:pfam10174 549 AVR-TNPEINDRIRLL-------EQEVARYKEESGKAQAEVERLLGilREVENEKNDKDKKIaELESLTlrqmkeqnkkv 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239950982 377 KSLKSTQDEinQARSKLSQLQESHQE--------AHRTLEQYDEALD------GAHGASLTnladlSEGVSLAERGG 439
Cdd:pfam10174 621 ANIKHGQQE--MKKKGAQLLEEARRRednladnsQQLQLEELMGALEktrqelDATKARLS-----STQQSLAEKDG 690
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
234-303 |
8.98e-03 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 38.06 E-value: 8.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239950982 234 DISQEIAQLQREKYSLEQDIREKEEAiRQKSNEVQELQNDLDRETSSLQELEAQKQ-----DAQDRLDEMDQQKA 303
Cdd:pfam03280 76 SAEEKQQRLAALRAQLPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQRA 149
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
248-308 |
9.64e-03 |
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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: 36.00 E-value: 9.64e-03
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gi 1239950982 248 SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 308
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
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