|
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 |
1.84e-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: 152.05 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 121 PWAVKSEDKAKYDAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 1039766566 200 PVPMSLPPALVPPSKR 215
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
218-313 |
2.25e-40 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 143.19 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 218 WVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALAFHLINQKLIkGI 297
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80
|
90
....*....|....*.
gi 1039766566 298 DPPHSLTPEMIPPSDR 313
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
121-215 |
1.82e-25 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 101.30 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 121 PWAVKsedkaKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763 6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
|
90
....*....|....*..
gi 1039766566 200 -PVPMSLPPALVPPSKR 215
Cdd:pfam12763 81 aDVPDELPDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
228-293 |
2.62e-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: 99.60 E-value: 2.62e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766566 228 YDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALAFHLINQKL 293
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
132-197 |
6.40e-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: 6.40e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039766566 132 YDAIFDSLSPV-DGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALE 197
Cdd:cd00052 1 YDQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
5.29e-24 |
|
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: 96.58 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 13 SSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 1039766566 93 SLSLAVPPPRF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
1.72e-22 |
|
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: 91.51 E-value: 1.72e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039766566 19 YEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLVACAQN 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-489 |
2.22e-15 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 76.12 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLEEQL 412
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR--------------LELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039766566 413 QEVRKkcAEEAQlisSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEI 489
Cdd:COG1579 83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-592 |
2.48e-15 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 78.41 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLE 409
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL--EPLQQHLQESQQ 487
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 488 EISSMQmrlemkDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTHQESSVRSSPEIAP 567
Cdd:COG4372 195 NAEKEE------ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260
....*....|....*....|....*
gi 1039766566 568 SDVTDESEAVTVAGNEKVTPRFDDD 592
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAAL 293
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-503 |
3.10e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDL-------QDEVQRESINLQKLQAQKQQVQELLGELDEQKA 406
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 486
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
170
....*....|....*..
gi 1039766566 487 QEISSMQMRLEMKDLET 503
Cdd:TIGR02168 421 QEIEELLKKLEEAELKE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-497 |
7.78e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
....*
gi 1039766566 493 QMRLE 497
Cdd:COG1196 406 EEAEE 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-498 |
5.49e-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: 69.70 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESInlqklqaqkqqvqeLLGELDEQKAQLEEQL 412
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--------------QISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
....*.
gi 1039766566 493 QMRLEM 498
Cdd:TIGR02168 823 RERLES 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-491 |
1.36e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDEQKAQLEEQL 412
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISS 491
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-497 |
1.61e-11 |
|
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: 68.16 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 329 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQL 408
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESgkAQLEPLQQHLQESQQE 488
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEE 448
|
....*....
gi 1039766566 489 ISSMQMRLE 497
Cdd:TIGR02168 449 LEELQEELE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-497 |
2.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
....*
gi 1039766566 493 QMRLE 497
Cdd:COG1196 413 LERLE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-497 |
2.26e-11 |
|
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: 67.77 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESIN-------LQKLQAQKQQVQELLGELDEQKA 406
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 486
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170
....*....|.
gi 1039766566 487 QEISSMQMRLE 497
Cdd:TIGR02168 929 LRLEGLEVRID 939
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-502 |
2.28e-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: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|....*
gi 1039766566 493 QMRLEM-----KDLE 502
Cdd:TIGR04523 495 EKELKKlneekKELE 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-497 |
2.80e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESInlqklQAQKQQVQELLGELDEQKAQLE 409
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-----YQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKCAEEAQL---ISSLKAEITSQESQIS-SYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ-- 483
Cdd:COG4717 153 ERLEELRELEEELEELeaeLAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEql 232
|
170
....*....|....
gi 1039766566 484 ESQQEISSMQMRLE 497
Cdd:COG4717 233 ENELEAAALEERLK 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-500 |
8.85e-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: 65.43 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDT----LNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEvqdlqdevqresinlqklqaqkqqvqelLGELDEQKAQ 407
Cdd:TIGR04523 456 IKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----------------------------LKKLNEEKKE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 408 LEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSR---------LQQETAQLEESVESGKAQLEPL 478
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEK 587
|
170 180
....*....|....*....|..
gi 1039766566 479 QQHLQESQQEISSMQMRLEMKD 500
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKE 609
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-497 |
9.68e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEE 410
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 411 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEIS 490
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
....*..
gi 1039766566 491 SMQMRLE 497
Cdd:COG1196 390 EALRAAA 396
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
339-511 |
3.40e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.50 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 339 NNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVR 416
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 417 KKCAEEAQLISSLKAEITSQESQI--------SSYEEELLKAREELSRLQQETAQLEESVES---GKAQLEPLQQHLQES 485
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQLqqeaqrilASLEAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVA 363
|
170 180
....*....|....*....|....*.
gi 1039766566 486 QQEISSMQMRLEMKDLETDNNQSNWS 511
Cdd:COG3206 364 RELYESLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-507 |
4.08e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 329 FSAIKELDTLNNEIVDLQREKnnveQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLqaqkqqvqelLGELDEQKAQL 408
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAE-EAQL----ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 483
Cdd:TIGR02169 771 EEDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180
....*....|....*....|....
gi 1039766566 484 ESQQEISSMQMRLEMKDLETDNNQ 507
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELE 874
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-497 |
4.24e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvQELLGELDEQKAQLEEQL 412
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL--------------EEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
....*
gi 1039766566 493 QMRLE 497
Cdd:COG1196 427 EEALA 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-489 |
4.39e-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: 63.54 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKA 406
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKE-----------------LYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 486
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
...
gi 1039766566 487 QEI 489
Cdd:TIGR02168 379 EQL 381
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-506 |
4.80e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqQVQELLGE----LDEQKAQLE 409
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-----------KEIEQLEQeeekLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEEL--LKAREELSRLQQETAQ---LEESVESGKAQLEPLQQHLQE 484
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAElskLEEEVSRIEARLREIEQKLNR 823
|
170 180
....*....|....*....|..
gi 1039766566 485 SQQEISSMQMrlEMKDLETDNN 506
Cdd:TIGR02169 824 LTLEKEYLEK--EIQELQEQRI 843
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-492 |
4.98e-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: 62.09 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 482
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|
gi 1039766566 483 QESQQEISSM 492
Cdd:COG4942 100 EAQKEELAEL 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-507 |
8.46e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 341 EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDEQKAQLEEQLQEVRKKCA 420
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------LELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 421 EEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKD 500
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
....*..
gi 1039766566 501 LETDNNQ 507
Cdd:COG1196 379 EELEELA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-493 |
8.55e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLEEQL 412
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--------------LEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAE---EAQLISS-------LKAEITSQESQISSYEEELLKAR----EELSRLQQETAQLEESVESGKAQLEPL 478
Cdd:COG4942 100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*
gi 1039766566 479 QQHLQESQQEISSMQ 493
Cdd:COG4942 180 LAELEEERAALEALK 194
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-454 |
1.07e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTS---------EVQDLQDEV--QRESINLQKlqaqkqqvqELLGEL 401
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIesLKRRISDLE---------DEILEL 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 402 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREEL 454
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-491 |
1.35e-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: 60.93 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDL-----------QDEVQRESINLQKLQAQKQQVQELLGEL 401
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 481
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
170
....*....|
gi 1039766566 482 LQESQQEISS 491
Cdd:COG4942 236 AAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-507 |
1.48e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 313 RSSLQKNITGSSpvADFSAIK-ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResINLQKLQAQK 391
Cdd:TIGR04523 227 NNQLKDNIEKKQ--QEINEKTtEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ--LKSEISDLNN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 392 QQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESG 471
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039766566 472 KAQLEPLQQHLQE-----SQQEISSMQMRLEMKDLETDNNQ 507
Cdd:TIGR04523 383 KQEIKNLESQINDleskiQNQEKLNQQKDEQIKKLQQEKEL 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-495 |
1.67e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 324 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvQELLGELDE 403
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQES----QISSYEEELLKAREELSRLQQETAQLEesvesgkAQLEPLQ 479
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAE-------AALRDLR 418
|
170
....*....|....*.
gi 1039766566 480 QHLQESQQEISSMQMR 495
Cdd:COG4913 419 RELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-497 |
1.69e-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: 60.55 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQR------ESINLQKLQAQKQQVQELLGELDE 403
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqkeelaELLRALYRLGRQPPLALLLSPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKA------------QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESG 471
Cdd:COG4942 132 LDAvrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180
....*....|....*....|....*.
gi 1039766566 472 KAQLEPLQQHLQESQQEISSMQMRLE 497
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAA 237
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
403-506 |
3.28e-09 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 55.72 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQ-----ESQiSSYEEELLK----------AREELSRLQQETAQLEES 467
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQaeiarEAQ-QNYERELVLhaedikalqaLREELNELKAEIAELKAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039766566 468 VESGKAQLEPLQQHLQES----QQEISSMQMRLEmkDLETDNN 506
Cdd:pfam07926 80 AESAKAELEESEESWEEQkkelEKELSELEKRIE--DLNEQNK 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-493 |
4.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEE 410
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 411 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEIS 490
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
...
gi 1039766566 491 SMQ 493
Cdd:COG1196 502 DYE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-489 |
4.92e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQrESINLQKLQAQKQQVQELlgELDEQKA---QL 408
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN-QLKDEQNKIKKQLSEKQK--ELEQNNKkikEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAE-----EAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 483
Cdd:TIGR04523 287 EKQLNQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
....*.
gi 1039766566 484 ESQQEI 489
Cdd:TIGR04523 367 EKQNEI 372
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
396-507 |
5.22e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLQEVRKKcaeeaqlISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 475
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 1039766566 476 EPLQQHLQESQQEISSMQMRL-----EMKDLETDNNQ 507
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELeelqkERQDLEQQRKQ 133
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-504 |
1.10e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqAQKQQVQELLGELDEQKA 406
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEQLQEVR----------KKCAEEAQLISSLKAEITSQ----ESQISSYEEELLKAREELSRLQQETAQLEESVESGK 472
Cdd:PRK02224 325 ELRDRLEECRvaaqahneeaESLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
170 180 190
....*....|....*....|....*....|..
gi 1039766566 473 AQLEPLQQHLQESQQEISSMQMRLemKDLETD 504
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELRERE--AELEAT 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
335-502 |
1.27e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 335 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTVKQRTSEVQDLQDEVQ----------------RESINLQKLQAQK 391
Cdd:COG4717 48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEeleeeleeleaeleelREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 392 QQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQL---ISSLKAEITSQESQISSYEEEL-LKAREELSRLQQETAQLEES 467
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 1039766566 468 VESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLE 502
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-504 |
1.95e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQ 411
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 412 LQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVesgkAQLEPLQQHLQESQQEISS 491
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV----KDLTKKISSLKEKIEKLES 531
|
170
....*....|....*
gi 1039766566 492 --MQMRLEMKDLETD 504
Cdd:TIGR04523 532 ekKEKESKISDLEDE 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-497 |
2.48e-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: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEvqRESINLQKLQAQKQQVQELLGELDEQKAQ 407
Cdd:COG4913 229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 408 LEEQLQEVRKKCAEEAQLISSLKAEITSQ--------ESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQ 479
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170
....*....|....*...
gi 1039766566 480 QHLQESQQEISSMQMRLE 497
Cdd:COG4913 387 AEAAALLEALEEELEALE 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-509 |
2.55e-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: 57.76 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQK--------------------- 391
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleerleeaeeelaeaeaei 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 392 -------QQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL 464
Cdd:TIGR02168 785 eeleaqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039766566 465 EESVESGKAQLEPLQQHLQESQQEIssMQMRLEMKDLETDNNQSN 509
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEAL--ALLRSELEELSEELRELE 907
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
330-502 |
2.88e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRT-SEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKaQL 408
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYE-----EELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 483
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
170
....*....|....*....
gi 1039766566 484 ESQQEissmqmRLEMKDLE 502
Cdd:PRK03918 705 EREKA------KKELEKLE 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
398-487 |
3.40e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 398 LGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEP 477
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90
....*....|
gi 1039766566 478 LQQHLQESQQ 487
Cdd:COG4942 109 LLRALYRLGR 118
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-483 |
4.97e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqellgeLDEQKAQLEEQLQ 413
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG---------------------IEAKINELEEEKE 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039766566 414 EVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE-------ESVESGKAQLEPLQQHLQ 483
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGGRAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-568 |
6.48e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQR------ESINLQKLQAQKQQVQELL---GE 400
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgERARALYRSGGSVSYLDVLlgsES 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDE--QKAQLEEQLQEVRKKCAEEAQlisSLKAEITSQESQISSYEEELLKAREELSR----LQQETAQLEESVESGKAQ 474
Cdd:COG3883 114 FSDflDRLSALSKIADADADLLEELK---ADKAELEAKKAELEAKLAELEALKAELEAakaeLEAQQAEQEALLAQLSAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 475 LEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTH 554
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
250
....*....|....
gi 1039766566 555 QESSVRSSPEIAPS 568
Cdd:COG3883 271 AAGAGAAAASAAGG 284
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-500 |
1.07e-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: 55.83 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLEEQL 412
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE--------------LRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
....*...
gi 1039766566 493 QMRLEMKD 500
Cdd:TIGR02168 371 ESRLEELE 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
333-580 |
1.21e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLK-----------EKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQEL-- 397
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEqtRNTLKSMEGSDGHAMKVAMgm 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 398 -------LGELD--EQKAQ-LEEQLQEVRKK---CAEEAQLISSLKAEITSQESQISSyEEELLKAREElsRLQQETAQL 464
Cdd:pfam15921 733 qkqitakRGQIDalQSKIQfLEEAMTNANKEkhfLKEEKNKLSQELSTVATEKNKMAG-ELEVLRSQER--RLKEKVANM 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 465 EESVESGKAQLEPLQQHLQESQQEISSMQMR--LEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANF-NEH 541
Cdd:pfam15921 810 EVALDKASLQFAECQDIIQRQEQESVRLKLQhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlSHH 889
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039766566 542 AEGQNNLESEPTH------QEssVRSSPEIAPSDVTDESEAVTVA 580
Cdd:pfam15921 890 SRKTNALKEDPTRdlkqllQE--LRSVINEEPTVQLSKAEDKGRA 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-497 |
1.37e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQL 408
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEE--ELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 486
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|.
gi 1039766566 487 QEISSMQMRLE 497
Cdd:PRK03918 331 KELEEKEERLE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-481 |
1.44e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQD-------LKEKEDTVKQRTSEVQDLQDEVQR-ESInlqklqaqkQQVQELLGELDEQ 404
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSkrkleekIRELEERIEELKKEIEELEEKVKElKEL---------KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 405 KAQLEEQLQEVRKKCAEEAQLISSLKAEItsqeSQISSYEEELLKAREELSRLQQETAQLEESV---ESGKAQLEPLQQH 481
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
396-493 |
1.74e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 53.90 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELD-----EQKAQLEEQLQEVRKKcAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRL----------QQE 460
Cdd:COG1566 71 QVLARLDptdlqAALAQAEAQLAAAEAQ-LARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQE 149
|
90 100 110
....*....|....*....|....*....|...
gi 1039766566 461 TAQLEESVESGKAQLEPLQQHLQESQQEISSMQ 493
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLREEE 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-456 |
1.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResiNLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039766566 413 QEVRKKcaeeaqlISSLKAEITSQESQISSYEEELLKAREELSR 456
Cdd:COG4913 415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
330-497 |
2.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKL-----QAQKQQVQELLGELD 402
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelRERFGDAPVdlgnaEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQhL 482
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-L 504
|
170
....*....|....*
gi 1039766566 483 QESQQEISSMQMRLE 497
Cdd:PRK02224 505 VEAEDRIERLEERRE 519
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
401-497 |
2.20e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDEQKAQLEEQLQEVRKKCAE--EAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPL 478
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100
....*....|....*....|.
gi 1039766566 479 QQH--LQESQQEISSMQMRLE 497
Cdd:COG3206 260 LQSpvIQQLRAQLAELEAELA 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
400-495 |
2.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLIS--SLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVEsgkaqLEP 477
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAE 473
|
90
....*....|....*...
gi 1039766566 478 LQQHLQESQQEISSMQMR 495
Cdd:COG4717 474 LLQELEELKAELRELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-509 |
2.89e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 397 LLGELDEQKAQLEEQ---------LQEVRKKCAEEAQL--ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE 465
Cdd:COG1196 194 ILGELERQLEPLERQaekaeryreLKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039766566 466 ESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSN 509
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
313-491 |
4.19e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 313 RSSLQKNI-TGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQrtsevqdlqdevqresinlqklqaqk 391
Cdd:COG3206 242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-------------------------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 392 qqvqellgeLDEQKAQLEEQLQEvrkkcaEEAQLISSLKAEITSQESQISSYEEELLKAREELSRL---QQETAQLEESV 468
Cdd:COG3206 296 ---------LRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREV 360
|
170 180
....*....|....*....|...
gi 1039766566 469 ESGKAQLEPLQQHLQESQQEISS 491
Cdd:COG3206 361 EVARELYESLLQRLEEARLAEAL 383
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
39-80 |
4.28e-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: 48.91 E-value: 4.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1039766566 39 AAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLV 80
Cdd:pfam12763 31 VSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
329-491 |
4.59e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 329 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDL--QDEVQRESINlqklqaqkqqvqellgeldeqka 406
Cdd:PRK04778 89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQELleSEEKNREEVE----------------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEQLQEVRKKCAEEA----QLISSLKAEITSQESQISSYEEE-----LLKAREELSRLQQETAQLEESVESGKAQLEP 477
Cdd:PRK04778 144 QLKDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELtesgdYVEAREILDQLEEELAALEQIMEEIPELLKE 223
|
170
....*....|....
gi 1039766566 478 LQQHLQESQQEISS 491
Cdd:PRK04778 224 LQTELPDQLQELKA 237
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
401-497 |
5.78e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.98 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEE----LLKAREELSR--LQQEtAQLEESVESGKAQ 474
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlaLEKGREDLAReaLERK-AELEAQAEALEAQ 106
|
90 100
....*....|....*....|...
gi 1039766566 475 LEPLQQHLQESQQEISSMQMRLE 497
Cdd:COG1842 107 LAQLEEQVEKLKEALRQLESKLE 129
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
346-618 |
7.09e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 346 QREKNNVEQdLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL----------QEV 415
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeaeeakkaEEL 1707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 416 RKKCAEEAQLISSLKAE-----ITSQESQISSYE-----EELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQES 485
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAeeenkIKAEEAKKEAEEdkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 486 QQEISSMQMRLEMKDLETD-------NNQSNWSSSPQSVLVNGATDYCSLSTSS--SETANFNEHAEGQNNLESEPTHQE 556
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNfaniiegGKEGNLVINDSKEMEDSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNKE 1867
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 557 SSVRSSPEIAPSDVTDESEAVTvagNEKVtprfddDKHSKEEDPFNVESSSLTDAVADTNLD 618
Cdd:PTZ00121 1868 ADFNKEKDLKEDDEEEIEEADE---IEKI------DKDDIEREIPNNNMAGKNNDIIDDKLD 1920
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
345-502 |
1.19e-06 |
|
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: 51.18 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 345 LQREKNNVEQDLKEKEDTVKQRTSEVQdLQDEVQR-------ESINLQKLQAQKQQVQEL--------LGELDEQKAQLE 409
Cdd:pfam04849 99 LTERNEALEEQLGSAREEILQLRHELS-KKDDLLQiysndaeESETESSCSTPLRRNESFsslhgcvqLDALQEKLRGLE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKC-----------AEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL-------EESVESG 471
Cdd:pfam04849 178 EENLKLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLlaqivdlQHKCKEL 257
|
170 180 190
....*....|....*....|....*....|.
gi 1039766566 472 KAQLEPLQQHLQESQQeiSSMQMRLEMKDLE 502
Cdd:pfam04849 258 GIENEELQQHLQASKE--AQRQLTSELQELQ 286
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
333-504 |
1.29e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVeqDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQL 412
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQ--LISSLKAEITSQESQISSYEE-------ELLKAREELSRLQQE--------TAQLEESVESGKAQL 475
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQlqqeaqriLASLEAELEALQARE 329
|
170 180 190
....*....|....*....|....*....|
gi 1039766566 476 EPLQQHLQESQQEISSM-QMRLEMKDLETD 504
Cdd:COG3206 330 ASLQAQLAQLEARLAELpELEAELRRLERE 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
323-502 |
1.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 323 SSPVADFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTVKQRTSEVQDLQdEVQRESINlqklqaqkqqvqelLG 399
Cdd:COG4913 600 SRYVLGFDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQRLA-EYSWDEID--------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLisslkaeitsqESQISSYEEELLKAREELSRLQQETAQLEESVEsgkaQLEPLQ 479
Cdd:COG4913 665 SAEREIAELEAELERLDASSDDLAAL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEEL 729
|
170 180
....*....|....*....|...
gi 1039766566 480 QHLQESQQEISSMQMRLEMKDLE 502
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLE 752
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-433 |
1.53e-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: 49.92 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqKQQVQELLGELDEQKAQLEEQL 412
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL----------EAELEEKKAELDEELAELEAEL 158
|
90 100
....*....|....*....|.
gi 1039766566 413 QEVRKKCAEeaqLISSLKAEI 433
Cdd:COG1579 159 EELEAEREE---LAAKIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
403-502 |
1.73e-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: 49.92 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 EQKAQLEEqLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 482
Cdd:COG1579 4 EDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100
....*....|....*....|....*..
gi 1039766566 483 QE--SQQEISSMQ-----MRLEMKDLE 502
Cdd:COG1579 83 GNvrNNKEYEALQkeiesLKRRISDLE 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-506 |
1.84e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQEL---LGELDEQKAQLE 409
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLesqISELKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKCAEEAQLISSLKA---------------------EITSQESQISSYEEELLKAREELSRLQQETAQ----- 463
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnke 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039766566 464 LEESVESGKAQLEPLQQHLQESQQEISSM-----QMRLEMKDLETDNN 506
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLneqisQLKKELTNSESENS 359
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
335-497 |
2.31e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.28 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 335 LDTLNNEIVDLQREKNNVEQDLKEKedtvkqrTSEVQDLQdevQResinlqklqaqkqqvqellgeLDEQKA------QL 408
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQST-------NSELEELQ---ER---------------------LDLLKAkaseaeQL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAEEAQLISSLKAEITSQES-------------QISSYEEELLKAREE---LSRLQQETAQLEESVESGK 472
Cdd:pfam05557 155 RQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseivknskselaRIPELEKELERLREHnkhLNENIENKLLLKEEVEDLK 234
|
170 180
....*....|....*....|....*
gi 1039766566 473 AQLEplqqHLQESQQEISSMQMRLE 497
Cdd:pfam05557 235 RKLE----REEKYREEAATLELEKE 255
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
346-505 |
2.44e-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: 51.01 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 346 QREKNNVEQDLKEKEDTVKQRTSEVQDL--QDEVQRESINlqklqaqkqqvqellgeldeqkaQLEEQLQEVRKKCAEEA 423
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELleSEEKNREEVE-----------------------ELKDKYRELRKTLLANR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 424 ----QLISSLKAEITSQESQISSYEE-----ELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQM 494
Cdd:pfam06160 142 fsygPAIDELEKQLAEIEEEFSQFEEltesgDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYR 221
|
170
....*....|...
gi 1039766566 495 RLEMKD--LETDN 505
Cdd:pfam06160 222 EMEEEGyaLEHLN 234
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
331-499 |
2.73e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIVDLQREKNnveQDLKEK-EDTVKQRTSEVQDLQDEV-QRESInlqklqaqkqqvqellgeLDEQKAQL 408
Cdd:PRK12704 47 AKKEAEAIKKEALLEAKEEI---HKLRNEfEKELRERRNELQKLEKRLlQKEEN------------------LDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 EEQLQEVRKKCAEeaqlISSLKAEITSQESQISSYEEELLKAREELSRLQQETAqleesvesgKAQLepLQQHLQESQQE 488
Cdd:PRK12704 106 EKREEELEKKEKE----LEQKQQELEKKEEELEELIEEQLQELERISGLTAEEA---------KEIL--LEKVEEEARHE 170
|
170
....*....|.
gi 1039766566 489 ISSMQMRLEMK 499
Cdd:PRK12704 171 AAVLIKEIEEE 181
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
222-319 |
2.94e-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: 46.60 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 222 PAEKAKYDEIFlKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALA----FHLINQKLikgI 297
Cdd:pfam12763 6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAmrliFDLVNGNI---A 81
|
90 100
....*....|....*....|..
gi 1039766566 298 DPPHSLTPEMIPPSDRSSLQKN 319
Cdd:pfam12763 82 DVPDELPDWLVPGSKAHLIQAN 103
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
402-507 |
3.16e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 481
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110
....*....|....*....|....*....|.
gi 1039766566 482 LQESQQEISSMQMRL-----EMKDLETDNNQ 507
Cdd:COG4372 82 LEELNEQLQAAQAELaqaqeELESLQEEAEE 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
402-503 |
3.29e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 481
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100
....*....|....*....|..
gi 1039766566 482 LQESQQEISSMQMRLEMKDLET 503
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSD 116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
331-503 |
4.49e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQ--------------------DEVQRESINLQKLQAQ 390
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgrelTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 391 KQQVQElLGELDEQKAQLEEQLQEVRKKCAEEAQLIS--SLKAEITSQESQISSY--------EEELLKAREELSRLQQE 460
Cdd:PRK03918 462 KRIEKE-LKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGE 540
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039766566 461 TAQLEESVESGKA---QLEPLQQHLQESQQEISSMQMRLEMKDLET 503
Cdd:PRK03918 541 IKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFES 586
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
345-505 |
4.52e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 345 LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEE-- 422
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 423 AQLISSLKAEitsQESQISSYEEELLKAREELSRLQQETAQLEE------------SVESGKAQLEPLQQHLQESQQEIS 490
Cdd:COG4717 373 AALLAEAGVE---DEEELRAALEQAEEYQELKEELEELEEQLEEllgeleellealDEEELEEELEELEEELEELEEELE 449
|
170 180
....*....|....*....|
gi 1039766566 491 SMQMRL-----EMKDLETDN 505
Cdd:COG4717 450 ELREELaeleaELEQLEEDG 469
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
331-485 |
6.59e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTVKQRTSEVQDLQDEVQR--ES--INLQKLqaqkqqvqELLG 399
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkQSytLNESEL--------ESVR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQ 479
Cdd:PRK04778 352 QLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
|
....*.
gi 1039766566 480 QHLQES 485
Cdd:PRK04778 432 RYLEKS 437
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
343-510 |
6.96e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 343 VDLQREKNNVEQDLKEKE---DTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKC 419
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQhelDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 420 AEEAQLISSLKAEI-----------TSQESQISSYEEELLKAREELSRLQQETAQ-------LEESVESGK--------- 472
Cdd:TIGR00606 898 QSLIREIKDAKEQDspletflekdqQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdIENKIQDGKddylkqket 977
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039766566 473 ------AQLEPLQQHlqesqQEISSMQMRLEMKDLETDNNQSNW 510
Cdd:TIGR00606 978 elntvnAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERW 1016
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
165-287 |
7.67e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.32 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 165 LGRVWELSDIDHDGKLDRDEFAvAMFLVYCALEKEPVPmSLPPALVPPSKRKTWVVSPAEK---AKYDEIFLKTDKDMDG 241
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFE-ALFRRLWATLFSEAD-TDGDGRISREEFVAGMESLFEAtvePFARAAFDLLDTDGDG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039766566 242 YVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALAFH 287
Cdd:COG5126 85 KISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-505 |
8.05e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKnnvEQDL-KEKEDTVKQRTSEVQDLQDEVQR--ESINlqklqaqkqqvqellgELDEQKAQLE 409
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQnnKIIS----------------QLNEQISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQL-------QEVRKKCAEEAQLISSLKAE-------ITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 475
Cdd:TIGR04523 349 KELtnsesenSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
170 180 190
....*....|....*....|....*....|
gi 1039766566 476 EPLQQHLQESQQEISSMQMRLEMKDLETDN 505
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-508 |
8.58e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRtSEVQDLQDevQRESINlqklqaqkqqvqELLGELDEQKAQLEEQLQ 413
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------ELIAERRETIEEKRERAE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 414 EVRKKCAEeaqlissLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESgKAQLEPLQQHLQESQQEISSMQ 493
Cdd:PRK02224 541 ELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAEDEIERLR 612
|
170
....*....|....*
gi 1039766566 494 MRLEmkDLETDNNQS 508
Cdd:PRK02224 613 EKRE--ALAELNDER 625
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
330-473 |
8.82e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqELLGELDEQKAQ 407
Cdd:COG2433 380 EALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-----------------ELEAELEEKDER 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 408 ---LEEQLQEVRKKCAEEAQL---ISSLKAEITSQESQIssyeEELLKAREELSRLQQETAQLEESVESGKA 473
Cdd:COG2433 443 ierLERELSEARSEERREIRKdreISRLDREIERLEREL----EEERERIEELKRKLERLKELWKLEHSGEL 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-506 |
9.39e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVqrESINLQKLqaqkqqvqellgELDEQKAQLEEQ 411
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL--EKLNNKYN------------DLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 412 LQEVRKKCAEEAQLISSLKAEITSQE---SQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQE 488
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
170 180
....*....|....*....|....*
gi 1039766566 489 ISSM-------QMRLEMKDLETDNN 506
Cdd:TIGR04523 255 LNQLkdeqnkiKKQLSEKQKELEQN 279
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
331-499 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDT-----VKQRTSEVQDLQDEVQR-----ESINLQklqaqkqqvqelLGE 400
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRiearlREIEQK------------LNR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDEQKAQLEEQLQEvrkkcaEEAQLIsslkaEITSQESQISSYEEELLKAREEL----SRLQQETAQLEESVESGKAQLE 476
Cdd:TIGR02169 824 LTLEKEYLEKEIQE------LQEQRI-----DLKEQIKSIEKEIENLNGKKEELeeelEELEAALRDLESRLGDLKKERD 892
|
170 180
....*....|....*....|...
gi 1039766566 477 PLQQHLQESQQEISSMQMRLEMK 499
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKK 915
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-509 |
1.22e-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: 48.90 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 397 LLGELDEQ------KAQLEEQLQEVRKKcAEEAQL------ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL 464
Cdd:TIGR02168 194 ILNELERQlkslerQAEKAERYKELKAE-LRELELallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039766566 465 EESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSN 509
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
396-465 |
1.36e-05 |
|
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: 43.83 E-value: 1.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE 465
Cdd:pfam12329 5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
398-494 |
1.64e-05 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 44.96 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 398 LGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQEsqissyeeelLKAREE-LSRLQQETAQLEESVESGKAQLE 476
Cdd:pfam02050 7 LAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAE----------LRNYQAfISQLDEAIAQQQQELAQAEAQVE 76
|
90
....*....|....*...
gi 1039766566 477 PLQQHLQESQQEISSMQM 494
Cdd:pfam02050 77 KAREEWQEARQERKSLEK 94
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
332-513 |
1.99e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQ-----------RTS------EVQDLQDEVQRESINLQKLQAQKQQV 394
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELREELDElrkelaelnkaGGSidklrkEIERLEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 395 QELLGELDEQKAQLE--EQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGK 472
Cdd:COG1340 143 KELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQ 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039766566 473 AQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSS 513
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
333-490 |
2.04e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.50 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKnnveqDLKEKEDTVKQRTSEVQdLQdEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQL 412
Cdd:pfam15905 152 KKMSSLSMELMKLRNKL-----EAKMKEVMAKQEGMEGK-LQ-VTQKN-----------------LEHSKGKVAQLEEKL 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITsqesQISSYEEELLKAREELsrlqqetAQLEESVESGKAQLEPLQQHLQESQQEIS 490
Cdd:pfam15905 208 VSTEKEKIEEKSETEKLLEYIT----ELSCVSEQVEKYKLDI-------AQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
327-486 |
2.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 327 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqAQKQQVQELLGELDEQK 405
Cdd:COG4913 685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 406 AQL--EEQLQEVRKKCAEEaqlISSLKAEITSQESQI----SSY-----------------------------EEELLKA 450
Cdd:COG4913 756 AAAlgDAVERELRENLEER---IDALRARLNRAEEELeramRAFnrewpaetadldadleslpeylalldrleEDGLPEY 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039766566 451 REELSRLQQET---------AQLEESVESGKAQLEPLQQHLQESQ 486
Cdd:COG4913 833 EERFKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
335-566 |
2.42e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 335 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQ 393
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 394 VQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE-ESVEsgk 472
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrERLE--- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 473 aQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGatdycslSTSSSETANFNEHAEGQNNLESE- 551
Cdd:pfam10174 469 -ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD-------SKLKSLEIAVEQKKEECSKLENQl 540
|
250
....*....|....*..
gi 1039766566 552 -PTHQ-ESSVRSSPEIA 566
Cdd:pfam10174 541 kKAHNaEEAVRTNPEIN 557
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
332-500 |
2.54e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQK--------QQVQELLGELDE 403
Cdd:TIGR00618 713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtaalqtgAELSHLAAEIQF 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQhlq 483
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ--- 866
|
170
....*....|....*..
gi 1039766566 484 eSQQEISSMQMRLEMKD 500
Cdd:TIGR00618 867 -EQAKIIQLSDKLNGIN 882
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
337-524 |
2.60e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 337 TLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqellGELDEQKAQLEEQLQEVR 416
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA-----------------ESSREQLQELEEQLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 417 kkcaeeaqlisSLKAEItsqESQISSYEEELLKAREELSR----LQQETAQLEESVESGKAQL----------------- 475
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLtsksqssssqselenrl 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766566 476 ----EPL---QQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPqSVLVNGATD 524
Cdd:pfam09787 173 hqltETLiqkQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGT-SINMEGISD 227
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
333-506 |
2.62e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 46.53 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQrEKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklQAQKQQVQELLGELDeqKAQLEEQL 412
Cdd:pfam12795 17 KLLQDLQQALSLLD-KIDASKQRAAAYQKALDDAPAELRELRQELAALQ------AKAEAAPKEILASLS--LEELEQRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISsyeeellKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQ-EISS 491
Cdd:pfam12795 88 LQTSAQLQELQNQLAQLNSQLIELQTRPE-------RAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAA 160
|
170
....*....|....*
gi 1039766566 492 MQMRLEMKDLETDNN 506
Cdd:pfam12795 161 LKAQIDMLEQELLSN 175
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
318-506 |
2.62e-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: 47.71 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 318 KNITGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ----RESINLQKLQAQKQQ 393
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 394 VQELLGELDEQKAQ----------LEEQLQEVRKKCA--------EEAQL-------------ISSLKAEITSQESQISS 442
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 443 YEEELLKAREELSR-----------------LQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLE-MKDLETD 504
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNqLKDEQNK 264
|
..
gi 1039766566 505 NN 506
Cdd:TIGR04523 265 IK 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
361-464 |
2.73e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 361 DTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQI 440
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 1039766566 441 SSYEEELLKAREELSRLQQETAQL 464
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
352-471 |
2.80e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 352 VEQDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKA 431
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039766566 432 EITSQESQISSYEEELLKAREELSRLQQETAQLEESVESG 471
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
334-468 |
3.01e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEqdlKEKEDTVKQRtsevqdlqdevqresinlqklqaqkqqvqelLGELDEQKAQLEEQLQ 413
Cdd:COG0542 412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039766566 414 EVRKKCAEEAQLIS---SLKAEITSQESQISSYEEELLKAREELSrlqQETAQLEESV 468
Cdd:COG0542 458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
332-489 |
3.24e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGEL---------- 401
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 -DEQK------AQLEEQLQEvRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQ 474
Cdd:COG1340 132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
170
....*....|....*
gi 1039766566 475 LEPLQQHLQESQQEI 489
Cdd:COG1340 211 ADELHKEIVEAQEKA 225
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
400-502 |
3.45e-05 |
|
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: 46.77 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRkkcaeeaQLISSLKAEITSQESQISSYEEEL------LKARE-----EL------SRLQQETA 462
Cdd:pfam03148 255 ETEDAKNKLEWQLKKTL-------QEIAELEKNIEALEKAIRDKEAPLklaqtrLENRTyrpnvELcrdeaqYGLVDEVK 327
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039766566 463 QLEESVESgkaqlepLQQHLQESQQEISSM---QMRLEmKDLE 502
Cdd:pfam03148 328 ELEETIEA-------LKQKLAEAEASLQALertRLRLE-EDIA 362
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-493 |
4.15e-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: 47.32 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEV------QRESINLQKLQAQKQQVQEL-LGELDEQ- 404
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltkkISSLKEKIEKLESEKKEKESkISDLEDEl 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 405 --------KAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQ-- 474
Cdd:TIGR04523 548 nkddfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEne 627
|
170 180
....*....|....*....|....
gi 1039766566 475 -LEPLQQHLQES----QQEISSMQ 493
Cdd:TIGR04523 628 kLSSIIKNIKSKknklKQEVKQIK 651
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
53-189 |
6.52e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 43.63 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 53 LGKIWDLADTDGKGVLSKQEFfVALRLVACAQNGLEVslsslslavppprFHDSSSPLlTSGPSVAELPWAVKSEDKAKY 132
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSEA-------------DTDGDGRI-SREEFVAGMESLFEATVEPFA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039766566 133 DAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAM 189
Cdd:COG5126 72 RAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
330-518 |
7.87e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkQQVQELLGELDEQKAQLE 409
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----------EAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQL------QEVRKKCAEEAQLISSLKAEITS--QESQissyEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 481
Cdd:TIGR00618 623 PEQdlqdvrLHLQQCSQELALKLTALHALQLTltQERV----REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039766566 482 LQESQQEISSMQMRLEMKDLETdNNQSNWSSSPQSVL 518
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREF-NEIENASSSLGSDL 734
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
344-504 |
7.96e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 344 DLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqKQQVQELlgELDEQKAQLEEQLQEVRKKCAEEa 423
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------------ALKSRKK--QMEKDNSELELKMEKVFQGTDEQ- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 424 qlissLKAEITSQESQISSYEEELLKAREELSRLQQETAQL-----EESVESGKAQL--EPLQQHLQESQQEISSMQMRL 496
Cdd:TIGR00606 303 -----LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektELLVEQGRLQLqaDRHQEHIRARDSLIQSLATRL 377
|
....*...
gi 1039766566 497 EMKDLETD 504
Cdd:TIGR00606 378 ELDGFERG 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
355-499 |
9.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 355 DLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLqaqkqqvqELLGELD-EQKAQLEEQLQEVRKKCAEEAQLiSSLKAEI 433
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIA--------ALLAEAGvEDEEELRAALEQAEEYQELKEEL-EELEEQL 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 434 TSQESQISSYEEELLKA--REELSRLQQETAQLEESVESGKAQLEPLQQHLQ--ESQQEISSMQMRLEMK 499
Cdd:COG4717 412 EELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEEL 481
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-487 |
9.91e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREknnveqDLKEKEDTVKQRTSEV-QDLQD-----EVQRESInlqklqaqkQQVQELLGELDEQKAQ 407
Cdd:PRK02224 303 GLDDADAEAVEARRE------ELEDRDEELRDRLEECrVAAQAhneeaESLREDA---------DDLEERAEELREEAAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 408 LEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQ 487
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
345-487 |
1.02e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.11 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 345 LQREKNNVEQDLKE------KEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqelLGEldEQKAQLEEQLQEVRKK 418
Cdd:pfam05672 25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 419 CAEEAQlisslkAEITSQESQISSYEEELLKAREELSRLQQETAQLeesvesgkaqlepLQQHLQESQQ 487
Cdd:pfam05672 85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI-------------MQQEEQERLE 134
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
335-487 |
1.05e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.79 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 335 LDTLNNEIVDLQREKNNVEQDLKEKedtvkqRTSEVQDLQDEVQREsinlqklqaqkqqvqellgeLDEQKAQLEEQLQE 414
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 415 VRKKCAEEAQLissLKAEItsqESQISSYEEELLKAREELSR----LQQETAQ-LEESVESGKAQLEP--------LQQH 481
Cdd:pfam01442 60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEklapYGEELRErLEQNVDALRARLAPyaeelrqkLAER 133
|
....*.
gi 1039766566 482 LQESQQ 487
Cdd:pfam01442 134 LEELKE 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
333-507 |
1.22e-04 |
|
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: 45.83 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQ-------RTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQK 405
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 406 AQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQE-------TAQLEESVESGKAQLEPL 478
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiagieakINELEEEKEDKALEIKKQ 453
|
170 180
....*....|....*....|....*....
gi 1039766566 479 QQHLQESQQEISSMQMRLEmkDLETDNNQ 507
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELY--DLKEEYDR 480
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
435-507 |
1.51e-04 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 41.40 E-value: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 435 SQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEmkDLETDNNQ 507
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLR--KLQEENDE 71
|
|
| DUF1090 |
pfam06476 |
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ... |
404-489 |
1.60e-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: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKAQLEEQLQEVRKKCAEEaqlisSLKAEitsqesqissYEEELLKAREELSRLQQEtaqLEESVESGKAQL-EPLQQHL 482
Cdd:pfam06476 39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAEREAE---LAEAQAKGDADKiAKRQRKL 100
|
....*..
gi 1039766566 483 QESQQEI 489
Cdd:pfam06476 101 AEARQEL 107
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
290-489 |
1.70e-04 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 44.17 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 290 NQKLIKGIDPPHSLTPEMIppsdRSSLQKN--ITGSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTVKQRT 367
Cdd:pfam15397 22 NLELIKAIQDTEDSTALKV----RKLLQQYekFGTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 368 SEVQDLQDEVQ-------RESINlqklqaQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQ---- 436
Cdd:pfam15397 95 AKIQKTQEELNflstykdKEYPV------KAVQIANLVRQLQQLKDSQQDELDELEEMRRMVLESLSRKIQKKKEKilss 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 437 --ESQISSYEEELL-KARE------ELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEI 489
Cdd:pfam15397 169 laEKTLSPYQESLLqKTRDnqvmlkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
334-493 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVD-------LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKA 406
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQ 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEQLQEVRKKCAE-EAQLISSLKAEITSQESQISSYEEEL-LKARE-----ELSR----------LQQE-----TAQL 464
Cdd:pfam01576 942 QLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIAQLEEQLeQESRErqaanKLVRrtekklkevlLQVEderrhADQY 1021
|
170 180
....*....|....*....|....*....
gi 1039766566 465 EESVESGKAQLEPLQQHLQESQQEISSMQ 493
Cdd:pfam01576 1022 KDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-497 |
2.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 397 LLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVE--SGKAQ 474
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQ 126
|
90 100
....*....|....*....|...
gi 1039766566 475 LEPLQQHLQESQQEISSMQMRLE 497
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLE 149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-509 |
2.47e-04 |
|
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: 44.67 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 398 LGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREE-------LSRLQQETAQLEESVES 470
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedLSSLEQEIENVKSELKE 762
|
90 100 110
....*....|....*....|....*....|....*....
gi 1039766566 471 GKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSN 509
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
445-494 |
2.48e-04 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 40.26 E-value: 2.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 445 EELLKAREELSRLQQE---TAQLEESVESGKAQLEPLQQHLQESQQEIssMQM 494
Cdd:cd22248 27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
341-502 |
2.65e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 341 EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQV----QELLGELDEQK------AQLEE 410
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpltRRMQRGEQTYAqletseEDVYH 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 411 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETaqlEESVESGKAQLEPLQQHLQESQQEIS 490
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT---EKLSEAEDMLACEQHALLRKLQPEQD 626
|
170
....*....|..
gi 1039766566 491 SMQMRLEMKDLE 502
Cdd:TIGR00618 627 LQDVRLHLQQCS 638
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
331-499 |
2.74e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 42.95 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIV-----DLQREKNNVEQDLKEkedtvkqRTSEVQDLQDE-VQREsinlqklqaqkqqvqELLGELDEQ 404
Cdd:pfam12072 43 AKKEAETKKKEALleakeEIHKLRAEAERELKE-------RRNELQRQERRlLQKE---------------ETLDRKDES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 405 KAQLEEQLQEVRKKCAEEAQLISSLKAEItsqESQISSYEEELlkarEELSRLQQETAqleesvesgKAQLepLQQHLQE 484
Cdd:pfam12072 101 LEKKEESLEKKEKELEAQQQQLEEKEEEL---EELIEEQRQEL----ERISGLTSEEA---------KEIL--LDEVEEE 162
|
170
....*....|....*
gi 1039766566 485 SQQEISSMQMRLEMK 499
Cdd:pfam12072 163 LRHEAAVMIKEIEEE 177
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
338-488 |
2.85e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 338 LNNEIVD-----LQREKNNVEQ---DLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqeLLGELDEQKAQLE 409
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKCAEEAQ-LISSLKAEItsqesqissyeEELLKAREELSRLQQETAQLEESVESGKA---QLEPLQQHLQES 485
Cdd:PRK00409 562 EEEDKLLEEAEKEAQqAIKEAKKEA-----------DEIIKELRQLQKGGYASVKAHELIEARKRlnkANEKKEKKKKKQ 630
|
...
gi 1039766566 486 QQE 488
Cdd:PRK00409 631 KEK 633
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
334-509 |
2.87e-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: 44.56 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTVKQRTSEVQDLQDEVqresinlqkLQAQKQQVQELLGELDEQKAQLEE 410
Cdd:COG3096 837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 411 QLQEVRKKCAEEAQL---ISSLKAEITSQESQISSYEEellkAREELSRLQQETAQLEESVE-------SGKAQL----- 475
Cdd:COG3096 908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039766566 476 ---EPLQQHLQESQQEISsmQMRLEMKDLETDNNQSN 509
Cdd:COG3096 984 dlnEKLRARLEQAEEARR--EAREQLRQAQAQYSQYN 1018
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
397-494 |
2.88e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 397 LLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQleesvesgkAQLE 476
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQE 213
|
90
....*....|....*...
gi 1039766566 477 PLQQHLQESQQEISSMQM 494
Cdd:PRK11448 214 RKQKRKEITDQAAKRLEL 231
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
406-496 |
2.97e-04 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 42.64 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 406 AQLEEQLQEVRKKCAEEAQLISSLKAEitsQESQISSYEEeLLKAREELSRLQ-QETAQLEESVESGKAQLEPLQQHLQE 484
Cdd:cd16855 4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
|
90
....*....|..
gi 1039766566 485 SQQEISSMQMRL 496
Cdd:cd16855 80 KAQELLQLRMEL 91
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
327-498 |
3.01e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 327 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTVKQ-RTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQ 404
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 405 --------KAQLEE----QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEEL----------------LKAR--EEL 454
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELqslkkqkaslerqlaeTEERyeLQL 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039766566 455 SRLQQETAQLEESVESGKAQlepLQQHLQEsQQEISSMQMRLEM 498
Cdd:pfam00038 259 ADYQELISELEAELQETRQE---MARQLRE-YQELLNVKLALDI 298
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
333-496 |
3.03e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKE---------KEDTVKQRtsEVQDLQDEVQRESINLQKLQAQKQQVQELLgELDE 403
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagiKDKLAKIR--EARDRQLAVAEDDLQALESELREQLEAGKL-EFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKAQLEEQLQEVRKKCAEeAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 483
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQ-ATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
|
170
....*....|...
gi 1039766566 484 ESQQEISSMQMRL 496
Cdd:pfam12128 517 ERQSALDELELQL 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-469 |
3.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTvKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDE-----QKA- 406
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 407 QLEEQLQEVRKKCAEEAqlISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVE 469
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
437-498 |
3.30e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.06 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 437 ESQISSYEEELLKAREELSRLQQETAQLEEsvESGKAQLEplQQHLQESQQEISSMQMRLEM 498
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEE--ERRQAEEE--AERLEQKRQEAEEEKERLEE 69
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
346-488 |
3.37e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.06 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 346 QREKNNVEQDLKEKEDTVKQRTSEVQDlqdevQRESINlqklqaqkqqvqellgELDEQKAQLEEQLQEVRKKCAEEAQL 425
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKAQEELEE-----SEETAE----------------ELEEERRQAEEEAERLEQKRQEAEEE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 426 ISSLKaeitsqESQISSyEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQE 488
Cdd:pfam20492 64 KERLE------ESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
403-502 |
3.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 EQKAQLEEQLQEVRKkcaEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 482
Cdd:PRK12704 50 EAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL 126
|
90 100
....*....|....*....|
gi 1039766566 483 QESQQEISSMQMRLEMKdLE 502
Cdd:PRK12704 127 EKKEEELEELIEEQLQE-LE 145
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
400-473 |
3.72e-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: 43.06 E-value: 3.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQ-----ESQISSYEEELLKAREELSRLQQETAQLEESVESGKA 473
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-502 |
3.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLqevrKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE---ESVESGK 472
Cdd:PRK03918 169 EVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELE 244
|
90 100 110
....*....|....*....|....*....|
gi 1039766566 473 AQLEPLQQHLQESQQEISSMQMRLEMKDLE 502
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKE 274
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
341-499 |
4.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 341 EIVDLQREKNNVEQDLkEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVR---- 416
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 417 ---KKCAEEAQL-----ISSLKAEITSQESQISSYEEELlkarEELSRLQQETAQLEESVESgkaqLEPLqqHLQESQQE 488
Cdd:PRK02224 652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVEA----LEAL--YDEAEELE 721
|
170
....*....|.
gi 1039766566 489 ISSMQMRLEMK 499
Cdd:PRK02224 722 SMYGDLRAELR 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-502 |
4.30e-04 |
|
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: 43.90 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 354 QDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEqLQEVRKKCAE-EAQLIS----S 428
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-----------------LERLRREREKAER-YQALLKEKREyEGYELLkekeA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 429 LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPL--------QQHLQESQQEISSMQ-----MR 495
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLErsiaeKE 314
|
....*..
gi 1039766566 496 LEMKDLE 502
Cdd:TIGR02169 315 RELEDAE 321
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
396-497 |
4.58e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKaeitsqesqissyeEELLKAREELSRLQQETAQLE---ESVESGK 472
Cdd:pfam13851 26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLT--------------EPLQKAQEEVEELRKQLENYEkdkQSLKNLK 91
|
90 100
....*....|....*....|....*
gi 1039766566 473 AQLEPLQQHLQESQQEISSMQMRLE 497
Cdd:pfam13851 92 ARLKVLEKELKDLKWEHEVLEQRFE 116
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
333-496 |
4.79e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQrEKNNVEQDLKekedtvkqrtsevQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:PRK09039 53 SALDRLNSQIAELA-DLLSLERQGN-------------QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLisslkaeitSQEsqissyeeellkAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:PRK09039 119 GELAQELDSEKQV---------SAR------------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
....
gi 1039766566 493 QMRL 496
Cdd:PRK09039 178 GRRL 181
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-468 |
4.94e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqellgELDEQKAQLEEQL 412
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE---------------------EKEKKISSLEKEL 619
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESV 468
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
401-507 |
5.28e-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: 41.46 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDEQKAQLEEQLQEVRKKC-AEEAQLISSLKAEITSQESQISSYEEEL---LKAR-----------EELSRLQQET---- 461
Cdd:pfam08614 19 LEAENAKLQSEPESVLPSTsSSKLSKASPQSASIQSLEQLLAQLREELaelYRSRgelaqrlvdlnEELQELEKKLrede 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039766566 462 ----------AQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEM-----KDLETDNNQ 507
Cdd:pfam08614 99 rrlaaleaerAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMaeeklRKLEKENRE 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-466 |
5.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQreknNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkQQVQELLGELDE-QKAQLEE 410
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETE----------KRLEELRKELEElEKKYSEE 659
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766566 411 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYE----------EELLKAREELSRLQQETAQLEE 466
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
400-504 |
5.90e-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: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE------ESVESGKA 473
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEkieryqEDLEELTE 361
|
90 100 110
....*....|....*....|....*....|.
gi 1039766566 474 QLEPLQQHLQESQQEISSMQMRLEMKDLETD 504
Cdd:COG3096 362 RLEEQEEVVEEAAEQLAEAEARLEAAEEEVD 392
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
404-508 |
6.92e-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: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKAQLEEQLqevRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVES-----------GK 472
Cdd:pfam06785 66 EKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdfaefrleSE 142
|
90 100 110
....*....|....*....|....*....|....*.
gi 1039766566 473 AQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQS 508
Cdd:pfam06785 143 EQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLES 178
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
333-491 |
7.12e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTVKQRTSEVQDLQDEVQR----------ESINLQKLQAQKQQVQELLG 399
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKA---REELSRLQqetaQLEESVESGKAQLE 476
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLE----RLKEEIEKSSKQRA 656
|
170 180
....*....|....*....|..
gi 1039766566 477 PL-------QQHLQESQQEISS 491
Cdd:TIGR00606 657 MLagatavySQFITQLTDENQS 678
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
337-504 |
7.33e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 337 TLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQ---DEVQRESINLQKLQAQKQQVQE----LLGELDEQK---- 405
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlSESERQRAELAEKLSKLQSELEsvssLLNEAEGKNikls 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 406 ---AQLEEQLQEVRKKCAEEAQL-------ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 475
Cdd:pfam01576 461 kdvSSLESQLQDTQELLQEETRQklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540
|
170 180
....*....|....*....|....*....
gi 1039766566 476 EPLQQHLQESQQEISSMQMRLEMKDLETD 504
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
345-500 |
7.66e-04 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 40.97 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 345 LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqkLQAQKQQVQELLGELDEQKAQLEEQLQEvrkkcaeeaq 424
Cdd:pfam16789 30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGT-----TSDKILQMKRYIKVVKERLKQEEKKVQD---------- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039766566 425 lisslkaeitsQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQ-EISSMQMRLEMKD 500
Cdd:pfam16789 95 -----------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQdEIGSALHLANQRK 160
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
396-497 |
8.21e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.76 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLQEVRKkcaeeaqlissLKAEITSQESQIssyeeELLKAReeLSRLQQETAQLEESVESGKAQL 475
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRT-----------LEAEIERLQSKI-----ERLKTQ--LEDLERELALLQAKERQLEKKL 103
|
90 100
....*....|....*....|..
gi 1039766566 476 EPLQQHLQESQQEISSMQMRLE 497
Cdd:pfam11559 104 KTLEQKLKNEKEELQRLKNALQ 125
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
334-500 |
8.22e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQELLGELDEQKAQLEEQ 411
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 412 LQEVRKKCAEEAQLISS----------LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 481
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEfneqskklleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
170 180
....*....|....*....|
gi 1039766566 482 LQESQQEISSMQMRLEM-KD 500
Cdd:PHA02562 395 KSELVKEKYHRGIVTDLlKD 414
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
334-496 |
8.68e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRE----SINLQKLQAQKQQVQELLGELDEQKAQLE 409
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 E------QLQEVRKKCAEEAQLISS-----------LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESV---- 468
Cdd:pfam01576 86 EeeersqQLQNEKKKMQQHIQDLEEqldeeeaarqkLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIseft 165
|
170 180 190
....*....|....*....|....*....|...
gi 1039766566 469 -----ESGKAQLEPLQQHLQESQqeISSMQMRL 496
Cdd:pfam01576 166 snlaeEEEKAKSLSKLKNKHEAM--ISDLEERL 196
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
400-502 |
9.49e-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: 43.02 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAE---ITSQESQISSYEEELLKAREELSRLQqetAQLEESVESGKAQLE 476
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQleqLRARIKELAARAPAWLAAQDALERLR---EQSGEALADSQEVTA 630
|
90 100
....*....|....*....|....*..
gi 1039766566 477 PLQQHL-QESQQEISSMQMRLEMKDLE 502
Cdd:COG3096 631 AMQQLLeREREATVERDELAARKQALE 657
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
440-508 |
9.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 440 ISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQS 508
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
398-504 |
1.00e-03 |
|
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: 39.52 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 398 LGELDEQKAQLEEQLQEvrkkcaeeaqlisslkaeitsQESQISSYEEELLKAREELSRLQQ-------ETAQLEESVES 470
Cdd:pfam20492 15 LKQYEEETKKAQEELEE---------------------SEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEM 73
|
90 100 110
....*....|....*....|....*....|....
gi 1039766566 471 GKAQLEPLQQHLQESQQEISSMQMRLEMKDLETD 504
Cdd:pfam20492 74 EAEEKEQLEAELAEAQEEIARLEEEVERKEEEAR 107
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
332-497 |
1.03e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREK--NNVEQDLKEKEDTVKQRTSEVQDLQDEVQ-----RESinlqklqaqkQQVQELLGELDEQ 404
Cdd:COG3524 160 LAESEELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAFRNRNGildpeATA----------EALLQLIATLEGQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 405 KAQLEEQLQEVRKKCAEEAqlisslkAEITSQESQISSYEEELLKAREELSrlqqeTAQLEESVESGKAQLEPLQQHLQE 484
Cdd:COG3524 230 LAELEAELAALRSYLSPNS-------PQVRQLRRRIAALEKQIAAERARLT-----GASGGDSLASLLAEYERLELEREF 297
|
170
....*....|...
gi 1039766566 485 SQQEISSMQMRLE 497
Cdd:COG3524 298 AEKAYTSALAALE 310
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
330-572 |
1.03e-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: 42.64 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNVEQ-DLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQEllgELDEQKA 406
Cdd:COG5185 243 SELEDLAQTSDKLEKLVEQNTDLRLeKLGENAESSKRLNENANNLIKQFEntKEKIAEYTKSIDIKKATE---SLEEQLA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 407 QLEEqLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKARE------ELSRLQQETAQLEESVESGKAQLEPLQQ 480
Cdd:COG5185 320 AAEA-EQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEnivgevELSKSSEELDSFKDTIESTKESLDEIPQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 481 HLQESQQEIS-------SMQMRlEMKDLETDNNQSNWSSSPQSVLVNGATDycSLSTSSSETANfnehaEGQNNLESEPT 553
Cdd:COG5185 399 NQRGYAQEILatledtlKAADR-QIEELQRQIEQATSSNEEVSKLLNELIS--ELNKVMREADE-----ESQSRLEEAYD 470
|
250
....*....|....*....
gi 1039766566 554 HQESSVRSSPEIAPSDVTD 572
Cdd:COG5185 471 EINRSVRSKKEDLNEELTQ 489
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
410-496 |
1.04e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 410 EQLQEVRKKCAEEAQLISSL-KAEITSQESQissYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQE 488
Cdd:pfam07111 484 EQLREERNRLDAELQLSAHLiQQEVGRAREQ---GEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEE 560
|
....*...
gi 1039766566 489 ISSMQMRL 496
Cdd:pfam07111 561 AASLRQEL 568
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
402-497 |
1.08e-03 |
|
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: 39.97 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEI-TSQESQ---ISSYE---EELLKAREELSRLQQETAQLEESVESGKAQ 474
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaILEAEnskAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100
....*....|....*....|...
gi 1039766566 475 LEPLQQHLQESQQEISSMQMRLE 497
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNS 104
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
344-480 |
1.10e-03 |
|
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: 39.49 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 344 DLQREKNNVE------QDLKEKEDTVKQRTSEVQDLQdevqresinlqklqaqkqqvqELLGELDEQKAQLEEqlqeVRK 417
Cdd:pfam18595 3 TLAEEKEELAelerkaRELQAKIDALQVVEKDLRSCI---------------------KLLEEIEAELAKLEE----AKK 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 418 KCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQetaQLEESVESGKAQLEPLQQ 480
Cdd:pfam18595 58 KLKELRDALEEKEIELRELERREERLQRQLENAQEKLERLRE---QAEEKREAAQARLEELRE 117
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
349-494 |
1.26e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.91 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 349 KNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqELLGELDEQKAQLEEQLQEVRKkcaEEAQLISS 428
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLKKE 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 429 LKA--EIT----SQESQISSYEEELLKAREELSRLQQETaqleesvesgKAQLEPLQQHLQESQQEISSMQM 494
Cdd:pfam14988 70 LQAlrPFAklkeSQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
400-519 |
1.30e-03 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 41.63 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQkaQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLK----AREE-LSRLQQETAQLEESVESgkaq 474
Cdd:pfam14992 9 EKDLQ--RLDEANQVLLLKIQEKEEEIQSLEREITLTRSLAEDEEREELNftimEKEDaLQELELETAKLEKKNEI---- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039766566 475 lepLQQHLQESQQEISsmqmRLEMKDleTDNNQSNWSSSPQSVLV 519
Cdd:pfam14992 83 ---LVKSVMELQRKLS----RKSDKN--TGLEQETLKQMLEELKV 118
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
336-499 |
1.31e-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: 42.41 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 336 DTLNNEIVDL-QREKnnvEQDLKEKED------------TVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGEL- 401
Cdd:pfam15921 377 DQLQKLLADLhKREK---ELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMEVQR--------------LEALLKAMk 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKcAEEAQLISSLKAeitsqesQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 481
Cdd:pfam15921 440 SECQGQMERQMAAIQGK-NESLEKVSSLTA-------QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
170
....*....|....*...
gi 1039766566 482 LQESQQEISSMQMRLEMK 499
Cdd:pfam15921 512 IEATNAEITKLRSRVDLK 529
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
330-484 |
1.46e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 330 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDE 403
Cdd:pfam12795 48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 404 QKAQLEEQLQ--EVRKKCAEEAQLIsSLKAEITSQESQISSYEEELLKA--REELSRLQQETAQLEesvesgKAQLEPLQ 479
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLLTLR------IQRLEQQL 200
|
....*
gi 1039766566 480 QHLQE 484
Cdd:pfam12795 201 QALQE 205
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
349-483 |
1.46e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 349 KNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEEaqLISS 428
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1039766566 429 LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 483
Cdd:pfam04012 88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK 142
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
334-497 |
1.51e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLE---E 410
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------------LTQKLTTAHRKEAENEallE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 411 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEEL------------------LKAREELSRLQQETAQLEESVESGK 472
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhqarlqaaqltlqladasLALREGRARWAQERETLQQSAEADK 317
|
170 180
....*....|....*....|....*...
gi 1039766566 473 AQLEPLQ---QHLQESQQEISSMQMRLE 497
Cdd:pfam07888 318 DRIEKLSaelQRLEERLQEERMEREKLE 345
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
328-610 |
1.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 328 DFSAIKELDTLNNeivDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqellgelDEQKAQ 407
Cdd:PHA02562 161 DISVLSEMDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN--------------------GENIAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 408 LEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL---EESVESG------KAQLEPL 478
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkvIKMYEKGgvcptcTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 479 QQHLQESQQEISSMQMRLEmkDLETDNNQSNwssspqsVLVNGATDycslsTSSSETANFNEHAEGQNNLESEpTHQESS 558
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLE--KLDTAIDELE-------EIMDEFNE-----QSKKLLELKNKISTNKQSLITL-VDKAKK 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 559 VRSSPEIAPSDVTDESEAVTVAGNEKVTPRFDDDKHSKEEDPFNVESSSLTD 610
Cdd:PHA02562 363 VKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-507 |
1.78e-03 |
|
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: 41.29 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039766566 435 SQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQ 507
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
340-476 |
1.96e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 340 NEIVDLQREKNNVEQDLKEKEDtVKQRTSEVQDLQDEVQ--RESINLQKlqaqkqqvqELLGELDEQKAQLEEQLQEVRK 417
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEeiHKKIKELA---------EEAQELHEEMIELYKEADELRK 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 418 KcAEEA-QLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLE 476
Cdd:COG1340 210 E-ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
335-502 |
1.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 335 LDTLNNEIVDLQREKNNvEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqeLLGELDEQKAQLEEQLQE 414
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQ-----------------LQEELEARLESLSESVSE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 415 VRKKCAEEAQLISSLKAEITSQESQissyEEELLKAREELSRLQqetAQLEESVESGKAQLEPLQQHL-QESQQEISSMQ 493
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAAR----APAWLAAQDALARLR---EQSGEEFEDSQDVTEYMQQLLeRERELTVERDE 649
|
....*....
gi 1039766566 494 MRLEMKDLE 502
Cdd:PRK04863 650 LAARKQALD 658
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
398-489 |
2.05e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 398 LGELDEQKAQLEEQL----QEVRKKCAEEAQ-LISSLKAEITSQESQISSYEEELLKA-REELSRLQQE-TAQLEESVES 470
Cdd:pfam01442 6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELQAKlGQNVEELRQRlEPYTEELRKR 85
|
90
....*....|....*....
gi 1039766566 471 GKAQLEPLQQHLQESQQEI 489
Cdd:pfam01442 86 LNADAEELQEKLAPYGEEL 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-497 |
2.07e-03 |
|
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: 41.59 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 399 GELDEQKAQLEEQLQEVRKKCAEeaqlISSLKAEITSQESQISSYEEELLKAREELSRLQQ--------ETAQLEESVES 470
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIER----LDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellkEKEALERQKEA 241
|
90 100
....*....|....*....|....*..
gi 1039766566 471 GKAQLEPLQQHLQESQQEISSMQMRLE 497
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLE 268
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
333-499 |
2.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEdtvkqrtSEVQDLQDEVQRESINLQKLQAQKQQVQEllgELDEQKAQLEEQL 412
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELE-------AQISELQEDLESERAARNKAEKQRRDLGE---ELEALKTELEDTL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 ------QEVR-KKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQES 485
Cdd:pfam01576 313 dttaaqQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392
|
170
....*....|....
gi 1039766566 486 QQEISSMQMRLEMK 499
Cdd:pfam01576 393 LRTLQQAKQDSEHK 406
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
333-518 |
2.24e-03 |
|
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: 41.55 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQdlqdevqresinlqklqaqkqqvqellgELDEQKAQLEEQL 412
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----------------------------ELKEQNEELEKQY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 qEVRKKCAEEAQL----ISSLKAEITSQESQISSYEEELLKAR----EELSRLQQETAQLEESVESGKAQLEPLQQHLQE 484
Cdd:pfam05667 387 -KVKKKTLDLLPDaeenIAKLQALVDASAQRLVELAGQWEKHRvpliEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039766566 485 SQQEISS---MQMRLeMKDLETDNNQSNWSSSPQSVL 518
Cdd:pfam05667 466 VAEEAKQkeeLYKQL-VAEYERLPKDVSRSAYTRRIL 501
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
400-508 |
2.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELS------RLQQETAQLEESVESGKA 473
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEELEE 362
|
90 100 110
....*....|....*....|....*....|....*
gi 1039766566 474 QLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQS 508
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS 397
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
340-503 |
2.75e-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: 40.12 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 340 NEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkQQVQELLGELDEQKAQLEEQLQEVRKKC 419
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA----------EEIQERLEELNQRWEELRELAEERRQRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 420 AEEAQL------ISSLKAEITSQESQISSYE-----EELLKAREELSRLQQETAQLEESVESgkaqLEPLQQHLQESQQE 488
Cdd:cd00176 103 EEALDLqqffrdADDLEQWLEEKEAALASEDlgkdlESVEELLKKHKELEEELEAHEPRLKS----LNELAEELLEEGHP 178
|
170
....*....|....*
gi 1039766566 489 ISSMQMRLEMKDLET 503
Cdd:cd00176 179 DADEEIEEKLEELNE 193
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
333-497 |
2.76e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNE----IVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVqresinlqklqaqkqqvQELLGELDEQKAQL 408
Cdd:pfam01576 176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI-----------------AELQAQIAELRAQL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 409 ---EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLE------PLQ 479
Cdd:pfam01576 239 akkEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQ 318
|
170
....*....|....*....
gi 1039766566 480 QHLQ-ESQQEISSMQMRLE 497
Cdd:pfam01576 319 QELRsKREQEVTELKKALE 337
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-504 |
2.85e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 342 IVDLQREK-NNVEQDLKEKEDTVKQR-------TSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKaqlEEQLQ 413
Cdd:pfam05483 262 LLEESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 414 EVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELS----RLQQETAQLEE--------SVE------------ 469
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEmtkfknnkEVEleelkkilaede 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039766566 470 ---SGKAQLEPLQQHLQESQQ-----------EISSMQMRL------------EMKDLETD 504
Cdd:pfam05483 419 kllDEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLtaiktseehylkEVEDLKTE 479
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
333-496 |
2.91e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 39.51 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQ-RTSEVQDLQDEVQresinlqklqaqkqqvqELLGELDEQKAQLEE- 410
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQEKLEQKEELGEGlTMIDFLQLQIENQ-----------------ALNEKIEERNKELKRl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 411 ---------QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESveSG---------- 471
Cdd:pfam13870 69 klkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvpallhd 146
|
170 180
....*....|....*....|....*....
gi 1039766566 472 ----KAQLEPLQQHLQESQQEISSMQMRL 496
Cdd:pfam13870 147 ydktKAEVEEKRKSVKKLRRKVKILEMRI 175
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
328-504 |
2.92e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 328 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTVKQRTSEVQDLQDEVQResinlqkLQAQKQQVQELLGE 400
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQ-------LEEKTKLQDENLKE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDEQKAQLEEQLQEVR----------KKCAEEAQLISSLKAEITSQ-ESQIssyeEELLKAREELSRLQQEtaqLEESVE 469
Cdd:pfam05483 287 LIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAHSFVVTE---FEATTC 359
|
170 180 190
....*....|....*....|....*....|....*
gi 1039766566 470 SGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETD 504
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE 394
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
333-534 |
2.97e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKKCAEEAQLISSLKAEITS----------QESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 482
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTltqklttahrKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAEL 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 483 QESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSE 534
Cdd:pfam07888 275 HQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAE 326
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
400-497 |
3.15e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 400 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSR-LQQETAQLEESVESGKAQLEPL 478
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeAQQAIKEAKKEADEIIKELRQL 596
|
90 100
....*....|....*....|.
gi 1039766566 479 QQHLQESQ--QEISSMQMRLE 497
Cdd:PRK00409 597 QKGGYASVkaHELIEARKRLN 617
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
333-508 |
3.35e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLqREKNNVE----QDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGE-------L 401
Cdd:pfam15921 510 RAIEATNAEITKL-RSRVDLKlqelQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaM 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEE---LLKAREELSR----LQQETAQLEESVESGKAQ 474
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvkLVNAGSERLRavkdIKQERDQLLNEVKTSRNE 668
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039766566 475 LEPLQQHLQ---------ESQQEISSMQMRLEMKDLETDNNQS 508
Cdd:pfam15921 669 LNSLSEDYEvlkrnfrnkSEEMETTTNKLKMQLKSAQSELEQT 711
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
333-461 |
3.39e-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: 40.39 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLN---NEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVqrESINLQKLQAQKQQVQELLGELDEQKAQLE 409
Cdd:smart00787 151 ENLEGLKedyKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL--EDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039766566 410 EQLQEVRK---KCAEEAQLISSLKAEITSQES------QISSYEEELLKAReeLSRLQQET 461
Cdd:smart00787 229 ELEEELQElesKIEDLTNKKSELNTEIAEAEKkleqcrGFTFKEIEKLKEQ--LKLLQSLT 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-502 |
3.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDtVKQRTSEVQDLQDEVQRESINLQKLQ------------AQKQQVQELLGE 400
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLTPEKLEKEleelekakeeieEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 LDEQKAQLEEQLQEVRK---KCA---------EEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETA------ 462
Cdd:PRK03918 417 LKKEIKELKKAIEELKKakgKCPvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseli 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 463 -------QLE-----------ESVESGKAQLEPLQQHLQESQQEISSMQMRLE-MKDLE 502
Cdd:PRK03918 497 klkelaeQLKeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkLEELK 555
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
329-509 |
3.58e-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: 40.71 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 329 FSAIKELDT-LNNEIVDLQREKNNVEQDLKEKEDTVKQRTS--EVQDLQD--EVQRESINLQKLQAQKQqVQELL----- 398
Cdd:COG5185 335 ETGIQNLTAeIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKDtiESTKESLDEIPQNQRGY-AQEILatled 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 399 --GELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEIT---------SQESQISSYEEELLKAREELSRLQQETAQLEES 467
Cdd:COG5185 414 tlKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkvmreadeeSQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039766566 468 VESGKAQLEPLQQHLQESQQEISSM--QMRLEMKDLETDNNQSN 509
Cdd:COG5185 494 VSTLKATLEKLRAKLERQLEGVRSKldQVAESLKDFMRARGYAH 537
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
333-518 |
3.81e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 412
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 QEVRKK---CAEEAQLISSLKAEITSQESQI--------------SSYEEELLKAREELSRLQQETAQLEESVES-GKAQ 474
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYdeiteriaeqeiaySELQEELEEILKQLEEIEKEQEKLSEMLQGlRKDE 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039766566 475 LEpLQQHLQESQQEISSMQMRLEmkdletdnnQSNWSSSPQSVL 518
Cdd:PRK04778 414 LE-AREKLERYRNKLHEIKRYLE---------KSNLPGLPEDYL 447
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
396-504 |
3.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 475
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
90 100 110
....*....|....*....|....*....|..
gi 1039766566 476 EPLQQH---LQESQQEISSMQMRLEMKDLETD 504
Cdd:COG1340 102 AELNKAggsIDKLRKEIERLEWRQQTEVLSPE 133
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
333-502 |
3.92e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.22 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTVKQ----RTSEVQ-DL-QDEVQRESINlqklqaqkqqVQELLGE--- 400
Cdd:pfam03148 64 KELEELDEEIELLLEEKRRLEKALEALEeplHIAQEcltlREKRQGiDLvHDEVEKELLK----------EVELIEGiqe 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 401 -LDEQKAQLEEQL---QEVRKKCA------EEAQLI----------S---SLKAEITSQESQISSYEE-------ELLKA 450
Cdd:pfam03148 134 lLQRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEwekftqdNIERA 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039766566 451 REELsrlqQETAQLEESVESGKAQ--------------------------LEPLQQHLQESQQEISSMQMrlEMKDLE 502
Cdd:pfam03148 214 EKER----AASAQLRELIDSILEQtandlraqadavnfalrkrieetedaKNKLEWQLKKTLQEIAELEK--NIEALE 285
|
|
| End3 |
pfam12761 |
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ... |
323-458 |
4.07e-03 |
|
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the sequential recruitment at endocytic sites of proteins that drive cargo sorting, membrane invagination and vesicle release. End3p is part of the coat module protein complex Pan1, along with Pan1p, Sla1p, and Sla2p. The proteins in this complex are regulated by phosphorylation events. End3p also regulates the cortical actin cytoskeleton. The subunits of the Pan1 complex are homologous to mammalian intersectin.
Pssm-ID: 432765 [Multi-domain] Cd Length: 200 Bit Score: 39.21 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 323 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTVKQRTSEvqdlqdevqresiNLQKLQAQKQQVQELLGELD 402
Cdd:pfam12761 84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGG-------------NRDESSKPALVKREFEQLLD 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766566 403 EQKAQLEEQLQEVRKKCAEEaqlISSLKAEITSQESQISSYEEELLKAREELSRLQ 458
Cdd:pfam12761 148 YKERQLRELEEGSGKSKPIN---LKSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
393-497 |
4.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 393 QVQELLGELDE------QKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEE 466
Cdd:COG3096 513 RLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039766566 467 SVESGKAQ----------LEPLQQH----LQESQQEISSMQMRLE 497
Cdd:COG3096 593 RIKELAARapawlaaqdaLERLREQsgeaLADSQEVTAAMQQLLE 637
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
336-485 |
4.27e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 38.78 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 336 DTLNNEIVDLQREknnVEQDLKEKEDTVKQRTSEVQ-DLQDEVQresinlqklqaqkqqvqELLGEL----DEQKAQLEE 410
Cdd:pfam01442 29 DRLEKETEALRER---LQKDLEEVRAKLEPYLEELQaKLGQNVE-----------------ELRQRLepytEELRKRLNA 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 411 QLQEVRKKCA---EEAQliSSLKAEITSQESQISSYEEEL-LKAREELSRLQQetaQLEESVESGKAQLEPLQQHLQES 485
Cdd:pfam01442 89 DAEELQEKLApygEELR--ERLEQNVDALRARLAPYAEELrQKLAERLEELKE---SLAPYAEEVQAQLSQRLQELREK 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
345-555 |
4.32e-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: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 345 LQREKNNVEQDLKEKEDTVKQRTSEVQDLqdEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQ 424
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLM 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 425 LISSLKAEITSQESQISSyEEELLKAREELSRLQQETAQLEESVESGKAqlepLQQHLQESQQeissmqmrlemkDLETD 504
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRL-LQTLHSQEIHIRDAHEVATSIREISCQQHT----LTQHIHTLQQ------------QKTTL 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039766566 505 NNQSNWSSSPQSVLVNGAtdycslSTSSSETANFNE------HAEGQNNLESEPTHQ 555
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQ------ATIDTRTSAFRDlqgqlaHAKKQQELQQRYAEL 442
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
344-497 |
4.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 344 DLQREKNNVEQDLK----EKEDT-----VKQRTSEVQDLQDEVQResinlqklqaqkqqvqellgeLDEQKAQLEEQL-- 412
Cdd:PRK02224 180 RVLSDQRGSLDQLKaqieEKEEKdlherLNGLESELAELDEEIER---------------------YEEQREQARETRde 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 413 -QEVRKKCAEEAQLISSLKAEITSQESQISSYE-------EELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQE 484
Cdd:PRK02224 239 aDEVLEEHEERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE 318
|
170
....*....|...
gi 1039766566 485 SQQEISSMQMRLE 497
Cdd:PRK02224 319 LEDRDEELRDRLE 331
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
426-512 |
4.77e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.00 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 426 ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVES-----GKA--QLEPLQQHLQESQQEISSMQMRLEM 498
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERelvlhAEDikALQALREELNELKAEIAELKAEAES 82
|
90
....*....|....
gi 1039766566 499 KDLETDNNQSNWSS 512
Cdd:pfam07926 83 AKAELEESEESWEE 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-492 |
4.90e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 341 EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCA 420
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766566 421 EEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEP----LQQHLQESQQEISSM 492
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdleeLERELERLEREIEAL 779
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
337-499 |
5.15e-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: 40.19 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 337 TLNNEIVDLQReknNVEQDLKEKEDTVKQRTSEVQDLQDeVQRESINLQKLQAQKQQVQELLG-----ELDEQKAQLEEQ 411
Cdd:pfam10174 551 RTNPEINDRIR---LLEQEVARYKEESGKAQAEVERLLG-ILREVENEKNDKDKKIAELESLTlrqmkEQNKKVANIKHG 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 412 LQEVRKKCAEEAQLISSLKAEIT--SQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEI 489
Cdd:pfam10174 627 QQEMKKKGAQLLEEARRREDNLAdnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEI 706
|
170
....*....|
gi 1039766566 490 ssmqmrLEMK 499
Cdd:pfam10174 707 ------LEMK 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
348-625 |
5.73e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 348 EKNNVEQDLKEKED-TVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQ-KAQLEEQLQEVRKKC------ 419
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKiKAEELKKAEEEKKKVeqlkkk 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 420 -AEEAQLISSLKAE----ITSQESQISSYEEELLKArEELSRLQQETAQLEESV---ESGKAQLEPLQQHLQESQQEISS 491
Cdd:PTZ00121 1642 eAEEKKKAEELKKAeeenKIKAAEEAKKAEEDKKKA-EEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 492 MQMRLEMKDLETDN----NQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTHQESSVRSSPEIAP 567
Cdd:PTZ00121 1721 LKKAEEENKIKAEEakkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039766566 568 SDVTDESEaVTVAGNEKVTPRFDDDKHskeedpfnVESSSLTDAVADTNLDFFQSDPF 625
Cdd:PTZ00121 1801 KDIFDNFA-NIIEGGKEGNLVINDSKE--------MEDSAIKEVADSKNMQLEEADAF 1849
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
316-495 |
6.24e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 316 LQKNITGSSPVADFSAIKELDTlnneivDLQREK-NNVEqdLKEKEDTV----KQRTSEVQDLQDEVQRESINLQKLQAQ 390
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKT------ELEKEKlKNIE--LTAHCDKLllenKELTQEASDMTLELKKHQEDIINCKKQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 391 KQQVQELLGELDEQKAQLEEQLQEVRKkcaEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLeesves 470
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL------ 599
|
170 180
....*....|....*....|....*
gi 1039766566 471 gKAQLEPLQQHLQESQQEISSMQMR 495
Cdd:pfam05483 600 -KKQIENKNKNIEELHQENKALKKK 623
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
437-497 |
6.68e-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: 36.09 E-value: 6.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039766566 437 ESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLE 497
Cdd:pfam06005 10 ETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
332-458 |
7.28e-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: 39.33 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRES-------INLQKLQAQKQQVQELLGELDEQ 404
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggISRESLVTAGALVAQAQANLLAT 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1039766566 405 KAQLEEQLQEVRkkcAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQ 458
Cdd:pfam00529 161 VAQLDQIYVQIT---QSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
331-513 |
7.58e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 331 AIKELDTLNNEIV-DLQREK---NNVEQ---DLKEKEDTVKqrtSEVQDLQDE--VQREsinlqKLQAQKQQVQELLGEL 401
Cdd:pfam01576 265 KIRELEAQISELQeDLESERaarNKAEKqrrDLGEELEALK---TELEDTLDTtaAQQE-----LRSKREQEVTELKKAL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 402 DEQKAQLEEQLQEVRKKcaeEAQLISSLKAEI-------TSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQ 474
Cdd:pfam01576 337 EEETRSHEAQLQEMRQK---HTQALEELTEQLeqakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ 413
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039766566 475 LEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSS 513
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
332-507 |
7.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 332 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELD----- 402
Cdd:TIGR00606 743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdld 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 ---EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQ 479
Cdd:TIGR00606 822 rtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
170 180
....*....|....*....|....*...
gi 1039766566 480 QHLQESQQEISSMQMRLEmkDLETDNNQ 507
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLE--KDQQEKEE 927
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
333-480 |
7.60e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKqRTSEVQDLQ-----DEVQR-ESInlqklqaqkqqvQELLGELDEQKA 406
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLAAQLDAAF-RQGEHTGLQlilsgEESQRgERI------------LAYFGYLNQARQ 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 407 QLEEQLQEVRKKCAEEAQLISSLKAE----ITSQESQissyEEELLKAREElsrlQQET-AQLEESVESGKAQLEPLQQ 480
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQqktlLYEQQAQ----QQKLEQARNE----RKKTlTGLESSLQKDQQQLSELRA 240
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
354-492 |
7.91e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 38.26 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 354 QDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqellgeldeqkaQLEEQLQEVRKkcaEEAQLISSLKAEI 433
Cdd:pfam06785 83 EGFKILEETLEELQSEEERLEEELS----------------------------QKEEELRRLTE---ENQQLQIQLQQIS 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039766566 434 TSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 492
Cdd:pfam06785 132 QDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
396-497 |
7.94e-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: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 396 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITS---QESQISSYEEELL-KAREELSRLQQE-------TAQL 464
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELdRAKEKLKKLLQEimikvkkLEEL 230
|
90 100 110
....*....|....*....|....*....|...
gi 1039766566 465 EESVESGKAQLEPLQQHLQESQQEISSMQMRLE 497
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-502 |
8.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELD---------- 402
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkgeikslk 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 403 -------EQK---AQLEEQLQEVRKKCAEEAQLISSLKAE-ITSQESQISSYEE------ELLKAREELSRLQQETAQLE 465
Cdd:PRK03918 546 kelekleELKkklAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPfyneylELKDAEKELEREEKELKKLE 625
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039766566 466 ESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLE 502
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
350-486 |
9.51e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 350 NNVEQDL---KEKEDTVKQRTSEVQDLQdEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQLQEVRkkcaeeAQLI 426
Cdd:PRK04863 283 VHLEEALelrRELYTSRRQLAAEQYRLV-EMARE-----------------LAELNEAESDLEQDYQAAS------DHLN 338
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039766566 427 SSLKAEItsQESQISSYEEELLK--------------AREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 486
Cdd:PRK04863 339 LVQTALR--QQEKIERYQADLEEleerleeqnevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ 410
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
338-483 |
9.57e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 38.92 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766566 338 LNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQ---DEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQE 414
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039766566 415 vrkkcaeEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQ---LEESVESGKAQLEPLQQHLQ 483
Cdd:pfam15294 211 -------STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAyrnMKEMLTKKNEQIKELRKRLS 275
|
|
| |
