|
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 |
3.21e-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: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 121 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 1034556461 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 ... |
254-350 |
1.96e-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: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 254 QWVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkG 333
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 1034556461 334 IDPPHVLTPEMIPPSDR 350
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
3.60e-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: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 13 SSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 1034556461 93 SLNLAVPPPRF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
265-330 |
1.55e-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: 1.55e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 265 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 330
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 ... |
121-218 |
1.80e-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: 104.38 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 121 PWAVKpedkaKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763 6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
|
90 100
....*....|....*....|
gi 1034556461 200 -PVPMSLPPALVPPSKRKTV 218
Cdd:pfam12763 81 aDVPDELPDWLVPGSKAHLI 100
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
132-197 |
5.89e-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: 5.89e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556461 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 |
2.46e-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: 2.46e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556461 19 YEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQN 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
367-562 |
3.69e-17 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 84.18 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 446
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 524
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034556461 525 EISSARSSPELLPSGVTDENEVTTAVTEKVCSELDNNR 562
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
370-526 |
4.96e-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: 78.43 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 449
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556461 450 KEVRKkcAEEAQlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:COG1579 83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-530 |
1.55e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISS 528
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEEL 405
|
..
gi 1034556461 529 AR 530
Cdd:COG1196 406 EE 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-540 |
3.61e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 361 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDE 440
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 520
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180
....*....|....*....|
gi 1034556461 521 DSQQEISSARSSPELLPSGV 540
Cdd:COG4913 423 ELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-534 |
4.75e-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: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 450
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 451 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSAR 530
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
....
gi 1034556461 531 SSPE 534
Cdd:TIGR02168 428 KKLE 431
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-530 |
4.59e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 449
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
.
gi 1034556461 530 R 530
Cdd:COG1196 385 A 385
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-568 |
6.72e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS-------KELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:TIGR02168 778 AEAEAE-------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034556461 530 RSSPELLPSGVTDENEVTTAVTEKVcSELDNNRHSKEED 568
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESEL-EALLNERASLEEA 888
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
370-528 |
8.25e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.36 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 528
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-536 |
1.06e-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: 72.40 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 366 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 445
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEES------------VESGKAQLE 513
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelqaeLEELEEELE 450
|
170 180
....*....|....*....|...
gi 1034556461 514 PLQQHLQDSQQEISSARSSPELL 536
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-531 |
1.12e-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: 72.01 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKA 443
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALA----------NEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 444 QLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 523
Cdd:TIGR02168 306 ILRERLANLERQ-------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
....*...
gi 1034556461 524 QEISSARS 531
Cdd:TIGR02168 379 EQLETLRS 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-531 |
3.98e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE--- 446
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeel 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 ----EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 522
Cdd:COG1196 333 eeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
....*....
gi 1034556461 523 QQEISSARS 531
Cdd:COG1196 413 LERLERLEE 421
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
347-506 |
5.09e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 66.49 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 347 PSDRASLQKNIIGsspvadfsAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqre 417
Cdd:COG1579 30 PAELAELEDELAA--------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 418 ntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSR 493
Cdd:COG1579 98 -----------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEE 160
|
170
....*....|...
gi 1034556461 494 LQQETAELEESVE 506
Cdd:COG1579 161 LEAEREELAAKIP 173
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-511 |
5.77e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 445
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EE---QLKEVRKKCAEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 511
Cdd:COG4717 173 AElqeELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
370-531 |
5.87e-12 |
|
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: 68.25 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 449
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAE---EAQLISS-------LKAELTSQESQISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPL 515
Cdd:COG4942 100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*.
gi 1034556461 516 QQHLQDSQQEISSARS 531
Cdd:COG4942 180 LAELEEERAALEALKA 195
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-530 |
8.07e-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: 69.32 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 450
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 451 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSAR 530
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-567 |
9.78e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQREntnlqklqaqkqqvqelLDELDEQKAQLEE 447
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKE-----------------IEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPL 515
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 516 QQHLQDSQQEISSARSSPEllpsGVTDENEVTTAVTEKVCSELDNNRHSKEE 567
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQ----ELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
364-531 |
1.08e-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: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 364 ADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKA 443
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 444 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 523
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
....*...
gi 1034556461 524 QEISSARS 531
Cdd:COG1196 449 EEEAELEE 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-531 |
1.20e-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: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 449
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
..
gi 1034556461 530 RS 531
Cdd:COG1196 427 EE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-531 |
1.21e-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: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 447
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 527
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
....
gi 1034556461 528 SARS 531
Cdd:COG1196 390 EALR 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
379-531 |
1.32e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.23 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 379 IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 458
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQ--- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556461 459 eaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:COG4372 89 ----LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
375-567 |
1.37e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.51 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 375 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRK 454
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 455 KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKA---QLEPLQQHLQDS 522
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKkqeEKQELIDQKEKE 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034556461 523 QQEISSARSSPELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEE 567
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
370-529 |
2.38e-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: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDL-----------QDEVQRENTNLQKLQAQKQQVQELLDEL 438
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 439 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 518
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
170
....*....|.
gi 1034556461 519 LQDSQQEISSA 529
Cdd:COG4942 236 AAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-568 |
3.10e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.35 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 441
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 442 KAQLEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESV-------ESGKAQLEP 514
Cdd:TIGR04523 290 LNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsesenSEKQRELEE 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 515 LQQHLQDSQQEISSARSSPELLPSGVTD-ENEVTTAvtEKVCSELDNNRHSKEED 568
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDlESKIQNQ--EKLNQQKDEQIKKLQQE 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
367-533 |
1.65e-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: 63.63 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRE-------------------------NTNL 421
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQkeelaellralyrlgrqpplalllsPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 422 QKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEL 501
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|..
gi 1034556461 502 EESVESGKAQLEPLQQHLQDSQQEISSARSSP 533
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
397-532 |
2.26e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 397 EDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQ 476
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLR--------------EELEQAREELEQLEEELEQARSE-------LEQLEEELEELNEQ 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 477 ISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSS 532
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-540 |
3.29e-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: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 447
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRKKCAEEAQLISSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQeis 527
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE--- 498
|
170
....*....|...
gi 1034556461 528 sARSSPELLPSGV 540
Cdd:COG1196 499 -AEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-530 |
3.47e-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: 63.92 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
.
gi 1034556461 530 R 530
Cdd:TIGR02168 914 R 914
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
392-528 |
4.68e-10 |
|
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: 59.56 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 392 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 470
Cdd:pfam08614 11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556461 471 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISS 528
Cdd:pfam08614 88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVA 138
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-520 |
8.30e-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: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKE-------DTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD--- 439
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaai 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 440 ----EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESG 508
Cdd:TIGR02169 430 agieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGG 509
|
170
....*....|..
gi 1034556461 509 KAQLEPLQQHLQ 520
Cdd:TIGR02169 510 RAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-549 |
1.93e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR----------------ENTNLQKLQAQKQQ 430
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgeraralyrsgGSVSYLDVLLGSES 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 431 VQELLDELD------EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREE----LSRLQQETAE 500
Cdd:COG3883 114 FSDFLDRLSalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034556461 501 LEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTA 549
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
367-536 |
1.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 445
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIS--TYE---EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLq 520
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL- 703
|
170
....*....|....*.
gi 1034556461 521 dsqQEISSARSSPELL 536
Cdd:PRK03918 704 ---EEREKAKKELEKL 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-536 |
2.55e-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: 60.16 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkAQLEP 514
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE---AQKEE 105
|
90 100
....*....|....*....|..
gi 1034556461 515 LQQHLQDSQQeiSSARSSPELL 536
Cdd:COG4942 106 LAELLRALYR--LGRQPPLALL 125
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-554 |
6.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVD----LQREKNNVE--QDLK-EKEDT-IKQRTSEVQDLqdEVQRENTNLQklqaqkqqvqelLDELDE 440
Cdd:TIGR02169 186 IERLDLIIDEKRQqlerLRREREKAEryQALLkEKREYeGYELLKEKEAL--ERQKEAIERQ------------LASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQEsqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 520
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190
....*....|....*....|....*....|....
gi 1034556461 521 DSQQEISSARSSPELLPSGVTDENEVTTAVTEKV 554
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-533 |
8.29e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------------------DL--------------QDE 413
Cdd:COG3883 55 ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsesfsDFldrlsalskiadadADL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 414 VQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR 493
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034556461 494 LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSP 533
Cdd:COG3883 215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-530 |
1.20e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL 449
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------QISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
.
gi 1034556461 530 R 530
Cdd:TIGR02168 830 E 830
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
367-568 |
1.49e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQEL 434
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 514
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 515 LQQhLQDSQQEISSARSSPELLPSGVTDENEVTTAVTEKVCS------ELDNNRHSKEED 568
Cdd:PRK02224 501 AED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEElreraaELEAEAEEKREA 559
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
440-531 |
1.65e-08 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 53.80 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 440 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 504
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79
|
90 100 110
....*....|....*....|....*....|.
gi 1034556461 505 VESGKAQLEPLQQHLQDS----QQEISSARS 531
Cdd:pfam07926 80 AESAKAELEESEESWEEQkkelEKELSELEK 110
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
371-532 |
2.86e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKA 443
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 444 QLEEQLKEVRKKCAEEAQLISSLKAELTSQES-------QISTYEEELAKAREELSRLQQETAELEESVESGKA------ 510
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404
|
170 180
....*....|....*....|...
gi 1034556461 511 -QLEPLQQHLQDSQQEISSARSS 532
Cdd:PRK02224 405 vDLGNAEDFLEELREERDELRER 427
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
372-533 |
2.97e-08 |
|
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: 57.52 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 372 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQ 430
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----------KSTLAGE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 431 VQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA------------- 487
Cdd:pfam10174 382 IRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKeriierlkeqrer 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 488 -----REELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSP 533
Cdd:pfam10174 462 edrerLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSG 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-518 |
3.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAREELSRLQQETAELEESV---ESGKAQLEPLQQH 518
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
350-531 |
3.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 350 RASLQKNIIGsspvadFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTIKQR--------------------TSE 406
Cdd:COG4913 596 RRIRSRYVLG------FDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERrealqrlaeyswdeidvasaERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 407 VQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELA 485
Cdd:COG4913 670 IAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034556461 486 KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLN 783
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
372-545 |
4.56e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 372 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQ 444
Cdd:COG4717 48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 445 LE--EQLKEVRKKCAEEAQLISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETA--------ELEESVESGKAQ 511
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....
gi 1034556461 512 LEPLQQHLQDSQQEISSARSSPELLPSGVTDENE 545
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
382-529 |
9.07e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.95 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 382 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 461
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 462 LISSLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAA 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-529 |
9.21e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 366 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqqVQELLDELDEQKAQL 445
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-----------YQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EEQLKEVRKkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQE 525
Cdd:COG4717 412 EELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAE 484
|
....
gi 1034556461 526 ISSA 529
Cdd:COG4717 485 LREL 488
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
366-528 |
1.12e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 55.61 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 366 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQL 445
Cdd:PRK04778 89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EEQLKEVRKKCAEEA----QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQ 516
Cdd:PRK04778 146 KDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQ 225
|
170
....*....|..
gi 1034556461 517 QHLQDSQQEISS 528
Cdd:PRK04778 226 TELPDQLQELKA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-501 |
1.25e-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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034556461 450 KEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 501
Cdd:COG4913 415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-529 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 355 KNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ----RENTNLQKLQAQKQQ 430
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 431 VQELLDELDEQKAQ----------LEEQLKEVRKKCA--------EEAQL-------------ISSLKAELTSQESQIST 479
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556461 480 YEEELAKAREELSR-----------------LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
368-522 |
1.33e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 55.23 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDe 440
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 qkaQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 520
Cdd:PRK04778 359 ---SLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
..
gi 1034556461 521 DS 522
Cdd:PRK04778 436 KS 437
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-532 |
1.53e-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: 55.03 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQ 448
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK--------------YNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 449 LKEVRKKCAEEAQLISSLKAELTSQE---SQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
....*..
gi 1034556461 526 ISSARSS 532
Cdd:TIGR04523 255 LNQLKDE 261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
370-525 |
1.69e-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: 55.03 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQL 449
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQN 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ 303
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
371-528 |
1.72e-07 |
|
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: 53.88 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREknnveqdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 450
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 451 EVRKKC-----------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQL 512
Cdd:pfam04849 182 KLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIEN 261
|
170
....*....|....*....
gi 1034556461 513 EPLQQHLQ---DSQQEISS 528
Cdd:pfam04849 262 EELQQHLQaskEAQRQLTS 280
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-528 |
1.77e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 450
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 451 EVRKKCAE-EAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------A 510
Cdd:TIGR02169 872 ELEAALRDlESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeL 951
|
170
....*....|....*...
gi 1034556461 511 QLEPLQQHLQDSQQEISS 528
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRA 969
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
398-501 |
2.22e-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: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 398 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 477
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 1034556461 478 STYEEELAKAREELSRLQQETAEL 501
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-517 |
2.43e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEivDLQREKNNVEQdLKEKEDTIKqrtSEVQDLQDEVQRENtnlqKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:PRK03918 510 EKLKKYNLE--ELEKKAEEYEK-LKEKLIKLK---GEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKEL 579
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 450 KEVRKKCAEEAQL-ISSLKA------ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQ 517
Cdd:PRK03918 580 EELGFESVEELEErLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
367-530 |
2.52e-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: 52.69 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE 440
Cdd:pfam12795 48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLK--EVRKKCAEEAQLIsSLKAELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQ 516
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLE 197
|
170
....*....|....
gi 1034556461 517 QHLQDSQQEISSAR 530
Cdd:pfam12795 198 QQLQALQELLNEKR 211
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
2.68e-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: 2.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034556461 32 GRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLV 80
Cdd:pfam12763 24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
434-534 |
2.80e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 434 LLDELDEQKAQLEEQlkevRKKcAEEAQLISS----LKAELT-----SQESQISTYEEELAKAREELSRLQQETAELEES 504
Cdd:COG1196 194 ILGELERQLEPLERQ----AEK-AERYRELKEelkeLEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110
....*....|....*....|....*....|
gi 1034556461 505 VESGKAQLEPLQQHLQDSQQEISSARSSPE 534
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELA 298
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
369-526 |
3.14e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.99 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL---------- 438
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 439 -DEQK------AQLEEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 511
Cdd:COG1340 132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
170
....*....|....*
gi 1034556461 512 LEPLQQHLQDSQQEI 526
Cdd:COG1340 211 ADELHKEIVEAQEKA 225
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
346-510 |
3.31e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.09 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 346 PPSDRASLQKNIIGSSPVADfsAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlq 422
Cdd:COG2433 361 PDVDRDEVKARVIRGLSIEE--ALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 423 klqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEELAKAREELSRLQqeta 499
Cdd:COG2433 436 ------------LEEKDERIERLERELSEARSEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLK---- 499
|
170
....*....|.
gi 1034556461 500 ELEESVESGKA 510
Cdd:COG2433 500 ELWKLEHSGEL 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-516 |
3.34e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL 434
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 ------LDELDEQKAQLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELEESV 505
Cdd:PRK03918 462 kriekeLKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEI 541
|
170
....*....|.
gi 1034556461 506 ESGKAQLEPLQ 516
Cdd:PRK03918 542 KSLKKELEKLE 552
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
354-528 |
3.41e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 354 QKNIIGSSPVADFSAIKELDTLNNEIVDLQREK-------NNVEQDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKL 424
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaearlAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 425 QAQKQQV----QELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQE 497
Cdd:COG3206 283 SARYTPNhpdvIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAE 352
|
170 180 190
....*....|....*....|....*....|.
gi 1034556461 498 TAELEESVESGKAQLEPLQQHLQDSQQEISS 528
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-536 |
3.69e-07 |
|
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: 54.29 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqelldELDEQKAQLEE 447
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------------ELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 527
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
....*....
gi 1034556461 528 SARSSPELL 536
Cdd:TIGR02168 369 ELESRLEEL 377
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
391-526 |
3.93e-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: 51.36 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 391 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 470
Cdd:pfam06785 83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 471 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEI 187
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-528 |
4.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 445
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 523
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
....*
gi 1034556461 524 QEISS 528
Cdd:PRK03918 331 KELEE 335
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
433-502 |
5.49e-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: 47.69 E-value: 5.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 502
Cdd:pfam12329 5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-525 |
5.57e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLE 446
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKCAEEAQ-------LISSLKAELTSQE-----------SQISTYE----EELAKAREELSRLQQETAELEES 504
Cdd:COG3883 79 AEIEERREELGERARalyrsggSVSYLDVLLGSESfsdfldrlsalSKIADADadllEELKADKAELEAKKAELEAKLAE 158
|
170 180
....*....|....*....|.
gi 1034556461 505 VESGKAQLEPLQQHLQDSQQE 525
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAE 179
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
370-517 |
5.93e-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: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 450 KEVRKKCAEEAQL-----------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQ 517
Cdd:pfam05667 411 DASAQRLVELAGQwekhrvplieeYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-523 |
6.11e-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: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 364 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqAQKQQVQELLDELDEQK 442
Cdd:COG4913 685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 443 AQL--EEQLKEVRKKCAEEAQLISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREE 490
Cdd:COG4913 756 AAAlgDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEER 835
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034556461 491 LSRLQQET---------AELEESVESGKAQLEPLQQHLQDSQ 523
Cdd:COG4913 836 FKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
370-531 |
9.35e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVeqDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQL 449
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQ--LISSLKAELTSQESQISTYEE-------ELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHL 519
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQlQQEAQRILASLEAELEALQARE 329
|
170
....*....|..
gi 1034556461 520 QDSQQEISSARS 531
Cdd:COG3206 330 ASLQAQLAQLEA 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
367-568 |
1.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqAQKQQVQELLDELDEQKAQ 444
Cdd:COG4913 229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA---------LRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 445 LEEQLKEVRKKCAEEAQLISSLKAE---------------LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK 509
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREEldeleaqirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 510 AQLEPLQQHLQDSQQEISSARSSpellpsgvtDENEVTTAVTEKvcSELDNNRHSKEED 568
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEA---------LEEALAEAEAAL--RDLRRELRELEAE 427
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
370-567 |
1.41e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNN-------VEQDLKEKEDTI----KQRTSEVQDLQDEVqrentnlqklqaqkqqvqelldel 438
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIerlkEQREREDRERLEEL------------------------ 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 439 deqkAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 518
Cdd:pfam10174 471 ----ESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 519 LQDSQQEISSARSSPELLPSGVTDENEVTTAVTE--KVCSELD----------NNRHSKEE 567
Cdd:pfam10174 540 LKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEEsgKAQAEVErllgilreveNEKNDKDK 600
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
439-568 |
1.94e-06 |
|
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: 48.06 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 439 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQistyeeelakareELSRLQQETAELEesVESGKAQLEPLQQ 517
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQ-------------ELAILEAENSKAE--VETLKAEIEEMAQ 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 518 HLQDSQQEISSARSSPELLPSGVTDENEvTTAVTEKVCSELDNNRHSKEED 568
Cdd:pfam10473 67 NLRDLELDLVTLRSEKENLTKELQKKQE-RVSELESLNSSLENLLEEKEQE 116
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
393-528 |
2.03e-06 |
|
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: 49.13 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 393 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 469
Cdd:pfam15619 6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 470 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 527
Cdd:pfam15619 69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141
|
.
gi 1034556461 528 S 528
Cdd:pfam15619 142 D 142
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
358-530 |
2.29e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 358 IGSSPVADfsAIKE----LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRtSEVQDLQDevQRENTNlqklqaqkqqvqE 433
Cdd:PRK02224 461 VEGSPHVE--TIEEdrerVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------E 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 434 LLDELDEQKAQLEEQLKEVRKKCAEeaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLE 513
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIR 595
|
170
....*....|....*..
gi 1034556461 514 PLQQHLQDSQQEISSAR 530
Cdd:PRK02224 596 TLLAAIADAEDEIERLR 612
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
357-549 |
2.32e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 357 IIGSSPVADF----SAIKELDTLNNEIVDLQREKnnvEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvq 432
Cdd:COG3883 108 LLGSESFSDFldrlSALSKIADADADLLEELKAD---KAELEAKKAELEAKLAELEALKAELE----------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 512
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034556461 513 EPLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTA 549
Cdd:COG3883 248 GAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
382-501 |
4.27e-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: 47.34 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 382 LQREKNNVEQDLKE------KEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKK 455
Cdd:pfam05672 25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034556461 456 CAEEAQlisslkAELTSQESQISTYEEELAKAREELSRLQQETAEL 501
Cdd:pfam05672 85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
350-512 |
4.55e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 350 RASLQKNI-IGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqk 428
Cdd:COG3206 242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 429 qqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVE 506
Cdd:COG3206 311 --AQRILASLEAELEALQAREASLQ---AQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384
|
....*.
gi 1034556461 507 SGKAQL 512
Cdd:COG3206 385 VGNVRV 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
433-531 |
4.73e-06 |
|
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: 48.77 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 499
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1034556461 500 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:COG1579 104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
381-517 |
4.92e-06 |
|
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: 46.42 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 381 DLQREKNNVE------QDLKEKEDTIKQRTSEV-------QDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEE 447
Cdd:pfam18595 3 TLAEEKEELAelerkaRELQAKIDALQVVEKDLrscikllEEIEAELAKLE--------------EAKKKLKELRDALEE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRkkcaeeaqlisslkaELTSQESQIstyEEELAKAREELSRLQQETaelEESVESGKAQLEPLQQ 517
Cdd:pfam18595 69 KEIELR---------------ELERREERL---QRQLENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-570 |
5.34e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE-------AQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEvrkkcaeeaqlissLKAELTSQESQISTYEEelAKAREELSRLQQETAELEESVESGKAQLEPLQQhLQDSQQEISSA 529
Cdd:COG4372 160 ES--------------LQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIES-LPRELAEELLE 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034556461 530 RSSPELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEEDPF 570
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
252-356 |
5.36e-06 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 45.83 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 252 LRQWvvspaEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLI 331
Cdd:pfam12763 4 LEEW-----EIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LV 76
|
90 100
....*....|....*....|....*..
gi 1034556461 332 KGI--DPPHVLTPEMIPPSDRASLQKN 356
Cdd:pfam12763 77 NGNiaDVPDELPDWLVPGSKAHLIQAN 103
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
371-539 |
5.88e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREknNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLK 450
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDADDLEERAEELREEAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 451 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSAR 530
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE 446
|
....*....
gi 1034556461 531 sspELLPSG 539
Cdd:PRK02224 447 ---ALLEAG 452
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-594 |
6.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 383 QREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------EV 452
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeEL 1707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 453 RKKCAEEAQlisslKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSArss 532
Cdd:PTZ00121 1708 KKKEAEEKK-----KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA--- 1779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 533 peLLPSGVTDENEVTTAVTEKVCSELDNN-----RHSKEEDPFNVDSS----SLTGPVADT-NLDFFQSDPF 594
Cdd:PTZ00121 1780 --VIEEELDEEDEKRRMEVDKKIKDIFDNfaniiEGGKEGNLVINDSKemedSAIKEVADSkNMQLEEADAF 1849
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
391-528 |
8.75e-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: 49.47 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 391 QDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA---QLEEQLKEVRKKCAEEA----QLI 463
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELD-----------------ELLESEEKNREeveELKDKYRELRKTLLANRfsygPAI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 464 SSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 528
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE 218
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
369-534 |
1.08e-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: 49.27 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTIKQRTSEVQDLQDEV------QRENTNLQKLQAQKQQVQELLD-- 436
Cdd:TIGR00606 743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGSDld 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 437 ----ELDEQKAQLEEQLK------EVRKKCAEEAQ-LISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELE 502
Cdd:TIGR00606 822 rtvqQVNQEKQEKQHELDtvvskiELNRKLIQDQQeQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
170 180 190
....*....|....*....|....*....|..
gi 1034556461 503 ESVESGKAQLEPLQQHLQDSQQEISSARSSPE 534
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
372-524 |
1.18e-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: 46.49 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 372 LDTLNNEIVDLQREKNNVEQDLKEKedtikqRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKE 451
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 452 VRKKCAEEAQLissLKAELtsqESQISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQH 518
Cdd:pfam01442 60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAER 133
|
....*.
gi 1034556461 519 LQDSQQ 524
Cdd:pfam01442 134 LEELKE 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-532 |
1.19e-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: 49.30 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 363 VADFSAikELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQK 442
Cdd:TIGR02169 296 IGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 443 AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-------EEELAKAREELSRLQQETAELEESVESGKAQLEPL 515
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
170
....*....|....*..
gi 1034556461 516 QQHLQDSQQEISSARSS 532
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQE 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-535 |
1.29e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 392 DLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaQKQQVQELLDELD-EQKAQLEEQLKEVRKKCAEEAQLiSSLKAEL 470
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEE--------LEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEEL-EELEEQL 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 471 tsqESQISTYEEELAKAREElsRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPEL 535
Cdd:COG4717 412 ---EELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
311-526 |
1.87e-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: 48.15 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 311 CGKLSKDQFALAFHLISqkliKGIDPPHVLTPEMIPPsdraslqkniigsspvadfsAIKEldtlnnEIVDLQREkNNVe 390
Cdd:pfam05622 246 CAQLQQAELSQADALLS----PSSDPGDNLAAEIMPA--------------------EIRE------KLIRLQHE-NKM- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 391 qdLKEK-EDTIKQRTSEVQdlqdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 469
Cdd:pfam05622 294 --LRLGqEGSYRERLTELQ------------------------QLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556461 470 LTSQESQ----------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQHLQDSQQEI 526
Cdd:pfam05622 348 LQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDM 415
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
383-525 |
2.06e-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: 44.52 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 383 QREKNNVEQDLKEKEDTIKQRTsevQDLQDEVQRentnlqklqaqkqqvqelLDELDEQ--KAQLEEQLKEVRKKCAEEA 460
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKAQ---EELEESEET------------------AEELEEErrQAEEEAERLEQKRQEAEEE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 461 qlisslKAELtsQESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:pfam20492 64 ------KERL--EESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
368-501 |
2.11e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIV-----DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLD----EL 438
Cdd:PRK12704 47 AKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK--------------LELLEkreeEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 439 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAR--EEL-SRLQQETAEL 501
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLTAEEAKEIllEKVeEEARHEAAVL 174
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
441-549 |
2.12e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQetaeLeesVESG---KAQLEPLQQ 517
Cdd:COG1566 88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQA----L---YKKGavsQQELDEARA 155
|
90 100 110
....*....|....*....|....*....|..
gi 1034556461 518 HLQDSQQEISSARSSPELLPSGVTDENEVTTA 549
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREEEELAAA 187
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-534 |
2.34e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 381 DLQREKNNVEQDLK----EKEDT-----IKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQK---AQLEEQ 448
Cdd:PRK02224 180 RVLSDQRGSLDQLKaqieEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERReelETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 449 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREE--LSRLQQETaeLEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagLDDADAEA--VEARREELEDRDEELRDRLEECRVAA 337
|
....*...
gi 1034556461 527 SSARSSPE 534
Cdd:PRK02224 338 QAHNEEAE 345
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
374-528 |
2.39e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 374 TLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVR 453
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 454 kkcaeeaqlisSLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISS 528
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELEN 170
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
367-530 |
2.48e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELD----TLNNEIVDLQREK-------NNVEQDLKEKEDTIKQRT-------SEVQDLQDEVQREntnlqklqaqk 428
Cdd:pfam01576 131 AKIKKLEedilLLEDQNSKLSKERklleeriSEFTSNLAEEEEKAKSLSklknkheAMISDLEERLKKE----------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 429 qqvQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIST----YEEELAK---AREELSRLQQETAEL 501
Cdd:pfam01576 200 ---EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAalarLEEETAQknnALKKIRELEAQISEL 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034556461 502 EESVESGKAQ--------------LEPLQQHLQDS------QQEISSAR 530
Cdd:pfam01576 277 QEDLESERAArnkaekqrrdlgeeLEALKTELEDTldttaaQQELRSKR 325
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
370-505 |
2.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQL 449
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---------------------IEEKEKKISSLEKEL 619
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESV 505
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
386-532 |
2.51e-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: 46.21 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 386 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 465
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556461 466 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL------QQHLQDSQQEISSARSS 532
Cdd:pfam04012 88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkarlkaAKAQEAVQTSLGSLSTS 160
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
371-505 |
2.51e-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: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEqdlKEKEDTIKQRtsevqdlqdevqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLK 450
Cdd:COG0542 412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556461 451 EVRKKCAEEAQLIS---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 505
Cdd:COG0542 458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
390-531 |
3.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 390 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 469
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAELEALQAEIDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 470 LTSQESQISTYEEELAK-AR------------------------------------------EELSRLQQETAELEESVE 506
Cdd:COG3883 74 IAEAEAEIEERREELGErARalyrsggsvsyldvllgsesfsdfldrlsalskiadadadllEELKADKAELEAKKAELE 153
|
170 180
....*....|....*....|....*
gi 1034556461 507 SGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQA 178
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
377-526 |
3.32e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.17 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 377 NEIVDLQREKNNVEQDLKEKEDTIKQRTsevQDLQDEVQRENTNlqklqaqkqqvqelldeldEQKAQLEEQLKevrkkc 456
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQ---EDLEKQAEIAREA-------------------QQNYERELVLH------ 52
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 457 AEEAQLISSLKAELtsqesqiSTYEEELAKAREELSRLQqetAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:pfam07926 53 AEDIKALQALREEL-------NELKAEIAELKAEAESAK---AELEESEESWEEQKKELEKELSELEKRI 112
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
435-526 |
3.38e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.33 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 507
Cdd:pfam01442 6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85
|
90
....*....|....*....
gi 1034556461 508 GKAQLEPLQQHLQDSQQEI 526
Cdd:pfam01442 86 LNADAEELQEKLAPYGEEL 104
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
382-529 |
3.39e-05 |
|
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: 44.83 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 382 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqellDELDEQKA---QLEEQLKEVRKKCAE 458
Cdd:pfam16789 30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS---------------DKILQMKRyikVVKERLKQEEKKVQD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 459 eaqlisslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ-EISSA 529
Cdd:pfam16789 95 --------------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQdEIGSA 152
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
371-567 |
3.55e-05 |
|
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: 47.64 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqkLQAQKQQVQELLDELDEQKAQLEE 447
Cdd:COG3096 837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEelakAREELSRLQQETAELEESVE-------SGKAQL----- 512
Cdd:COG3096 908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556461 513 ---EPLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTAvtekvcseLDNNRHSKEE 567
Cdd:COG3096 984 dlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS--------LKSSRDAKQQ 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-567 |
3.55e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 357 IIGSSPVADFSAIKELdtlnNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLD 436
Cdd:TIGR02169 147 FISMSPVERRKIIDEI----AGVAEFDRKK----EKALEELEEVEENIERLDLIIDEKRQQ-----------------LE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 437 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 512
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 513 EPL--------QQHLQDSQQEISSARSSPELLPSGVTD-ENEVTTAVTE--KVCSELDNNRHSKEE 567
Cdd:TIGR02169 282 KDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDaEERLAKLEAEidKLLAEIEELEREIEE 347
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
435-566 |
3.56e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 46.14 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKaQLEEQLKEVRKKcAEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQET------------ 498
Cdd:pfam12795 2 LDELEKAK-LDEAAKKKLLQD-LQQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAeaapkeilasls 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 499 -AELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTAVTekvcSELDNNRHSKE 566
Cdd:pfam12795 80 lEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIR----NRLNGPAPPGE 144
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
354-535 |
4.81e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 354 QKNIIGSSPVADfSAIKELDtLNNEIVDLQREKNNVEQDLKEK----------------EDTIKQRTSEV-QDLQDEVQR 416
Cdd:COG3206 86 QIEILKSRPVLE-RVVDKLN-LDEDPLGEEASREAAIERLRKNltvepvkgsnvieisyTSPDPELAAAVaNALAEAYLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 417 ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcAEEAQlisslkAELTS--QESQISTYEEELAKAREELSRL 494
Cdd:COG3206 164 QNLELR------------REEARKALEFLEEQLPELRKE-LEEAE------AALEEfrQKNGLVDLSEEAKLLLQQLSEL 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034556461 495 QQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPEL 535
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI 265
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
433-526 |
4.86e-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: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQL 512
Cdd:pfam11932 34 KKIDKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TEREL 95
|
90
....*....|....
gi 1034556461 513 EPLQQHLQDSQQEI 526
Cdd:pfam11932 96 VPLMLKMLDRLEQF 109
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-562 |
4.86e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLE--- 446
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE-----------------SLQEELAALEQELQals 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 -EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:COG4372 178 eAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034556461 526 ISSARSSPELLPSGVTDENEVTTAVTEKVCSELDNNR 562
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
433-538 |
5.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYE---EELAKAREELSRLQQETAELEESVESGK 509
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLE 258
|
90 100
....*....|....*....|....*....
gi 1034556461 510 AQLEPLQQHLQDSQQEISSARSSPELLPS 538
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE 287
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
386-567 |
6.07e-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: 45.14 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 386 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaEEAQL--- 462
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLkke 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 463 ------ISSLKAeltSQESQISTYEEELAKAREELSRLQQEtAELEESVEsgKAQLEplqQHLQDSQQEISSARSSPELL 536
Cdd:pfam14988 70 lqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDRE-AHLQFLKE--KALLE---KQLQELRILELGERATRELK 140
|
170 180 190
....*....|....*....|....*....|.
gi 1034556461 537 PSGVTDENEVTTAVTEKVCSELDNNRHSKEE 567
Cdd:pfam14988 141 RKAQALKLAAKQALSEFCRSIKRENRQLQKE 171
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
351-527 |
6.45e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 351 ASLQKNIIGSSPVADFSAIKELDT-----LNNEIVDLQREKNNVEQdlKEKEDTIKQRTSEVQdLQdEVQREntnlqklq 425
Cdd:pfam15905 125 ASLEKQLLELTRVNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEA--KMKEVMAKQEGMEGK-LQ-VTQKN-------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 426 aqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkaelTSQESQISTYEEELAKAREELSRLQQETAELEESV 505
Cdd:pfam15905 193 ---------LEHSKGKVAQLEEKLVSTEKEKIEE-----------KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELL 252
|
170 180
....*....|....*....|..
gi 1034556461 506 ESGKAQLEPLQQHLQDSQQEIS 527
Cdd:pfam15905 253 KEKNDEIESLKQSLEEKEQELS 274
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
433-531 |
6.59e-05 |
|
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: 46.87 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQ------LEEQLKEVRKKCAEEAQLISSLKaELTSQESQISTYEEELAkarEELSRLQQETAELEESVE 506
Cdd:COG3096 499 ELLRRYRSQQALaqrlqqLRAQLAELEQRLRQQQNAERLLE-EFCQRIGQQLDAAEELE---ELLAELEAQLEELEEQAA 574
|
90 100
....*....|....*....|....*
gi 1034556461 507 SGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAA 599
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
433-536 |
6.72e-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: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDE--------QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-------EEELAKAREELSRLQQE 497
Cdd:TIGR02168 217 ELKAELRElelallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevselEEEIEELQKELYALANE 296
|
90 100 110
....*....|....*....|....*....|....*....
gi 1034556461 498 TAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELL 536
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
371-536 |
6.83e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQLE---E 447
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------------LTQKLTTAHRKEAENEallE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAR------------------EELSRLQQETAELEESVESGK 509
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltlqladaslalrEGRARWAQERETLQQSAEADK 317
|
170 180
....*....|....*....|....*..
gi 1034556461 510 AQLEPLQQHLQDSQQEISSARSSPELL 536
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKL 344
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
434-535 |
7.13e-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: 45.30 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 434 LLD--ELDEQKAQLEEQLKEVRKkcaeeaqlisslkaeltsqesQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 511
Cdd:COG1579 9 LLDlqELDSELDRLEHRLKELPA---------------------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELE 67
|
90 100
....*....|....*....|....
gi 1034556461 512 LEPLQQHLQDSQQEISSARSSPEL 535
Cdd:COG1579 68 IEEVEARIKKYEEQLGNVRNNKEY 91
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
441-527 |
7.24e-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: 42.98 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 513
Cdd:pfam20492 7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79
|
90
....*....|....
gi 1034556461 514 PLQQHLQDSQQEIS 527
Cdd:pfam20492 80 QLEAELAEAQEEIA 93
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-567 |
7.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 384 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQL 462
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 463 ISSLKAELTSQESQISTYEEELAKARE----------ELSRLQQETAELE-----------ESVESGKAQLEPLQQH--- 518
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEyle 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 519 LQDSQQEISSARSSPELLPSGVT---DENEVTTAVTEKVCSELD--NNRHSKEE 567
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDkafEELAETEKRLEELRKELEelEKKYSEEE 660
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
373-586 |
8.40e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 373 DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEV 452
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 453 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQeissarsS 532
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASER-------K 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 533 PELLPSgvtdENEVTTAVTEKVCSELDNNRhskeedpfnVDSSSLTGPVADTNL 586
Cdd:pfam07888 253 VEGLGE----ELSSMAAQRDRTQAELHQAR---------LQAAQLTLQLADASL 293
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
435-531 |
8.45e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 514
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90
....*....|....*..
gi 1034556461 515 LQQHLQDSQQEISSARS 531
Cdd:TIGR02168 759 LEAEIEELEERLEEAEE 775
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
350-526 |
8.78e-05 |
|
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: 44.94 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 350 RASLQKNII--GSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQ 427
Cdd:pfam15397 41 RKLLQQYEKfgTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKDKEYPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 428 KQQVQELL------------DELDEqkaqLEEQLKEVRKKCAEEAQLISslKAELTS-QESQISTYEEEL-AKARE---- 489
Cdd:pfam15397 118 KAVQIANLvrqlqqlkdsqqDELDE----LEEMRRMVLESLSRKIQKKK--EKILSSlAEKTLSPYQESLlQKTRDnqvm 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034556461 490 --ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:pfam15397 192 lkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
435-532 |
1.11e-04 |
|
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: 45.13 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRkkcaeeaQLISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEP 514
Cdd:pfam09787 49 LEELRQERDLLREEIQKLR-------GQIQQLRTELQELEAQ---QQEEAESSREQLQELEEQLATERSARREAEAELER 118
|
90
....*....|....*...
gi 1034556461 515 LQQHLQDSQQEISSARSS 532
Cdd:pfam09787 119 LQEELRYLEEELRRSKAT 136
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
378-538 |
1.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 378 EIVDLQREKNNVEQDLkEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkca 457
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR---- 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 458 eeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaQLEPLQQ---HLQDSQQEISSARSSPE 534
Cdd:PRK02224 648 -----IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRErreALENRVEALEALYDEAE 718
|
....
gi 1034556461 535 LLPS 538
Cdd:PRK02224 719 ELES 722
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
369-588 |
1.15e-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: 45.87 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVD----LQRE---KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 441
Cdd:pfam05483 288 IEKKDHLTKELEDikmsLQRSmstQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 442 KAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 521
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 522 SQQEISSArsspELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEE-----DPFNVDSSSLTGPVADTNLDF 588
Cdd:pfam05483 448 REKEIHDL----EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcDKLLLENKELTQEASDMTLEL 515
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
379-526 |
1.20e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 379 IVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkQQVQELLDELDEQKAQlEEQLKEVRKKCA 457
Cdd:pfam13868 157 ILEYLKEKAEREEEREaEREEIEEEKEREIARLRAQQEKA-----------QDEKAERDELRAKLYQ-EEQERKERQKER 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 458 EEAQLISSLKAELT-SQESQIS----TYEEELAKAREELSRLQQETAELEEsVESGKAQ--LEPLQQHLQDSQQEI 526
Cdd:pfam13868 225 EEAEKKARQRQELQqAREEQIElkerRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEkrRMKRLEHRRELEKQI 299
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-523 |
1.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQreknNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEE 447
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEE 659
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 448 QLKEVRKKCAEEAQLISSLKAELtsqesqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 523
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
446-536 |
1.25e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 446 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90
....*....|.
gi 1034556461 526 ISSARSSPELL 536
Cdd:PRK09039 132 SARALAQVELL 142
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
371-526 |
1.26e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 448
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 449 LKEVRKKCAEEAQLISS----------LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 518
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEfneqskklleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
....*...
gi 1034556461 519 LQDSQQEI 526
Cdd:PHA02562 395 KSELVKEK 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
370-544 |
1.29e-04 |
|
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: 45.50 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDlKEKEDTIKQRTSEVQDLQDEVQR---ENtnlqklqaqkqqvqELLDELDEQKAQLE 446
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELERlreHN--------------KHLNENIENKLLLK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKC-------AEEAQL---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLE 513
Cdd:pfam05557 228 EEVEDLKRKLereekyrEEAATLeleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSAR 307
|
170 180 190
....*....|....*....|....*....|.
gi 1034556461 514 PLQQHLQDSQQEISSARSSpellpsgVTDEN 544
Cdd:pfam05557 308 QLEKARRELEQELAQYLKK-------IEDLN 331
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
433-528 |
1.31e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 512
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212
|
90
....*....|....*.
gi 1034556461 513 EPLQQHLQDSQQEISS 528
Cdd:PRK11448 213 ERKQKRKEITDQAAKR 228
|
|
| DUF1090 |
pfam06476 |
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ... |
441-526 |
1.38e-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: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 519
Cdd:pfam06476 39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100
|
....*..
gi 1034556461 520 QDSQQEI 526
Cdd:pfam06476 101 AEARQEL 107
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
382-551 |
1.50e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 382 LQREKNNVEQDLKEKEDTikqRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELL--DELDEQKAQ--------------- 444
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKlelekekrdrkraee 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 445 -----LEEQLKEVRKKCAEEAQLISSLKAELtsQESQISTYEEELAKAREELSRLQQETAE---LEES---VESGKAQLE 513
Cdd:pfam17380 492 qrrkiLEKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEErrrIQEQmrkATEERSRLE 569
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034556461 514 PLQQHLQDSQQEISSARSSPELlpsgvtdenEVTTAVT 551
Cdd:pfam17380 570 AMEREREMMRQIVESEKARAEY---------EATTPIT 598
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-588 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 373 DTLNNEIVDL-QREKnnvEQDLKEKED------------TIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL- 438
Cdd:pfam15921 377 DQLQKLLADLhKREK---ELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMEVQR--------------LEALLKAMk 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 439 DEQKAQLEEQLKEVRKKcAEEAQLISSLKAELTSQESQISTYEEELAKAREEL-------SRLQQETAELEESVESGKAQ 511
Cdd:pfam15921 440 SECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLessertvSDLTASLQEKERAIEATNAE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 512 LEPLQ----------QHLQDSQQEISSARSSPELLPSGVTDENEVTTAVTEKVCSELD-NNRHSKEEDPFNVDSSSLTGP 580
Cdd:pfam15921 519 ITKLRsrvdlklqelQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlVGQHGRTAGAMQVEKAQLEKE 598
|
....*...
gi 1034556461 581 VADTNLDF 588
Cdd:pfam15921 599 INDRRLEL 606
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
436-525 |
1.62e-04 |
|
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: 43.38 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 436 DELDE---QKAQLEEQLKEVrkkcaeEAQLiSSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 512
Cdd:pfam08614 64 EELAElyrSRGELAQRLVDL------NEEL-QELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDEL 136
|
90
....*....|...
gi 1034556461 513 EPLQqhLQDSQQE 525
Cdd:pfam08614 137 VALQ--LQLNMAE 147
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
369-525 |
1.85e-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: 45.34 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDE 440
Cdd:TIGR00618 713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQF 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHL 519
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQA 869
|
....*.
gi 1034556461 520 QDSQQE 525
Cdd:TIGR00618 870 KIIQLS 875
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
365-563 |
2.05e-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: 45.10 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 365 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTIKQRTSEVQDLQDEVQR--ENTNlqklqaqkqQVQELL 435
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQleEKTK---------LQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 436 DELDEQKAQLEEQLKEVR----------KKCAEEAQLISSLKAELTSQ-ESQIstyeEELAKAREE----LSRLQQETAE 500
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAhsfvVTEFEATTCS 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556461 501 LEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLpSGVTDENEVTTAVTEKVCSE----LDNNRH 563
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVELEELKKILAEdeklLDEKKQ 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-506 |
2.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTiKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDE-----QKA- 443
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556461 444 QLEEQLKEVRKKCAEEAqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 506
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
365-562 |
2.08e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 365 DFSAIKELDTLNNEIVDLQR----EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldelde 440
Cdd:TIGR00606 686 VFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL------------------------ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 qkaqLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREE----LSRLQQETAELEESVESGKAQLE- 513
Cdd:TIGR00606 742 ----KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTdvtiMERFQMELKDVERKIAQQAAKLQg 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556461 514 --------PLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTAVTEKVcSELDNNR 562
Cdd:TIGR00606 818 sdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT-NELKSEK 873
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
368-567 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 368 AIKELDTLNNEIVDLQREknnVEQDLKEKEDTIKQRtsevQDLQDEVQRENTnlqklqaqkqqvqELLDELDEQKAQlee 447
Cdd:pfam01576 262 ALKKIRELEAQISELQED---LESERAARNKAEKQR----RDLGEELEALKT-------------ELEDTLDTTAAQ--- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 qlKEVR-KKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP-----------L 515
Cdd:pfam01576 319 --QELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaelqaelrtL 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 516 QQHLQDSQQEISSARSSPELLPSGVTDENEVTTAVTEKVC---SELDNNRHSKEE 567
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSklqSELESVSSLLNE 451
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
434-535 |
2.33e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 434 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELE------- 502
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEeakslaq 401
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1034556461 503 ----------ESVESGKAQLEPLQQHLQDSQQEISSARSSPEL 535
Cdd:pfam05701 402 aareelrkakEEAEQAKAAASTVESRLEAVLKEIEAAKASEKL 444
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
370-531 |
2.39e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDL------QREKNnveQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA 443
Cdd:PRK09039 53 SALDRLNSQIAELadllslERQGN---QDLQDSVANLRASLSAAEAERSRLQ-----------------ALLAELAGAGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 444 QLEEQLKEVRKKCAEEAQLISslkaeltSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ--- 520
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSA-------RALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNval 185
|
170
....*....|..
gi 1034556461 521 -DSQQEISSARS 531
Cdd:PRK09039 186 aQRVQELNRYRS 197
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
377-513 |
2.50e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 377 NEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLEEQLKEVRKKc 456
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELA-------EEAQELHEEMIELYKEADELRKE- 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556461 457 AEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 513
Cdd:COG1340 211 ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
327-556 |
2.56e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 327 SQKLIKGIDPPHVLTPEMIPPSDRASLQkniigsspvadfsAIKELDTLNNEIVD-------LQREKNNVEQDLKEKEDT 399
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERARRQ-------------AQQERDELADEIASgasgksaLQDEKRRLEARIAQLEEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 400 IKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQLISSLKAELTSQESQIS 478
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 479 TYEEEL-AKARE-----ELSR----------LQQE-----TAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLP 537
Cdd:pfam01576 978 QLEEQLeQESRErqaanKLVRrtekklkevlLQVEderrhADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
250
....*....|....*....
gi 1034556461 538 SGVTDENEVTTAVTEKVCS 556
Cdd:pfam01576 1058 RELDDATESNESMNREVST 1076
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
434-528 |
2.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 434 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--SGKAQ 511
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQ 126
|
90
....*....|....*..
gi 1034556461 512 LEPLQQHLQDSQQEISS 528
Cdd:COG4717 127 LLPLYQELEALEAELAE 143
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
365-568 |
2.83e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 365 DFSAIKELDTL--------NNEIVDLQREKNNVEQDLKEKEDTI-------KQRTSEVQDLQDE-VQRENTNLQKLQAQK 428
Cdd:PHA02562 161 DISVLSEMDKLnkdkirelNQQIQTLDMKIDHIQQQIKTYNKNIeeqrkknGENIARKQNKYDElVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 429 QQVQELLDELDEQ----------KAQLEEQLKEVRKK---------CAEEAQLISSLKAELTSQESQISTYE---EELAK 486
Cdd:PHA02562 241 DELLNLVMDIEDPsaalnklntaAAKIKSKIEQFQKVikmyekggvCPTCTQQISEGPDRITKIKDKLKELQhslEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 487 AREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPSGVTDEN-EVTTAVTEKVcsELDNNRHSK 565
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAeELAKLQDELD--KIVKTKSEL 398
|
...
gi 1034556461 566 EED 568
Cdd:PHA02562 399 VKE 401
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
437-510 |
2.92e-04 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 43.44 E-value: 2.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 437 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 510
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
370-530 |
3.20e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 449
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKK---CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDE 413
|
....
gi 1034556461 527 SSAR 530
Cdd:PRK04778 414 LEAR 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
435-525 |
3.26e-04 |
|
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: 44.66 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRK---------KCAEE-----AQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQ 496
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERqlkslerqaEKAERykelkAELreleLALLVLRLEELREELEELQEELKEAEEELEELTA 260
|
90 100
....*....|....*....|....*....
gi 1034556461 497 ETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKE 289
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
370-530 |
3.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 449
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR--------------EKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAREELSRL--QQET---------------AELEESVESGKAQL 512
Cdd:COG1340 81 DELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLewRQQTevlspeeekelvekiKELEKELEKAKKAL 156
|
170
....*....|....*...
gi 1034556461 513 EpLQQHLQDSQQEISSAR 530
Cdd:COG1340 157 E-KNEKLKELRAELKELR 173
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
364-530 |
3.51e-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: 44.13 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 364 ADFSAIKEL---DTLNNEivdLQREKNNVEQDLKEKEDtikQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDE 440
Cdd:pfam15964 347 ANFEKTKALiqcEQLKSE---LERQKERLEKELASQQE---KRAQEKEALRKEMKKEREELGAT----------MLALSQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 441 QKAQLEEQ--------------LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA-REELSRLQQETAELEESV 505
Cdd:pfam15964 411 NVAQLEAQvekvtreknslvsqLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEhREYRTKTGRQLEIKDQEI 490
|
170 180
....*....|....*....|....*
gi 1034556461 506 ESGKAQLEPLQQHLQDSQQEISSAR 530
Cdd:pfam15964 491 EKLGLELSESKQRLEQAQQDAARAR 515
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-536 |
3.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQR---EKNNVE---QDLKEKEDTIKQRTSE----VQDLQD----EVQRENTNLQKLQAQKQQVQELL 435
Cdd:PRK03918 314 KRLSRLEEEINGIEErikELEEKEerlEELKKKLKELEKRLEEleerHELYEEakakKEELERLKKRLTGLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 436 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQET 498
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKEL 468
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034556461 499 AELEESVESGKAQLEPLQQHLQDsQQEISSARSSPELL 536
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQL 505
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
353-506 |
4.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 353 LQKNIIGSSP----VADFSAIKELDTL-------NNEIVDLQREKNNVEQD---LKEKEDTIKQRTSEVQDLQDEVQREN 418
Cdd:PRK01156 117 IEKNILGISKdvflNSIFVGQGEMDSLisgdpaqRKKILDEILEINSLERNydkLKDVIDMLRAEISNIDYLEEKLKSSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 419 TNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQET 498
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSSLEDMKNRYESEIKTAESDLSMELEKN 272
|
....*...
gi 1034556461 499 AELEESVE 506
Cdd:PRK01156 273 NYYKELEE 280
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
433-534 |
4.43e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKA------QLEEQLKEVRKKCAEEAQLIsSLKAELTSQESQISTYEEELAkarEELSRLQQETAELEESVE 506
Cdd:PRK04863 500 ELLRRLREQRHlaeqlqQLRMRLSELEQRLRQQQRAE-RLLAEFCKRLGKNLDDEDELE---QLQEELEARLESLSESVS 575
|
90 100
....*....|....*....|....*....
gi 1034556461 507 SGKAQLEPLQQHLQDSQQEISS-ARSSPE 534
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRlAARAPA 604
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
393-551 |
4.54e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 393 LKEKEDTIKQR-TSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 467
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESAEQMKSAG------ERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 468 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELL-----PSGV 540
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALesfeaPSGG 1269
|
170
....*....|.
gi 1034556461 541 TDENEVTTAVT 551
Cdd:NF041483 1270 GKGNGVKAGAA 1280
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
465-525 |
4.63e-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: 39.86 E-value: 4.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 465 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhLQDSQQE 525
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQ--IENNLLE 59
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
362-527 |
4.71e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 362 PVADfsaikELDTLNNEIVD-----LQREKNNVEQ----------DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQA 426
Cdd:pfam15921 242 PVED-----QLEALKSESQNkiellLQQHQDRIEQliseheveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 427 QKqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQlisslkaELtsqESQISTYEEELAKAREELSRLQQETAELEEsve 506
Cdd:pfam15921 317 RQ------LSDLESTVSQLRSELREAKRMYEDKIE-------EL---EKQLVLANSELTEARTERDQFSQESGNLDD--- 377
|
170 180
....*....|....*....|.
gi 1034556461 507 sgkaQLEPLQQHLQDSQQEIS 527
Cdd:pfam15921 378 ----QLQKLLADLHKREKELS 394
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
370-515 |
5.91e-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: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQR----------ENTNLQKLQAQKQQVQELLD 436
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 437 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA---REELSRLQQetaeLEESVESGKAQLE 513
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER----LKEEIEKSSKQRA 656
|
..
gi 1034556461 514 PL 515
Cdd:TIGR00606 657 ML 658
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
373-693 |
5.92e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 373 DTLNNEIVDLQR------EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlQKLQAQKQQVQELLDELDEQKAQLE 446
Cdd:pfam03528 140 ESAEREIADLRRrlsegqEEENLEDEMKKAQEDAEKLRSVVMPMEKEI-------AALKAKLTEAEDKIKELEASKMKEL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKCAEEAQLISslkAELTSQESQISTYEEELAKAREELSRL----QQETAELEESVESGKAQLEPLQQHLQDS 522
Cdd:pfam03528 213 NHYLEAEKSCRTDLEMYV---AVLNTQKSVLQEDAEKLRKELHEVCHLleqeRQQHNQLKHTWQKANDQFLESQRLLMRD 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 523 QQEISSARSSPELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEEdpfnvdSSSLTGPVADTNLDffQSDPFVGSDPFKD 602
Cdd:pfam03528 290 MQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREH------TVSIHAVFSPAGVE--TSAPLSNVEEQIN 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 603 DPFGKIDPF-------GGDPF-KGSDPFASDCFFRQSTDPFATSSTDPFSA-ANNSSITSVETLKHNDpFAPggtvVAAS 673
Cdd:pfam03528 362 SAHGSVHSLdtdvvlgAGDSFnKQEDPFKEGLRRAQSTDSLGSSSSLQHKFlGHNQKAKSAGNLDESD-FGP----LVGA 436
|
330 340
....*....|....*....|.
gi 1034556461 674 DSATDPF-ASVFGNESFGGGF 693
Cdd:pfam03528 437 DSVSENFdTSSLGSLKMPSGF 457
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
436-542 |
6.12e-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: 43.79 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 436 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQ-------------ETAELE 502
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalrqqekieryqeDLEELT 360
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034556461 503 ESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPSGVTD 542
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
433-534 |
6.22e-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: 42.70 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 501
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
|
90 100 110
....*....|....*....|....*....|...
gi 1034556461 502 EESVESGKAQLEPLQQHLQDSQQEISSARSSPE 534
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
369-552 |
6.36e-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: 42.38 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 446
Cdd:pfam16591 42 QKKLDELKQQLQQLKTTFTSPEnvRLLQEQLQLIQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVrkkcAEEAQLISSLKAELTSQESQISTY----EEELAKAreelsrLQQETAELEESVESGKAQLEPLQ-QHLQD 521
Cdd:pfam16591 122 EADSRR----AAQYQAISELKRQVQMARYQVRGYtftpNEDSEQA------AYQQLDAALASLDQLRQALAGDPgAALQQ 191
|
170 180 190
....*....|....*....|....*....|.
gi 1034556461 522 SQQEISSARSSPELLPSGVTDENEVTTAVTE 552
Cdd:pfam16591 192 LTSALQGYRDALDTFKAAVAAIEQARQEMTS 222
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
375-529 |
6.51e-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: 43.63 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 375 LNNEIVDLQREKNNVEQDLKEKE-DTIK------QRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEE 447
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEgKNIKlskdvsSLESQLQDTQELLQEETRQKLNLSTR-------LRQLEDERNSLQE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 448 QL-KEVRKKCAEEAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL- 519
Cdd:pfam01576 504 QLeEEEEAKRNVERQLstlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELd 583
|
170
....*....|....*
gi 1034556461 520 -----QDSQQEISSA 529
Cdd:pfam01576 584 dllvdLDHQRQLVSN 598
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
433-534 |
7.46e-04 |
|
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: 41.73 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 507
Cdd:pfam06785 58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134
|
90 100 110
....*....|....*....|....*....|...
gi 1034556461 508 ------GKAQLEPLQQHLQDSQQEISSARSSPE 534
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEEQRSVLE 167
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
381-508 |
7.55e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 40.07 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 381 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEA 460
Cdd:pfam04871 5 ELESEASSLKNENTELKAELQELSKQYNSLEQK------------------ESQAKELEAEVKKLEEALKKLKAELSEEK 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 461 QLISSLKAEL-------TSQESQISTYEEELAKAREELSRLQQETAELEESVESG 508
Cdd:pfam04871 67 QKEKEKQSELddlllllGDLEEKVEKYKARLKELGEEVLSDDEDDDEDDEEDDEE 121
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
435-524 |
7.82e-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: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 511
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603
|
90 100
....*....|....*....|....
gi 1034556461 512 -------LEPLQQH----LQDSQQ 524
Cdd:COG3096 604 wlaaqdaLERLREQsgeaLADSQE 627
|
|
| Nnf1 |
pfam03980 |
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ... |
433-508 |
8.68e-04 |
|
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: 39.54 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 506
Cdd:pfam03980 33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101
|
..
gi 1034556461 507 SG 508
Cdd:pfam03980 102 AQ 103
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
328-567 |
9.24e-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: 42.79 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 328 QKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVAdfsaIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTI---- 400
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifll 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 401 KQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLE-EQLKEVrkKCAEEAQLISSLKAELTSQES---- 475
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEE----------HYLKEVEDLKTELEkEKLKNI--ELTAHCDKLLLENKELTQEASdmtl 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 476 QISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPSGVTDE---NEVTTAVTE 552
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEvlkKEKQMKILE 593
|
250
....*....|....*
gi 1034556461 553 KVCSELDNNRHSKEE 567
Cdd:pfam05483 594 NKCNNLKKQIENKNK 608
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
371-567 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDE-------QKA 443
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAE--------------TELCAEAEEmrarlaaRKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 444 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgkaqLEPLQQHLQDSQ 523
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKK----LEEDILLLEDQN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 524 QEISSARSSPEL----LPSGVTDENEVTTAVT------EKVCSELDnNRHSKEE 567
Cdd:pfam01576 148 SKLSKERKLLEEriseFTSNLAEEEEKAKSLSklknkhEAMISDLE-ERLKKEE 200
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
433-531 |
1.11e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELeesvesgKAQL 512
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-------KEER 80
|
90
....*....|....*....
gi 1034556461 513 EPLQQHLQDSQQEISSARS 531
Cdd:COG1340 81 DELNEKLNELREELDELRK 99
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
370-535 |
1.13e-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: 42.80 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD----ELDEQKAQ- 444
Cdd:pfam15921 349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDhlrrELDDRNMEv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 445 --LEEQLKEVRKKCaeEAQLISSLKA---------ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 513
Cdd:pfam15921 429 qrLEALLKAMKSEC--QGQMERQMAAiqgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
170 180
....*....|....*....|..
gi 1034556461 514 PLQQHLQDSQQEISSARSSPEL 535
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDL 528
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
433-526 |
1.16e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES----- 507
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrar 290
|
90
....*....|....*....
gi 1034556461 508 GKAQLEPLQQHLQDSQQEI 526
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQA 309
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
433-578 |
1.19e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKK----CAEEAQLISSLKAEltsqesqistyEEELAKAREELSRLQQETAELEESVESG 508
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKhqqlCEEKNALQEQLQAE-----------TELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 509 KAQLEP--------------LQQHLQDSQQEIS---SARSSPELlpSGVTDENEVTTAVTEKVCSELDNNRHSKE----E 567
Cdd:pfam01576 81 ESRLEEeeersqqlqnekkkMQQHIQDLEEQLDeeeAARQKLQL--EKVTTEAKIKKLEEDILLLEDQNSKLSKErkllE 158
|
170
....*....|.
gi 1034556461 568 DPFNVDSSSLT 578
Cdd:pfam01576 159 ERISEFTSNLA 169
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
373-567 |
1.26e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 373 DTLNNEIVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQdevQRENTNLQKLqaqkqqvqELLDELDEQKAQLEEQLKE 451
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKkHQEDIINCKKQEERMLK---QIENLEEKEM--------NLRDELESVREEFIQKGDE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 452 VRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREE-------LSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 524
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034556461 525 EISSARSSPELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEE 567
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
346-501 |
1.27e-03 |
|
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: 40.69 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 346 PPSDRASLQKNIIGSSPVADFSAikELDTLNNEIVDLQREKNNVEQDLKEKEDtikqrtsEVQDLQDEVQREntnlqklq 425
Cdd:pfam08614 35 PSTSSSKLSKASPQSASIQSLEQ--LLAQLREELAELYRSRGELAQRLVDLNE-------ELQELEKKLRED-------- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 426 aqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSqeSQIstyeeELAKAREELSRLQQETAEL 501
Cdd:pfam08614 98 ------ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVA--LQL-----QLNMAEEKLRKLEKENREL 160
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
437-525 |
1.32e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 437 ELDEQ----KAQLEEQLKEVRKKCAEEAQL-----ISSLKAELTSQESQISTYEEELA-----KAREELSRLQQ--ETAE 500
Cdd:pfam05672 28 EREEQerleKEEEERLRKEELRRRAEEERArreeeARRLEEERRREEEERQRKAEEEAeereqREQEEQERLQKqkEEAE 107
|
90 100
....*....|....*....|....*
gi 1034556461 501 LEESVESGKAQLEpLQQHLQDSQQE 525
Cdd:pfam05672 108 AKAREEAERQRQE-REKIMQQEEQE 131
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
389-529 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 389 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELDE---QKAQLEEQLKEVRKKCAEEAQLI 463
Cdd:pfam13949 98 VRSKFREHEEDLELLSGPDEDLEAFLpsSRRAKNSPSVEEQVAKLRELLNKLNElkrEREQLLKDLKEKARNDDISPKLL 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 464 SSLKAEL-TSQESQIstYEEELAKAREELSRLQQETA---ELEESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:pfam13949 178 LEKARLIaPNQEEQL--FEEELEKYDPLQNRLEQNLHkqeELLKEITEANNEFLQDKRVDSEKQRQREEA 245
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
53-189 |
1.37e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 53 LGKIWDLADTDGKGILNKQEFfVALRLVACAQNGLEvslsslnlavppprfHDTSSPLLISGTSAAELPWAVKPED-KAK 131
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSE---------------ADTDGDGRISREEFVAGMESLFEATvEPF 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 132 YDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAM 189
Cdd:COG5126 71 ARAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| End3 |
pfam12761 |
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ... |
360-495 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 360 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE---VQREntnlqklqaqkqqvqelLD 436
Cdd:pfam12761 84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGGNRDESSKpalVKRE-----------------FE 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 437 ELDEQKaqlEEQLKEVR--KKCAEEAQLiSSLKAELTSQESQISTYEEELAKAREELSRLQ 495
Cdd:pfam12761 144 QLLDYK---ERQLRELEegSGKSKPINL-KSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
370-504 |
1.42e-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: 40.67 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQdeVQRENTnlqklqaqkqqvqELLDELDEQKAQLEE-- 447
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQEKLEQKEE-LGEGLTMIDFLQ--LQIENQ-------------ALNEKIEERNKELKRlk 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556461 448 --------QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEES 504
Cdd:pfam13870 70 lkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ 134
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
370-503 |
1.45e-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: 41.72 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDeqkaQLEEQL 449
Cdd:pfam17097 133 DTLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECW-----------------ELLNELE----RLRDQR 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 503
Cdd:pfam17097 192 ITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEK 245
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
377-525 |
1.48e-03 |
|
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: 40.89 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 377 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqVQELLDELDEQKAQLEEQLKEVRKKC 456
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE----------IQERLEELNQRWEELRELAEERRQRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 457 AEEAQL------ISSLKAELTSQESQISTYE-----EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 525
Cdd:cd00176 103 EEALDLqqffrdADDLEQWLEEKEAALASEDlgkdlESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADE 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
390-535 |
1.49e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 390 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA- 468
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAr 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 469 --ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQEISSARSSPEL 535
Cdd:PRK04863 595 iqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL-DEEIERLSQPGGSED 672
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
447-526 |
1.78e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 38.92 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
369-530 |
1.80e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVEQDL---------------KEKE--DTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqv 431
Cdd:COG1340 94 LDELRKELAELNKAGGSIDKLRKEIerlewrqqtevlspeEEKElvEKIKELEKELEKAKKALEKNEKLK---------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 432 qELLDELDEQKAQLEE---QLKEVrkkcAEEAQlisSLKAELTSQESQIstyeEELakaREELSRLQQETAELEESVESG 508
Cdd:COG1340 164 -ELRAELKELRKEAEEihkKIKEL----AEEAQ---ELHEEMIELYKEA----DEL---RKEADELHKEIVEAQEKADEL 228
|
170 180
....*....|....*....|..
gi 1034556461 509 KAQLEPLQQHLQDSQQEISSAR 530
Cdd:COG1340 229 HEEIIELQKELRELRKELKKLR 250
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
390-516 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 390 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 469
Cdd:pfam01576 4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 470 -------LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 516
Cdd:pfam01576 70 kqeleeiLHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ 123
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
375-525 |
2.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 375 LNNEIVD-----LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLE 446
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKCAEEAQ-LISSLKaeltsqesqistyeEELAKAREELSRLQQETA------ELEESVESGKAQLEPLQQHL 519
Cdd:PRK00409 562 EEEDKLLEEAEKEAQqAIKEAK--------------KEADEIIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKK 627
|
....*.
gi 1034556461 520 QDSQQE 525
Cdd:PRK00409 628 KKQKEK 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-501 |
2.18e-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: 41.97 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLk 450
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL- 945
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 451 evrkkcAEEAQLisslkaELTSQESQISTYEEELAKAREELSRLQQETAEL 501
Cdd:TIGR02168 946 ------SEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
311-568 |
2.20e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 311 CGKLSKDQFALAFHLISQKLIKGiDPPHVLTPEMIPPSDRASLQKNIIGSSPVADFS-AIKELDTLNNEIVDLQ-REKNN 388
Cdd:COG5185 197 KAEPSGTVNSIKESETGNLGSES-TLLEKAKEIINIEEALKGFQDPESELEDLAQTSdKLEKLVEQNTDLRLEKlGENAE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 389 VEQDLKEKEDTIKqrtSEVQDLQDEVqRENTNLQKLQAQKQQVQELLDELdEQKAQLEEQLKEVRKKCAEEAQLISSLKA 468
Cdd:COG5185 276 SSKRLNENANNLI---KQFENTKEKI-AEYTKSIDIKKATESLEEQLAAA-EAEQELEESKRETETGIQNLTAEIEQGQE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 469 ELTSQESQISTYEEELAkAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPS---------- 538
Cdd:COG5185 351 SLTENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADrqieelqrqi 429
|
250 260 270
....*....|....*....|....*....|.
gi 1034556461 539 -GVTDENEVTTAVTEKVCSELDNNRHSKEED 568
Cdd:COG5185 430 eQATSSNEEVSKLLNELISELNKVMREADEE 460
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
382-568 |
2.30e-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: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 382 LQREKNNVEQDLKEKEDTI-KQRTSEVQDLQdevQRentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEA 460
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCeKLEKIHLQESA---QS------------------LKEREQQLQTKEQIHLQETRKKAVVL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 461 QLISSLKAELTSQESQISTYEEELAKARE------ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPE 534
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034556461 535 LLPS---GVTDENEVTTAVTEKVCSELDNNrhSKEED 568
Cdd:TIGR00618 574 ILTQcdnRSKEDIPNLQNITVRLQDLTEKL--SEAED 608
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
380-532 |
2.46e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 380 VDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqkLQAQKQQVQEL------LDELDEQKAQLEEQL---- 449
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ---IQHLKSKTNELkseklqIGTNLQRRQQFEEQLvels 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 450 -------KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGK------ 509
Cdd:TIGR00606 895 tevqsliREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVknihgymKDIENKIQDGKddylkq 974
|
170 180 190
....*....|....*....|....*....|..
gi 1034556461 510 ---------AQLEPLQQHLQDSQQEISSARSS 532
Cdd:TIGR00606 975 ketelntvnAQLEECEKHQEKINEDMRLMRQD 1006
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
370-525 |
2.71e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKN----NVEQDLKEKEDTIKQRTS---EVQDLQDEVQRentnlqklQAQKQQVQELLDELDEQK 442
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNrrrsKIKEQNNRDIAGIKDKLAkirEARDRQLAVAE--------DDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 443 AQLEEQLKEVRKKCAEE------AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 516
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS 512
|
....*....
gi 1034556461 517 QHLQDSQQE 525
Cdd:pfam12128 513 RRLEERQSA 521
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
374-546 |
2.79e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 374 TLNNEIVDLQREKNNVEQDL--KEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKE 451
Cdd:PRK10929 83 ELRQQLNNERDEPRSVPPNMstDALEQEILQVSSQLLEKSRQAQQEQ--------------DRAREISDSLSQLPQQQTE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 452 VRKKCAE----------------EAQLiSSLKAELTSQESQISTYE-EEL-AKAREELSRLQQETAelEESVESGKAQLE 513
Cdd:PRK10929 149 ARRQLNEierrlqtlgtpntplaQAQL-TALQAESAALKALVDELElAQLsANNRQELARLRSELA--KKRSQQLDAYLQ 225
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034556461 514 PLQQHLQDS-QQEISSARSSPEL-------LPSGVTDENEV 546
Cdd:PRK10929 226 ALRNQLNSQrQREAERALESTELlaeqsgdLPKSIVAQFKI 266
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
433-536 |
3.15e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 38.40 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCaeeaQLISSLKAELTSQ-ESQISTYEEELAKAREEL-SRLQQETAELEESVESGKA 510
Cdd:smart00502 7 ELLTKLRKKAAELEDALKQLISII----QEVEENAADVEAQiKAAFDELRNALNKRKKQLlEDLEEQKENKLKVLEQQLE 82
|
90 100
....*....|....*....|....*....
gi 1034556461 511 QLEPLQQHLQDSQQEISSA---RSSPELL 536
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEAlnsGDPTELL 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
435-528 |
3.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlE 513
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---D 1063
|
90
....*....|....*
gi 1034556461 514 PLQQHLQDSQQEISS 528
Cdd:PRK04863 1064 ELHARLSANRSRRNQ 1078
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
436-521 |
3.45e-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: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 436 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAeleESVESGKAQL 512
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLREQSG---EALADSQEVT 629
|
....*....
gi 1034556461 513 EPLQQHLQD 521
Cdd:COG3096 630 AAMQQLLER 638
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
435-531 |
3.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ-----QE------------ 497
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQtalrqQEkieryqadleel 360
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034556461 498 TAELEES---VESGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:PRK04863 361 EERLEEQnevVEEADEQQEENEARAEAAEEEVDELKS 397
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
372-534 |
3.56e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 372 LDTLNnEIVDLQREKNNVEQDLKEKEDTIKQRtsevqdlqDEVQRENtnlqklqaqkqqvqellDELDEQKAQLEEQLKE 451
Cdd:PRK11281 45 LDALN-KQKLLEAEDKLVQQDLEQTLALLDKI--------DRQKEET-----------------EQLKQQLAQAPAKLRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 452 VRKKcaeeaqlISSLKAELTSQesqistyeeelakAREELSRLQQetAELEESVESGKAQLEPLQQHLQDSQQEISSARS 531
Cdd:PRK11281 99 AQAE-------LEALKDDNDEE-------------TRETLSTLSL--RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT 156
|
...
gi 1034556461 532 SPE 534
Cdd:PRK11281 157 QPE 159
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
367-587 |
3.83e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREknnVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAqK---QQVQELLDELDEQ 441
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETL---IASRQEERQETSAELNQLLRTLDDQWKekRDELNGELSAA-DaavAKDRSELEALEDQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 442 KAQLEEQLKEVRKKCAEEAQLISS--------LKAELTSQESQISTYEEELAKAREE----LSRLQQETAELEESVESGK 509
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSelenleerLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 510 A---------------QLEPLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTAVTEKVcSELDNNRHSKEEDPFNVDS 574
Cdd:pfam12128 411 AvaeddlqaleselreQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFD-ERIERAREEQEAANAEVER 489
|
250
....*....|...
gi 1034556461 575 SSLTGPVADTNLD 587
Cdd:pfam12128 490 LQSELRQARKRRD 502
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
383-512 |
3.85e-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: 40.29 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 383 QREKNNVEQDLKEKEDTIKQRTSEVQD----LQDEVQREntnlqklQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE 458
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIELkerrLAEEAERE-------EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556461 459 EaqlisslkaeltsQESQI----STYEEELAKAREELSRLQQETAELEESVESGKAQL 512
Cdd:pfam13868 294 E-------------LEKQIeereEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
394-534 |
3.91e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 394 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 472
Cdd:NF041483 520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 473 QESQISTYEEELAKAREELSRLQQETA--------ELEESVESGKAQLEPLQQHLQD-SQQEISSARSSPE 534
Cdd:NF041483 584 AEERLTAAEEALADARAEAERIRREAAeeterlrtEAAERIRTLQAQAEQEAERLRTeAAADASAARAEGE 654
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
433-557 |
3.95e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 512
Cdd:COG0542 411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034556461 513 EPLQQHLQDSQQEISSARSSPELLPSGVTDENEVTTAVTEKVCSE 557
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEE 515
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
469-528 |
4.02e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.86 E-value: 4.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 469 ELTSQ-ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 528
Cdd:pfam06005 4 ELLEQlETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRG 64
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
438-524 |
4.19e-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: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 438 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 488
Cdd:COG3096 295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374
|
90 100 110
....*....|....*....|....*....|....*.
gi 1034556461 489 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 524
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409
|
|
| CCDC-167 |
pfam15188 |
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ... |
435-490 |
4.37e-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: 36.87 E-value: 4.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 490
Cdd:pfam15188 5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
371-526 |
4.46e-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: 40.72 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQR--EKNNVEQDLKEKEDTIKQRTSEVQ-DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqLEE 447
Cdd:TIGR00618 585 DIPNLQNITVRLQDltEKLSEAEDMLACEQHALLRKLQPEqDLQDVRLHLQQCSQELALKLTALHALQLTLTQER--VRE 662
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556461 448 QLKEVRKkcaEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 526
Cdd:TIGR00618 663 HALSIRV---LPKELLASRQLALQKMQSEK----EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
435-525 |
5.06e-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: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVrkKCAEEAqlISSLKAE------------LTSQESQISTYEEELAKAREELSRLQQETAELE 502
Cdd:pfam01920 11 LQLLAQQIKQLETQLKEL--ELALEE--LELLDEDtkvykligdvlvKQDKEEVKEQLEERKETLEKEIKTLEKQLEKLE 86
|
90 100
....*....|....*....|...
gi 1034556461 503 EsvesgkaQLEPLQQHLQDSQQE 525
Cdd:pfam01920 87 K-------ELEELKEELYKKFGQ 102
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
375-520 |
6.04e-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: 39.69 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 375 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 451
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 452 vrkkcaeEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAE---LEESVESGKAQLEPLQQHLQ 520
Cdd:pfam15294 211 -------STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAyrnMKEMLTKKNEQIKELRKRLS 275
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
374-503 |
6.51e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 39.84 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 374 TLNNEIVDLQREKNNVEqdlkekeDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQK---AQLEEQL- 449
Cdd:pfam03148 230 ILEQTANDLRAQADAVN-------FALRKRIEETEDAKNKLEWQ-------------LKKTLQEIAELEkniEALEKAIr 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 450 -KEVRKKCAE-----------------EAQLisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 503
Cdd:pfam03148 290 dKEAPLKLAQtrlenrtyrpnvelcrdEAQY--GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEE 359
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
437-524 |
6.66e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 437 ELDEQKAQLEEQ---LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEELAK-------------- 486
Cdd:PRK04863 294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAasdhlnlvqtalrQQEKIERYQADLEEleerleeqnevvee 373
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034556461 487 AREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 524
Cdd:PRK04863 374 ADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQQ 410
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
369-495 |
6.74e-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: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE- 447
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAt 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034556461 448 --QLKEVRK-KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ 495
Cdd:pfam00529 161 vaQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
364-531 |
6.84e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 364 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTIKQ-RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 441
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 442 --------KAQLEE----QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEesvESGK 509
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETE---ERYE 255
|
170 180
....*....|....*....|..
gi 1034556461 510 AQLEPLQQHLQDSQQEISSARS 531
Cdd:pfam00038 256 LQLADYQELISELEAELQETRQ 277
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
378-536 |
6.85e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.12 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 378 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD---ELDEQKAQLEE--QLKEV 452
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDtmqHLQEDRADLQAtvELLQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 453 R------------KKCAEEAQLISSLKAELTSQ-ESQISTYEEEL------AKA-----REELSRLQQETAELEESVESG 508
Cdd:pfam07111 271 RvqslthmlalqeEELTRKIQPSDSLEPEFPKKcRSLLNRWREKVfalmvqLKAqdlehRDSVKQLRGQVAELQEQVTSQ 350
|
170 180
....*....|....*....|....*...
gi 1034556461 509 KAQLEPLQQHLQDSQQEISSARSSPELL 536
Cdd:pfam07111 351 SQEQAILQRALQDKAAEVEVERMSAKGL 378
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
367-496 |
6.99e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 367 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTikqrtSEVQDLQDE----VQRENTNLQKLQAQKQQVQELLD------ 436
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQQRQEAR-----REREELQREeerlVQKEEQLDARAEKLDNLENQLEErekals 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 437 ----ELDEQKAQLEEQLKEVRKKCAEEA--QLISSLKAELTSQESQISTYEEElaKAREELSRLQQ 496
Cdd:PRK12705 116 arelELEELEKQLDNELYRVAGLTPEQArkLLLKLLDAELEEEKAQRVKKIEE--EADLEAERKAQ 179
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
440-532 |
7.51e-03 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 39.89 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 440 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQETAELEESVESGKAqlepLQ 516
Cdd:PRK09841 311 EQIVNVDNQLNELTFREAEISQLYKKDHPTYRALLEKRQTLEQERKRLNKRVSAMpstQQEVLRLSRDVEAGRA----VY 386
|
90
....*....|....*.
gi 1034556461 517 QHLQDSQQEISSARSS 532
Cdd:PRK09841 387 LQLLNRQQELSISKSS 402
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
433-495 |
8.64e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.68 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 433 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEELAKA--------------REELSRLQ 495
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLqskIERLKTQLEDLERELALLQAKERQLekklktleqklkneKEELQRLK 121
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
347-529 |
8.86e-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: 39.28 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 347 PSDRASLQK--NIIGSSPVADFSAIKEL---------------DTLNNEIVDLQREKNNVEQDlkeKEDTIKQRTSEVQD 409
Cdd:cd22656 22 PTTEEEYRKrlGISSDIDDKLSSDFDPLldayksikdhctdfkDDTYPSIVSLAGDIYNYAQN---AGGTIDSYYAEILE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 410 LQDEVQrENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKA 487
Cdd:cd22656 99 LIDDLA-DATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034556461 488 REELSRLQQETAEL-EESVESGKAQLEPLQQHLQDSQQEISSA 529
Cdd:cd22656 178 RKEIKDLQKELEKLnEEYAAKLKAKIDELKALIADDEAKLAAA 220
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
370-486 |
8.87e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 37.16 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 370 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEQL 449
Cdd:pfam13863 13 LALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFD------------------------KFLKENDAKRRRALKKA 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034556461 450 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAK 486
Cdd:pfam13863 69 EEETKLKKEKEKEIKKLTAQIEELKSEISKLEEKLEE 105
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
378-521 |
9.04e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 37.16 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 378 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEeqlkevrKKCA 457
Cdd:pfam13863 7 EMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFD----------KFLKENDAKRRRAL-------KKAE 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 458 EEAQlisslkaeltsqesQISTYEEELAKAREELSRLQQETAELEESVEsgkaQLEPLQQHLQD 521
Cdd:pfam13863 70 EETK--------------LKKEKEKEIKKLTAQIEELKSEISKLEEKLE----EYKPYEDFLEK 115
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
360-528 |
9.08e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.56 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 360 SSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQEL---LD 436
Cdd:COG5185 305 IDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELdsfKD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 437 ELDEQKAQLEEQLKEVRKKCAEEAQlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEES-VESGKAQLEPL 515
Cdd:COG5185 385 TIESTKESLDEIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEES 461
|
170
....*....|...
gi 1034556461 516 QQHLQDSQQEISS 528
Cdd:COG5185 462 QSRLEEAYDEINR 474
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
390-545 |
9.10e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 390 EQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqelLDELDEQKAQLEE--QLKEVRKKCAEE----AQLI 463
Cdd:pfam10174 124 EHERQAKELFLLRKTLEEMELRIETQKQT----------------LGARDESIKKLLEmlQSKGLPKKSGEEdwerTRRI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 464 SSLKAELTSQESQISTYEEELAKAREELSR---LQQETAE---LEESVESGKAQLEPLQQHLQDSQQEISSARSSPELlp 537
Cdd:pfam10174 188 AEAEMQLGHLEVLLDQKEKENIHLREELHRrnqLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLL-- 265
|
....*...
gi 1034556461 538 sGVTDENE 545
Cdd:pfam10174 266 -HTEDREE 272
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
371-558 |
9.10e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLKEKEdtikqrtSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 450
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKE-------SSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 451 EvrkkcAEEAQLISSLKAELTSQ----ESQISTYEEELAKAREELSRL--------------QQETAELEE-SVESGKAQ 511
Cdd:pfam10174 542 K-----AHNAEEAVRTNPEINDRirllEQEVARYKEESGKAQAEVERLlgilrevenekndkDKKIAELESlTLRQMKEQ 616
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034556461 512 LEPLQQhLQDSQQEISsaRSSPELLPSGVTDENEVTTAVTEKVCSEL 558
Cdd:pfam10174 617 NKKVAN-IKHGQQEMK--KKGAQLLEEARRREDNLADNSQQLQLEEL 660
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
378-513 |
9.13e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.67 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 378 EIVDLQREKNNV-EQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqelldeldeqkaQLEEQLKEVRKKC 456
Cdd:pfam12718 14 ERAEELEEKVKElEQENLEKEQEIKSLTHKNQQLEEEVE----------------------------KLEEQLKEAKEKA 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556461 457 AEEAQL----------ISSLKAEL-TSQESQISTYE--EELAKAREELSR----LQQETAELEESVESGKAQLE 513
Cdd:pfam12718 66 EESEKLktnnenltrkIQLLEEELeESDKRLKETTEklRETDVKAEHLERkvqaLEQERDEWEKKYEELEEKYK 139
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
395-530 |
9.13e-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: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 395 EKEDTIKQRTSEVQDLQDEVQ------------RENTNLQKLQAQKQQVQELLDELDEQKAQLE-------EQLKEVRKK 455
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKqqifalsevvqrRPHFSYEDAVGLLGENSDLNEKLRARLEQAEearrearEQLRQAQAQ 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 456 CAEEAQLISSLKA--------------ELTSQESQISTYEEELAKAR-----EELSRLQQETAELEESVESGKAQLEPLQ 516
Cdd:COG3096 1014 YSQYNQVLASLKSsrdakqqtlqeleqELEELGVQADAEAEERARIRrdelhEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
170
....*....|....
gi 1034556461 517 QHLQDSQQEISSAR 530
Cdd:COG3096 1094 KRLRKAERDYKQER 1107
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
307-476 |
9.63e-03 |
|
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: 39.23 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 307 DTKDcgkLSKDQFALA---FHLISQ--------KLIKGIDppHVLTPE-MIPPSDRASLQKNIIGSSPVADfsAIKEL-D 373
Cdd:smart00787 110 DVKL---LMDKQFQLVktfARLEAKkmwyewrmKLLEGLK--EGLDENlEGLKEDYKLLMKELELLNSIKP--KLRDRkD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 374 TLNNEIVDLQREKNNVEQ-----------DLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQK 442
Cdd:smart00787 183 ALEEELRQLKQLEDELEDcdpteldrakeKLKKLLQEIMIKVKKLEELEEELQELESK--------------IEDLTNKK 248
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034556461 443 AQLEEQLKEVRKKCAE----EAQLISSLKAELTSQESQ 476
Cdd:smart00787 249 SELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
435-512 |
9.89e-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: 37.03 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 435 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAELTSQEsqisTYEEELAKAREELSRLQQET-AELEESVESGKA 510
Cdd:cd06503 39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERILEQAkAEIEQEKEKALA 113
|
..
gi 1034556461 511 QL 512
Cdd:cd06503 114 EL 115
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
369-506 |
9.96e-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: 39.13 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 369 IKELDTL-----NNEIVDLQ-REKNNVEQDLKEKEDTIKQRTSE--VQDLQDEVQREntnlqklqaqkqqvQELLDELDE 440
Cdd:pfam13868 8 LRELNSKllaakCNKERDAQiAEKKRIKAEEKEEERRLDEMMEEerERALEEEEEKE--------------EERKEERKR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556461 441 QKAQLEEQLKEvRKKCAEEAQLISSLKAELTsQESQISTYEEELAKAREELSRLQQETAELEESVE 506
Cdd:pfam13868 74 YRQELEEQIEE-REQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE 137
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
371-542 |
1.00e-02 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 371 ELDTLNNEIVDLQREKNNVEQDLK----EKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDEQKAQLE 446
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQLDKKHQawleEQKEQKREARTEKQAYWQVVEGALDAQ-------------LALLKAAIAARR 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556461 447 EQLKEVRKKCAEE-----------AQLISSLKAELTSQESQIS-------------------------TYEEELAKAREE 490
Cdd:pfam12128 743 SGAKAELKALETWykrdlaslgvdPDVIAKLKREIRTLERKIEriavrrqevlryfdwyqetwlqrrpRLATQLSNIERA 822
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034556461 491 LSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSARSSPELLPSGVTD 542
Cdd:pfam12128 823 ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| |
