|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
66-162 |
8.72e-42 |
|
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: 147.04 E-value: 8.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 66 QWVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkG 145
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 2462506005 146 IDPPHVLTPEMIPPSDR 162
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
77-142 |
4.05e-27 |
|
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: 104.61 E-value: 4.05e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506005 77 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 142
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
179-342 |
2.66e-16 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 81.49 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 258
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 336
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194
|
....*.
gi 2462506005 337 EISSMQ 342
Cdd:COG4372 195 NAEKEE 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
182-338 |
7.75e-16 |
|
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: 77.66 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 261
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506005 262 KEVRKkcAEEAQlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 338
Cdd:COG1579 83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-358 |
3.50e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISS 340
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEEL 405
|
170
....*....|....*...
gi 2462506005 341 MQMKLMEMKDLENHNSQL 358
Cdd:COG1196 406 EEAEEALLERLERLEEEL 423
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-347 |
4.24e-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: 76.25 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 262
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 263 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
....*
gi 2462506005 343 MKLME 347
Cdd:TIGR02168 428 KKLEE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-359 |
5.51e-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: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSm 341
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS- 493
|
170
....*....|....*...
gi 2462506005 342 qmKLMEMKDLENHNSQLN 359
Cdd:TIGR04523 494 --KEKELKKLNEEKKELE 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
173-342 |
9.80e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.34 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 173 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDE 252
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 332
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|
gi 2462506005 333 DSQQEISSMQ 342
Cdd:COG4913 423 ELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-350 |
2.19e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 262
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 263 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
....*...
gi 2462506005 343 MKLMEMKD 350
Cdd:TIGR02168 936 VRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-357 |
5.23e-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: 72.78 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 178 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 257
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-----AQLEPLQQHLQ 332
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450
|
170 180
....*....|....*....|....*
gi 2462506005 333 DSQQEISSMQMKLMEMKDLENHNSQ 357
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQ 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-359 |
6.13e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 261
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 341
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170
....*....|....*....
gi 2462506005 342 QMKLME-MKDLENHNSQLN 359
Cdd:COG1196 385 AEELLEaLRAAAELAAQLE 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-350 |
9.60e-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: 72.01 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS-------KELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEEL-------AKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 334
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170
....*....|....*.
gi 2462506005 335 QQEISSMQMKLMEMKD 350
Cdd:TIGR02168 858 AAEIEELEELIEELES 873
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-359 |
3.54e-12 |
|
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: 70.09 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKA 255
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALA----------NEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 335
Cdd:TIGR02168 306 ILRERLANLERQ-------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180
....*....|....*....|....*
gi 2462506005 336 QEISSMQMKLMEMK-DLENHNSQLN 359
Cdd:TIGR02168 379 EQLETLRSKVAQLElQIASLNNEIE 403
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-323 |
5.60e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 180 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 257
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EE---QLKEVRKKCAEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 323
Cdd:COG4717 173 AElqeELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-359 |
6.25e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 69.28 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 253
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 254 KAQLEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 333
Cdd:TIGR04523 290 LNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190
....*....|....*....|....*....|
gi 2462506005 334 SQQEISSM----QMKLMEMKDLENHNSQLN 359
Cdd:TIGR04523 368 KQNEIEKLkkenQSYKQEIKNLESQINDLE 397
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
204-358 |
6.78e-12 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 64.57 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 204 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 282
Cdd:pfam08614 11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 283 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 358
Cdd:pfam08614 88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-357 |
7.99e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 180 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 259
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 339
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170
....*....|....*...
gi 2462506005 340 SMQMKLMEMKDLENHNSQ 357
Cdd:COG1196 390 EALRAAAELAAQLEELEE 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-338 |
8.78e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 176 ADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKA 255
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 335
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
...
gi 2462506005 336 QEI 338
Cdd:COG1196 449 EEE 451
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
159-318 |
9.14e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 65.72 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 159 PSDRASLQKNIIGsspvadfsAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqre 229
Cdd:COG1579 30 PAELAELEDELAA--------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 230 ntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSR 305
Cdd:COG1579 98 -----------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEE 160
|
170
....*....|...
gi 2462506005 306 LQQETAELEESVE 318
Cdd:COG1579 161 LEAEREELAAKIP 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-342 |
2.15e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 261
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAE---EAQLISS-------LKAELTSQESQISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPL 327
Cdd:COG4942 100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*
gi 2462506005 328 QQHLQDSQQEISSMQ 342
Cdd:COG4942 180 LAELEEERAALEALK 194
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-340 |
2.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 261
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 340
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
191-350 |
2.66e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 66.08 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 191 IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 270
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 271 eaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:COG4372 89 ----LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-359 |
2.74e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 178 FSAIKELDTLNNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDEQKAQL 257
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAE-EAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 332
Cdd:TIGR02169 771 EEDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180
....*....|....*....|....*...
gi 2462506005 333 DSQQEISSMQMKLMEMK-DLENHNSQLN 359
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEeELEELEAALR 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
183-353 |
3.20e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQREntnlqklqaqkqqvqelLDELDEQKAQLEE 259
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKE-----------------IEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPL 327
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREI 817
|
170 180 190
....*....|....*....|....*....|
gi 2462506005 328 QQHLQDSQQEI----SSMQMKLMEMKDLEN 353
Cdd:TIGR02169 818 EQKLNRLTLEKeyleKEIQELQEQRIDLKE 847
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-340 |
3.64e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDL-----------QDEVQRENTNLQKLQAQKQQVQELLDEL 250
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 330
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
170
....*....|
gi 2462506005 331 LQDSQQEISS 340
Cdd:COG4942 236 AAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
179-352 |
7.80e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 257
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 337
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
170
....*....|....*
gi 2462506005 338 ISSMQMKLMEMKDLE 352
Cdd:PRK03918 703 LEEREKAKKELEKLE 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-354 |
1.80e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 341
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170
....*....|...
gi 2462506005 342 QMKLMEMKDLENH 354
Cdd:TIGR02168 914 RRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-342 |
2.17e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 180 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 259
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 QLKEVRKKCAEEAQLISSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 339
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
...
gi 2462506005 340 SMQ 342
Cdd:COG1196 502 DYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-341 |
7.14e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 252 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL 331
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|
gi 2462506005 332 QDSQQEISSM 341
Cdd:COG4942 100 EAQKEELAEL 109
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
245-359 |
1.01e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.07 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 324
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462506005 325 EPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 359
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLE 135
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-332 |
1.17e-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: 62.01 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKE-------DTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD--- 251
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaai 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 252 ----EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESG 320
Cdd:TIGR02169 430 agieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGG 509
|
170
....*....|..
gi 2462506005 321 KAQLEPLQQHLQ 332
Cdd:TIGR02169 510 RAVEEVLKASIQ 521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-339 |
1.48e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 187 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRK 266
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 267 KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKAQLEPLQQHLQDSQQE 337
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
..
gi 2462506005 338 IS 339
Cdd:TIGR04523 598 KK 599
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
184-447 |
1.75e-09 |
|
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: 61.38 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 184 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQ 242
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----------KSTLAGE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 243 VQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETaE 312
Cdd:pfam10174 382 IRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR-E 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 313 LEESVEsgKAQLEPLQQHLQDSQQEISSMQMKLME----MKDLENHNSQLNwcSSPHSIlvngatdycsLSTSSSETANL 388
Cdd:pfam10174 461 REDRER--LEELESLKKENKDLKEKVSALQPELTEkessLIDLKEHASSLA--SSGLKK----------DSKLKSLEIAV 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506005 389 NEHVEGQSNLESE--PIHQ-ESPARSSPELLPSGVTDENEVTTAVTE--KVCSELD----------NNRHSKEE 447
Cdd:pfam10174 527 EQKKEECSKLENQlkKAHNaEEAVRTNPEINDRIRLLEQEVARYKEEsgKAQAEVErllgilreveNEKNDKDK 600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
179-347 |
4.04e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRenTNLQKLQAQKQQVQELLDELDEQKAQ 256
Cdd:COG4913 229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 257 LEEQLKEVRKKCAEEAQLISSLKAELTSQ--------ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 328
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170
....*....|....*....
gi 2462506005 329 QHLQDSQQEISSMQMKLME 347
Cdd:COG4913 387 AEAAALLEALEEELEALEE 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-336 |
4.46e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 326
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90
....*....|
gi 2462506005 327 LQQHLQDSQQ 336
Cdd:COG4942 109 LLRALYRLGR 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-342 |
5.04e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL 261
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------QISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 341
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
.
gi 2462506005 342 Q 342
Cdd:TIGR02168 830 E 830
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-360 |
7.17e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 260
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 261 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 340
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180
....*....|....*....|.
gi 2462506005 341 MQMKLMEMKD-LENHNSQLNW 360
Cdd:TIGR04523 536 KESKISDLEDeLNKDDFELKK 556
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
182-352 |
7.78e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVeqDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQL 261
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQ--LISSLKAELTSQESQI----STY----------EEELAKAREEL-SRLQQETAELEESVESGKAQL 324
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELaelsARYtpnhpdvialRAQIAALRAQLqQEAQRILASLEAELEALQARE 329
|
170 180
....*....|....*....|....*...
gi 2462506005 325 EPLQQHLQDSQQEISSMQMKLMEMKDLE 352
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-359 |
8.59e-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: 58.88 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKlqaqkqqvqELLDELDEQKAQLEEQ 260
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 261 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS------ 334
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqq 409
|
170 180 190
....*....|....*....|....*....|
gi 2462506005 335 -QQEISSMQ----MKLMEMKDLENHNSQLN 359
Cdd:TIGR04523 410 kDEQIKKLQqekeLLEKEIERLKETIIKNN 439
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-354 |
9.73e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 166 QKNIIGSSPVADfSAIKELDtLNNEIVDLQREKNNVEQDLKEK----------------EDTIKQRTSEV--------QD 221
Cdd:COG3206 86 QIEILKSRPVLE-RVVDKLN-LDEDPLGEEASREAAIERLRKNltvepvkgsnvieisyTSPDPELAAAVanalaeayLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 222 LQDEVQRENTNlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAE--EAQLISSLKAELTSQESQISTYEEELAKA 299
Cdd:COG3206 164 QNLELRREEAR------------KALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506005 300 REELSRLQQETAELEESVESGKAQLEPLQQH--LQDSQQEISSMQMKLMEMKD--LENH 354
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSAryTPNH 290
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
252-358 |
1.01e-08 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 54.18 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 252 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 316
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462506005 317 VESGKAQLEPLQQHLQDS----QQEISSMQMKLmemKDLENHNSQL 358
Cdd:pfam07926 80 AESAKAELEESEESWEEQkkelEKELSELEKRI---EDLNEQNKLL 122
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
245-349 |
1.42e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.60 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDE-------LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELA--KAREELSR--LQQEtA 311
Cdd:COG1842 16 ALLDKaedpekmLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkaRLAleKGREDLAReaLERK-A 94
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462506005 312 ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 349
Cdd:COG1842 95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELK 132
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
183-350 |
1.48e-08 |
|
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: 56.96 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREknnveqdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 262
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 263 EVRKKC-----------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQL 324
Cdd:pfam04849 182 KLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIEN 261
|
170 180
....*....|....*....|....*.
gi 2462506005 325 EPLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:pfam04849 262 EELQQHLQASKEAQRQLTSELQELQD 287
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-355 |
1.50e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 167 KNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ----RENTNLQKLQAQKQQ 242
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 243 VQELLDELDEQKAQ----------LEEQLKEVRKKCA--------EEAQL-------------ISSLKAELTSQESQIST 291
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 292 YEEELAKAREELSR-----------------LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 354
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
.
gi 2462506005 355 N 355
Cdd:TIGR04523 265 I 265
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
194-358 |
1.57e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 58.26 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 194 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 273
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 274 LISSLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLM 346
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
170 180
....*....|....*....|...
gi 2462506005 347 E-----------MKDLENHNSQL 358
Cdd:pfam01576 254 EetaqknnalkkIRELEAQISEL 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
179-340 |
1.58e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------------------DL--------------QDE 225
Cdd:COG3883 55 ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsesfsDFldrlsalskiadadADL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 226 VQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR 305
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
170 180 190
....*....|....*....|....*....|....*
gi 2462506005 306 LQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 340
Cdd:COG3883 215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-352 |
1.81e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 257
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 335
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|....*..
gi 2462506005 336 QEISSMQMKLMEMKDLE 352
Cdd:PRK03918 331 KELEEKEERLEELKKKL 347
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
184-352 |
2.24e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 184 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD----- 251
Cdd:COG4717 48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 252 ----EQKAQLEEQLKEVR---KKCAEEAQLISSLKAELTSQESQISTYEEELAKA--------REELSRLQQETAELEES 316
Cdd:COG4717 128 lplyQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462506005 317 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 352
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-358 |
2.58e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLN--------NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL 250
Cdd:TIGR02169 269 EIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK--------------LEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS-------------------------- 304
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyrekleklkreinelkreldrlqee 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506005 305 --RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQL 358
Cdd:TIGR02169 415 lqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAaDLSKYEQEL 471
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-342 |
4.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 162 RASLQKNIIGsspvadFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTIKQR--------------------TSE 218
Cdd:COG4913 596 RRIRSRYVLG------FDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERrealqrlaeyswdeidvasaERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 219 VQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELA 297
Cdd:COG4913 670 IAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462506005 298 KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL 782
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-353 |
5.89e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKA 255
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEVRKKCAEEAQLISSLKAELTSQES-------QISTYEEELAKAREELSRLQQETAELEESVESGKA------ 322
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404
|
170 180 190
....*....|....*....|....*....|...
gi 2462506005 323 -QLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 353
Cdd:PRK02224 405 vDLGNAEDFLEELREERDELREREAELEaTLRT 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-330 |
6.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQistyEEELAKAREELSRLQQETAELEESV---ESGKAQLEPLQQH 330
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
183-341 |
7.94e-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: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 262
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 263 EVRKKCAE-EAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------A 322
Cdd:TIGR02169 872 ELEAALRDlESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeL 951
|
170
....*....|....*....
gi 2462506005 323 QLEPLQQHLQDSQQEISSM 341
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRAL 970
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-340 |
7.96e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 166 QKNIIGSSPVADFSAIKELDTLNNEIVDLQREK-------NNVEQDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKL 236
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaearlAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 237 QAQKQQV----QELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQE 309
Cdd:COG3206 283 SARYTPNhpdvIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAE 352
|
170 180 190
....*....|....*....|....*....|.
gi 2462506005 310 TAELEESVESGKAQLEPLQQHLQDSQQEISS 340
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-313 |
8.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462506005 262 KEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 313
Cdd:COG4913 415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
205-357 |
9.68e-08 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 52.98 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 205 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 281
Cdd:pfam15619 6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 282 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 339
Cdd:pfam15619 69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141
|
170
....*....|....*...
gi 2462506005 340 SMQMKLmemkDLENHNSQ 357
Cdd:pfam15619 142 DLERKL----ELENKSFR 155
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
178-341 |
1.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 178 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqqVQELLDELDEQKAQL 257
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-----------YQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQE 337
Cdd:COG4717 412 EELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAE 484
|
....
gi 2462506005 338 ISSM 341
Cdd:COG4717 485 LREL 488
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
158-322 |
1.66e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.86 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 158 PPSDRASLQKNIIGSSPVADfsAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlq 234
Cdd:COG2433 361 PDVDRDEVKARVIRGLSIEE--ALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 235 klqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEELAKAREELSRLQqeta 311
Cdd:COG2433 436 ------------LEEKDERIERLERELSEARSEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLK---- 499
|
170
....*....|.
gi 2462506005 312 ELEESVESGKA 322
Cdd:COG2433 500 ELWKLEHSGEL 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
179-344 |
1.76e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQEL 246
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 326
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
170
....*....|....*...
gi 2462506005 327 LQQhLQDSQQEISSMQMK 344
Cdd:PRK02224 501 AED-LVEAEDRIERLEER 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-313 |
1.82e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 210 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 289
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 2462506005 290 STYEEELAKAREELSRLQQETAEL 313
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
179-350 |
2.05e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelldeLDEQKAQLE 258
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE------------------------IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKCAEE------------AQLISSLKA-------------ELTSQESQISTYEEELAKAREELSRLQQETAEL 313
Cdd:COG3883 90 ERARALYRSGGSVsyldvllgsesfSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462506005 314 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
180-334 |
2.10e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 180 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDe 252
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 qkaQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 332
Cdd:PRK04778 359 ---SLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
..
gi 2462506005 333 DS 334
Cdd:PRK04778 436 KS 437
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
182-338 |
2.15e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCA--EEAQLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 337
Cdd:COG4372 167 AALEQELQalSEAEAEQALDELLKEANRNAEKEEElaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
.
gi 2462506005 338 I 338
Cdd:COG4372 247 D 247
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
178-359 |
2.25e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.07 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 178 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQL 257
Cdd:PRK04778 89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAEEA----QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQ 328
Cdd:PRK04778 146 KDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQ 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462506005 329 QHLQDSQQEISS----MQMK---------LMEMKDLENHNSQLN 359
Cdd:PRK04778 226 TELPDQLQELKAgyreLVEEgyhldhldiEKEIQDLKEQIDENL 269
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-320 |
2.98e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 201 VEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 280
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462506005 281 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 320
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-358 |
3.10e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKAQLEEQlkevRKKcAEEAQLISS----LKAELT-----SQESQISTYEEELAKAREELSRLQQETAELEES 316
Cdd:COG1196 194 ILGELERQLEPLERQ----AEK-AERYRELKEelkeLEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462506005 317 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
179-345 |
3.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLE 258
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKCAEEAQ-------LISSLKAELTSQE-----------SQISTYE----EELAKAREELSRLQQETAELEES 316
Cdd:COG3883 79 AEIEERREELGERARalyrsggSVSYLDVLLGSESfsdfldrlsalSKIADADadllEELKADKAELEAKKAELEAKLAE 158
|
170 180
....*....|....*....|....*....
gi 2462506005 317 VESGKAQLEPLQQHLQDSQQEISSMQMKL 345
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQL 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-335 |
4.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 176 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqAQKQQVQELLDELDEQK 254
Cdd:COG4913 685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 255 AQL--EEQLKEVRKKCAEEAQLISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREE 302
Cdd:COG4913 756 AAAlgDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEER 835
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462506005 303 LSRLQQET---------AELEESVESGKAQLEPLQQHLQDSQ 335
Cdd:COG4913 836 FKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-359 |
4.49e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQL 261
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGKAQLEPL-QQHLQD 333
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKSEISDLnNQKEQD 307
|
170 180
....*....|....*....|....*.
gi 2462506005 334 SQQEISSmQMKLMEmKDLENHNSQLN 359
Cdd:TIGR04523 308 WNKELKS-ELKNQE-KKLEEIQNQIS 331
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-350 |
4.54e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 180 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL 246
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 ------LDELDEQKAQLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELE--- 314
Cdd:PRK03918 462 kriekeLKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgei 541
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462506005 315 ESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-353 |
7.32e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 170 IGSSPVADfsAIKE----LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRtSEVQDLQDevQRENTNlqklqaqkqqvqE 245
Cdd:PRK02224 461 VEGSPHVE--TIEEdrerVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------E 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKAQLEEQLKEVRKKCAEeaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLE 325
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIR 595
|
170 180
....*....|....*....|....*...
gi 2462506005 326 PLQQHLQDSQQEISSMQMKLMEMKDLEN 353
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELND 623
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
251-350 |
8.12e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 330
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100
....*....|....*....|
gi 2462506005 331 LQDSQQEISSMQMKLMEMKD 350
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQE 101
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
182-329 |
8.78e-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: 52.34 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506005 262 KEVRKKCAEEAQL-----------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQ 329
Cdd:pfam05667 411 DASAQRLVELAGQwekhrvplieeYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
181-338 |
9.92e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL---------- 250
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 -DEQK------AQLEEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 323
Cdd:COG1340 132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
170
....*....|....*
gi 2462506005 324 LEPLQQHLQDSQQEI 338
Cdd:COG1340 211 ADELHKEIVEAQEKA 225
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
162-324 |
1.24e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 162 RASLQKNI-IGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqk 240
Cdd:COG3206 242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 241 qqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVE 318
Cdd:COG3206 311 --AQRILASLEAELEALQAREASLQ---AQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384
|
....*.
gi 2462506005 319 SGKAQL 324
Cdd:COG3206 385 VGNVRV 390
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
203-341 |
1.32e-06 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 49.43 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 203 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 282
Cdd:pfam06785 83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506005 283 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 341
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
190-359 |
1.38e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 190 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQD-EVQRENTNLQK--LQAQKQQVQELLDELDEQKAQLEEQLKEV-- 264
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKrEAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 265 --RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKA---QLEPLQQHLQ---DSQQ 336
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQsqeQDSE 187
|
170 180 190
....*....|....*....|....*....|
gi 2462506005 337 EISSMQMKLMEMKDLEN-------HNSQLN 359
Cdd:pfam05557 188 IVKNSKSELARIPELEKelerlreHNKHLN 217
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
179-339 |
1.47e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 49.99 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE 252
Cdd:pfam12795 48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLK--EVRKKCAEEAQLIsSLKAELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQ 328
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLE 197
|
170
....*....|.
gi 2462506005 329 QHLQDSQQEIS 339
Cdd:pfam12795 198 QQLQALQELLN 208
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
245-314 |
1.59e-06 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 46.15 E-value: 1.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 314
Cdd:pfam12329 5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
1-27 |
1.96e-06 |
|
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: 46.50 E-value: 1.96e-06
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-359 |
2.06e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKnnvEQDL-KEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 260
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 261 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAreelsrlQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 340
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
170
....*....|....*....
gi 2462506005 341 MQmklMEMKDLENHNSQLN 359
Cdd:TIGR04523 438 NN---SEIKDLTNQDSVKE 453
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-358 |
2.93e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEqkaqLEEQLKEVRKKCAEEAQLIsslkAELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVESGKAQL 324
Cdd:COG4717 70 LKELKE----LEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAEL 141
|
90 100 110
....*....|....*....|....*....|....
gi 2462506005 325 EPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAEL 175
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-350 |
3.47e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDT----LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQ 256
Cdd:TIGR04523 456 IKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 257 LEEQLKEVRKKcaeeaqlISSLKAELTSqesqiSTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 336
Cdd:TIGR04523 536 KESKISDLEDE-------LNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
170
....*....|....
gi 2462506005 337 EISSMQMKLMEMKD 350
Cdd:TIGR04523 604 EIEEKEKKISSLEK 617
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-359 |
3.64e-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: 50.83 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--- 318
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462506005 319 ----SGKAQLEPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 359
Cdd:TIGR02168 274 levsELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELE 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-351 |
4.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 4.13e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506005 281 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 351
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
64-168 |
4.71e-06 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 45.83 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 64 LRQWvvspaEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLI 143
Cdd:pfam12763 4 LEEW-----EIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LV 76
|
90 100
....*....|....*....|....*..
gi 2462506005 144 KGI--DPPHVLTPEMIPPSDRASLQKN 168
Cdd:pfam12763 77 NGNiaDVPDELPDWLVPGSKAHLIQAN 103
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-350 |
5.10e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-----QKAQ 256
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----------KISDLEDELNKddfelKKEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 257 LEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEplqqhlqdsqq 336
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE----------- 627
|
170
....*....|....
gi 2462506005 337 EISSMQMKLMEMKD 350
Cdd:TIGR04523 628 KLSSIIKNIKSKKN 641
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-345 |
6.42e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---------ISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAE 312
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703
|
90 100 110
....*....|....*....|....*....|...
gi 2462506005 313 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 345
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
247-358 |
7.13e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 323
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462506005 324 -------LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:COG3096 604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLLEREREATVERDEL 649
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
248-353 |
7.55e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 248 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL 327
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100
....*....|....*....|....*....
gi 2462506005 328 QQHLQDSQQEISSMQM---KLMEMKDLEN 353
Cdd:PRK12704 137 IEEQLQELERISGLTAeeaKEILLEKVEE 165
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
203-355 |
8.06e-06 |
|
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: 49.08 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 203 QDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA---QLEEQLKEVRKKCAEEA----QLI 275
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELD-----------------ELLESEEKNREeveELKDKYRELRKTLLANRfsygPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 276 SSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 349
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGy 228
|
....*.
gi 2462506005 350 DLENHN 355
Cdd:pfam06160 229 ALEHLN 234
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
202-350 |
9.48e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 202 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAE 281
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAE-------LEALQAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 282 LTSQESQISTYEEELAKAREEL------------------------------------SRLQQETAELEESVESGKAQLE 325
Cdd:COG3883 67 IDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELE 146
|
170 180
....*....|....*....|....*
gi 2462506005 326 PLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKA 171
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
180-349 |
1.22e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 180 AIKELDTLNNEIV-----DLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdevQRENtnlqklqaqkqqvqelldeldeqk 254
Cdd:PRK12704 47 AKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLL------QKEE------------------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 255 aQLEEQLKEVRKKcaeeaqlisslKAELTSQESQISTYEEELAKAREELSRLQQET-AELEE----SVESGKAQLepLQQ 329
Cdd:PRK12704 97 -NLDRKLELLEKR-----------EEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERisglTAEEAKEIL--LEK 162
|
170 180
....*....|....*....|
gi 2462506005 330 HLQDSQQEISSMqMKLMEMK 349
Cdd:PRK12704 163 VEEEARHEAAVL-IKEIEEE 181
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
182-357 |
1.38e-05 |
|
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: 48.58 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDlKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqKQQVQELLDELDEQKAQLEEQL 261
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELER-----------LREHNKHLNENIENKLLLKEEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKC-------AEEAQL---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLEPLQ 328
Cdd:pfam05557 231 EDLKRKLereekyrEEAATLeleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSARQLE 310
|
170 180 190
....*....|....*....|....*....|
gi 2462506005 329 QHLQDSQQEISSMQMKLMEM-KDLENHNSQ 357
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLnKKLKRHKAL 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-315 |
1.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQreknNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEE 259
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEE 659
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506005 260 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYE----------EELAKAREELSRLQQETAELEE 315
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
183-317 |
1.48e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.54 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEqdlKEKEDTIKQRtsevqdlqdevqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLK 262
Cdd:COG0542 412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 263 EVRKKCAEEAQLIS---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 317
Cdd:COG0542 458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
245-345 |
1.55e-05 |
|
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: 46.84 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 311
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462506005 312 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 345
Cdd:COG1579 104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
186-434 |
1.60e-05 |
|
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: 47.45 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 186 TLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVR 265
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 266 kkcaeeaqlisSLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISSM 341
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELENR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 342 QMKLMEmkDLENHNSQLNWCSSPHSILVngatdyCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPelLPSGVT 421
Cdd:pfam09787 172 LHQLTE--TLIQKQTMLEALSTEKNSLV------LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRN--VPGLFS 241
|
250
....*....|...
gi 2462506005 422 DENEVTTAVTEKV 434
Cdd:pfam09787 242 ESDSDRAGMYGKV 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
246-358 |
1.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 325
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462506005 326 P---------LQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEERLEELRELEEELEEL 168
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
198-345 |
1.72e-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: 46.60 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 198 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 277
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 278 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhlqdSQQEISSMQMKL 345
Cdd:pfam04012 88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLK-----ARLKAAKAQEAV 150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-358 |
2.22e-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: 47.45 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 268 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 347
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|..
gi 2462506005 348 M-KDLENHNSQL 358
Cdd:COG4942 95 LrAELEAQKEEL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-358 |
2.23e-05 |
|
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: 48.14 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 169 IIGSSPVADFSAIKELdtlnNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLD 248
Cdd:TIGR02169 147 FISMSPVERRKIIDEI----AGVAEFDRKK----EKALEELEEVEENIERLDLIIDEKRQQ-----------------LE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 324
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462506005 325 EPL--------QQHLQDSQQEISSMQ----MKLMEMKDLENHNSQL 358
Cdd:TIGR02169 282 KDLgeeeqlrvKEKIGELEAEIASLErsiaEKERELEDAEERLAKL 327
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
184-336 |
2.34e-05 |
|
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: 45.33 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 184 LDTLNNEIVDLQREKNNVEQDLKEKedtikqRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKE 263
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 264 VRKKCAEEAQLissLKAELtsqESQISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQH 330
Cdd:pfam01442 60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAER 133
|
....*.
gi 2462506005 331 LQDSQQ 336
Cdd:pfam01442 134 LEELKE 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
175-349 |
2.80e-05 |
|
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: 47.76 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 175 VADFSAikELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQK 254
Cdd:TIGR02169 296 IGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 255 AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-------EEELAKAREELSRLQQETAELEESVESGKAQLEPL 327
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
170 180
....*....|....*....|..
gi 2462506005 328 QQHLQDSQQEISSMQMKLMEMK 349
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLK 475
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
123-342 |
2.83e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.38 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 123 CGKLSKDQFALAFHLISqkliKGIDPPHVLTPEMIPPsdraslqkniigsspvadfsAIKEldtlnnEIVDLQREkNNVe 202
Cdd:pfam05622 246 CAQLQQAELSQADALLS----PSSDPGDNLAAEIMPA--------------------EIRE------KLIRLQHE-NKM- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 203 qdLKEK-EDTIKQRTSEVQdlqdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 281
Cdd:pfam05622 294 --LRLGqEGSYRERLTELQ------------------------QLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462506005 282 LTSQESQ----------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQHLQDSQQEISSMQ 342
Cdd:pfam05622 348 LQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAME 419
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
183-347 |
2.99e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 260
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 261 LKEVRKKCAEEAQLISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 337
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
170
....*....|
gi 2462506005 338 ISSMQMKLME 347
Cdd:PHA02562 395 KSELVKEKYH 404
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
199-329 |
3.14e-05 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 43.73 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 199 NNVEQDLKEkedTIKQrtseVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRkkcaeeaqlissl 278
Cdd:pfam18595 29 QVVEKDLRS---CIKL----LEEIEAELAKLE--------------EAKKKLKELRDALEEKEIELR------------- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462506005 279 kaELTSQESQIstyEEELAKAREELSRLQQETaelEESVESGKAQLEPLQQ 329
Cdd:pfam18595 75 --ELERREERL---QRQLENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
245-338 |
3.55e-05 |
|
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: 45.69 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQL 324
Cdd:pfam11932 34 KKIDKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TEREL 95
|
90
....*....|....
gi 2462506005 325 EPLQQHLQDSQQEI 338
Cdd:pfam11932 96 VPLMLKMLDRLEQF 109
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
191-357 |
3.93e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 191 IVDLQREK-NNVEQDLKEKEDTIKQR-------TSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqlEEQLK 262
Cdd:pfam05483 262 LLEESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 263 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEE--------SVE------------ 318
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEmtkfknnkEVEleelkkilaede 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462506005 319 ---SGKAQLEPLQQHLQDSQQ-----------EISSMQMKLMEMKDLENHNSQ 357
Cdd:pfam05483 419 kllDEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLTAIKTSEEHYLK 471
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
177-358 |
4.47e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 177 DFSAIKELDTLNNeivDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENT-NLQKLQAQKQQVQELLDELDEQKA 255
Cdd:PHA02562 161 DISVLSEMDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETAELEESVESGKAQLEP 326
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462506005 327 LQQHLQDSQQ---EISSMQMKLMEMK-DLENHNSQL 358
Cdd:PHA02562 318 LDTAIDELEEimdEFNEQSKKLLELKnKISTNKQSL 353
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
181-357 |
4.69e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTIKQRTSEVQDLQDEV------QRENTNLQKLQAQKQQVQELLD-- 248
Cdd:TIGR00606 743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGSDld 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ----ELDEQKAQLEEQLK------EVRKKCAEEAQ-LISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELE 314
Cdd:TIGR00606 822 rtvqQVNQEKQEKQHELDtvvskiELNRKLIQDQQeQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462506005 315 ESVESGKAQLEPLQQHLQDSQQEissmQMKLMEMKDLENHNSQ 357
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNKKAQ 940
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
182-359 |
5.01e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDL------QREKNnveQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA 255
Cdd:PRK09039 53 SALDRLNSQIAELadllslERQGN---QDLQDSVANLRASLSAAEAERSRLQ-----------------ALLAELAGAGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEvrkkcaeeaqlissLKAELTSQEsQIStyeeelAKAREELSRLQQETAELeesvesgKAQLEPLQQHLQDSQ 335
Cdd:PRK09039 113 AAEGRAGE--------------LAQELDSEK-QVS------ARALAQVELLNQQIAAL-------RRQLAALEAALDASE 164
|
170 180
....*....|....*....|....
gi 2462506005 336 QEISSMQMKLmemKDLenhNSQLN 359
Cdd:PRK09039 165 KRDRESQAKI---ADL---GRRLN 182
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
245-343 |
5.03e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 324
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212
|
90
....*....|....*....
gi 2462506005 325 EPLQQHLQDSQQEISSMQM 343
Cdd:PRK11448 213 ERKQKRKEITDQAAKRLEL 231
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
247-338 |
5.16e-05 |
|
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: 44.56 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 319
Cdd:pfam01442 6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85
|
90
....*....|....*....
gi 2462506005 320 GKAQLEPLQQHLQDSQQEI 338
Cdd:pfam01442 86 LNADAEELQEKLAPYGEEL 104
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
253-352 |
5.18e-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: 43.37 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 325
Cdd:pfam20492 7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79
|
90 100
....*....|....*....|....*..
gi 2462506005 326 PLQQHLQDSQQEISSMQMKlMEMKDLE 352
Cdd:pfam20492 80 QLEAELAEAQEEIARLEEE-VERKEEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-441 |
5.42e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 195 QREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------EV 264
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeEL 1707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 265 RKKCAEE---------AQLISSLKAE-LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 334
Cdd:PTZ00121 1708 KKKEAEEkkkaeelkkAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 335 QQEISSMQMKlMEMKDLENHNSQLNWCSSPHSILVN-------GATDYCSLSTSS--SETANLNEHVEGQSNLESEPIHQ 405
Cdd:PTZ00121 1788 EDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINdskemedSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNK 1866
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462506005 406 ESPARSSPELLPSgvtDENEVTTAvteKVCSELDNN 441
Cdd:PTZ00121 1867 EADFNKEKDLKED---DEEEIEEA---DEIEKIDKD 1896
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
194-313 |
5.62e-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: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 194 LQREKNNVEQDLKE------KEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKK 267
Cdd:pfam05672 25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462506005 268 CAEEAQlisslkAELTSQESQISTYEEELAKAREELSRLQQETAEL 313
Cdd:pfam05672 85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-350 |
5.78e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 326
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100
....*....|....*....|....
gi 2462506005 327 LQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEA 782
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-357 |
5.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 193 DLQREKNNVeqdLKEKEDTIKQRtsEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL---KEVRKKCA 269
Cdd:PRK02224 180 RVLSDQRGS---LDQLKAQIEEK--EEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRdeaDEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 270 EEAQLISSLKAELTSQESQIS-------TYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAeterereELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170
....*....|....*.
gi 2462506005 343 MKLMEMK-DLENHNSQ 357
Cdd:PRK02224 328 DRLEECRvAAQAHNEE 343
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-359 |
6.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQR---EKNNVE---QDLKEKEDTIKQRTSE----VQDLQD----EVQRENTNLQKLQAQKQQVQELL 247
Cdd:PRK03918 314 KRLSRLEEEINGIEErikELEEKEerlEELKKKLKELEKRLEEleerHELYEEakakKEELERLKKRLTGLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 248 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQET 310
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKEL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462506005 311 AELEESVESGKAQLEPLQQHLQDsQQEISSMQMKLMEMKDLENHNSQLN 359
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYN 516
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
185-354 |
6.72e-05 |
|
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: 46.04 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 185 DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEV 264
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 265 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQEISSMQMK 344
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEE 259
|
170
....*....|
gi 2462506005 345 LMEMKDLENH 354
Cdd:pfam07888 260 LSSMAAQRDR 269
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-338 |
8.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREknNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLK 262
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDADDLEERAEELREEAA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506005 263 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 338
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
179-366 |
9.80e-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: 46.12 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKAQLE 258
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL----------SEAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKcAEEAQLISSLKAELTSQESqistYEEELAKAREELS--RLQQETAELEESVESGKAQLEPLQQHLQDSQQ 336
Cdd:TIGR00618 623 PEQDLQDVR-LHLQQCSQELALKLTALHA----LQLTLTQERVREHalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
170 180 190
....*....|....*....|....*....|..
gi 2462506005 337 EISSMQMKLMEMKDLENHNSQL--NWCSSPHS 366
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREfnEIENASSS 729
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-317 |
1.21e-04 |
|
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: 45.40 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQL 261
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---------------------IEEKEKKISSLEKEL 619
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESV 317
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
251-351 |
1.28e-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: 42.67 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQ------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ 323
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100
....*....|....*....|....*...
gi 2462506005 324 LEPLQQHLQDSQQEISSMQMKLMEMKDL 351
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNSSLENL 109
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
189-348 |
1.37e-04 |
|
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: 43.97 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 189 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQV-QELLDELDEQKAQLEEQLKEVRK- 266
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEALDLQQFf 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 267 -KCAEEAQLISSLKAELTSQE------------SQISTYEEELAKAREELSRLQQETAELEESVESG-----KAQLEPLQ 328
Cdd:cd00176 113 rDADDLEQWLEEKEAALASEDlgkdlesveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDadeeiEEKLEELN 192
|
170 180
....*....|....*....|
gi 2462506005 329 QHLQDSQQEISSMQMKLMEM 348
Cdd:cd00176 193 ERWEELLELAEERQKKLEEA 212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
190-355 |
1.50e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 190 EIVDLQREKNNVEQDLkEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR---- 265
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 266 ---KKCAEEAQL-----ISSLKAELTSQESQISTYEEELakarEELSRLQQETAELEESV---ESGKAQLEPLQQHLQD- 333
Cdd:PRK02224 652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVealEALYDEAEELESMYGDl 727
|
170 180
....*....|....*....|....*.
gi 2462506005 334 ----SQQEISSMQMKLMEMKDLENHN 355
Cdd:PRK02224 728 raelRQRNVETLERMLNETFDLVYQN 753
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
246-345 |
1.71e-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: 43.36 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSlkaelTSQESQISTyeEELAKAREELSRLQQETAELE---ESVESGKA 322
Cdd:pfam13851 21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSE-----IQQENKRLT--EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92
|
90 100
....*....|....*....|...
gi 2462506005 323 QLEPLQQHLQDSQQEISSMQMKL 345
Cdd:pfam13851 93 RLKVLEKELKDLKWEHEVLEQRF 115
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
253-359 |
1.72e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQ 329
Cdd:COG1566 88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELDEARAALDAAQA 162
|
90 100 110
....*....|....*....|....*....|
gi 2462506005 330 HLQDSQQEISSMQMKLMEMKDLENHNSQLN 359
Cdd:COG1566 163 QLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
182-355 |
1.85e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 261
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKK---CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ------ 332
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQglrkde 413
|
170 180
....*....|....*....|....*
gi 2462506005 333 -DSQQEISSMQMKLMEMK-DLENHN 355
Cdd:PRK04778 414 lEAREKLERYRNKLHEIKrYLEKSN 438
|
|
| DUF1090 |
pfam06476 |
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ... |
253-338 |
1.91e-04 |
|
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of unknown function and is known as YqjC in E. coli.
Pssm-ID: 428965 [Multi-domain] Cd Length: 109 Bit Score: 41.46 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 331
Cdd:pfam06476 39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100
|
....*..
gi 2462506005 332 QDSQQEI 338
Cdd:pfam06476 101 AEARQEL 107
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
182-353 |
1.97e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQdLKEKEDTIKQRTSEVQ----DLQDEVQREN----TNLQKLQAQKQQVQELL----DE 249
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKqqafALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLrqrlEQ 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 250 LDEQKAQLEEQLKEVRKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlEPLQ 328
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---DELH 1066
|
170 180
....*....|....*....|....*....
gi 2462506005 329 QHLQDSQQEISSMQMKL----MEMKDLEN 353
Cdd:PRK04863 1067 ARLSANRSRRNQLEKQLtfceAEMDNLTK 1095
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
255-358 |
2.30e-04 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 43.02 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 255 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 333
Cdd:cd16855 4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
|
90 100
....*....|....*....|....*.
gi 2462506005 334 SQQEISSMQMKLME-MKDLENHNSQL 358
Cdd:cd16855 80 KAQELLQLRMELADkFKKTIQLLSKL 105
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
198-343 |
2.32e-04 |
|
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: 43.22 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 198 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaEEAQL--- 274
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLkke 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506005 275 ------ISSLKAeltSQESQISTYEEELAKAREELSRLQQETaeleesvesgKAQLEPLQQHLQDSQQEISSMQM 343
Cdd:pfam14988 70 lqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
249-322 |
2.44e-04 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 43.44 E-value: 2.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506005 249 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 322
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
286-359 |
2.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506005 286 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 359
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELG 89
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
194-337 |
3.03e-04 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 42.13 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 194 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEeaq 273
Cdd:pfam16789 30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTSDK------------ILQMKRYIKVVKERLKQEEKKVQD--- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506005 274 lisslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 337
Cdd:pfam16789 95 -----------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQD 147
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
181-350 |
3.11e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVE-----QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKA 255
Cdd:pfam13868 132 IDEFNEEQAEWKELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QlEEQLKEVRKKCAEEAQLISSLKAELT-SQESQIS----TYEEELAKAREELSRLQQETAELEEsvesgKAQLEPLQQH 330
Cdd:pfam13868 212 Q-EEQERKERQKEREEAEKKARQRQELQqAREEQIElkerRLAEEAEREEEEFERMLRKQAEDEE-----IEQEEAEKRR 285
|
170 180
....*....|....*....|....*..
gi 2462506005 331 LQDSQ--QEISSM-----QMKLMEMKD 350
Cdd:pfam13868 286 MKRLEhrRELEKQieereEQRAAEREE 312
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
196-337 |
3.37e-04 |
|
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: 41.06 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 196 REKNnvEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQ--KAQLEEQLKEVRKKCAEEAq 273
Cdd:pfam20492 1 REEA--EREKQELEERLKQYEEETKKAQEELEES--------------EETAEELEEErrQAEEEAERLEQKRQEAEEE- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506005 274 lisslKAELtsQESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 337
Cdd:pfam20492 64 -----KERL--EESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
252-358 |
3.51e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 252 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-------- 323
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462506005 324 --LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:PRK04863 610 daLARLREQsgeeFEDSQDVTEYMQQLLERERELTVERDEL 650
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-432 |
3.64e-04 |
|
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: 43.95 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLK-----------EKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL 250
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 DEQ----KAQLE------EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREEL----SRLQQETAELEES 316
Cdd:pfam15921 733 QKQitakRGQIDalqskiQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLrsqeRRLKEKVANMEVA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 317 VESGKAQLEPLQQHLQDSQQEisSMQMKL---MEMKDLENHNSQLNWCSSPHSILVNGATDYCSLSTSSSETANLNEHVE 393
Cdd:pfam15921 813 LDKASLQFAECQDIIQRQEQE--SVRLKLqhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHS 890
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462506005 394 GQSNlesepIHQESPARSSPELLP---SGVTDENEVTTAVTE 432
Cdd:pfam15921 891 RKTN-----ALKEDPTRDLKQLLQelrSVINEEPTVQLSKAE 927
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
162-338 |
3.95e-04 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 43.02 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 162 RASLQKNII--GSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQ 239
Cdd:pfam15397 41 RKLLQQYEKfgTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKDKEYPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 240 KQQVQELL------------DELDEqkaqLEEQLKEVRKKCAEEAQLISslKAELTS-QESQISTYEEEL-AKARE---- 301
Cdd:pfam15397 118 KAVQIANLvrqlqqlkdsqqDELDE----LEEMRRMVLESLSRKIQKKK--EKILSSlAEKTLSPYQESLlQKTRDnqvm 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462506005 302 --ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 338
Cdd:pfam15397 192 lkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
245-354 |
4.35e-04 |
|
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: 43.08 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 313
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462506005 314 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 354
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
245-352 |
4.36e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 324
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100
....*....|....*....|....*...
gi 2462506005 325 EPLQQHLQDSQQEISSMQMKLMEMKDLE 352
Cdd:COG1340 88 NELREELDELRKELAELNKAGGSIDKLR 115
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
181-337 |
4.65e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDE 252
Cdd:TIGR00618 713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQF 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHL 331
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQA 869
|
....*.
gi 2462506005 332 QDSQQE 337
Cdd:TIGR00618 870 KIIQLS 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-318 |
4.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTiKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDE-----QKA- 255
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506005 256 QLEEQLKEVRKKCAEEAqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 318
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
182-339 |
4.70e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKnnveqDLKEKEDTIKQRTSEVQdLQdEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQL 261
Cdd:pfam15905 152 KKMSSLSMELMKLRNKL-----EAKMKEVMAKQEGMEGK-LQ-VTQKN-----------------LEHSKGKVAQLEEKL 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 262 KEVRKKCAEEaqlisslkaelTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 339
Cdd:pfam15905 208 VSTEKEKIEE-----------KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-358 |
4.78e-04 |
|
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: 43.57 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD----ELDEQKAQ- 256
Cdd:pfam15921 349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDhlrrELDDRNMEv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 257 --LEEQLKEVRKKCA--------------EEAQLISSLKAELTSQesqistyEEELAKAREELSRLQQETAELEESVESG 320
Cdd:pfam15921 429 qrLEALLKAMKSECQgqmerqmaaiqgknESLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTLESSERTVSDL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462506005 321 KAQLEPLQQHLQDSQQEISSMQ----MKLMEMKDLENHNSQL 358
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRsrvdLKLQELQHLKNEGDHL 543
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
177-354 |
4.84e-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: 43.56 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 177 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDE 249
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQ-------LEEKTKLQDENLKE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 250 LDEQKAQLEEQLKEVR----------KKCAEEAQLISSLKAELTSQ-ESQIstyeEELAKAREE----LSRLQQETAELE 314
Cdd:pfam05483 287 LIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAhsfvVTEFEATTCSLE 362
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462506005 315 ESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 354
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
259-358 |
4.90e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 40.46 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 338
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100
....*....|....*....|
gi 2462506005 339 SSMqmkLMEMKDLENHNSQL 358
Cdd:pfam04871 77 DDL---LLLLGDLEEKVEKY 93
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
245-347 |
5.12e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 41.36 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgk 321
Cdd:COG2825 33 RILQESPEGKaaqKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLS--EEERQKKERELQKKQQE------------ 98
|
90 100
....*....|....*....|....*.
gi 2462506005 322 aqlepLQQHLQDSQQEISSMQMKLME 347
Cdd:COG2825 99 -----LQRKQQEAQQDLQKRQQELLQ 119
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
184-359 |
5.13e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 184 LDTLNnEIVDLQREKNNVEQDLKEKEDTIKQRtsevqdlqDEVQRENtnlqklqaqkqqvqellDELDEQKAQLEEQLKE 263
Cdd:PRK11281 45 LDALN-KQKLLEAEDKLVQQDLEQTLALLDKI--------DRQKEET-----------------EQLKQQLAQAPAKLRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 264 VRKKcaeeaqlISSLKAELTSQESQ------ISTYEEELAKAREELSRLQQETAELEesvesgkAQLEPLQQHLQDSQQE 337
Cdd:PRK11281 99 AQAE-------LEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYN-------SQLVSLQTQPERAQAA 164
|
170 180
....*....|....*....|..
gi 2462506005 338 ISSMQMKLMEMkdlenhNSQLN 359
Cdd:PRK11281 165 LYANSQRLQQI------RNLLK 180
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-353 |
5.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 196 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQL 274
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 275 ISSLKAELTSQESQISTYEEELAKARE----------ELSRLQQETAELE-----------ESVESGKAQLEPLQQH--- 330
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEyle 606
|
170 180
....*....|....*....|...
gi 2462506005 331 LQDSQQEIssmQMKLMEMKDLEN 353
Cdd:PRK03918 607 LKDAEKEL---EREEKELKKLEE 626
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
181-350 |
5.83e-04 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 42.38 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 258
Cdd:pfam16591 42 QKKLDELKQQLQQLKTTFTSPEnvRLLQEQLQLIQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVrkkcAEEAQLISSLKAEL-------------TSQES------QISTYEEELAKAREEL-----SRLQQETAELE 314
Cdd:pfam16591 122 EADSRR----AAQYQAISELKRQVqmaryqvrgytftPNEDSeqaayqQLDAALASLDQLRQALagdpgAALQQLTSALQ 197
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462506005 315 E---SVEsgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:pfam16591 198 GyrdALD----TFKAAVAAIEQARQEMTSQGDEIVRISD 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-359 |
5.93e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 202 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 281
Cdd:pfam01576 4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 282 -------LTSQESQISTYEEELAKAREELSRLQQETAELEEsvesgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD---- 350
Cdd:pfam01576 70 kqeleeiLHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE-------QLDEEEAARQKLQLEKVTTEAKIKKLEEdill 142
|
....*....
gi 2462506005 351 LENHNSQLN 359
Cdd:pfam01576 143 LEDQNSKLS 151
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
190-342 |
6.16e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 190 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA 269
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506005 270 EEAQLISSlKAELTSQESQIstyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:PRK01156 661 EIDSIIPD-LKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
183-337 |
6.32e-04 |
|
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: 43.40 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqkLQAQKQQVQELLDELDEQKAQLEE 259
Cdd:COG3096 837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 QLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEelakAREELSRLQQETAELEESVE-------SGKAQL----- 324
Cdd:COG3096 908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983
|
170
....*....|....*.
gi 2462506005 325 ---EPLQQHLQDSQQE 337
Cdd:COG3096 984 dlnEKLRARLEQAEEA 999
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
193-352 |
6.38e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 193 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE---EQLKEVRKKCA 269
Cdd:pfam07888 168 EEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERLN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 270 EEAQLISSLKAELTSQESQISTYEEELAKAR------------------EELSRLQQETAELEESVESGKAQLEPLQQHL 331
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltlqladaslalrEGRARWAQERETLQQSAEADKDRIEKLSAEL 327
|
170 180
....*....|....*....|.
gi 2462506005 332 QDSQQeisSMQMKLMEMKDLE 352
Cdd:pfam07888 328 QRLEE---RLQEERMEREKLE 345
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
165-357 |
6.43e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 165 LQKNIIGSSP----VADFSAIKELDTL-------NNEIVDLQREKNNVEQD---LKEKEDTIKQRTSEVQDLQDEVQREN 230
Cdd:PRK01156 117 IEKNILGISKdvflNSIFVGQGEMDSLisgdpaqRKKILDEILEINSLERNydkLKDVIDMLRAEISNIDYLEEKLKSSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 231 TNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQET 310
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSSLEDMKNRYESEIKTAESDLSMELEKN 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 311 AELEESVE---------------------SGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQ 357
Cdd:PRK01156 273 NYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYND 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
189-325 |
6.84e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 189 NEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLEEQLKEVRKKc 268
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELA-------EEAQELHEEMIELYKEADELRKE- 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 269 AEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 325
Cdd:COG1340 211 ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
182-347 |
6.90e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 261
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR--------------EKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAREELSRL--QQET---------------AELEESVESGKAQL 324
Cdd:COG1340 81 DELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLewRQQTevlspeeekelvekiKELEKELEKAKKAL 156
|
170 180
....*....|....*....|...
gi 2462506005 325 EpLQQHLQDSQQEISSMQMKLME 347
Cdd:COG1340 157 E-KNEKLKELRAELKELRKEAEE 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
280-359 |
7.38e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 280 AELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL----MEMKDLENHN 355
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEI 92
|
....
gi 2462506005 356 SQLN 359
Cdd:COG4942 93 AELR 96
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
245-359 |
7.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 324
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462506005 325 EPLQ-------------QHLQDSQQ--------------EISSMQMKLMEMKDLENHNSQLN 359
Cdd:COG1340 102 AELNkaggsidklrkeiERLEWRQQtevlspeeekelveKIKELEKELEKAKKALEKNEKLK 163
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
277-358 |
7.69e-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: 39.09 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 277 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqleplqqHLQDsqqEISSMQM--KLME--MKDLE 352
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANE-----------ILND---ELIALQIenNLLEekLRKLQ 66
|
....*.
gi 2462506005 353 NHNSQL 358
Cdd:cd22887 67 EENDEL 72
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
182-345 |
7.84e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKN----NVEQDLKEKEDTIKQRTS---EVQDLQDEVQRentnlqklQAQKQQVQELLDELDEQK 254
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNrrrsKIKEQNNRDIAGIKDKLAkirEARDRQLAVAE--------DDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 255 AQLEEQLKEVRKKCAEE------AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 328
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS 512
|
170
....*....|....*..
gi 2462506005 329 QHLQDSQQEISSMQMKL 345
Cdd:pfam12128 513 RRLEERQSALDELELQL 529
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
256-358 |
8.02e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEVRKKCAEEAQLISslKAELtsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE---PLQQHLQ 332
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLG--LAPG--RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAK 785
|
90 100
....*....|....*....|....*.
gi 2462506005 333 DSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQ 811
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
245-351 |
1.10e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES----- 319
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrar 290
|
90 100 110
....*....|....*....|....*....|..
gi 2462506005 320 GKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 351
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
260-343 |
1.10e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 QLKEVRKKCAE-------EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVesgkAQLEplQQhlQ 332
Cdd:PRK11637 48 QLKSIQQDIAAkeksvrqQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASI----AKLE--QQ--Q 119
|
90
....*....|.
gi 2462506005 333 DSQQEISSMQM 343
Cdd:PRK11637 120 AAQERLLAAQL 130
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
187-358 |
1.12e-03 |
|
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: 42.40 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 187 LNNEI---------VDLQREKNNVEQDLKEKEDTIKqrtseVQDLQDEVQRE-NTNLQKLQAQKQQVQE----------L 246
Cdd:pfam05483 188 LNNNIekmilafeeLRVQAENARLEMHFKLKEDHEK-----IQHLEEEYKKEiNDKEKQVSLLLIQITEkenkmkdltfL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQ-------LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-AELEES-- 316
Cdd:pfam05483 263 LEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELnk 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462506005 317 --------VESGKAQLEPLQQHLQDSQQ--EISSMQMKLMEMkDLENHNSQL 358
Cdd:pfam05483 343 akaahsfvVTEFEATTCSLEELLRTEQQrlEKNEDQLKIITM-ELQKKSSEL 393
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
245-358 |
1.25e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 324
Cdd:COG0542 411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462506005 325 EPLQ---QHLQDSQQEISSMQMKLMEMKDLENHNSQL 358
Cdd:COG0542 471 EEIQelkEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
259-351 |
1.43e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKCAEEAQLisslKAELTSQEsqISTYEEELAKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDS 334
Cdd:pfam07111 484 EQLREERNRLDAELQL----SAHLIQQE--VGRAREQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQES 557
|
90
....*....|....*..
gi 2462506005 335 QQEISSMQMKLMEMKDL 351
Cdd:pfam07111 558 TEEAASLRQELTQQQEI 574
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
176-353 |
1.47e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 176 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTIKQ-RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 253
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 254 --------KAQLEE----QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK 321
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQL 258
|
170 180 190
....*....|....*....|....*....|...
gi 2462506005 322 AQLEPLQQHLQDSQQEI-SSMQMKLMEMKDLEN 353
Cdd:pfam00038 259 ADYQELISELEAELQETrQEMARQLREYQELLN 291
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
187-350 |
1.58e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 187 LNNEIVD-----LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLE 258
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 259 EQLKEVRKKCAEEAQlisslkaeltsqesqistyeEELAKAREELSRLQQETAELE-ESVESGKAQ-LEPLQQHLQDSQQ 336
Cdd:PRK00409 562 EEEDKLLEEAEKEAQ--------------------QAIKEAKKEADEIIKELRQLQkGGYASVKAHeLIEARKRLNKANE 621
|
170
....*....|....
gi 2462506005 337 EISSMQMKLMEMKD 350
Cdd:PRK00409 622 KKEKKKKKQKEKQE 635
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
201-353 |
1.66e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 41.07 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 201 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELDE---QKAQLEEQLKEVRKKCAEEAQLI 275
Cdd:pfam13949 98 VRSKFREHEEDLELLSGPDEDLEAFLpsSRRAKNSPSVEEQVAKLRELLNKLNElkrEREQLLKDLKEKARNDDISPKLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 276 SSLKAEL-TSQESQIstYEEELAKAREELSRLQQETA---ELEESVESGKAQLEPLQQHLQDSQQEISSMqmklmeMKDL 351
Cdd:pfam13949 178 LEKARLIaPNQEEQL--FEEELEKYDPLQNRLEQNLHkqeELLKEITEANNEFLQDKRVDSEKQRQREEA------LQKL 249
|
..
gi 2462506005 352 EN 353
Cdd:pfam13949 250 EN 251
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
205-342 |
1.72e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 205 LKEKEDTIKQR-TSEVQDLQDEVQRENTnlqklqAQKQQVQELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 279
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESA------EQMKSAGERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506005 280 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
258-343 |
1.74e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQE 337
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-DSEKQ 130
|
....*.
gi 2462506005 338 ISSMQM 343
Cdd:PRK09039 131 VSARAL 136
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
182-345 |
1.87e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 39.90 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQdeVQRENTnlqklqaqkqqvqELLDELDEQKAQLEE-- 259
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQEKLEQKEE-LGEGLTMIDFLQ--LQIENQ-------------ALNEKIEERNKELKRlk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 --------QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESveSG----------- 320
Cdd:pfam13870 70 lkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvpallhdy 147
|
170 180
....*....|....*....|....*...
gi 2462506005 321 ---KAQLEPLQQHLQDSQQEISSMQMKL 345
Cdd:pfam13870 148 dktKAEVEEKRKSVKKLRRKVKILEMRI 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-342 |
1.90e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 139 SQKLIKGIDPPHVLTPEMIPPSDRASLQkniigsspvadfsAIKELDTLNNEIVD-------LQREKNNVEQDLKEKEDT 211
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERARRQ-------------AQQERDELADEIASgasgksaLQDEKRRLEARIAQLEEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 212 IKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQLISSLKAELTSQESQIS 290
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIA 977
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506005 291 TYEEEL---AKAREELSRL------------------QQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 342
Cdd:pfam01576 978 QLEEQLeqeSRERQAANKLvrrtekklkevllqvedeRRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
177-427 |
1.91e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 177 DFSAIKELDTLNNEIVDLQR----EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldelde 252
Cdd:TIGR00606 686 VFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL------------------------ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 qkaqLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREE----LSRLQQETAELEESVESGKAQLE- 325
Cdd:TIGR00606 742 ----KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTdvtiMERFQMELKDVERKIAQQAAKLQg 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 326 --------PLQQHLQDSQQEISSMQMKLMEMKDL-ENHNSQLNWCSSPHSILvngATDYCSLSTSSSETANLNEHVEGQS 396
Cdd:TIGR00606 818 sdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLiQDQQEQIQHLKSKTNEL---KSEKLQIGTNLQRRQQFEEQLVELS 894
|
250 260 270
....*....|....*....|....*....|.
gi 2462506005 397 NLESEPIHQESPARSspELLPSGVTDENEVT 427
Cdd:TIGR00606 895 TEVQSLIREIKDAKE--QDSPLETFLEKDQQ 923
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
294-343 |
1.95e-03 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 37.57 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462506005 294 EELAKAREELSRLQQE---TAELEESVESGKAQLEPLQQHLQDSQQEIssMQM 343
Cdd:cd22248 27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
247-359 |
2.02e-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: 40.36 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKaQLEEQLKEVRKKcAEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQeTAELEESVESGKA 322
Cdd:pfam12795 2 LDELEKAK-LDEAAKKKLLQD-LQQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASL 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462506005 323 QLEPLQQHLQDSQQEISSMQmklmemKDLENHNSQLN 359
Cdd:pfam12795 79 SLEELEQRLLQTSAQLQELQ------NQLAQLNSQLI 109
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
182-327 |
2.02e-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: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQR----------ENTNLQKLQAQKQQVQELLD 248
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA---REELSRLQQetaeLEESVESGKAQLE 325
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER----LKEEIEKSSKQRA 656
|
..
gi 2462506005 326 PL 327
Cdd:TIGR00606 657 ML 658
|
|
| Nnf1 |
pfam03980 |
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ... |
245-320 |
2.10e-03 |
|
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.
Pssm-ID: 461118 Cd Length: 103 Bit Score: 38.38 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 318
Cdd:pfam03980 33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101
|
..
gi 2462506005 319 SG 320
Cdd:pfam03980 102 AQ 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-313 |
2.11e-03 |
|
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: 41.58 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLk 262
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL- 945
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462506005 263 evrkkcAEEAQLisslkaELTSQESQISTYEEELAKAREELSRLQQETAEL 313
Cdd:TIGR02168 946 ------SEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
192-354 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 192 VDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEEQLKEvRKKCAEE 271
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK-------TNELKSEKLQIGTNLQR-RQQFEEQ 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 272 AQLISSlkaELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQlepLQQHLQDSQQEISSmqmKLMEMKDL 351
Cdd:TIGR00606 890 LVELST---EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK---AQDKVNDIKEKVKN---IHGYMKDI 960
|
...
gi 2462506005 352 ENH 354
Cdd:TIGR00606 961 ENK 963
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
189-308 |
2.31e-03 |
|
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: 38.77 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 189 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKc 268
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462506005 269 AEEAQliSSLKAELTSQESQISTYEEELAKAREELSRLQQ 308
Cdd:pfam07926 80 AESAK--AELEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| End3 |
pfam12761 |
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ... |
172-307 |
2.31e-03 |
|
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the sequential recruitment at endocytic sites of proteins that drive cargo sorting, membrane invagination and vesicle release. End3p is part of the coat module protein complex Pan1, along with Pan1p, Sla1p, and Sla2p. The proteins in this complex are regulated by phosphorylation events. End3p also regulates the cortical actin cytoskeleton. The subunits of the Pan1 complex are homologous to mammalian intersectin.
Pssm-ID: 432765 [Multi-domain] Cd Length: 200 Bit Score: 39.98 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 172 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE---VQREntnlqklqaqkqqvqelLD 248
Cdd:pfam12761 84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGGNRDESSKpalVKRE-----------------FE 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ELDEQKaqlEEQLKEVRK-KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ 307
Cdd:pfam12761 144 QLLDYK---ERQLRELEEgSGKSKPINLKSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
246-350 |
2.43e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 38.73 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKAQLEEQ-------LKEVRKKCAEEaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsve 318
Cdd:pfam17675 10 LLEELDKQLEDAEKErdayisfLKKLEKETPEE---LEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEE--- 83
|
90 100 110
....*....|....*....|....*....|..
gi 2462506005 319 sgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 350
Cdd:pfam17675 84 ----ELEALDEEEEEFWREYNALQLQLLEFQD 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
202-342 |
2.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 202 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA- 280
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAr 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506005 281 --ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqdsQQEISSMQ 342
Cdd:PRK04863 595 iqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL---DEEIERLS 665
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
245-347 |
2.61e-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: 38.71 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELtsqESQISTYEEELAKAREELSRLQQEtaeleesvesgk 321
Cdd:pfam03938 9 KILEESPEGKaaqAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQE------------ 73
|
90 100
....*....|....*....|....*.
gi 2462506005 322 aqlepLQQHLQDSQQEISSMQMKLME 347
Cdd:pfam03938 74 -----LQQLQQKAQQELQKKQQELLQ 94
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
246-349 |
2.67e-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: 41.17 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 246 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELEESVESGK 321
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEEAKSLAQ 401
|
90 100 110
....*....|....*....|....*....|.
gi 2462506005 322 AQLEPLQQHLQDSQQ---EISSMQMKLMEMK 349
Cdd:pfam05701 402 AAREELRKAKEEAEQakaAASTVESRLEAVL 432
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
193-315 |
2.75e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 38.53 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 193 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEA 272
Cdd:pfam04871 5 ELESEASSLKNENTELKAELQELSKQYNSLEQK------------------ESQAKELEAEVKKLEEALKKLKAELSEEK 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462506005 273 QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 315
Cdd:pfam04871 67 QKEKEKQSELDDLLLLLGDLEEKVEKYKARLKELGEEVLSDDE 109
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
159-360 |
2.82e-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: 40.43 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 159 PSDRASLQK--NIIGSSPVADFSAIKEL---------------DTLNNEIVDLQREKNNVEQDlkeKEDTIKQRTSEVQD 221
Cdd:cd22656 22 PTTEEEYRKrlGISSDIDDKLSSDFDPLldayksikdhctdfkDDTYPSIVSLAGDIYNYAQN---AGGTIDSYYAEILE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 222 LQDEVQrENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKA 299
Cdd:cd22656 99 LIDDLA-DATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462506005 300 REELSRLQQETAEL-EESVESGKAQLEPLQQHLQDSQQEIssmQMKLMEMKDLENHNSQLNW 360
Cdd:cd22656 178 RKEIKDLQKELEKLnEEYAAKLKAKIDELKALIADDEAKL---AAALRLIADLTAADTDLDN 236
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
198-359 |
2.85e-03 |
|
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: 39.50 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 198 KNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaeeaqli 275
Cdd:pfam13851 22 RNNLEliKSLKEEIAELKKKEERNEKLMSEIQQENKRLT----------EPLQKAQEEVEELRKQLENYEK--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 276 ssLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE-PLQQHLQDSQQEISSMQMKLMEM-KDLEN 353
Cdd:pfam13851 83 --DKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEaAIQDVQQKTGLKNLLLEKKLQALgETLEK 160
|
....*.
gi 2462506005 354 HNSQLN 359
Cdd:pfam13851 161 KEAQLN 166
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-341 |
2.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 324
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
90
....*....|....*..
gi 2462506005 325 EPLQQHLQDSQQEISSM 341
Cdd:COG1196 763 EELERELERLEREIEAL 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-350 |
2.98e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDE-------QKA 255
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAE--------------TELCAEAEEmrarlaaRKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 335
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS 151
|
170
....*....|....*
gi 2462506005 336 QEISSMQMKLMEMKD 350
Cdd:pfam01576 152 KERKLLEERISEFTS 166
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
249-337 |
3.03e-03 |
|
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: 38.87 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ELDEQKAQLEEQLK----EVRKKCAEEAQLissLKAELTSQESQISTYEEELAK-----AREELSRLQQ--ETAELEESV 317
Cdd:pfam05672 36 EKEEEERLRKEELRrraeEERARREEEARR---LEEERRREEEERQRKAEEEAEereqrEQEEQERLQKqkEEAEAKARE 112
|
90 100
....*....|....*....|
gi 2462506005 318 ESGKAQLEpLQQHLQDSQQE 337
Cdd:pfam05672 113 EAERQRQE-REKIMQQEEQE 131
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
257-359 |
3.09e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 257 LEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 336
Cdd:COG2433 378 IEEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455
|
90 100
....*....|....*....|...
gi 2462506005 337 EISSMQMKLMEMKDLENHNSQLN 359
Cdd:COG2433 456 EERREIRKDREISRLDREIERLE 478
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
187-344 |
3.19e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 187 LNNEIVDLQREKNNVEQDLKEKE-DTIK------QRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEE 259
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEgKNIKlskdvsSLESQLQDTQELLQEETRQKLNLSTR-------LRQLEDERNSLQE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 260 QL-KEVRKKCAEEAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL- 331
Cdd:pfam01576 504 QLeEEEEAKRNVERQLstlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELd 583
|
170
....*....|....*....
gi 2462506005 332 -----QDSQ-QEISSMQMK 344
Cdd:pfam01576 584 dllvdLDHQrQLVSNLEKK 602
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
182-315 |
3.63e-03 |
|
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.
Pssm-ID: 407241 [Multi-domain] Cd Length: 360 Bit Score: 40.17 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDeqkaQLEEQL 261
Cdd:pfam17097 133 DTLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECW-----------------ELLNELE----RLRDQR 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462506005 262 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 315
Cdd:pfam17097 192 ITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEK 245
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
250-336 |
3.69e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 250 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 300
Cdd:COG3096 295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462506005 301 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 336
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
245-355 |
3.70e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 39.42 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 319
Cdd:pfam06785 58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462506005 320 ------GKAQLEPLQQHLQDSQQEISSmQMKLMEMKDLENHN 355
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEE-QRSVLEKRQDQIEN 175
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
281-347 |
3.80e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.48 E-value: 3.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 281 ELTSQ-ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 347
Cdd:pfam06005 4 ELLEQlETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-329 |
3.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQ----- 256
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikslk 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 257 ------------LEEQLKEVRKKCAEEAQLISSLKA------------------------ELTSQESQISTYEEELAKAR 300
Cdd:PRK03918 546 kelekleelkkkLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKKLE 625
|
170 180
....*....|....*....|....*....
gi 2462506005 301 EELSRLQQETAELEESVESGKAQLEPLQQ 329
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
176-349 |
3.85e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 40.66 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 176 ADFSAIKEL---DTLNNEivdLQREKNNVEQDLKEKEDtikQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDE 252
Cdd:pfam15964 347 ANFEKTKALiqcEQLKSE---LERQKERLEKELASQQE---KRAQEKEALRKEMKKEREELGAT----------MLALSQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 253 QKAQLEEQLKEVRKkcaEEAQLISSLKA---ELTSQESQISTYEEELakaREELSRLQQETAELEESVESGKAQlepLQQ 329
Cdd:pfam15964 411 NVAQLEAQVEKVTR---EKNSLVSQLEEaqkQLASQEMDVTKVCGEM---RYQLNQTKMKKDEAEKEHREYRTK---TGR 481
|
170 180
....*....|....*....|
gi 2462506005 330 HLQDSQQEISSMQMKLMEMK 349
Cdd:pfam15964 482 QLEIKDQEIEKLGLELSESK 501
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
182-366 |
4.30e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNE----IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQL 257
Cdd:pfam01576 176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE--------------LQAQIAELRAQLAKK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 258 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE------PLQQHL 331
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQQEL 321
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462506005 332 QDS-QQEISSMQMKLMEmkDLENHNSQLNWCSSPHS 366
Cdd:pfam01576 322 RSKrEQEVTELKKALEE--ETRSHEAQLQEMRQKHT 355
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
182-353 |
4.33e-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: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 182 KELDTLNNEIVDLQREKNNVEQDLKEKEDTI----------KQRTSEvqDL-QDEVQRentnlqklqaqkqqvqELLDEL 250
Cdd:pfam03148 64 KELEELDEEIELLLEEKRRLEKALEALEEPLhiaqecltlrEKRQGI--DLvHDEVEK----------------ELLKEV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 D----------EQKAQLEEQL---KEVRKKCA------EEAQLI----------S---SLKAELTSQESQISTYEE---- 294
Cdd:pfam03148 126 EliegiqellqRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEwekf 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 295 ----------ELAKA---REELSRLQQETAELEES---------------VESGKAQLEplqQHLQDSQQEISSMQmklM 346
Cdd:pfam03148 206 tqdnieraekERAASaqlRELIDSILEQTANDLRAqadavnfalrkrieeTEDAKNKLE---WQLKKTLQEIAELE---K 279
|
....*..
gi 2462506005 347 EMKDLEN 353
Cdd:pfam03148 280 NIEALEK 286
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
252-358 |
4.39e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 252 EQKAQLEEQLKEVRKK-----------CAEE-----AQLISS--LKAELTSQESQISTYEEELAKAREELSRLQQETAEL 313
Cdd:PRK10246 380 EQLRQWQQQLTHAEQKlnalpaitltlTADEvaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462506005 314 EESVESGKAQLEPLQQHLQD----SQQEissmqmklMEMKDLENHNSQL 358
Cdd:PRK10246 460 NAALNEMRQRYKEKTQQLADvktiCEQE--------ARIKDLEAQRAQL 500
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
191-352 |
4.60e-03 |
|
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: 39.90 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 191 IVDLQ-REKNNVEQDLKEKEDTIKQRTSE--VQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLKEvRKK 267
Cdd:pfam13868 23 ERDAQiAEKKRIKAEEKEEERRLDEMMEEerERALEEEEEKE--------------EERKEERKRYRQELEEQIEE-REQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 268 CAEEAQLISSLKAELTsQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqlepLQQHLQDSQQEissmQMKLME 347
Cdd:pfam13868 88 KRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWKELEKE----EEREED 154
|
....*
gi 2462506005 348 MKDLE 352
Cdd:pfam13868 155 ERILE 159
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
181-307 |
4.65e-03 |
|
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: 39.71 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 181 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE- 259
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAt 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462506005 260 --QLKEVRK-KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ 307
Cdd:pfam00529 161 vaQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
245-359 |
4.66e-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: 38.06 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSlKAELTSQESQISTYEEELAKAREELSRLQQetaeleesvesgkaQL 324
Cdd:TIGR02473 27 AEFERLETQLQQLIKYREEYEQQALEKVGAGTS-ALELSNYQRFIRQLDQRIQQQQQELALLQQ--------------EV 91
|
90 100 110
....*....|....*....|....*....|....*
gi 2462506005 325 EPLQQHLQDSQQEIssMQMKLMEMKDLENHNSQLN 359
Cdd:TIGR02473 92 EAKRERLLEARREL--KALEKLKEKKQKEYRAEEA 124
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
140-409 |
4.85e-03 |
|
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: 40.48 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 140 QKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVAdfsaIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTI---- 212
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifll 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 213 KQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLE-EQLKEVrkKCAEEAQLISSLKAELTSQES---- 287
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEE----------HYLKEVEDLKTELEkEKLKNI--ELTAHCDKLLLENKELTQEASdmtl 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 288 QISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIssmQMKLmemkdlenHNSQLNWCSSPHSI 367
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKL--------DKSEENARSIEYEV 582
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462506005 368 LVNGAtdycSLSTSSSETANLNEHVEGQSNlESEPIHQESPA 409
Cdd:pfam05483 583 LKKEK----QMKILENKCNNLKKQIENKNK-NIEELHQENKA 619
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
194-358 |
4.96e-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: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 194 LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQ--DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC 268
Cdd:TIGR00618 641 LALKLTALHAlqlTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 269 AEEAQLISSLKAELTSQES-----------------QISTYEEELAKARE--------ELSRLQQETA----ELEESVES 319
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDalnqslkelmhqartvlKARTEAHFNNNEEVtaalqtgaELSHLAAEIQffnrLREEDTHL 800
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462506005 320 GKAQLEPLQQHLQDSQQEISSMQMKLmeMKDLENHNSQL 358
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNLQCETL--VQEEEQFLSRL 837
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
190-349 |
5.02e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.12 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 190 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD---ELDEQKAQLEE--QLKEV 264
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDtmqHLQEDRADLQAtvELLQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 265 R------------KKCAEEAQLISSLKAELTSQ-ESQISTYEEEL------AKA-----REELSRLQQETAELEESVESG 320
Cdd:pfam07111 271 RvqslthmlalqeEELTRKIQPSDSLEPEFPKKcRSLLNRWREKVfalmvqLKAqdlehRDSVKQLRGQVAELQEQVTSQ 350
|
170 180 190
....*....|....*....|....*....|.
gi 2462506005 321 KAQLEPLQQHLQD--SQQEISSMQMKLMEMK 349
Cdd:pfam07111 351 SQEQAILQRALQDkaAEVEVERMSAKGLQME 381
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
247-342 |
5.26e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 37.65 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKCAEEA-----QLISSLKAELTSQESQISTYEEELAKAREELSRLQQEtaelEESVE--S 319
Cdd:pfam02050 21 LEELQQYRAEYQQQLSGAGQGISAAElrnyqAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQE----RKSLEklR 96
|
90 100
....*....|....*....|....*...
gi 2462506005 320 GKAQLEplQQHLQDSQQ-----EISSMQ 342
Cdd:pfam02050 97 EREKKE--ERKEQNRREqkqldELAARL 122
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
194-312 |
5.71e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 194 LQREKNNVEQDLKEKEDTikqRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELL--DELDEQKAQ--------------- 256
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKlelekekrdrkraee 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506005 257 -----LEEQLKEVRKKCAEEAQLISSLKAELtsQESQISTYEEELAKAREELSRLQQETAE 312
Cdd:pfam17380 492 qrrkiLEKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
179-308 |
5.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTikqrtSEVQDLQDE----VQRENTNLQKLQAQKQQVQELLD------ 248
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQQRQEAR-----REREELQREeerlVQKEEQLDARAEKLDNLENQLEErekals 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506005 249 ----ELDEQKAQLEEQLKEVRKKCAEEA--QLISSLKAELTSQESQISTYEEElaKAREELSRLQQ 308
Cdd:PRK12705 116 arelELEELEKQLDNELYRVAGLTPEQArkLLLKLLDAELEEEKAQRVKKIEE--EADLEAERKAQ 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
194-357 |
6.56e-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: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 194 LQREKNNVEQDLKEKEDTIKQRtsevQDLQDEVQRENTNLQKLQAQKQQVQE---LLDELDEQKA------QLEEQLKEV 264
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQ----SSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTltqhihTLQQQKTTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 265 RKKCAEEAQLISSLKAELTSQESQISTYEEE---LAKAREELsRLQQETAELEESVESGKAQLEPLQQ-HLQDSQQEISS 340
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKE 470
|
170
....*....|....*..
gi 2462506005 341 MQMKLmemKDLENHNSQ 357
Cdd:TIGR00618 471 REQQL---QTKEQIHLQ 484
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-336 |
6.67e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ELDEQKAQLEEQ---LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEELAK-------------- 298
Cdd:PRK04863 294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAasdhlnlvqtalrQQEKIERYQADLEEleerleeqnevvee 373
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462506005 299 AREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 336
Cdd:PRK04863 374 ADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQQ 410
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
248-338 |
6.75e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 248 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAeLEESVESGKAQLEPL 327
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEEL 359
|
90
....*....|.
gi 2462506005 328 QQHLqDSQQEI 338
Cdd:COG3096 360 TERL-EEQEEV 369
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
206-329 |
6.81e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 39.81 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 206 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 284
Cdd:NF041483 520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462506005 285 QESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQ 329
Cdd:NF041483 584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
247-324 |
7.08e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.42 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAELTSQEsqisTYEEELAKAREELSRLQQET-AELEESVESGKA 322
Cdd:cd06503 39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERILEQAkAEIEQEKEKALA 113
|
..
gi 2462506005 323 QL 324
Cdd:cd06503 114 EL 115
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
245-350 |
7.13e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 37.24 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 245 ELLDELDEQKAQLEEQLKEVRKKCaeeaQLISSLKAELTSQ-ESQISTYEEELAKAREEL-SRLQQETAELEESVESGKA 322
Cdd:smart00502 7 ELLTKLRKKAAELEDALKQLISII----QEVEENAADVEAQiKAAFDELRNALNKRKKQLlEDLEEQKENKLKVLEQQLE 82
|
90 100
....*....|....*....|....*...
gi 2462506005 323 QLEPLQQHLQDSQQEISsmqmKLMEMKD 350
Cdd:smart00502 83 SLTQKQEKLSHAINFTE----EALNSGD 106
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
254-347 |
7.93e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.56 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 254 KAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgkaqlepLQQHLQD 333
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQE-----------------FQRKQQK 80
|
90
....*....|....
gi 2462506005 334 SQQEISSMQMKLME 347
Cdd:smart00935 81 LQQDLQKRQQEELQ 94
|
|
| CCDC-167 |
pfam15188 |
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ... |
247-302 |
7.96e-03 |
|
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, has not, as yet, been determined. Members of this family remain uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between and 103 amino acids in length.
Pssm-ID: 464553 [Multi-domain] Cd Length: 82 Bit Score: 36.10 E-value: 7.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 302
Cdd:pfam15188 5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
179-359 |
7.98e-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: 39.82 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 179 SAIKELDTLNNEIVDLQREknnVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAqK---QQVQELLDELDEQ 253
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETL---IASRQEERQETSAELNQLLRTLDDQWKekRDELNGELSAA-DaavAKDRSELEALEDQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 254 KAQLEEQLKEVRKKCAEEAQLISS--------LKAELTSQESQISTYEEELAKAREE----LSRLQQETAELEESVESGK 321
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSelenleerLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQL 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462506005 322 A-------QLE-PLQQHLQDSQQEISSMQMKLMEmkDLENHNSQLN 359
Cdd:pfam12128 411 AvaeddlqALEsELREQLEAGKLEFNEEEYRLKS--RLGELKLRLN 454
|
|
| MCP2201-like_sensor |
cd19411 |
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ... |
251-347 |
8.30e-03 |
|
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.
Pssm-ID: 438629 [Multi-domain] Cd Length: 138 Bit Score: 37.23 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 251 DEQKAQLEEQLKEVRKKCAEeaqLISSLKAELTSQESQisTYEEELAKAREELSRLQQETAELeesVESGKA-------- 322
Cdd:cd19411 35 PAERAKELARIAAARARITE---LLKKLEKLITSPEGK--ALLAAIAEARAAYLAARDKVLEL---KKAGDReearalll 106
|
90 100
....*....|....*....|....*.
gi 2462506005 323 -QLEPLQQHLQDSQQEISSMQMKLME 347
Cdd:cd19411 107 gELRPAQAAYLAALDALVDYQEELMD 132
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-359 |
8.49e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 183 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIK-----------QRT----------SEVQDLQDEVQRENtnlQKLQAQKQ 241
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleeetaQKNnalkkireleAQISELQEDLESER---AARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 242 QVQELLDELDEQKAQLEEQL------KEVR-KKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR--------- 305
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTLdttaaqQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEqleqakrnk 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506005 306 ---------LQQETAELEE---SVESGK-----------AQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQLN 359
Cdd:pfam01576 373 anlekakqaLESENAELQAelrTLQQAKqdsehkrkkleGQLQELQARLSESERQRAELAEKLSKLQsELESVSSLLN 450
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
165-345 |
8.52e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 38.84 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 165 LQKNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNveqdlKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQA--QKQQ 242
Cdd:PRK06669 1 MPKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKEKE-----RLREEEEEQVEQLREEANDEAKEIIEEAEEDAFeiVEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 243 VQELLDELDEQKAQLEEQLKEVRKKCA-EEAQLISSLKAELtsQESQISTYEEELAKAREE-LSRLQQETAELEESVESG 320
Cdd:PRK06669 76 EEEAKEELLKKTDEASSIIEKLQMQIErEQEEWEEELERLI--EEAKAEGYEEGYEKGREEgLEEVRELIEQLNKIIEKL 153
|
170 180
....*....|....*....|....*
gi 2462506005 321 KAQLEplqQHLQDSQQEISSMQMKL 345
Cdd:PRK06669 154 IKKRE---EILESSEEEIVELALDI 175
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
249-393 |
9.21e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 38.65 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 249 ELDEQKAQLEEQLKEVRKKCA--EEAQlisSLKAELTSQesqistYEEELAKAREELSRLQ------------------- 307
Cdd:pfam17045 43 ELLSARNTLERKHKEIGLLRQqlEELE---KGKQELVAK------YEQQLQKLQEELSKLKrsyeklqrkqlkeareeak 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 308 -QETAELEESVESGKAQ------LEPLQQHLQdSQQEISSMQmklMEMKDLENHNSQLNwcSSPHSILVNGATdyCSLST 380
Cdd:pfam17045 114 sREEDRSELSRLNGKLEefrqksLEWEQQRLQ-YQQQVASLE---AQRKALAEQSSLIQ--SAAYQVQLEGRK--QCLEA 185
|
170
....*....|...
gi 2462506005 381 SSSETANLNEHVE 393
Cdd:pfam17045 186 SQSEIQRLRSKLE 198
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
176-327 |
9.23e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.29 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 176 ADFSAIKELDTLNNEIVDLQReknnVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqELLDELDEQKA 255
Cdd:COG0497 238 GEGGALDLLGQALRALERLAE----YDPSLAELAERLESALIELEEAASELRRYLDSLEFDP-------ERLEEVEERLA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 256 QLE----------EQLKEVRKKCAEEAqlisslkAELTSQESQISTYEEELAKAREE-------LSRLQQETA-ELEESV 317
Cdd:COG0497 307 LLRrlarkygvtvEELLAYAEELRAEL-------AELENSDERLEELEAELAEAEAElleaaekLSAARKKAAkKLEKAV 379
|
170
....*....|
gi 2462506005 318 EsgkAQLEPL 327
Cdd:COG0497 380 T---AELADL 386
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
247-344 |
9.87e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 36.43 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506005 247 LDELDEQKAQLEEQLKEVrkKCAEEAqlISSLKAELTSQESqIST--YEEELAKAREElsrLQQETAELEESVESGKAQL 324
Cdd:pfam01920 11 LQLLAQQIKQLETQLKEL--ELALEE--LELLDEDTKVYKL-IGDvlVKQDKEEVKEQ---LEERKETLEKEIKTLEKQL 82
|
90 100
....*....|....*....|
gi 2462506005 325 EPLQQHLQDSQQEISSMQMK 344
Cdd:pfam01920 83 EKLEKELEELKEELYKKFGQ 102
|
|
| |
