|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
121-215 |
3.11e-43 |
|
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: 151.66 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 121 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 4503593 200 PVPMSLPPALVPPSKR 215
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
218-313 |
2.07e-41 |
|
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: 146.65 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 218 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 297
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80
|
90
....*....|....*.
gi 4503593 298 DPPHVLTPEMIPPSDR 313
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
3.46e-28 |
|
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: 108.90 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 13 SSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 4503593 93 SLNLAVPPPRF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
228-293 |
1.56e-26 |
|
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: 103.07 E-value: 1.56e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503593 228 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 293
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
121-215 |
2.45e-26 |
|
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: 103.99 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 121 PWAVKpedkaKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763 6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
|
90
....*....|....*..
gi 4503593 200 -PVPMSLPPALVPPSKR 215
Cdd:pfam12763 81 aDVPDELPDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
132-197 |
5.76e-25 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 98.45 E-value: 5.76e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503593 132 YDAIFDSLSPVN-GFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALE 197
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
2.48e-24 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 96.91 E-value: 2.48e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503593 19 YEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQN 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-493 |
9.30e-17 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 83.03 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 409
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 487
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194
|
....*.
gi 4503593 488 EISSMQ 493
Cdd:COG4372 195 NAEKEE 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-489 |
6.43e-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: 78.04 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503593 413 KEVRKkcAEEAQlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:COG1579 83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-509 |
5.27e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISS 491
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEEL 405
|
170
....*....|....*...
gi 4503593 492 MQMKLMEMKDLENHNSQL 509
Cdd:COG1196 406 EEAEEALLERLERLEEEL 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-510 |
1.91e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.75 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSm 492
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS- 493
|
170
....*....|....*...
gi 4503593 493 qmKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 494 --KEKELKKLNEEKKELE 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-498 |
4.54e-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: 76.63 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
....*
gi 4503593 494 MKLME 498
Cdd:TIGR02168 428 KKLEE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-493 |
1.42e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 324 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDE 403
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 483
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|
gi 4503593 484 DSQQEISSMQ 493
Cdd:COG4913 423 ELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-501 |
2.14e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
....*...
gi 4503593 494 MKLMEMKD 501
Cdd:TIGR02168 936 VRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-508 |
5.40e-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: 73.17 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 329 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 408
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-----AQLEPLQQHLQ 483
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450
|
170 180
....*....|....*....|....*
gi 4503593 484 DSQQEISSMQMKLMEMKDLENHNSQ 508
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQ 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-510 |
8.23e-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: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 412
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170
....*....|....*....
gi 4503593 493 QMKLME-MKDLENHNSQLN 510
Cdd:COG1196 385 AEELLEaLRAAAELAAQLE 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-501 |
8.77e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS-------KELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEEL-------AKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 485
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170
....*....|....*.
gi 4503593 486 QQEISSMQMKLMEMKD 501
Cdd:TIGR02168 858 AAEIEELEELIEELES 873
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-510 |
1.76e-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: 71.20 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 404
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 405 KAQLEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 484
Cdd:TIGR04523 290 LNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190
....*....|....*....|....*....|
gi 4503593 485 SQQEISSM----QMKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 368 KQNEIEKLkkenQSYKQEIKNLESQINDLE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-510 |
3.42e-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: 70.47 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKA 406
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALA----------NEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:TIGR02168 306 ILRERLANLERQ-------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180
....*....|....*....|....*
gi 4503593 487 QEISSMQMKLMEMK-DLENHNSQLN 510
Cdd:TIGR02168 379 EQLETLRSKVAQLElQIASLNNEIE 403
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
355-509 |
5.67e-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: 64.95 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 355 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 433
Cdd:pfam08614 11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 434 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 509
Cdd:pfam08614 88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
310-469 |
6.85e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 66.10 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 310 PSDRASLQKNIIGsspvadfsAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqre 380
Cdd:COG1579 30 PAELAELEDELAA--------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 381 ntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSR 456
Cdd:COG1579 98 -----------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEE 160
|
170
....*....|...
gi 4503593 457 LQQETAELEESVE 469
Cdd:COG1579 161 LEAEREELAAKIP 173
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
331-474 |
7.40e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 408
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EE---QLKEVRKKCAEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 474
Cdd:COG4717 173 AElqeELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
342-501 |
9.66e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.62 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 342 IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 421
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 422 eaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:COG4372 89 ----LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-508 |
1.00e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 410
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 490
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170
....*....|....*...
gi 4503593 491 SMQMKLMEMKDLENHNSQ 508
Cdd:COG1196 390 EALRAAAELAAQLEELEE 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-489 |
1.17e-11 |
|
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: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 327 ADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKA 406
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
...
gi 4503593 487 QEI 489
Cdd:COG1196 449 EEE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-510 |
1.90e-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: 68.17 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 329 FSAIKELDTLNNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDEQKAQL 408
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAE-EAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 483
Cdd:TIGR02169 771 EEDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180
....*....|....*....|....*...
gi 4503593 484 DSQQEISSMQMKLMEMK-DLENHNSQLN 510
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEeELEELEAALR 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-504 |
2.04e-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: 68.17 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQREntnlqklqaqkqqvqelLDELDEQKAQLEE 410
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKE-----------------IEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPL 478
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREI 817
|
170 180 190
....*....|....*....|....*....|
gi 4503593 479 QQHLQDSQQEI----SSMQMKLMEMKDLEN 504
Cdd:TIGR02169 818 EQKLNRLTLEKeyleKEIQELQEQRIDLKE 847
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-493 |
2.78e-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: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAE---EAQLISS-------LKAELTSQESQISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPL 478
Cdd:COG4942 100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*
gi 4503593 479 QQHLQDSQQEISSMQ 493
Cdd:COG4942 180 LAELEEERAALEALK 194
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-491 |
2.88e-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: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 412
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-491 |
4.33e-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: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDL-----------QDEVQRENTNLQKLQAQKQQVQELLDEL 401
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 481
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
170
....*....|
gi 4503593 482 LQDSQQEISS 491
Cdd:COG4942 236 AAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
330-503 |
5.10e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 408
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
170
....*....|....*
gi 4503593 489 ISSMQMKLMEMKDLE 503
Cdd:PRK03918 703 LEEREKAKKELEKLE 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-505 |
1.96e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170
....*....|...
gi 4503593 493 QMKLMEMKDLENH 505
Cdd:TIGR02168 914 RRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-493 |
2.92e-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: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 410
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRKKCAEEAQLISSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 490
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
...
gi 4503593 491 SMQ 493
Cdd:COG1196 502 DYE 504
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
335-598 |
3.24e-10 |
|
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: 64.07 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 335 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQ 393
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----------KSTLAGE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 394 VQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETaE 463
Cdd:pfam10174 382 IRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR-E 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 464 LEESVEsgKAQLEPLQQHLQDSQQEISSMQMKLME----MKDLENHNSQLNwcSSPHSIlvngatdycsLSTSSSETANL 539
Cdd:pfam10174 461 REDRER--LEELESLKKENKDLKEKVSALQPELTEkessLIDLKEHASSLA--SSGLKK----------DSKLKSLEIAV 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503593 540 NEHVEGQSNLESE--PIHQ-ESPARSSPELLPSGVTDENEVTTAVTE--KVCSELD----------NNRHSKEE 598
Cdd:pfam10174 527 EQKKEECSKLENQlkKAHNaEEAVRTNPEINDRIRLLEQEVARYKEEsgKAQAEVErllgilreveNEKNDKDK 600
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
396-510 |
4.13e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 4503593 476 EPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 510
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLE 135
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
338-490 |
5.93e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 338 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRK 417
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 418 KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
..
gi 4503593 489 IS 490
Cdd:TIGR04523 598 KK 599
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
333-483 |
8.80e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKE-------DTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD--- 402
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaai 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 403 ----EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESG 471
Cdd:TIGR02169 430 agieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGG 509
|
170
....*....|..
gi 4503593 472 KAQLEPLQQHLQ 483
Cdd:TIGR02169 510 RAVEEVLKASIQ 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-492 |
9.17e-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: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 403 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL 482
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|
gi 4503593 483 QDSQQEISSM 492
Cdd:COG4942 100 EAQKEELAEL 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-510 |
2.43e-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: 61.19 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKlqaqkqqvqELLDELDEQKAQLEEQ 411
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 412 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS------ 485
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqq 409
|
170 180 190
....*....|....*....|....*....|
gi 4503593 486 -QQEISSMQ----MKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 410 kDEQIKKLQqekeLLEKEIERLKETIIKNN 439
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
318-510 |
2.86e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 318 KNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ----RENTNLQKLQAQKQQ 393
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 394 VQELLDELDEQKAQ----------LEEQLKEVRKKCA--------EEAQL-------------ISSLKAELTSQESQIST 442
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 443 YEEELAKAREELSR-----------------LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
....*.
gi 4503593 506 N-SQLN 510
Cdd:TIGR04523 265 IkKQLS 270
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-511 |
3.06e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 411
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 412 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180
....*....|....*....|.
gi 4503593 492 MQMKLMEMKD-LENHNSQLNW 511
Cdd:TIGR04523 536 KESKISDLEDeLNKDDFELKK 556
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
403-509 |
3.12e-09 |
|
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: 55.72 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 403 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 467
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503593 468 VESGKAQLEPLQQHLQDS----QQEISSMQMKLmemKDLENHNSQL 509
Cdd:pfam07926 80 AESAKAELEESEESWEEQkkelEKELSELEKRI---EDLNEQNKLL 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-498 |
4.99e-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: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRenTNLQKLQAQKQQVQELLDELDEQKAQ 407
Cdd:COG4913 229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 408 LEEQLKEVRKKCAEEAQLISSLKAELTSQ--------ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 479
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170
....*....|....*....
gi 4503593 480 QHLQDSQQEISSMQMKLME 498
Cdd:COG4913 387 AEAAALLEALEEELEALEE 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-493 |
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: 60.46 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------QISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
.
gi 4503593 493 Q 493
Cdd:TIGR02168 830 E 830
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
398-487 |
5.71e-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: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 477
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90
....*....|
gi 4503593 478 LQQHLQDSQQ 487
Cdd:COG4942 109 LLRALYRLGR 118
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
345-509 |
6.42e-09 |
|
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: 59.80 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 345 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 424
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 425 LISSLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLM 497
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
170 180
....*....|....*....|...
gi 4503593 498 E-----------MKDLENHNSQL 509
Cdd:pfam01576 254 EetaqknnalkkIRELEAQISEL 276
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
334-501 |
8.48e-09 |
|
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: 58.11 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREknnveqdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 414 EVRKKC-----------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQL 475
Cdd:pfam04849 182 KLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIEN 261
|
170 180
....*....|....*....|....*.
gi 4503593 476 EPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam04849 262 EELQQHLQASKEAQRQLTSELQELQD 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-503 |
1.19e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 408
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|....*..
gi 4503593 487 QEISSMQMKLMEMKDLE 503
Cdd:PRK03918 331 KELEEKEERLEELKKKL 347
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-509 |
1.60e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLN--------NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL 401
Cdd:TIGR02169 269 EIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK--------------LEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS-------------------------- 455
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyrekleklkreinelkreldrlqee 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 4503593 456 --RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQL 509
Cdd:TIGR02169 415 lqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAaDLSKYEQEL 471
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-491 |
1.68e-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: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------------------DL--------------QDE 376
Cdd:COG3883 55 ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsesfsDFldrlsalskiadadADL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 377 VQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR 456
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
170 180 190
....*....|....*....|....*....|....*
gi 4503593 457 LQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:COG3883 215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
396-500 |
1.84e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.60 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDE-------LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELA--KAREELSR--LQQEtA 462
Cdd:COG1842 16 ALLDKaedpekmLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkaRLAleKGREDLAReaLERK-A 94
|
90 100 110
....*....|....*....|....*....|....*...
gi 4503593 463 ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 500
Cdd:COG1842 95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELK 132
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
333-503 |
1.93e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVeqDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQ--LISSLKAELTSQESQI----STY----------EEELAKAREEL-SRLQQETAELEESVESGKAQL 475
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELaelsARYtpnhpdvialRAQIAALRAQLqQEAQRILASLEAELEALQARE 329
|
170 180
....*....|....*....|....*...
gi 4503593 476 EPLQQHLQDSQQEISSMQMKLMEMKDLE 503
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
335-503 |
2.69e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 335 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTIKQRTSEVQDLQDEVQRENT----------------NLQKLQAQK 391
Cdd:COG4717 48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEELEEeleeleaeleelreelEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 392 QQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAELEES 467
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503593 468 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 503
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
317-499 |
2.91e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 317 QKNIIGSSPVADfSAIKELDtLNNEIVDLQREKNNVEQDLKEK----------------EDTIKQRTSEV--------QD 372
Cdd:COG3206 86 QIEILKSRPVLE-RVVDKLN-LDEDPLGEEASREAAIERLRKNltvepvkgsnvieisyTSPDPELAAAVanalaeayLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 373 LQDEVQRENTNlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAE--EAQLISSLKAELTSQESQISTYEEELAKA 450
Cdd:COG3206 164 QNLELRREEAR------------KALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 4503593 451 REELSRLQQETAELEESVESGKAQLEPLQQH--LQDSQQEISSMQMKLMEM 499
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAEL 282
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
356-508 |
3.39e-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: 54.52 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 356 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 432
Cdd:pfam15619 6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 433 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 490
Cdd:pfam15619 69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141
|
170
....*....|....*...
gi 4503593 491 SMQMKLmemkDLENHNSQ 508
Cdd:pfam15619 142 DLERKL----ELENKSFR 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-481 |
4.02e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQistyEEELAKAREELSRLQQETAELEESV---ESGKAQLEPLQQH 481
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-504 |
4.41e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKA 406
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQES-------QISTYEEELAKAREELSRLQQETAELEESVESGKA------ 473
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404
|
170 180 190
....*....|....*....|....*....|...
gi 4503593 474 -QLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 504
Cdd:PRK02224 405 vDLGNAEDFLEELREERDELREREAELEaTLRT 437
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-493 |
5.58e-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: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 313 RASLQKNIIGsspvadFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTIKQR--------------------TSE 369
Cdd:COG4913 596 RRIRSRYVLG------FDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERrealqrlaeyswdeidvasaERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 370 VQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELA 448
Cdd:COG4913 670 IAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4503593 449 KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL 782
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-492 |
6.48e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 414 EVRKKCAE-EAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------A 473
Cdd:TIGR02169 872 ELEAALRDlESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeL 951
|
170
....*....|....*....
gi 4503593 474 QLEPLQQHLQDSQQEISSM 492
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRAL 970
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
333-489 |
1.11e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCA--EEAQLISSLKaELTSQESQISTYEEELAKA---REELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:COG4372 167 AALEQELQalSEAEAEQALD-ELLKEANRNAEKEEELAEAeklIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
..
gi 4503593 488 EI 489
Cdd:COG4372 246 ED 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-464 |
1.23e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 4503593 413 KEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 464
Cdd:COG4913 415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-510 |
1.35e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQL 412
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGKAQLEPL-QQHLQD 484
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKSEISDLnNQKEQD 307
|
170 180
....*....|....*....|....*.
gi 4503593 485 SQQEISSmQMKLMEmKDLENHNSQLN 510
Cdd:TIGR04523 308 WNKELKS-ELKNQE-KKLEEIQNQIS 331
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
330-495 |
1.40e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQEL 397
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 477
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
170
....*....|....*...
gi 4503593 478 LQQhLQDSQQEISSMQMK 495
Cdd:PRK02224 501 AED-LVEAEDRIERLEER 517
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
329-492 |
1.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 329 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqqVQELLDELDEQKAQL 408
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-----------YQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQE 488
Cdd:COG4717 412 EELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAE 484
|
....
gi 4503593 489 ISSM 492
Cdd:COG4717 485 LREL 488
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
329-510 |
1.61e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.84 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 329 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQL 408
Cdd:PRK04778 89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAEEA----QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQ 479
Cdd:PRK04778 146 KDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQ 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4503593 480 QHLQDSQQEISS----MQMK---------LMEMKDLENHNSQLN 510
Cdd:PRK04778 226 TELPDQLQELKAgyreLVEEgyhldhldiEKEIQDLKEQIDENL 269
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
317-491 |
1.85e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 317 QKNIIGSSPVADFSAIKELDTLNNEIVDLQREK-------NNVEQDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKL 387
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaearlAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 388 QAQKQQV----QELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQE 460
Cdd:COG3206 283 SARYTPNhpdvIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAE 352
|
170 180 190
....*....|....*....|....*....|.
gi 4503593 461 TAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
331-485 |
1.90e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.84 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 331 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDe 403
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 qkaQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 483
Cdd:PRK04778 359 ---SLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
..
gi 4503593 484 DS 485
Cdd:PRK04778 436 KS 437
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-501 |
2.03e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelldeLDEQKAQLE 409
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE------------------------IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKCAEE------------AQLISSLKA-------------ELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:COG3883 90 ERARALYRSGGSVsyldvllgsesfSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 4503593 465 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
309-473 |
2.14e-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: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 309 PPSDRASLQKNIIGSSPVADfsAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlq 385
Cdd:COG2433 361 PDVDRDEVKARVIRGLSIEE--ALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 386 klqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEELAKAREELSRLQqeta 462
Cdd:COG2433 436 ------------LEEKDERIERLERELSEARSEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLK---- 499
|
170
....*....|.
gi 4503593 463 ELEESVESGKA 473
Cdd:COG2433 500 ELWKLEHSGEL 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
331-501 |
2.23e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL 397
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 ------LDELDEQKAQLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELE--- 465
Cdd:PRK03918 462 kriekeLKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgei 541
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503593 466 ESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
361-464 |
2.32e-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: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 361 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 440
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 4503593 441 STYEEELAKAREELSRLQQETAEL 464
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
2.89e-07 |
|
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: 49.68 E-value: 2.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 4503593 32 GRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLV 80
Cdd:pfam12763 24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-496 |
3.66e-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: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLE 409
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKCAEEAQ-------LISSLKAELTSQE-----------SQISTYE----EELAKAREELSRLQQETAELEES 467
Cdd:COG3883 79 AEIEERREELGERARalyrsggSVSYLDVLLGSESfsdfldrlsalSKIADADadllEELKADKAELEAKKAELEAKLAE 158
|
170 180
....*....|....*....|....*....
gi 4503593 468 VESGKAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQL 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
352-471 |
3.79e-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: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 352 VEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 431
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 4503593 432 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 471
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-509 |
3.98e-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: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKAQLEEQlkevRKKcAEEAQLISS----LKAELT-----SQESQISTYEEELAKAREELSRLQQETAELEES 467
Cdd:COG1196 194 ILGELERQLEPLERQ----AEK-AERYRELKEelkeLEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 4503593 468 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
402-501 |
4.80e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 481
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100
....*....|....*....|
gi 4503593 482 LQDSQQEISSMQMKLMEMKD 501
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQE 101
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
332-500 |
5.14e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL---------- 401
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 -DEQK------AQLEEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEL---------- 464
Cdd:COG1340 132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELykeadelrke 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 4503593 465 -----EESVESGKA------QLEPLQQHLQDSQQEISSMQMKLMEMK 500
Cdd:COG1340 211 adelhKEIVEAQEKadelheEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
321-504 |
5.44e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 321 IGSSPVADfsAIKE----LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRtSEVQDLQDevQRENTNlqklqaqkqqvqE 396
Cdd:PRK02224 461 VEGSPHVE--TIEEdrerVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------E 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKAQLEEQLKEVRKKCAEeaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLE 476
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIR 595
|
170 180
....*....|....*....|....*...
gi 4503593 477 PLQQHLQDSQQEISSMQMKLMEMKDLEN 504
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELND 623
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
341-510 |
5.49e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.59 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 341 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQD-EVQRENTNLQK--LQAQKQQVQELLDELDEQKAQLEEQLKEV-- 415
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKrEAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 416 --RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKA---QLEPLQQHLQ---DSQQ 487
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQsqeQDSE 187
|
170 180 190
....*....|....*....|....*....|
gi 4503593 488 EISSMQMKLMEMKDLEN-------HNSQLN 510
Cdd:pfam05557 188 IVKNSKSELARIPELEKelerlreHNKHLN 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
327-486 |
5.98e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 327 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqAQKQQVQELLDELDEQK 405
Cdd:COG4913 685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 406 AQL--EEQLKEVRKKCAEEAQLISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREE 453
Cdd:COG4913 756 AAAlgDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEER 835
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4503593 454 LSRLQQET---------AELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:COG4913 836 FKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
354-492 |
6.30e-07 |
|
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: 50.59 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 354 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 433
Cdd:pfam06785 83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503593 434 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
333-480 |
6.59e-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: 53.11 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503593 413 KEVRKKCAEEAQL-----------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQ 480
Cdd:pfam05667 411 DASAQRLVELAGQwekhrvplieeYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-510 |
7.76e-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: 53.10 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKnnvEQDL-KEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 411
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 412 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAreelsrlQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
170
....*....|....*....
gi 4503593 492 MQmklMEMKDLENHNSQLN 510
Cdd:TIGR04523 438 NN---SEIKDLTNQDSVKE 453
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
396-465 |
9.20e-07 |
|
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: 47.30 E-value: 9.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 465
Cdd:pfam12329 5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
330-490 |
9.89e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 50.76 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE 403
Cdd:pfam12795 48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLK--EVRKKCAEEAQLIsSLKAELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQ 479
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLE 197
|
170
....*....|.
gi 4503593 480 QHLQDSQQEIS 490
Cdd:pfam12795 198 QQLQALQELLN 208
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-501 |
1.45e-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: 51.94 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDT----LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQ 407
Cdd:TIGR04523 456 IKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 408 LEEQLKEVRKKcaeeaqlISSLKAELTSqesqiSTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:TIGR04523 536 KESKISDLEDE-------LNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
170
....*....|....
gi 4503593 488 EISSMQMKLMEMKD 501
Cdd:TIGR04523 604 EIEEKEKKISSLEK 617
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-501 |
1.75e-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: 51.94 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-----QKAQ 407
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----------KISDLEDELNKddfelKKEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 408 LEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEplqqhlqdsqq 487
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE----------- 627
|
170
....*....|....
gi 4503593 488 EISSMQMKLMEMKD 501
Cdd:TIGR04523 628 KLSSIIKNIKSKKN 641
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
313-475 |
2.57e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 313 RASLQKNI-IGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqk 391
Cdd:COG3206 242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 392 qqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVE 469
Cdd:COG3206 311 --AQRILASLEAELEALQAREASLQ---AQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384
|
....*.
gi 4503593 470 SGKAQL 475
Cdd:COG3206 385 VGNVRV 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-509 |
3.64e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEqkaqLEEQLKEVRKKCAEEAQLIsslkAELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVESGKAQL 475
Cdd:COG4717 70 LKELKE----LEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAEL 141
|
90 100 110
....*....|....*....|....*....|....
gi 4503593 476 EPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAEL 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-510 |
3.73e-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: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--- 469
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4503593 470 ----SGKAQLEPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 510
Cdd:TIGR02168 274 levsELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELE 322
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
337-585 |
4.52e-06 |
|
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: 49.37 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 337 TLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVR 416
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 417 kkcaeeaqlisSLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISSM 492
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELENR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 493 QMKLMEmkDLENHNSQLNWCSSPHSILVngatdyCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPelLPSGVT 572
Cdd:pfam09787 172 LHQLTE--TLIQKQTMLEALSTEKNSLV------LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRN--VPGLFS 241
|
250
....*....|...
gi 4503593 573 DENEVTTAVTEKV 585
Cdd:pfam09787 242 ESDSDRAGMYGKV 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
432-502 |
4.62e-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: 4.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503593 432 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 502
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
333-508 |
4.66e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDlKEKEDTIKQRTSEVQDLQDEVQR---ENtnlqklqaqkqqvqELLDELDEQKAQLE 409
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELERlreHN--------------KHLNENIENKLLLK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKC-------AEEAQL---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLE 476
Cdd:pfam05557 228 EEVEDLKRKLereekyrEEAATLeleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSAR 307
|
170 180 190
....*....|....*....|....*....|...
gi 4503593 477 PLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQ 508
Cdd:pfam05557 308 QLEKARRELEQELAQYLKKIEDLnKKLKRHKAL 340
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-508 |
6.01e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 342 IVDLQREK-NNVEQDLKEKEDTIKQR-------TSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqlEEQLK 413
Cdd:pfam05483 262 LLEESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEE--------SVE------------ 469
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEmtkfknnkEVEleelkkilaede 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4503593 470 ---SGKAQLEPLQQHLQDSQQ-----------EISSMQMKLMEMKDLENHNSQ 508
Cdd:pfam05483 419 kllDEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLTAIKTSEEHYLK 471
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
354-506 |
6.06e-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: 49.85 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 354 QDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA---QLEEQLKEVRKKCAEEA----QLI 426
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELD-----------------ELLESEEKNREeveELKDKYRELRKTLLANRfsygPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 427 SSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 500
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGy 228
|
....*.
gi 4503593 501 DLENHN 506
Cdd:pfam06160 229 ALEHLN 234
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
222-319 |
6.96e-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: 45.44 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 222 PAEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLIKGI--DP 299
Cdd:pfam12763 6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LVNGNiaDV 83
|
90 100
....*....|....*....|
gi 4503593 300 PHVLTPEMIPPSDRASLQKN 319
Cdd:pfam12763 84 PDELPDWLVPGSKAHLIQAN 103
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
345-464 |
7.22e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.96 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 345 LQREKNNVEQDLKE------KEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKK 418
Cdd:pfam05672 25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503593 419 CAEEAQlisslkAELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:pfam05672 85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-466 |
7.89e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQreknNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEE 410
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEE 659
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503593 411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYE----------EELAKAREELSRLQQETAELEE 466
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
399-504 |
7.93e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 399 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL 478
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100
....*....|....*....|....*....
gi 4503593 479 QQHLQDSQQEISSMQM---KLMEMKDLEN 504
Cdd:PRK12704 137 IEEQLQELERISGLTAeeaKEILLEKVEE 165
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-496 |
8.61e-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: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---------ISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAE 463
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703
|
90 100 110
....*....|....*....|....*....|...
gi 4503593 464 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
398-509 |
8.71e-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: 49.95 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 474
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503593 475 -------LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG3096 604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLLEREREATVERDEL 649
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
353-501 |
9.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 353 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAE 432
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAE-------LEALQAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 433 LTSQESQISTYEEELAKAREEL------------------------------------SRLQQETAELEESVESGKAQLE 476
Cdd:COG3883 67 IDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELE 146
|
170 180
....*....|....*....|....*
gi 4503593 477 PLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKA 171
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
274-493 |
1.05e-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: 48.92 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 274 CGKLSKDQFALAFHLISqkliKGIDPPHVLTPEMIPPsdraslqkniigsspvadfsAIKEldtlnnEIVDLQREkNNVe 353
Cdd:pfam05622 246 CAQLQQAELSQADALLS----PSSDPGDNLAAEIMPA--------------------EIRE------KLIRLQHE-NKM- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 354 qdLKEK-EDTIKQRTSEVQdlqdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 432
Cdd:pfam05622 294 --LRLGqEGSYRERLTELQ------------------------QLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503593 433 LTSQESQ----------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQHLQDSQQEISSMQ 493
Cdd:pfam05622 348 LQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAME 419
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
331-500 |
1.16e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 331 AIKELDTLNNEIV-----DLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdevQRENtnlqklqaqkqqvqelldeldeqk 405
Cdd:PRK12704 47 AKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLL------QKEE------------------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 406 aQLEEQLKEVRKKcaeeaqlisslKAELTSQESQISTYEEELAKAREELSRLQQET-AELEE----SVESGKAQLepLQQ 480
Cdd:PRK12704 97 -NLDRKLELLEKR-----------EEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERisglTAEEAKEIL--LEK 162
|
170 180
....*....|....*....|
gi 4503593 481 HLQDSQQEISSMqMKLMEMK 500
Cdd:PRK12704 163 VEEEARHEAAVL-IKEIEEE 181
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
344-480 |
1.23e-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: 45.27 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 344 DLQREKNNVE------QDLKEKEDTIKQRTSEV-------QDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEE 410
Cdd:pfam18595 3 TLAEEKEELAelerkaRELQAKIDALQVVEKDLrscikllEEIEAELAKLE--------------EAKKKLKELRDALEE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRkkcaeeaqlisslkaELTSQESQIstyEEELAKAREELSRLQQETaelEESVESGKAQLEPLQQ 480
Cdd:pfam18595 69 KEIELR---------------ELERREERL---QRQLENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
404-503 |
1.24e-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: 45.29 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 476
Cdd:pfam20492 7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79
|
90 100
....*....|....*....|....*..
gi 4503593 477 PLQQHLQDSQQEISSMQMKlMEMKDLE 503
Cdd:pfam20492 80 QLEAELAEAQEEIARLEEE-VERKEEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
346-618 |
1.44e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 346 QREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------EV 415
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeEL 1707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 416 RKKCAEE---------AQLISSLKAE-LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 485
Cdd:PTZ00121 1708 KKKEAEEkkkaeelkkAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 486 QQEISSMQMKlMEMKDLENHNSQLNWCSSPHSILVN-------GATDYCSLSTSS--SETANLNEHVEGQSNLESEPIHQ 556
Cdd:PTZ00121 1788 EDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINdskemedSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNK 1866
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503593 557 ESPARSSPELLPSgvtDENEVTTAvteKVCSELDNNrhSKEEDPFNVDSSSLTGPVADTNLD 618
Cdd:PTZ00121 1867 EADFNKEKDLKED---DEEEIEEA---DEIEKIDKD--DIEREIPNNNMAGKNNDIIDDKLD 1920
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
332-508 |
1.44e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTIKQRTSEVQDLQDEV------QRENTNLQKLQAQKQQVQELLD-- 399
Cdd:TIGR00606 743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGSDld 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 400 ----ELDEQKAQLEEQLK------EVRKKCAEEAQ-LISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELE 465
Cdd:TIGR00606 822 rtvqQVNQEKQEKQHELDtvvskiELNRKLIQDQQeQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 4503593 466 ESVESGKAQLEPLQQHLQDSQQEissmQMKLMEMKDLENHNSQ 508
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNKKAQ 940
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
396-496 |
1.48e-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: 47.23 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 462
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 4503593 463 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:COG1579 104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
335-487 |
1.56e-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: 46.10 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 335 LDTLNNEIVDLQREKNNVEQDLKEKedtikqRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKE 414
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 415 VRKKCAEEAQLissLKAELtsqESQISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQH 481
Cdd:pfam01442 60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAER 133
|
....*.
gi 4503593 482 LQDSQQ 487
Cdd:pfam01442 134 LEELKE 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-504 |
1.63e-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: 48.91 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 320 IIGSSPVADFSAIKELdtlnNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLD 399
Cdd:TIGR02169 147 FISMSPVERRKIIDEI----AGVAEFDRKK----EKALEELEEVEENIERLDLIIDEKRQQ-----------------LE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 400 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 4503593 476 EPL--------QQHLQDSQQEISSMQ----MKLMEMKDLEN 504
Cdd:TIGR02169 282 KDLgeeeqlrvKEKIGELEAEIASLErsiaEKERELEDAEE 322
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
349-496 |
1.74e-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: 46.98 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 349 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 428
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 429 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhlqdSQQEISSMQMKL 496
Cdd:pfam04012 88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLK-----ARLKAAKAQEAV 150
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-509 |
2.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 476
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 4503593 477 P---------LQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEERLEELRELEEELEEL 168
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
334-468 |
2.16e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.15 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEqdlKEKEDTIKQRtsevqdlqdevqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLK 413
Cdd:COG0542 412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 414 EVRKKCAEEAQLIS---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 468
Cdd:COG0542 458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
326-500 |
2.60e-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: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 326 VADFSAikELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQK 405
Cdd:TIGR02169 296 IGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 406 AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-------EEELAKAREELSRLQQETAELEESVESGKAQLEPL 478
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
170 180
....*....|....*....|..
gi 4503593 479 QQHLQDSQQEISSMQMKLMEMK 500
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLK 475
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
419-509 |
2.80e-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: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 419 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 498
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|..
gi 4503593 499 M-KDLENHNSQL 509
Cdd:COG4942 95 LrAELEAQKEEL 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-510 |
2.88e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQR---EKNNVE---QDLKEKEDTIKQRTSE----VQDLQD----EVQRENTNLQKLQAQKQQVQELL 398
Cdd:PRK03918 314 KRLSRLEEEINGIEErikELEEKEerlEELKKKLKELEKRLEEleerHELYEEakakKEELERLKKRLTGLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 399 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQET 461
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKEL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 4503593 462 AELEESVESGKAQLEPLQQHLQDsQQEISSMQMKLMEMKDLENHNSQLN 510
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYN 516
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
334-498 |
3.44e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 411
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 412 LKEVRKKCAEEAQLISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
170
....*....|
gi 4503593 489 ISSMQMKLME 498
Cdd:PHA02562 395 KSELVKEKYH 404
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
336-505 |
3.62e-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: 47.20 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 336 DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEV 415
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 416 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQEISSMQMK 495
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEE 259
|
170
....*....|
gi 4503593 496 LMEMKDLENH 505
Cdd:pfam07888 260 LSSMAAQRDR 269
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
398-489 |
4.05e-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: 44.95 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 470
Cdd:pfam01442 6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85
|
90
....*....|....*....
gi 4503593 471 GKAQLEPLQQHLQDSQQEI 489
Cdd:pfam01442 86 LNADAEELQEKLAPYGEEL 104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
330-517 |
4.55e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKAQLE 409
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL----------SEAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKcAEEAQLISSLKAELTSQESqistYEEELAKAREELS--RLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:TIGR00618 623 PEQDLQDVR-LHLQQCSQELALKLTALHA----LQLTLTQERVREHalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
170 180 190
....*....|....*....|....*....|..
gi 4503593 488 EISSMQMKLMEMKDLENHNSQL--NWCSSPHS 517
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREfnEIENASSS 729
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
344-508 |
4.71e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 344 DLQREKNNVeqdLKEKEDTIKQRtsEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL---KEVRKKCA 420
Cdd:PRK02224 180 RVLSDQRGS---LDQLKAQIEEK--EEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRdeaDEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 421 EEAQLISSLKAELTSQESQISTYE-------EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170
....*....|....*.
gi 4503593 494 MKLMEMK-DLENHNSQ 508
Cdd:PRK02224 328 DRLEECRvAAQAHNEE 343
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
328-509 |
4.73e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 328 DFSAIKELDTLNNeivDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENT-NLQKLQAQKQQVQELLDELDEQKA 406
Cdd:PHA02562 161 DISVLSEMDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETAELEESVESGKAQLEP 477
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503593 478 LQQHLQDSQQ---EISSMQMKLMEMK-DLENHNSQL 509
Cdd:PHA02562 318 LDTAIDELEEimdEFNEQSKKLLELKnKISTNKQSL 353
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
402-502 |
4.83e-05 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 44.21 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQ------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ 474
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100
....*....|....*....|....*...
gi 4503593 475 LEPLQQHLQDSQQEISSMQMKLMEMKDL 502
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNSSLENL 109
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
396-489 |
5.11e-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: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQL 475
Cdd:pfam11932 34 KKIDKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TEREL 95
|
90
....*....|....
gi 4503593 476 EPLQQHLQDSQQEI 489
Cdd:pfam11932 96 VPLMLKMLDRLEQF 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-468 |
5.26e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---------------------IEEKEKKISSLEKEL 619
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESV 468
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
398-501 |
5.88e-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: 46.97 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 477
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100
....*....|....*....|....
gi 4503593 478 LQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEA 782
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
346-488 |
6.26e-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: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 346 QREKNNVEQDLKEKEDTIKQRTsevQDLQDEVQRentnlqklqaqkqqvqelLDELDEQ--KAQLEEQLKEVRKKCAEEA 423
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKAQ---EELEESEET------------------AEELEEErrQAEEEAERLEQKRQEAEEE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503593 424 qlisslKAELtsQESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:pfam20492 64 ------KERL--EESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
396-494 |
6.76e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 475
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212
|
90
....*....|....*....
gi 4503593 476 EPLQQHLQDSQQEISSMQM 494
Cdd:PRK11448 213 ERKQKRKEITDQAAKRLEL 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-489 |
7.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREknNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLK 413
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDADDLEERAEELREEAA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503593 414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
333-583 |
7.34e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLK-----------EKEDTIKQRTSEVQDLQDEVQR--------ENTNLQKLQAQKQQ 393
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEQtrntlksmEGSDGHAMKVAMGM 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 394 VQEL------LDELDEQKAQLEEQLKEVRKkcaeEAQLISSLKAELTSQESQISTYEEELAKAREEL----SRLQQETAE 463
Cdd:pfam15921 733 QKQItakrgqIDALQSKIQFLEEAMTNANK----EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLrsqeRRLKEKVAN 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 464 LEESVESGKAQLEPLQQHLQDSQQEisSMQMKL---MEMKDLENHNSQLNWCSSPHSILVNGATDYCSLSTSSSETANLN 540
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQE--SVRLKLqhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFL 886
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 4503593 541 EHVEGQSNlesepIHQESPARSSPELLP---SGVTDENEVTTAVTE 583
Cdd:pfam15921 887 SHHSRKTN-----ALKEDPTRDLKQLLQelrSVINEEPTVQLSKAE 927
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
328-505 |
7.82e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 328 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTIKQRTSEVQDLQDEVQR--ENTNlqklqaqkqQVQELL 398
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQleEKTK---------LQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 399 DELDEQKAQLEEQLKEVR----------KKCAEEAQLISSLKAELTSQ-ESQIstyeEELAKAREE----LSRLQQETAE 463
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAhsfvVTEFEATTCS 360
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4503593 464 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
349-494 |
8.43e-05 |
|
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: 44.76 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 349 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaEEAQL--- 425
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLkke 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503593 426 ------ISSLKAeltSQESQISTYEEELAKAREELSRLQQETaeleesvesgKAQLEPLQQHLQDSQQEISSMQM 494
Cdd:pfam14988 70 lqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
342-501 |
8.71e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 342 IVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkQQVQELLDELDEQKAQlEEQLKEVRKKCA 420
Cdd:pfam13868 157 ILEYLKEKAEREEEREaEREEIEEEKEREIARLRAQQEKA-----------QDEKAERDELRAKLYQ-EEQERKERQKER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 421 EEAQLISSLKAELT-SQESQIS----TYEEELAKAREELSRLQQETAELEEsvesgKAQLEPLQQHLQDSQ--QEISSM- 492
Cdd:pfam13868 225 EEAEKKARQRQELQqAREEQIElkerRLAEEAEREEEEFERMLRKQAEDEE-----IEQEEAEKRRMKRLEhrRELEKQi 299
|
170
....*....|...
gi 4503593 493 ----QMKLMEMKD 501
Cdd:pfam13868 300 eereEQRAAEREE 312
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
333-510 |
1.05e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDL------QREKNnveQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA 406
Cdd:PRK09039 53 SALDRLNSQIAELadllslERQGN---QDLQDSVANLRASLSAAEAERSRLQ-----------------ALLAELAGAGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEvrkkcaeeaqlissLKAELTSQEsQIStyeeelAKAREELSRLQQETAELeesvesgKAQLEPLQQHLQDSQ 486
Cdd:PRK09039 113 AAEGRAGE--------------LAQELDSEK-QVS------ARALAQVELLNQQIAAL-------RRQLAALEAALDASE 164
|
170 180
....*....|....*....|....
gi 4503593 487 QEISSMQMKLmemKDLenhNSQLN 510
Cdd:PRK09039 165 KRDRESQAKI---ADL---GRRLN 182
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
314-509 |
1.23e-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: 45.19 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 314 ASLQKNIIGSSPVADFSAIKELDT-----LNNEIVDLQREKNNVEQdlKEKEDTIKQRTSEVQdLQdEVQREntnlqklq 388
Cdd:pfam15905 125 ASLEKQLLELTRVNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEA--KMKEVMAKQEGMEGK-LQ-VTQKN-------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 389 aqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkaelTSQESQISTYEEELAKAREELSRLQQETAELEESV 468
Cdd:pfam15905 193 ---------LEHSKGKVAQLEEKLVSTEKEKIEE-----------KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELL 252
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4503593 469 ESGKAQLEPLQQHLQDSQQEISSMQMKLME-MKDLENHNSQL 509
Cdd:pfam15905 253 KEKNDEIESLKQSLEEKEQELSKQIKDLNEkCKLLESEKEEL 294
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
345-501 |
1.25e-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: 43.29 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 345 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqellDELDEQKA---QLEEQLKEVRKKCAE 421
Cdd:pfam16789 30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS---------------DKILQMKRyikVVKERLKQEEKKVQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 422 eaqlisslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam16789 95 --------------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQDEIGSALHLANQRK 160
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
341-506 |
1.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 341 EIVDLQREKNNVEQDLkEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR---- 416
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 417 ---KKCAEEAQL-----ISSLKAELTSQESQISTYEEELakarEELSRLQQETAELEESV---ESGKAQLEPLQQHLQD- 484
Cdd:PRK02224 652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVealEALYDEAEELESMYGDl 727
|
170 180
....*....|....*....|....*.
gi 4503593 485 ----SQQEISSMQMKLMEMKDLENHN 506
Cdd:PRK02224 728 raelRQRNVETLERMLNETFDLVYQN 753
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
165-287 |
1.39e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.86 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 165 LGRVWELSDIDHDGMLDRDEFAvAMFLVYCALEKEPVPmSLPPALVPPSKRKTWVVSPAEK---AKYDEIFLKTDKDMDG 241
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFE-ALFRRLWATLFSEAD-TDGDGRISREEFVAGMESLFEAtvePFARAAFDLLDTDGDG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503593 242 FVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFH 287
Cdd:COG5126 85 KISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
397-496 |
1.42e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSlkaelTSQESQISTyeEELAKAREELSRLQQETAELE---ESVESGKA 473
Cdd:pfam13851 21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSE-----IQQENKRLT--EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92
|
90 100
....*....|....*....|...
gi 4503593 474 QLEPLQQHLQDSQQEISSMQMKL 496
Cdd:pfam13851 93 RLKVLEKELKDLKWEHEVLEQRF 115
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
340-499 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 340 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQV-QELLDELDEQKAQLEEQLKEVRK- 417
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEALDLQQFf 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 418 -KCAEEAQLISSLKAELTSQE------------SQISTYEEELAKAREELSRLQQETAELEESVESG-----KAQLEPLQ 479
Cdd:cd00176 113 rDADDLEQWLEEKEAALASEDlgkdlesveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDadeeiEEKLEELN 192
|
170 180
....*....|....*....|
gi 4503593 480 QHLQDSQQEISSMQMKLMEM 499
Cdd:cd00176 193 ERWEELLELAEERQKKLEEA 212
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
338-509 |
1.53e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 338 LNNEI---------VDLQREKNNVEQDLKEKEDTIKqrtseVQDLQDEVQRE-NTNLQKLQAQKQQVQE----------L 397
Cdd:pfam05483 188 LNNNIekmilafeeLRVQAENARLEMHFKLKEDHEK-----IQHLEEEYKKEiNDKEKQVSLLLIQITEkenkmkdltfL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQ-------LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-AELEES-- 467
Cdd:pfam05483 263 LEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELnk 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4503593 468 --------VESGKAQLEPLQQHLQDSQQ--EISSMQMKLMEMkDLENHNSQL 509
Cdd:pfam05483 343 akaahsfvVTEFEATTCSLEELLRTEQQrlEKNEDQLKIITM-ELQKKSSEL 393
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
336-509 |
1.67e-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: 45.49 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 336 DTLNNEIVDL-QREKnnvEQDLKEKED------------TIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL- 401
Cdd:pfam15921 377 DQLQKLLADLhKREK---ELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMEVQR--------------LEALLKAMk 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 DEQKAQLEEQLKEVRKKcAEEAQLISSLKAELTSQesqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 481
Cdd:pfam15921 440 SECQGQMERQMAAIQGK-NESLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
170 180 190
....*....|....*....|....*....|..
gi 4503593 482 LQDSQQEISSMQ----MKLMEMKDLENHNSQL 509
Cdd:pfam15921 512 IEATNAEITKLRsrvdLKLQELQHLKNEGDHL 543
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
406-509 |
1.69e-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: 43.41 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 406 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 484
Cdd:cd16855 4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
|
90 100
....*....|....*....|....*.
gi 4503593 485 SQQEISSMQMKLME-MKDLENHNSQL 509
Cdd:cd16855 80 KAQELLQLRMELADkFKKTIQLLSKL 105
|
|
| DUF1090 |
pfam06476 |
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ... |
404-489 |
1.74e-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: 41.84 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 482
Cdd:pfam06476 39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100
|
....*..
gi 4503593 483 QDSQQEI 489
Cdd:pfam06476 101 AEARQEL 107
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
333-506 |
1.93e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKK---CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ------ 483
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQglrkde 413
|
170 180
....*....|....*....|....*
gi 4503593 484 -DSQQEISSMQMKLMEMK-DLENHN 506
Cdd:PRK04778 414 lEAREKLERYRNKLHEIKrYLEKSN 438
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
313-489 |
1.95e-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: 44.17 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 313 RASLQKNII--GSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQ 390
Cdd:pfam15397 41 RKLLQQYEKfgTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKDKEYPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 391 KQQVQELL------------DELDEqkaqLEEQLKEVRKKCAEEAQLISslKAELTS-QESQISTYEEEL-AKARE---- 452
Cdd:pfam15397 118 KAVQIANLvrqlqqlkdsqqDELDE----LEEMRRMVLESLSRKIQKKK--EKILSSlAEKTLSPYQESLlQKTRDnqvm 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 4503593 453 --ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:pfam15397 192 lkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
404-510 |
2.15e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQ 480
Cdd:COG1566 88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELDEARAALDAAQA 162
|
90 100 110
....*....|....*....|....*....|
gi 4503593 481 HLQDSQQEISSMQMKLMEMKDLENHNSQLN 510
Cdd:COG1566 163 QLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
347-504 |
2.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 347 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQL 425
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 426 ISSLKAELTSQESQISTYEEELAKARE----------ELSRLQQETAELE-----------ESVESGKAQLEPLQQH--- 481
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEyle 606
|
170 180
....*....|....*....|...
gi 4503593 482 LQDSQQEIssmQMKLMEMKDLEN 504
Cdd:PRK03918 607 LKDAEKEL---EREEKELKKLEE 626
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
398-504 |
2.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlE 476
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---D 1063
|
90 100 110
....*....|....*....|....*....|..
gi 4503593 477 PLQQHLQDSQQEISSMQMKL----MEMKDLEN 504
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLtfceAEMDNLTK 1095
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
334-503 |
2.40e-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: 44.50 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQLE---E 410
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------------LTQKLTTAHRKEAENEallE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAR------------------EELSRLQQETAELEESVESGK 472
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltlqladaslalrEGRARWAQERETLQQSAEADK 317
|
170 180 190
....*....|....*....|....*....|.
gi 4503593 473 AQLEPLQQHLQDSQQeisSMQMKLMEMKDLE 503
Cdd:pfam07888 318 DRIEKLSAELQRLEE---RLQEERMEREKLE 345
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
353-510 |
2.41e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 353 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 432
Cdd:pfam01576 4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 433 -------LTSQESQISTYEEELAKAREELSRLQQETAELEEsvesgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD---- 501
Cdd:pfam01576 70 kqeleeiLHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE-------QLDEEEAARQKLQLEKVTTEAKIKKLEEdill 142
|
....*....
gi 4503593 502 LENHNSQLN 510
Cdd:pfam01576 143 LEDQNSKLS 151
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-469 |
2.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTiKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDE-----QKA- 406
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503593 407 QLEEQLKEVRKKCAEEAqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 469
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
332-488 |
2.57e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDE 403
Cdd:TIGR00618 713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQF 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHL 482
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQA 869
|
....*.
gi 4503593 483 QDSQQE 488
Cdd:TIGR00618 870 KIIQLS 875
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
410-509 |
2.61e-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: 41.62 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100
....*....|....*....|
gi 4503593 490 SSMqmkLMEMKDLENHNSQL 509
Cdd:pfam04871 77 DDL---LLLLGDLEEKVEKY 93
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
437-510 |
2.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503593 437 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 510
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELG 89
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
400-473 |
3.05e-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: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503593 400 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 473
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
333-498 |
3.09e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 412
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR--------------EKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 413 KEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAREELSRL--QQET---------------AELEESVESGKAQL 475
Cdd:COG1340 81 DELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLewRQQTevlspeeekelvekiKELEKELEKAKKAL 156
|
170 180
....*....|....*....|...
gi 4503593 476 EpLQQHLQDSQQEISSMQMKLME 498
Cdd:COG1340 157 E-KNEKLKELRAELKELRKEAEE 178
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
396-503 |
3.12e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100
....*....|....*....|....*...
gi 4503593 476 EPLQQHLQDSQQEISSMQMKLMEMKDLE 503
Cdd:COG1340 88 NELREELDELRKELAELNKAGGSIDKLR 115
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
396-505 |
3.32e-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: 43.85 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 464
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 4503593 465 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
403-509 |
3.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 403 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-------- 474
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 4503593 475 --LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:PRK04863 610 daLARLREQsgeeFEDSQDVTEYMQQLLERERELTVERDEL 650
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
396-510 |
3.92e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503593 476 EPLQ-------------QHLQDSQQ--------------EISSMQMKLMEMKDLENHNSQLN 510
Cdd:COG1340 102 AELNkaggsidklrkeiERLEWRQQtevlspeeekelveKIKELEKELEKAKKALEKNEKLK 163
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
407-509 |
3.97e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEVRKKCAEEAQLISslKAELtsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE---PLQQHLQ 483
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLG--LAPG--RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAK 785
|
90 100
....*....|....*....|....*.
gi 4503593 484 DSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQ 811
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
340-476 |
4.03e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 340 NEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLEEQLKEVRKKc 419
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELA-------EEAQELHEEMIELYKEADELRKE- 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 420 AEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 476
Cdd:COG1340 211 ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
316-508 |
4.50e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 316 LQKNIIGSSP----VADFSAIKELDTL-------NNEIVDLQREKNNVEQD---LKEKEDTIKQRTSEVQDLQDEVQREN 381
Cdd:PRK01156 117 IEKNILGISKdvflNSIFVGQGEMDSLisgdpaqRKKILDEILEINSLERNydkLKDVIDMLRAEISNIDYLEEKLKSSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 382 TNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQET 461
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSSLEDMKNRYESEIKTAESDLSMELEKN 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 462 AELEESVE---------------------SGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQ 508
Cdd:PRK01156 273 NYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYND 340
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
400-488 |
4.58e-04 |
|
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: 41.56 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 400 ELDEQKAQLEEQLK----EVRKKCAEEAQLissLKAELTSQESQISTYEEELAK-----AREELSRLQQ--ETAELEESV 468
Cdd:pfam05672 36 EKEEEERLRKEELRrraeEERARREEEARR---LEEERRREEEERQRKAEEEAEereqrEQEEQERLQKqkEEAEAKARE 112
|
90 100
....*....|....*....|
gi 4503593 469 ESGKAQLEpLQQHLQDSQQE 488
Cdd:pfam05672 113 EAERQRQE-REKIMQQEEQE 131
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
341-493 |
5.47e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 341 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA 420
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503593 421 EEAQLISSlKAELTSQESQIstyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:PRK01156 661 EIDSIIPD-LKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
328-578 |
5.48e-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: 43.88 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 328 DFSAIKELDTLNNEIVDLQR----EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldelde 403
Cdd:TIGR00606 686 VFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL------------------------ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 qkaqLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREE----LSRLQQETAELEESVESGKAQLE- 476
Cdd:TIGR00606 742 ----KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTdvtiMERFQMELKDVERKIAQQAAKLQg 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 477 --------PLQQHLQDSQQEISSMQMKLMEMKDL-ENHNSQLNWCSSPHSILvngATDYCSLSTSSSETANLNEHVEGQS 547
Cdd:TIGR00606 818 sdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLiQDQQEQIQHLKSKTNEL---KSEKLQIGTNLQRRQQFEEQLVELS 894
|
250 260 270
....*....|....*....|....*....|.
gi 4503593 548 NLESEPIHQESPARSspELLPSGVTDENEVT 578
Cdd:TIGR00606 895 TEVQSLIREIKDAKE--QDSPLETFLEKDQQ 923
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
291-560 |
5.79e-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: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 291 QKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVAdfsaIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTI---- 363
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifll 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 364 KQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLE-EQLKEVrkKCAEEAQLISSLKAELTSQES---- 438
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEE----------HYLKEVEDLKTELEkEKLKNI--ELTAHCDKLLLENKELTQEASdmtl 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 439 QISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIssmQMKLmemkdlenHNSQLNWCSSPHSI 518
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKL--------DKSEENARSIEYEV 582
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 4503593 519 LVNGAtdycSLSTSSSETANLNEHVEGQSNlESEPIHQESPA 560
Cdd:pfam05483 583 LKKEK----QMKILENKCNNLKKQIENKNK-NIEELHQENKA 619
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
410-502 |
6.25e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKCAEEAQLisslKAELTSQEsqISTYEEELAKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDS 485
Cdd:pfam07111 484 EQLREERNRLDAELQL----SAHLIQQE--VGRAREQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQES 557
|
90
....*....|....*..
gi 4503593 486 QQEISSMQMKLMEMKDL 502
Cdd:pfam07111 558 TEEAASLRQELTQQQEI 574
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
396-498 |
6.31e-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: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgk 472
Cdd:COG2825 33 RILQESPEGKaaqKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLS--EEERQKKERELQKKQQE------------ 98
|
90 100
....*....|....*....|....*.
gi 4503593 473 aqlepLQQHLQDSQQEISSMQMKLME 498
Cdd:COG2825 99 -----LQRKQQEAQQDLQKRQQELLQ 119
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
396-502 |
6.89e-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: 43.42 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES----- 470
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrar 290
|
90 100 110
....*....|....*....|....*....|..
gi 4503593 471 GKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 502
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
428-509 |
7.53e-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: 39.47 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 428 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqleplqqHLQDsqqEISSMQM--KLME--MKDLE 503
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANE-----------ILND---ELIALQIenNLLEekLRKLQ 66
|
....*.
gi 4503593 504 NHNSQL 509
Cdd:cd22887 67 EENDEL 72
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
334-488 |
7.57e-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: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqkLQAQKQQVQELLDELDEQKAQLEE 410
Cdd:COG3096 837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEelakAREELSRLQQETAELEESVE-------SGKAQL----- 475
Cdd:COG3096 908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983
|
170
....*....|....*.
gi 4503593 476 ---EPLQQHLQDSQQE 488
Cdd:COG3096 984 dlnEKLRARLEQAEEA 999
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-493 |
7.59e-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: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 290 SQKLIKGIDPPHVLTPEMIPPSDRASLQkniigsspvadfsAIKELDTLNNEIVD-------LQREKNNVEQDLKEKEDT 362
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERARRQ-------------AQQERDELADEIASgasgksaLQDEKRRLEARIAQLEEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 363 IKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQLISSLKAELTSQESQIS 441
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIA 977
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503593 442 TYEEEL-AKARE-----ELSR----------LQQE-----TAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:pfam01576 978 QLEEQLeQESRErqaanKLVRrtekklkevlLQVEderrhADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
332-501 |
8.00e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 42.00 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 409
Cdd:pfam16591 42 QKKLDELKQQLQQLKTTFTSPEnvRLLQEQLQLIQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVrkkcAEEAQLISSLKAEL-------------TSQES------QISTYEEELAKAREEL-----SRLQQETAELE 465
Cdd:pfam16591 122 EADSRR----AAQYQAISELKRQVqmaryqvrgytftPNEDSeqaayqQLDAALASLDQLRQALagdpgAALQQLTSALQ 197
|
170 180 190
....*....|....*....|....*....|....*....
gi 4503593 466 E---SVEsgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam16591 198 GyrdALD----TFKAAVAAIEQARQEMTSQGDEIVRISD 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
333-496 |
8.19e-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: 43.29 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKN----NVEQDLKEKEDTIKQRTS---EVQDLQDEVQRentnlqklQAQKQQVQELLDELDEQK 405
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNrrrsKIKEQNNRDIAGIKDKLAkirEARDRQLAVAE--------DDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 406 AQLEEQLKEVRKKCAEE------AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 479
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS 512
|
170
....*....|....*..
gi 4503593 480 QHLQDSQQEISSMQMKL 496
Cdd:pfam12128 513 RRLEERQSALDELELQL 529
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
335-510 |
9.08e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 335 LDTLNnEIVDLQREKNNVEQDLKEKEDTIKQRtsevqdlqDEVQRENtnlqklqaqkqqvqellDELDEQKAQLEEQLKE 414
Cdd:PRK11281 45 LDALN-KQKLLEAEDKLVQQDLEQTLALLDKI--------DRQKEET-----------------EQLKQQLAQAPAKLRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 415 VRKKcaeeaqlISSLKAELTSQESQ------ISTYEEELAKAREELSRLQQETAELEesvesgkAQLEPLQQHLQDSQQE 488
Cdd:PRK11281 99 AQAE-------LEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYN-------SQLVSLQTQPERAQAA 164
|
170 180
....*....|....*....|..
gi 4503593 489 ISSMQMKLMEMkdlenhNSQLN 510
Cdd:PRK11281 165 LYANSQRLQQI------RNLLK 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
431-510 |
9.25e-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: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 431 AELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL----MEMKDLENHN 506
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEI 92
|
....
gi 4503593 507 SQLN 510
Cdd:COG4942 93 AELR 96
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
327-500 |
9.63e-04 |
|
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: 42.97 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 327 ADFSAIKEL---DTLNNEivdLQREKNNVEQDLKEKEDtikQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDE 403
Cdd:pfam15964 347 ANFEKTKALiqcEQLKSE---LERQKERLEKELASQQE---KRAQEKEALRKEMKKEREELGAT----------MLALSQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVRKkcaEEAQLISSLKA---ELTSQESQISTYEEELakaREELSRLQQETAELEESVESGKAQlepLQQ 480
Cdd:pfam15964 411 NVAQLEAQVEKVTR---EKNSLVSQLEEaqkQLASQEMDVTKVCGEM---RYQLNQTKMKKDEAEKEHREYRTK---TGR 481
|
170 180
....*....|....*....|
gi 4503593 481 HLQDSQQEISSMQMKLMEMK 500
Cdd:pfam15964 482 QLEIKDQEIEKLGLELSESK 501
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
333-478 |
9.76e-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: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQR----------ENTNLQKLQAQKQQVQELLD 399
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 400 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA---REELSRLQQetaeLEESVESGKAQLE 476
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER----LKEEIEKSSKQRA 656
|
..
gi 4503593 477 PL 478
Cdd:TIGR00606 657 ML 658
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
343-505 |
1.00e-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: 43.11 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 343 VDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEEQLKEvRKKCAEE 422
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK-------TNELKSEKLQIGTNLQR-RQQFEEQ 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 423 AQLISSlkaELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQlepLQQHLQDSQQEISSmqmKLMEMKDL 502
Cdd:TIGR00606 890 LVELST---EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK---AQDKVNDIKEKVKN---IHGYMKDI 960
|
...
gi 4503593 503 ENH 505
Cdd:TIGR00606 961 ENK 963
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
356-493 |
1.12e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 356 LKEKEDTIKQR-TSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 430
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESAEQMKSAG------ERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503593 431 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
327-504 |
1.12e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 327 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTIKQ-RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 404
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 405 --------KAQLEE----QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK 472
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQL 258
|
170 180 190
....*....|....*....|....*....|...
gi 4503593 473 AQLEPLQQHLQDSQQEI-SSMQMKLMEMKDLEN 504
Cdd:pfam00038 259 ADYQELISELEAELQETrQEMARQLREYQELLN 291
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
338-495 |
1.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 338 LNNEIVDLQREKNNVEQDLKEKE-DTIK------QRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEE 410
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEgKNIKlskdvsSLESQLQDTQELLQEETRQKLNLSTR-------LRQLEDERNSLQE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QL-KEVRKKCAEEAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL- 482
Cdd:pfam01576 504 QLeEEEEAKRNVERQLstlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELd 583
|
170
....*....|....*....
gi 4503593 483 -----QDSQ-QEISSMQMK 495
Cdd:pfam01576 584 dllvdLDHQrQLVSNLEKK 602
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
445-494 |
1.28e-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: 38.34 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 4503593 445 EELAKAREELSRLQQE---TAELEESVESGKAQLEPLQQHLQDSQQEIssMQM 494
Cdd:cd22248 27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
332-503 |
1.30e-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: 41.83 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTL-----NNEIVDLQ-REKNNVEQDLKEKEDTIKQRTSE--VQDLQDEVQREntnlqklqaqkqqvQELLDELDE 403
Cdd:pfam13868 8 LRELNSKllaakCNKERDAQiAEKKRIKAEEKEEERRLDEMMEEerERALEEEEEKE--------------EERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEvRKKCAEEAQLISSLKAELTsQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqlepLQQHLQ 483
Cdd:pfam13868 74 YRQELEEQIEE-REQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143
|
170 180
....*....|....*....|
gi 4503593 484 DSQQEissmQMKLMEMKDLE 503
Cdd:pfam13868 144 ELEKE----EEREEDERILE 159
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
344-471 |
1.35e-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: 39.69 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 344 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEA 423
Cdd:pfam04871 5 ELESEASSLKNENTELKAELQELSKQYNSLEQK------------------ESQAKELEAEVKKLEEALKKLKAELSEEK 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 4503593 424 QLISSLKAEL-------TSQESQISTYEEELAKAREELSRLQQETAELEESVESG 471
Cdd:pfam04871 67 QKEKEKQSELddlllllGDLEEKVEKYKARLKELGEEVLSDDEDDDEDDEEDDEE 121
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
53-189 |
1.35e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 53 LGKIWDLADTDGKGILNKQEFfVALRLVACAQNGLEvslsslnlavppprfHDTSSPLLISGTSAAELPWAVKPED-KAK 131
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSE---------------ADTDGDGRISREEFVAGMESLFEATvEPF 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503593 132 YDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAM 189
Cdd:COG5126 71 ARAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
352-504 |
1.36e-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: 41.84 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 352 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELDE---QKAQLEEQLKEVRKKCAEEAQLI 426
Cdd:pfam13949 98 VRSKFREHEEDLELLSGPDEDLEAFLpsSRRAKNSPSVEEQVAKLRELLNKLNElkrEREQLLKDLKEKARNDDISPKLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 427 SSLKAEL-TSQESQIstYEEELAKAREELSRLQQETA---ELEESVESGKAQLEPLQQHLQDSQQEISSMqmklmeMKDL 502
Cdd:pfam13949 178 LEKARLIaPNQEEQL--FEEELEKYDPLQNRLEQNLHkqeELLKEITEANNEFLQDKRVDSEKQRQREEA------LQKL 249
|
..
gi 4503593 503 EN 504
Cdd:pfam13949 250 EN 251
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
411-494 |
1.38e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 QLKEVRKKCAE-------EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVesgkAQLEplQQhlQ 483
Cdd:PRK11637 48 QLKSIQQDIAAkeksvrqQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASI----AKLE--QQ--Q 119
|
90
....*....|.
gi 4503593 484 DSQQEISSMQM 494
Cdd:PRK11637 120 AAQERLLAAQL 130
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
398-510 |
1.39e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKaQLEEQLKEVRKKcAEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQeTAELEESVESGKA 473
Cdd:pfam12795 2 LDELEKAK-LDEAAKKKLLQD-LQQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASL 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 4503593 474 QLEPLQQHLQDSQQEISSMQmklmemKDLENHNSQLN 510
Cdd:pfam12795 79 SLEELEQRLLQTSAQLQELQ------NQLAQLNSQLI 109
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
334-501 |
1.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDE-------QKA 406
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAE--------------TELCAEAEEmrarlaaRKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS 151
|
170
....*....|....*
gi 4503593 487 QEISSMQMKLMEMKD 501
Cdd:pfam01576 152 KERKLLEERISEFTS 166
|
|
| Nnf1 |
pfam03980 |
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ... |
396-471 |
1.49e-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: 38.77 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 469
Cdd:pfam03980 33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101
|
..
gi 4503593 470 SG 471
Cdd:pfam03980 102 AQ 103
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
340-459 |
1.50e-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: 39.54 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 340 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKc 419
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 4503593 420 AEEAQliSSLKAELTSQESQISTYEEELAKAREELSRLQQ 459
Cdd:pfam07926 80 AESAK--AELEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
333-496 |
1.53e-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: 40.28 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQdeVQRENTnlqklqaqkqqvqELLDELDEQKAQLEE-- 410
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQEKLEQKEE-LGEGLTMIDFLQ--LQIENQ-------------ALNEKIEERNKELKRlk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 411 --------QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESveSG----------- 471
Cdd:pfam13870 70 lkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvpallhdy 147
|
170 180
....*....|....*....|....*...
gi 4503593 472 ---KAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:pfam13870 148 dktKAEVEEKRKSVKKLRRKVKILEMRI 175
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
345-463 |
1.54e-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: 42.42 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 345 LQREKNNVEQDLKEKEDTikqRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELL--DELDEQKAQ--------------- 407
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKlelekekrdrkraee 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503593 408 -----LEEQLKEVRKKCAEEAQLISSLKAELtsQESQISTYEEELAKAREELSRLQQETAE 463
Cdd:pfam17380 492 qrrkiLEKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
397-501 |
1.57e-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: 39.50 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKAQLEEQ-------LKEVRKKCAEEaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsve 469
Cdd:pfam17675 10 LLEELDKQLEDAEKErdayisfLKKLEKETPEE---LEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEE--- 83
|
90 100 110
....*....|....*....|....*....|..
gi 4503593 470 sgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam17675 84 ----ELEALDEEEEEFWREYNALQLQLLEFQD 111
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
338-501 |
1.64e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 338 LNNEIVD-----LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLE 409
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 410 EQLKEVRKKCAEEAQlisslkaeltsqesqistyeEELAKAREELSRLQQETAELE-ESVESGKAQ-LEPLQQHLQDSQQ 487
Cdd:PRK00409 562 EEEDKLLEEAEKEAQ--------------------QAIKEAKKEADEIIKELRQLQkGGYASVKAHeLIEARKRLNKANE 621
|
170
....*....|....
gi 4503593 488 EISSMQMKLMEMKD 501
Cdd:PRK00409 622 KKEKKKKKQKEKQE 635
|
|
| End3 |
pfam12761 |
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ... |
323-458 |
1.65e-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: 40.75 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 323 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE---VQREntnlqklqaqkqqvqelLD 399
Cdd:pfam12761 84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGGNRDESSKpalVKRE-----------------FE 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503593 400 ELDEQKaqlEEQLKEVR--KKCAEEAQLiSSLKAELTSQESQISTYEEELAKAREELSRLQ 458
Cdd:pfam12761 144 QLLDYK---ERQLRELEegSGKSKPINL-KSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
341-500 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 341 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD---ELDEQKAQLEE--QLKEV 415
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDtmqHLQEDRADLQAtvELLQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 416 R------------KKCAEEAQLISSLKAELTSQ-ESQISTYEEEL------AKA-----REELSRLQQETAELEESVESG 471
Cdd:pfam07111 271 RvqslthmlalqeEELTRKIQPSDSLEPEFPKKcRSLLNRWREKVfalmvqLKAqdlehRDSVKQLRGQVAELQEQVTSQ 350
|
170 180 190
....*....|....*....|....*....|.
gi 4503593 472 KAQLEPLQQHLQD--SQQEISSMQMKLMEMK 500
Cdd:pfam07111 351 SQEQAILQRALQDkaAEVEVERMSAKGLQME 381
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
396-509 |
1.82e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG0542 411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470
|
90 100 110
....*....|....*....|....*....|....*..
gi 4503593 476 EPLQ---QHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG0542 471 EEIQelkEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
333-517 |
1.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNE----IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQL 408
Cdd:pfam01576 176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE--------------LQAQIAELRAQLAKK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE------PLQQHL 482
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQQEL 321
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503593 483 QDS-QQEISSMQMKLMEmkDLENHNSQLNWCSSPHS 517
Cdd:pfam01576 322 RSKrEQEVTELKKALEE--ETRSHEAQLQEMRQKHT 355
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
397-500 |
2.03e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 397 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELEESVESGK 472
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEEAKSLAQ 401
|
90 100 110
....*....|....*....|....*....|.
gi 4503593 473 AQLEPLQQHLQDSQQ---EISSMQMKLMEMK 500
Cdd:pfam05701 402 AAREELRKAKEEAEQakaAASTVESRLEAVL 432
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
400-544 |
2.07e-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: 40.96 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 400 ELDEQKAQLEEQLKEVRKKCA--EEAQlisSLKAELTSQesqistYEEELAKAREELSRLQ------------------- 458
Cdd:pfam17045 43 ELLSARNTLERKHKEIGLLRQqlEELE---KGKQELVAK------YEQQLQKLQEELSKLKrsyeklqrkqlkeareeak 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 459 -QETAELEESVESGKAQ------LEPLQQHLQdSQQEISSMQmklMEMKDLENHNSQLNwcSSPHSILVNGATdyCSLST 531
Cdd:pfam17045 114 sREEDRSELSRLNGKLEefrqksLEWEQQRLQ-YQQQVASLE---AQRKALAEQSSLIQ--SAAYQVQLEGRK--QCLEA 185
|
170
....*....|...
gi 4503593 532 SSSETANLNEHVE 544
Cdd:pfam17045 186 SQSEIQRLRSKLE 198
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
396-506 |
2.18e-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: 40.19 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 470
Cdd:pfam06785 58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 4503593 471 ------GKAQLEPLQQHLQDSQQEISSmQMKLMEMKDLENHN 506
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEE-QRSVLEKRQDQIEN 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
345-509 |
2.34e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 345 LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQ--DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC 419
Cdd:TIGR00618 641 LALKLTALHAlqlTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 420 AEEAQLISSLKAELTSQES-----------------QISTYEEELAKARE--------ELSRLQQETA----ELEESVES 470
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDalnqslkelmhqartvlKARTEAHFNNNEEVtaalqtgaELSHLAAEIQffnrLREEDTHL 800
|
170 180 190
....*....|....*....|....*....|....*....
gi 4503593 471 GKAQLEPLQQHLQDSQQEISSMQMKLmeMKDLENHNSQL 509
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNLQCETL--VQEEEQFLSRL 837
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
349-510 |
2.35e-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: 40.27 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 349 KNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaeeaqli 426
Cdd:pfam13851 22 RNNLEliKSLKEEIAELKKKEERNEKLMSEIQQENKRLT----------EPLQKAQEEVEELRKQLENYEK--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 427 ssLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE-PLQQHLQDSQQEISSMQMKLMEM-KDLEN 504
Cdd:pfam13851 83 --DKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEaAIQDVQQKTGLKNLLLEKKLQALgETLEK 160
|
....*.
gi 4503593 505 HNSQLN 510
Cdd:pfam13851 161 KEAQLN 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-464 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLk 413
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL- 945
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 4503593 414 evrkkcAEEAQLisslkaELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:TIGR02168 946 ------SEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
333-466 |
2.46e-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: 41.33 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDeqkaQLEEQL 412
Cdd:pfam17097 133 DTLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECW-----------------ELLNELE----RLRDQR 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 4503593 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 466
Cdd:pfam17097 192 ITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEK 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
334-510 |
2.51e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIK-----------QRT----------SEVQDLQDEVQRENtnlQKLQAQKQ 392
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleeetaQKNnalkkireleAQISELQEDLESER---AARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 393 QVQELLDELDEQKAQLEEQL------KEVR-KKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR--------- 456
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTLdttaaqQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEqleqakrnk 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 457 ---------LQQETAELEE---SVESGK-----------AQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQLN 510
Cdd:pfam01576 373 anlekakqaLESENAELQAelrTLQQAKqdsehkrkkleGQLQELQARLSESERQRAELAEKLSKLQsELESVSSLLN 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-480 |
2.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVqrENTNLQKLQAQKQQVQELLDELDEQKAQ--- 407
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEiks 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 408 --------------LEEQLKEVRKKCAEEAQLISSLKA------------------------ELTSQESQISTYEEELAK 449
Cdd:PRK03918 544 lkkelekleelkkkLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKK 623
|
170 180 190
....*....|....*....|....*....|.
gi 4503593 450 AREELSRLQQETAELEESVESGKAQLEPLQQ 480
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
396-498 |
2.60e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELtsqESQISTYEEELAKAREELSRLQQEtaeleesvesgk 472
Cdd:pfam03938 9 KILEESPEGKaaqAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQE------------ 73
|
90 100
....*....|....*....|....*.
gi 4503593 473 aqlepLQQHLQDSQQEISSMQMKLME 498
Cdd:pfam03938 74 -----LQQLQQKAQQELQKKQQELLQ 94
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
409-494 |
2.63e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQE 488
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-DSEKQ 130
|
....*.
gi 4503593 489 ISSMQM 494
Cdd:PRK09039 131 VSARAL 136
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
432-498 |
2.87e-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: 37.25 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 432 ELTSQ-ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 498
Cdd:pfam06005 4 ELLEQlETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
333-504 |
2.88e-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: 40.99 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTI----------KQRTSEvqDL-QDEVQRentnlqklqaqkqqvqELLDEL 401
Cdd:pfam03148 64 KELEELDEEIELLLEEKRRLEKALEALEEPLhiaqecltlrEKRQGI--DLvHDEVEK----------------ELLKEV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 D----------EQKAQLEEQL---KEVRKKCA------EEAQLI----------S---SLKAELTSQESQISTYEE---- 445
Cdd:pfam03148 126 EliegiqellqRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEwekf 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 446 ----------ELAKA---REELSRLQQETAELEES---------------VESGKAQLEplqQHLQDSQQEISSMQmklM 497
Cdd:pfam03148 206 tqdnieraekERAASaqlRELIDSILEQTANDLRAqadavnfalrkrieeTEDAKNKLE---WQLKKTLQEIAELE---K 279
|
....*..
gi 4503593 498 EMKDLEN 504
Cdd:pfam03148 280 NIEALEK 286
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
353-493 |
3.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 353 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA- 431
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAr 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503593 432 --ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqdsQQEISSMQ 493
Cdd:PRK04863 595 iqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL---DEEIERLS 665
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
345-508 |
3.29e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 345 LQREKNNVEQDLKEKEDTIKQRtsevQDLQDEVQRENTNLQKLQAQKQQVQE---LLDELDEQKA------QLEEQLKEV 415
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQ----SSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTltqhihTLQQQKTTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 416 RKKCAEEAQLISSLKAELTSQESQISTYEEE---LAKAREELsRLQQETAELEESVESGKAQLEPLQQ-HLQDSQQEISS 491
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKE 470
|
170
....*....|....*..
gi 4503593 492 MQMKLmemKDLENHNSQ 508
Cdd:TIGR00618 471 REQQL---QTKEQIHLQ 484
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
336-501 |
3.52e-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: 41.25 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 336 DTLNNEIVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQdevQRENTNLQKLqaqkqqvqELLDELDEQKAQLEEQLKE 414
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKkHQEDIINCKKQEERMLK---QIENLEEKEM--------NLRDELESVREEFIQKGDE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 415 VRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREE-------LSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
|
170
....*....|....
gi 4503593 488 EISSMQMKLMEMKD 501
Cdd:pfam05483 644 ELASAKQKFEEIID 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
325-507 |
3.67e-03 |
|
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: 41.26 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 325 PVADfsaikELDTLNNEivdlqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDE-LDE 403
Cdd:pfam15921 242 PVED-----QLEALKSE------SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqARN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 404 QKAQLEEQLKEVRKKCAeeaQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELeeSVESGKA--QLEPLQQH 481
Cdd:pfam15921 311 QNSMYMRQLSDLESTVS---QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF--SQESGNLddQLQKLLAD 385
|
170 180
....*....|....*....|....*.
gi 4503593 482 LQDSQQEISSMQMKLMEMKDLENHNS 507
Cdd:pfam15921 386 LHKREKELSLEKEQNKRLWDRDTGNS 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-492 |
3.73e-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: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
90
....*....|....*..
gi 4503593 476 EPLQQHLQDSQQEISSM 492
Cdd:COG1196 763 EELERELERLEREIEAL 779
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
396-510 |
3.75e-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: 38.84 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSlKAELTSQESQISTYEEELAKAREELSRLQQetaeleesvesgkaQL 475
Cdd:TIGR02473 27 AEFERLETQLQQLIKYREEYEQQALEKVGAGTS-ALELSNYQRFIRQLDQRIQQQQQELALLQQ--------------EV 91
|
90 100 110
....*....|....*....|....*....|....*
gi 4503593 476 EPLQQHLQDSQQEIssMQMKLMEMKDLENHNSQLN 510
Cdd:TIGR02473 92 EAKRERLLEARREL--KALEKLKEKKQKEYRAEEA 124
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
408-510 |
3.87e-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: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 408 LEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:COG2433 378 IEEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455
|
90 100
....*....|....*....|...
gi 4503593 488 EISSMQMKLMEMKDLENHNSQLN 510
Cdd:COG2433 456 EERREIRKDREISRLDREIERLE 478
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
396-501 |
4.40e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 38.01 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCaeeaQLISSLKAELTSQ-ESQISTYEEELAKAREEL-SRLQQETAELEESVESGKA 473
Cdd:smart00502 7 ELLTKLRKKAAELEDALKQLISII----QEVEENAADVEAQiKAAFDELRNALNKRKKQLlEDLEEQKENKLKVLEQQLE 82
|
90 100
....*....|....*....|....*...
gi 4503593 474 QLEPLQQHLQDSQQEISsmqmKLMEMKD 501
Cdd:smart00502 83 SLTQKQEKLSHAINFTE----EALNSGD 106
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
401-487 |
4.56e-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: 41.09 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 401 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 451
Cdd:COG3096 295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374
|
90 100 110
....*....|....*....|....*....|....*.
gi 4503593 452 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 487
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
335-509 |
4.63e-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: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 335 LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 414
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 415 VRKKC--------AEEAQLISSLKaELTSQESQISTYEEELA-KAREEL---SRLQQ---ETAELEESVESGKAQLEPLQ 479
Cdd:pfam01576 438 LQSELesvssllnEAEGKNIKLSK-DVSSLESQLQDTQELLQeETRQKLnlsTRLRQledERNSLQEQLEEEEEAKRNVE 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4503593 480 QHLQDSQQEISSMQMKLMEM---------------KDLENHNSQL 509
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDagtlealeegkkrlqRELEALTQQL 561
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
398-493 |
4.72e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 38.03 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAEEA-----QLISSLKAELTSQESQISTYEEELAKAREELSRLQQEtaelEESVE--S 470
Cdd:pfam02050 21 LEELQQYRAEYQQQLSGAGQGISAAElrnyqAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQE----RKSLEklR 96
|
90 100
....*....|....*....|....*...
gi 4503593 471 GKAQLEplQQHLQDSQQ-----EISSMQ 493
Cdd:pfam02050 97 EREKKE--ERKEQNRREqkqldELAARL 122
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
403-509 |
4.73e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 403 EQKAQLEEQLKEVRKK-----------CAEE-----AQLISS--LKAELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:PRK10246 380 EQLRQWQQQLTHAEQKlnalpaitltlTADEvaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4503593 465 EESVESGKAQLEPLQQHLQD----SQQEissmqmklMEMKDLENHNSQL 509
Cdd:PRK10246 460 NAALNEMRQRYKEKTQQLADvktiCEQE--------ARIKDLEAQRAQL 500
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
316-496 |
4.82e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.00 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 316 LQKNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNveqdlKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQA--QKQQ 393
Cdd:PRK06669 1 MPKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKEKE-----RLREEEEEQVEQLREEANDEAKEIIEEAEEDAFeiVEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 394 VQELLDELDEQKAQLEEQLKEVRKKCA-EEAQLISSLKAELtsQESQISTYEEELAKAREE-LSRLQQETAELEESVESG 471
Cdd:PRK06669 76 EEEAKEELLKKTDEASSIIEKLQMQIErEQEEWEEELERLI--EEAKAEGYEEGYEKGREEgLEEVRELIEQLNKIIEKL 153
|
170 180
....*....|....*....|....*
gi 4503593 472 KAQLEplqQHLQDSQQEISSMQMKL 496
Cdd:PRK06669 154 IKKRE---EILESSEEEIVELALDI 175
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
357-480 |
4.96e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 357 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 435
Cdd:NF041483 520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503593 436 QESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQ 480
Cdd:NF041483 584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
398-495 |
5.79e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 37.20 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVrkKCAEEAqlISSLKAELTSQESqIST--YEEELAKAREElsrLQQETAELEESVESGKAQL 475
Cdd:pfam01920 11 LQLLAQQIKQLETQLKEL--ELALEE--LELLDEDTKVYKL-IGDvlVKQDKEEVKEQ---LEERKETLEKEIKTLEKQL 82
|
90 100
....*....|....*....|
gi 4503593 476 EPLQQHLQDSQQEISSMQMK 495
Cdd:pfam01920 83 EKLEKELEELKEELYKKFGQ 102
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
332-458 |
5.84e-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: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE- 410
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAt 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 4503593 411 --QLKEVRK-KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ 458
Cdd:pfam00529 161 vaQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
396-511 |
6.01e-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: 39.66 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREELSRLQQETAEL-EESVESGK 472
Cdd:cd22656 121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLnEEYAAKLK 200
|
90 100 110
....*....|....*....|....*....|....*....
gi 4503593 473 AQLEPLQQHLQDSQQEIssmQMKLMEMKDLENHNSQLNW 511
Cdd:cd22656 201 AKIDELKALIADDEAKL---AAALRLIADLTAADTDLDN 236
|
|
| CCDC-167 |
pfam15188 |
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ... |
398-453 |
6.20e-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: 36.49 E-value: 6.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 453
Cdd:pfam15188 5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
333-499 |
6.22e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 40.22 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 333 KELDTLNNEIVDL----QREKNNV---EQDLKEKEDTikqRTSEVQDLQDEVQR----ENTNLQKLQAQKQQVQELLDEL 401
Cdd:pfam09726 444 QENDLLQTKLHNAvsakQKDKQTVqqlEKRLKAEQEA---RASAEKQLAEEKKRkkeeEATAARAVALAAASRGECTESL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLkaELTSQEsqISTYEEElAKARE----ELSRLQQETAELEESVES------- 470
Cdd:pfam09726 521 KQRKRELESEIKKLTHDIKLKEEQIREL--EIKVQE--LRKYKES-EKDTEvlmsALSAMQDKNQHLENSLSAetrikld 595
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503593 471 -------GKAQLEPLQQHLQDSQQEISSMQMKLMEM 499
Cdd:pfam09726 596 lfsalgdAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
330-459 |
6.58e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTikqrtSEVQDLQDE----VQRENTNLQKLQAQKQQVQELLD------ 399
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQQRQEAR-----REREELQREeerlVQKEEQLDARAEKLDNLENQLEErekals 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503593 400 ----ELDEQKAQLEEQLKEVRKKCAEEA--QLISSLKAELTSQESQISTYEEElaKAREELSRLQQ 459
Cdd:PRK12705 116 arelELEELEKQLDNELYRVAGLTPEQArkLLLKLLDAELEEEKAQRVKKIEE--EADLEAERKAQ 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
334-489 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 334 ELDTLNNEIVDLQR--EKNNVEQDLKEKEDTIKQRTSEVQ-DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqLEE 410
Cdd:TIGR00618 585 DIPNLQNITVRLQDltEKLSEAEDMLACEQHALLRKLQPEqDLQDVRLHLQQCSQELALKLTALHALQLTLTQER--VRE 662
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503593 411 QLKEVRKkcaEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:TIGR00618 663 HALSIRV---LPKELLASRQLALQKMQSEK----EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
356-496 |
7.06e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 39.66 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 356 LKEKEDTIKQRTSEVQDLQDEVQRentnlqKLQAQKQQVQELLDE-------------LDEQKAQLEEQLKEVRKKCAEE 422
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQR------LQILCTSAEKELRYErgknldlkqhnslLQEENIKIKAELKQAQQKLLDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 423 AQLISSLKAELtsqesqistyeeelakareelSRLQQETAELE----ESVESGKAQ---LEPLQQH---LQDSQQEISSM 492
Cdd:pfam15742 75 TKMCSSLTAEW---------------------KHCQQKIRELElevlKQAQSIKSQnslQEKLAQEksrVADAEEKILEL 133
|
....
gi 4503593 493 QMKL 496
Cdd:pfam15742 134 QQKL 137
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
400-487 |
7.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 400 ELDEQKAQLEEQ---LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEELAK-------------- 449
Cdd:PRK04863 294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAasdhlnlvqtalrQQEKIERYQADLEEleerleeqnevvee 373
|
90 100 110
....*....|....*....|....*....|....*...
gi 4503593 450 AREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 487
Cdd:PRK04863 374 ADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQQ 410
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
330-510 |
7.68e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 330 SAIKELDTLNNEIVDLQREknnVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAqK---QQVQELLDELDEQ 404
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETL---IASRQEERQETSAELNQLLRTLDDQWKekRDELNGELSAA-DaavAKDRSELEALEDQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 405 KAQLEEQLKEVRKKCAEEAQLISS--------LKAELTSQESQISTYEEELAKAREE----LSRLQQETAELEESVESGK 472
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSelenleerLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQL 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4503593 473 A-------QLE-PLQQHLQDSQQEISSMQMKLMEmkDLENHNSQLN 510
Cdd:pfam12128 411 AvaeddlqALEsELREQLEAGKLEFNEEEYRLKS--RLGELKLRLN 454
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
346-475 |
7.79e-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: 39.52 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 346 QREKNNVEQDLKEKEDTIKQRTSEVQD----LQDEVQREntnlqklQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE 421
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIELkerrLAEEAERE-------EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503593 422 EaqlisslkaeltsQESQI----STYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:pfam13868 294 E-------------LEKQIeereEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
399-489 |
8.46e-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: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 399 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAeLEESVESGKAQLEPL 478
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEEL 359
|
90
....*....|.
gi 4503593 479 QQHLqDSQQEI 489
Cdd:COG3096 360 TERL-EEQEEV 369
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
344-509 |
8.52e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 344 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 423
Cdd:pfam07888 56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 424 QLISSLKAELTSQESQISTYEEELAKA----REELSRLQQETAELEESVE----------SGKAQLEPLQQHLQDSQQEI 489
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAgaqrKEEEAERKQLQAKLQQTEEelrslskefqELRNSLAQRDTQVLQLQDTI 215
|
170 180
....*....|....*....|
gi 4503593 490 SSMQMKLMEMKDLENHNSQL 509
Cdd:pfam07888 216 TTLTQKLTTAHRKEAENEAL 235
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
346-500 |
8.64e-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: 39.52 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 346 QREKNNV--------EQDLKEKEdtikQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE----QKAQLEEQLK 413
Cdd:pfam13868 97 LQEREQMdeiveriqEEDQAEAE----EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeylkEKAEREEERE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 414 EVRKKCAEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQETA----ELEEsVESGKAQLEPLQQHLQdsQQEI 489
Cdd:pfam13868 173 AEREEIEEEKERE---IARLRAQQEKAQDEKAERDELRAKLYQEEQERKerqkEREE-AEKKARQRQELQQARE--EQIE 246
|
170
....*....|.
gi 4503593 490 SSMQMKLMEMK 500
Cdd:pfam13868 247 LKERRLAEEAE 257
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
398-475 |
8.82e-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: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 398 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAELTSQEsqisTYEEELAKAREELSRLQQET-AELEESVESGKA 473
Cdd:cd06503 39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERILEQAkAEIEQEKEKALA 113
|
..
gi 4503593 474 QL 475
Cdd:cd06503 114 EL 115
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
405-498 |
8.83e-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: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 405 KAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgkaqlepLQQHLQD 484
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQE-----------------FQRKQQK 80
|
90
....*....|....
gi 4503593 485 SQQEISSMQMKLME 498
Cdd:smart00935 81 LQQDLQKRQQEELQ 94
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
338-462 |
9.36e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 38.92 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503593 338 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 414
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 4503593 415 vrkkcaeEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA 462
Cdd:pfam15294 211 -------STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTA 251
|
|
| |
