|
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 |
2.09e-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: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 121 PWAVKSEDKAKYDAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 755507765 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 ... |
253-349 |
2.20e-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: 143.57 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 253 QWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALAFHLINQKLIkG 332
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 755507765 333 IDPPHSLTPEMIPPSDR 349
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
121-218 |
1.48e-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: 101.68 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 121 PWAVKsedkaKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763 6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
|
90 100
....*....|....*....|
gi 755507765 200 -PVPMSLPPALVPPSKRKTV 218
Cdd:pfam12763 81 aDVPDELPDWLVPGSKAHLI 100
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
264-329 |
1.91e-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: 99.99 E-value: 1.91e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755507765 264 YDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALAFHLINQKL 329
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
132-197 |
4.68e-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: 98.83 E-value: 4.68e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755507765 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 |
5.39e-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: 96.96 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 13 SSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 755507765 93 SLSLAVPPPRF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
1.28e-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: 91.90 E-value: 1.28e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755507765 19 YEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLVACAQN 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
366-628 |
7.22e-16 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 80.33 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLE 445
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL--EPLQQHLQESQQ 523
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 524 EISSMQmrlemkDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTHQESSVRSSPEIAP 603
Cdd:COG4372 195 NAEKEE------ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260
....*....|....*....|....*
gi 755507765 604 SDVTDESEAVTVAGNEKVTPRFDDD 628
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAAL 293
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
369-525 |
1.11e-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: 77.27 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLEEQL 448
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR--------------LELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755507765 449 QEVRKkcAEEAQlisSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEI 525
Cdd:COG1579 83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-539 |
2.18e-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: 77.79 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDL-------QDEVQRESINLQKLQAQKQQVQELLGELDEQKA 442
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 522
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
170
....*....|....*..
gi 755507765 523 QEISSMQMRLEMKDLET 539
Cdd:TIGR02168 421 QEIEELLKKLEEAELKE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-533 |
5.90e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
....*
gi 755507765 529 QMRLE 533
Cdd:COG1196 406 EEAEE 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-534 |
3.62e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESInlqklqaqkqqvqeLLGELDEQKAQLEEQL 448
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--------------QISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
....*.
gi 755507765 529 QMRLEM 534
Cdd:TIGR02168 823 RERLES 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-527 |
9.74e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDEQKAQLEEQL 448
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISS 527
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-533 |
1.19e-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: 68.54 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 365 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQL 444
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESgkAQLEPLQQHLQESQQE 524
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEE 448
|
....*....
gi 755507765 525 ISSMQMRLE 533
Cdd:TIGR02168 449 LEELQEELE 457
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-538 |
1.52e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.12 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|....*
gi 755507765 529 QMRLEM-----KDLE 538
Cdd:TIGR04523 495 EKELKKlneekKELE 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-533 |
1.57e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESInlqklQAQKQQVQELLGELDEQKAQLE 445
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-----YQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKCAEEAQL---ISSLKAEITSQESQIS-SYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ-- 519
Cdd:COG4717 153 ERLEELRELEEELEELeaeLAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEql 232
|
170
....*....|....
gi 755507765 520 ESQQEISSMQMRLE 533
Cdd:COG4717 233 ENELEAAALEERLK 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-533 |
1.68e-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: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESIN-------LQKLQAQKQQVQELLGELDEQKA 442
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 522
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170
....*....|.
gi 755507765 523 QEISSMQMRLE 533
Cdd:TIGR02168 929 LRLEGLEVRID 939
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-533 |
1.68e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
....*
gi 755507765 529 QMRLE 533
Cdd:COG1196 413 LERLE 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
368-536 |
4.68e-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: 66.58 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDT----LNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEvqdlqdevqresinlqklqaqkqqvqelLGELDEQKAQ 443
Cdd:TIGR04523 456 IKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----------------------------LKKLNEEKKE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 444 LEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSR---------LQQETAQLEESVESGKAQLEPL 514
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEK 587
|
170 180
....*....|....*....|..
gi 755507765 515 QQHLQESQQEISSMQMRLEMKD 536
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKE 609
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-533 |
8.44e-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: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEE 446
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEIS 526
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
....*..
gi 755507765 527 SMQMRLE 533
Cdd:COG1196 390 EALRAAA 396
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
365-543 |
2.90e-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: 64.32 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 365 FSAIKELDTLNNEIVDLQREKnnveQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLqaqkqqvqelLGELDEQKAQL 444
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAE-EAQL----ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 519
Cdd:TIGR02169 771 EEDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180
....*....|....*....|....
gi 755507765 520 ESQQEISSMQMRLEMKDLETDNNQ 543
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-525 |
2.91e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKA 442
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKE-----------------LYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 522
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
...
gi 755507765 523 QEI 525
Cdd:TIGR02168 379 EQL 381
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-542 |
3.08e-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: 63.93 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqQVQELLGE----LDEQKAQLE 445
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-----------KEIEQLEQeeekLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEEL--LKAREELSRLQQETAQ---LEESVESGKAQLEPLQQHLQE 520
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAElskLEEEVSRIEARLREIEQKLNR 823
|
170 180
....*....|....*....|..
gi 755507765 521 SQQEISSMQMrlEMKDLETDNN 542
Cdd:TIGR02169 824 LTLEKEYLEK--EIQELQEQRI 843
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-547 |
3.24e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 375 NNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVR 452
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 453 KKCAEEAQLISSLKAEITSQESQI--------SSYEEELLKAREELSRLQQETAQLEESVES---GKAQLEPLQQHLQES 521
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQLqqeaqrilASLEAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVA 363
|
170 180
....*....|....*....|....*.
gi 755507765 522 QQEISSMQMRLEMKDLETDNNQSNWS 547
Cdd:COG3206 364 RELYESLLQRLEEARLAEALTVGNVR 389
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-533 |
3.25e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvQELLGELDEQKAQLEEQL 448
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL--------------EEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
....*
gi 755507765 529 QMRLE 533
Cdd:COG1196 427 EEALA 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
439-528 |
4.55e-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: 62.47 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 439 EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 518
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|
gi 755507765 519 QESQQEISSM 528
Cdd:COG4942 100 EAQKEELAEL 109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
369-490 |
6.36e-10 |
|
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: 60.32 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTS---------EVQDLQDEV--QRESINLQKlqaqkqqvqELLGEL 437
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIesLKRRISDLE---------DEILEL 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755507765 438 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREEL 490
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-543 |
6.48e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 377 EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDEQKAQLEEQLQEVRKKCA 456
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------LELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 457 EEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKD 536
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
....*..
gi 755507765 537 LETDNNQ 543
Cdd:COG1196 379 EELEELA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
369-529 |
7.74e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLEEQL 448
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--------------LEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAE---EAQLISS-------LKAEITSQESQISSYEEELLKAR----EELSRLQQETAQLEESVESGKAQLEPL 514
Cdd:COG4942 100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*
gi 755507765 515 QQHLQESQQEISSMQ 529
Cdd:COG4942 180 LAELEEERAALEALK 194
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-543 |
8.84e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 349 RSSLQKNITGSSpvADFSAIK-ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResINLQKLQAQK 427
Cdd:TIGR04523 227 NNQLKDNIEKKQ--QEINEKTtEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ--LKSEISDLNN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 428 QQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESG 507
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 755507765 508 KAQLEPLQQHLQE-----SQQEISSMQMRLEMKDLETDNNQ 543
Cdd:TIGR04523 383 KQEIKNLESQINDleskiQNQEKLNQQKDEQIKKLQQEKEL 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
360-531 |
1.22e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 360 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvQELLGELDE 439
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 440 QKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQES----QISSYEEELLKAREELSRLQQETAQLEesvesgkAQLEPLQ 515
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAE-------AALRDLR 418
|
170
....*....|....*.
gi 755507765 516 QHLQESQQEISSMQMR 531
Cdd:COG4913 419 RELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
366-527 |
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 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQR---------------------------ESI 418
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqkeelaellralyrlgrqpplalllspEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 419 NLQKLQAQ-----KQQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRL 493
Cdd:COG4942 132 LDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|....
gi 755507765 494 QQETAQLEESVESGKAQLEPLQQHLQESQQEISS 527
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
439-542 |
1.56e-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: 56.49 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 439 EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQ-----ESQiSSYEEELLK----------AREELSRLQQETAQLEES 503
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQaeiarEAQ-QNYERELVLhaedikalqaLREELNELKAEIAELKAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 755507765 504 VESGKAQLEPLQQHLQES----QQEISSMQMRLEmkDLETDNN 542
Cdd:pfam07926 80 AESAKAELEESEESWEEQkkelEKELSELEKRIE--DLNEQNK 120
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
432-543 |
2.08e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLQEVRKKcaeeaqlISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 755507765 512 EPLQQHLQESQQEISSMQMRL-----EMKDLETDNNQ 543
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELeelqkERQDLEQQRKQ 133
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
368-542 |
2.93e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQrESINLQKLQAQKQQVQELlgELDEQKA---QL 444
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN-QLKDEQNKIKKQLSEKQK--ELEQNNKkikEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAE-----EAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 519
Cdd:TIGR04523 287 EKQLNQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
170 180
....*....|....*....|....*...
gi 755507765 520 ESQQEISSM-----QMRLEMKDLETDNN 542
Cdd:TIGR04523 367 EKQNEIEKLkkenqSYKQEIKNLESQIN 394
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-529 |
3.36e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEE 446
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEIS 526
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
...
gi 755507765 527 SMQ 529
Cdd:COG1196 502 DYE 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
370-540 |
5.55e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqAQKQQVQELLGELDEQKA 442
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEEQLQEVR----------KKCAEEAQLISSLKAEITSQ----ESQISSYEEELLKAREELSRLQQETAQLEESVESGK 508
Cdd:PRK02224 325 ELRDRLEECRvaaqahneeaESLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
170 180 190
....*....|....*....|....*....|..
gi 755507765 509 AQLEPLQQHLQESQQEISSMQMRLemKDLETD 540
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELRERE--AELEAT 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
371-538 |
7.58e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 371 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTVKQRTSEVQDLQDEVQ----------------RESINLQKLQAQK 427
Cdd:COG4717 48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEeleeeleeleaeleelREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 428 QQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQL---ISSLKAEITSQESQISSYEEEL-LKAREELSRLQQETAQLEES 503
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 755507765 504 VESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLE 538
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
368-540 |
1.36e-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: 58.49 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQ 447
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 448 LQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVesgkAQLEPLQQHLQESQQEISS 527
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV----KDLTKKISSLKEKIEKLES 531
|
170
....*....|....*
gi 755507765 528 --MQMRLEMKDLETD 540
Cdd:TIGR04523 532 ekKEKESKISDLEDE 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-533 |
1.83e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEvqRESINLQKLQAQKQQVQELLGELDEQKAQ 443
Cdd:COG4913 229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 444 LEEQLQEVRKKCAEEAQLISSLKAEITSQ--------ESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170
....*....|....*...
gi 755507765 516 QHLQESQQEISSMQMRLE 533
Cdd:COG4913 387 AEAAALLEALEEELEALE 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-545 |
2.08e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQK--------------------- 427
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleerleeaeeelaeaeaei 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 428 -------QQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL 500
Cdd:TIGR02168 785 eeleaqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755507765 501 EESVESGKAQLEPLQQHLQESQQEIssMQMRLEMKDLETDNNQSN 545
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEAL--ALLRSELEELSEELRELE 907
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
366-538 |
2.10e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRT-SEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKaQL 444
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYE-----EELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 519
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
170
....*....|....*....
gi 755507765 520 ESQQEissmqmRLEMKDLE 538
Cdd:PRK03918 705 EREKA------KKELEKLE 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
434-523 |
3.24e-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: 56.70 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 434 LGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90
....*....|
gi 755507765 514 LQQHLQESQQ 523
Cdd:COG4942 109 LLRALYRLGR 118
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-519 |
3.58e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqellgeLDEQKAQLEEQLQ 449
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG---------------------IEAKINELEEEKE 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755507765 450 EVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE-------ESVESGKAQLEPLQQHLQ 519
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGGRAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
366-604 |
6.13e-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: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQR------ESINLQKLQAQKQQVQELL---GE 436
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgERARALYRSGGSVSYLDVLlgsES 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDE--QKAQLEEQLQEVRKKCAEEAQlisSLKAEITSQESQISSYEEELLKAREELSR----LQQETAQLEESVESGKAQ 510
Cdd:COG3883 114 FSDflDRLSALSKIADADADLLEELK---ADKAELEAKKAELEAKLAELEALKAELEAakaeLEAQQAEQEALLAQLSAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 511 LEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTH 590
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
250
....*....|....
gi 755507765 591 QESSVRSSPEIAPS 604
Cdd:COG3883 271 AAGAGAAAASAAGG 284
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-536 |
7.98e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLEEQL 448
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE--------------LRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
....*...
gi 755507765 529 QMRLEMKD 536
Cdd:TIGR02168 371 ESRLEELE 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
369-616 |
8.46e-08 |
|
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: 56.28 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLK-----------EKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQEL-- 433
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEqtRNTLKSMEGSDGHAMKVAMgm 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 434 -------LGELD--EQKAQ-LEEQLQEVRKK---CAEEAQLISSLKAEITSQESQISSyEEELLKAREElsRLQQETAQL 500
Cdd:pfam15921 733 qkqitakRGQIDalQSKIQfLEEAMTNANKEkhfLKEEKNKLSQELSTVATEKNKMAG-ELEVLRSQER--RLKEKVANM 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 501 EESVESGKAQLEPLQQHLQESQQEISSMQMR--LEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSETANF-NEH 577
Cdd:pfam15921 810 EVALDKASLQFAECQDIIQRQEQESVRLKLQhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlSHH 889
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 755507765 578 AEGQNNLESEPTH------QEssVRSSPEIAPSDVTDESEAVTVA 616
Cdd:pfam15921 890 SRKTNALKEDPTRdlkqllQE--LRSVINEEPTVQLSKAEDKGRA 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-517 |
1.02e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQD-------LKEKEDTVKQRTSEVQDLQDEVQR-ESInlqklqaqkQQVQELLGELDEQ 440
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSkrkleekIRELEERIEELKKEIEELEEKVKElKEL---------KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 441 KAQLEEQLQEVRKKCAEEAQLISSLKAEItsqeSQISSYEEELLKAREELSRLQQETAQLEESV---ESGKAQLEPLQQH 517
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-533 |
1.08e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQL 444
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEE--ELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 522
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|.
gi 755507765 523 QEISSMQMRLE 533
Cdd:PRK03918 331 KELEEKEERLE 341
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
366-533 |
1.35e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKL-----QAQKQQVQELLGELD 438
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelRERFGDAPVdlgnaEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 439 EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQhL 518
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-L 504
|
170
....*....|....*
gi 755507765 519 QESQQEISSMQMRLE 533
Cdd:PRK02224 505 VEAEDRIERLEERRE 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-492 |
1.45e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResiNLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755507765 449 QEVRKKcaeeaqlISSLKAEITSQESQISSYEEELLKAREELSR 492
Cdd:COG4913 415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
436-531 |
1.77e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLIS--SLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVEsgkaqLEP 513
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAE 473
|
90
....*....|....*...
gi 755507765 514 LQQHLQESQQEISSMQMR 531
Cdd:COG4717 474 LLQELEELKAELRELAEE 491
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
432-529 |
1.78e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 53.90 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELD-----EQKAQLEEQLQEVRKKcAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRL----------QQE 496
Cdd:COG1566 71 QVLARLDptdlqAALAQAEAQLAAAEAQ-LARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQE 149
|
90 100 110
....*....|....*....|....*....|...
gi 755507765 497 TAQLEESVESGKAQLEPLQQHLQESQQEISSMQ 529
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLREEE 182
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
437-533 |
2.11e-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: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDEQKAQLEEQLQEVRKKCAE--EAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPL 514
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100
....*....|....*....|.
gi 755507765 515 QQH--LQESQQEISSMQMRLE 533
Cdd:COG3206 260 LQSpvIQQLRAQLAELEAELA 280
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-545 |
2.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 433 LLGELDEQKAQLEEQ---------LQEVRKKCAEEAQL--ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE 501
Cdd:COG1196 194 ILGELERQLEPLERQaekaeryreLKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755507765 502 ESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSN 545
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
365-527 |
2.71e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.07 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 365 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDL--QDEVQRESINlqklqaqkqqvqellgeldeqka 442
Cdd:PRK04778 89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQELleSEEKNREEVE----------------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEEQLQEVRKKCAEEA----QLISSLKAEITSQESQISSYEEE-----LLKAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:PRK04778 144 QLKDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELtesgdYVEAREILDQLEEELAALEQIMEEIPELLKE 223
|
170
....*....|....
gi 755507765 514 LQQHLQESQQEISS 527
Cdd:PRK04778 224 LQTELPDQLQELKA 237
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
437-533 |
3.66e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 51.75 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEE----LLKAREELSR--LQQEtAQLEESVESGKAQ 510
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlaLEKGREDLAReaLERK-AELEAQAEALEAQ 106
|
90 100
....*....|....*....|...
gi 755507765 511 LEPLQQHLQESQQEISSMQMRLE 533
Cdd:COG1842 107 LAQLEEQVEKLKEALRQLESKLE 129
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
349-527 |
4.01e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 349 RSSLQKNI-TGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQrtsevqdlqdevqresinlqklqaqk 427
Cdd:COG3206 242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-------------------------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 428 qqvqellgeLDEQKAQLEEQLQEvrkkcaEEAQLISSLKAEITSQESQISSYEEELLKAREELSRL---QQETAQLEESV 504
Cdd:COG3206 296 ---------LRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREV 360
|
170 180
....*....|....*....|...
gi 755507765 505 ESGKAQLEPLQQHLQESQQEISS 527
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 |
4.40e-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: 4.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 755507765 39 AAAFLKKSGLPDLILGKIWDLADTDGKGVLSKQEFFVALRLV 80
Cdd:pfam12763 31 VSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
382-654 |
4.81e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 382 QREKNNVEQdLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL----------QEV 451
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeaeeakkaEEL 1707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 452 RKKCAEEAQLISSLKAE-----ITSQESQISSYE-----EELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQES 521
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAeeenkIKAEEAKKEAEEdkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 522 QQEISSMQMRLEMKDLETD-------NNQSNWSSSPQSVLVNGATDYCSLSTSS--SETANFNEHAEGQNNLESEPTHQE 592
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNfaniiegGKEGNLVINDSKEMEDSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNKE 1867
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507765 593 SSVRSSPEIAPSDVTDESEAVTvagNEKVtprfddDKHSKEEDPFNVESSSLTDAVADTNLD 654
Cdd:PTZ00121 1868 ADFNKEKDLKEDDEEEIEEADE---IEKI------DKDDIEREIPNNNMAGKNNDIIDDKLD 1920
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
381-538 |
7.10e-07 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 51.95 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 381 LQREKNNVEQDLKEKEDTVKQRTSEVQdLQDEVQR-------ESINLQKLQAQKQQVQEL--------LGELDEQKAQLE 445
Cdd:pfam04849 99 LTERNEALEEQLGSAREEILQLRHELS-KKDDLLQiysndaeESETESSCSTPLRRNESFsslhgcvqLDALQEKLRGLE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKC-----------AEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL-------EESVESG 507
Cdd:pfam04849 178 EENLKLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLlaqivdlQHKCKEL 257
|
170 180 190
....*....|....*....|....*....|.
gi 755507765 508 KAQLEPLQQHLQESQQeiSSMQMRLEMKDLE 538
Cdd:pfam04849 258 GIENEELQQHLQASKE--AQRQLTSELQELQ 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
359-538 |
1.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 359 SSPVADFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTVKQRTSEVQDLQdEVQRESINlqklqaqkqqvqelLG 435
Cdd:COG4913 600 SRYVLGFDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQRLA-EYSWDEID--------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLisslkaeitsqESQISSYEEELLKAREELSRLQQETAQLEESVEsgkaQLEPLQ 515
Cdd:COG4913 665 SAEREIAELEAELERLDASSDDLAAL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEEL 729
|
170 180
....*....|....*....|...
gi 755507765 516 QHLQESQQEISSMQMRLEMKDLE 538
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLE 752
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
369-469 |
1.04e-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: 50.69 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqKQQVQELLGELDEQKAQLEEQL 448
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL----------EAELEEKKAELDEELAELEAEL 158
|
90 100
....*....|....*....|.
gi 755507765 449 QEVRKKCAEeaqLISSLKAEI 469
Cdd:COG1579 159 EELEAEREE---LAAKIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
439-538 |
1.10e-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: 50.69 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 439 EQKAQLEEqLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 518
Cdd:COG1579 4 EDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100
....*....|....*....|....*..
gi 755507765 519 QE--SQQEISSMQ-----MRLEMKDLE 538
Cdd:COG1579 83 GNvrNNKEYEALQkeiesLKRRISDLE 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-542 |
1.15e-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: 52.33 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQEL---LGELDEQKAQLE 445
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLesqISELKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKCAEEAQLISSLKA---------------------EITSQESQISSYEEELLKAREELSRLQQETAQ----- 499
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnke 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755507765 500 LEESVESGKAQLEPLQQHLQESQQEISSM-----QMRLEMKDLETDNN 542
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLneqisQLKKELTNSESENS 359
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
371-533 |
1.17e-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: 52.05 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 371 LDTLNNEIVDLQREKNNVEQDLKEKedtvkqrTSEVQDLQdevQResinlqklqaqkqqvqellgeLDEQKA------QL 444
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQST-------NSELEELQ---ER---------------------LDLLKAkaseaeQL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAEEAQLISSLKAEITSQES-------------QISSYEEELLKAREE---LSRLQQETAQLEESVESGK 508
Cdd:pfam05557 155 RQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseivknskselaRIPELEKELERLREHnkhLNENIENKLLLKEEVEDLK 234
|
170 180
....*....|....*....|....*
gi 755507765 509 AQLEplqqHLQESQQEISSMQMRLE 533
Cdd:pfam05557 235 RKLE----REEKYREEAATLELEKE 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
369-540 |
1.21e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVeqDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQL 448
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQ--LISSLKAEITSQESQISSYEE-------ELLKAREELSRLQQE--------TAQLEESVESGKAQL 511
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQlqqeaqriLASLEAELEALQARE 329
|
170 180 190
....*....|....*....|....*....|
gi 755507765 512 EPLQQHLQESQQEISSM-QMRLEMKDLETD 540
Cdd:COG3206 330 ASLQAQLAQLEARLAELpELEAELRRLERE 359
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
382-541 |
1.44e-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: 51.78 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 382 QREKNNVEQDLKEKEDTVKQRTSEVQDL--QDEVQRESINlqklqaqkqqvqellgeldeqkaQLEEQLQEVRKKCAEEA 459
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELleSEEKNREEVE-----------------------ELKDKYRELRKTLLANR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 460 ----QLISSLKAEITSQESQISSYEE-----ELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQM 530
Cdd:pfam06160 142 fsygPAIDELEKQLAEIEEEFSQFEEltesgDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYR 221
|
170
....*....|...
gi 755507765 531 RLEMKD--LETDN 541
Cdd:pfam06160 222 EMEEEGyaLEHLN 234
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
438-543 |
1.60e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110
....*....|....*....|....*....|.
gi 755507765 518 LQESQQEISSMQMRL-----EMKDLETDNNQ 543
Cdd:COG4372 82 LEELNEQLQAAQAELaqaqeELESLQEEAEE 112
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
367-546 |
2.48e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIVDLQREKNnveQDLKEK-EDTVKQRTSEVQDLQDEV-QRESInlqklqaqkqqvqellgeLDEQKAQL 444
Cdd:PRK12704 47 AKKEAEAIKKEALLEAKEEI---HKLRNEfEKELRERRNELQKLEKRLlQKEEN------------------LDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 EEQLQEVRKKCAEeaqlISSLKAEITSQESQISSYEEELLKAREELSRLQQETAqleesvesgKAQLepLQQHLQESQQE 524
Cdd:PRK12704 106 EKREEELEKKEKE----LEQKQQELEKKEEELEELIEEQLQELERISGLTAEEA---------KEIL--LEKVEEEARHE 170
|
170 180
....*....|....*....|..
gi 755507765 525 ISSMQMRLEMKDLETDNNQSNW 546
Cdd:PRK12704 171 AAVLIKEIEEEAKEEADKKAKE 192
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
251-355 |
2.49e-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: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 251 LRQWvvspaEKAKYDEIFlKTDKDMDGYVSGLEVRETFLKTGLPSALLAHIWSLCDTKGCGKLSKDQFALA----FHLIN 326
Cdd:pfam12763 4 LEEW-----EIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAmrliFDLVN 77
|
90 100
....*....|....*....|....*....
gi 755507765 327 QKLikgIDPPHSLTPEMIPPSDRSSLQKN 355
Cdd:pfam12763 78 GNI---ADVPDELPDWLVPGSKAHLIQAN 103
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-541 |
2.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 381 LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEE-- 458
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 459 AQLISSLKAEitsQESQISSYEEELLKAREELSRLQQETAQLEE------------SVESGKAQLEPLQQHLQESQQEIS 526
Cdd:COG4717 373 AALLAEAGVE---DEEELRAALEQAEEYQELKEELEELEEQLEEllgeleellealDEEELEEELEELEEELEELEEELE 449
|
170 180
....*....|....*....|
gi 755507765 527 SMQMRL-----EMKDLETDN 541
Cdd:COG4717 450 ELREELaeleaELEQLEEDG 469
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
438-539 |
3.08e-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: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100
....*....|....*....|..
gi 755507765 518 LQESQQEISSMQMRLEMKDLET 539
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSD 116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
367-539 |
3.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQ--------------------DEVQRESINLQKLQAQ 426
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgrelTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 427 KQQVQElLGELDEQKAQLEEQLQEVRKKCAEEAQLIS--SLKAEITSQESQISSY--------EEELLKAREELSRLQQE 496
Cdd:PRK03918 462 KRIEKE-LKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGE 540
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755507765 497 TAQLEESVESGKA---QLEPLQQHLQESQQEISSMQMRLEMKDLET 539
Cdd:PRK03918 541 IKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFES 586
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-541 |
4.31e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKnnvEQDL-KEKEDTVKQRTSEVQDLQDEVQR--ESINlqklqaqkqqvqellgELDEQKAQLE 445
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQnnKIIS----------------QLNEQISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQL-------QEVRKKCAEEAQLISSLKAE-------ITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:TIGR04523 349 KELtnsesenSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
170 180 190
....*....|....*....|....*....|
gi 755507765 512 EPLQQHLQESQQEISSMQMRLEMKDLETDN 541
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
379-546 |
4.43e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 379 VDLQREKNNVEQDLKEKE---DTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKC 455
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQhelDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 456 AEEAQLISSLKAEI-----------TSQESQISSYEEELLKAREELSRLQQETAQ-------LEESVESGK--------- 508
Cdd:TIGR00606 898 QSLIREIKDAKEQDspletflekdqQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdIENKIQDGKddylkqket 977
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755507765 509 ------AQLEPLQQHlqesqQEISSMQMRLEMKDLETDNNQSNW 546
Cdd:TIGR00606 978 elntvnAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERW 1016
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
370-544 |
4.84e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRtSEVQDLQDevQRESINlqklqaqkqqvqELLGELDEQKAQLEEQLQ 449
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------ELIAERRETIEEKRERAE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 450 EVRKKCAEeaqlissLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESgKAQLEPLQQHLQESQQEISSMQ 529
Cdd:PRK02224 541 ELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAEDEIERLR 612
|
170
....*....|....*
gi 755507765 530 MRLEmkDLETDNNQS 544
Cdd:PRK02224 613 EKRE--ALAELNDER 625
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
367-521 |
4.87e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTVKQRTSEVQDLQDEVQR--ES--INLQKLqaqkqqvqELLG 435
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkQSytLNESEL--------ESVR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:PRK04778 352 QLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
|
....*.
gi 755507765 516 QHLQES 521
Cdd:PRK04778 432 RYLEKS 437
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
368-542 |
5.52e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVqrESINLQKLqaqkqqvqellgELDEQKAQLEEQ 447
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL--EKLNNKYN------------DLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 448 LQEVRKKCAEEAQLISSLKAEITSQE---SQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQE 524
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
170 180
....*....|....*....|....*
gi 755507765 525 ISSM-------QMRLEMKDLETDNN 542
Cdd:TIGR04523 255 LNQLkdeqnkiKKQLSEKQKELEQN 279
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-535 |
7.39e-06 |
|
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: 49.68 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDT-----VKQRTSEVQDLQDEVQR-----ESINLQklqaqkqqvqelLGE 436
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRiearlREIEQK------------LNR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDEQKAQLEEQLQEvrkkcaEEAQLIsslkaEITSQESQISSYEEELLKAREEL----SRLQQETAQLEESVESGKAQLE 512
Cdd:TIGR02169 824 LTLEKEYLEKEIQE------LQEQRI-----DLKEQIKSIEKEIENLNGKKEELeeelEELEAALRDLESRLGDLKKERD 892
|
170 180
....*....|....*....|...
gi 755507765 513 PLQQHLQESQQEISSMQMRLEMK 535
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKK 915
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
366-509 |
8.73e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqELLGELDEQKAQ 443
Cdd:COG2433 380 EALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-----------------ELEAELEEKDER 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507765 444 ---LEEQLQEVRKKCAEEAQL---ISSLKAEITSQESQIssyeEELLKAREELSRLQQETAQLEESVESGKA 509
Cdd:COG2433 443 ierLERELSEARSEERREIRKdreISRLDREIERLEREL----EEERERIEELKRKLERLKELWKLEHSGEL 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
433-545 |
9.15e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 433 LLGELDEQ------KAQLEEQLQEVRKKcAEEAQL------ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL 500
Cdd:TIGR02168 194 ILNELERQlkslerQAEKAERYKELKAE-LRELELallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 755507765 501 EESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSN 545
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 ... |
432-501 |
9.81e-06 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 44.22 E-value: 9.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE 501
Cdd:pfam12329 5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
434-530 |
1.08e-05 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 45.35 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 434 LGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQEsqissyeeelLKAREE-LSRLQQETAQLEESVESGKAQLE 512
Cdd:pfam02050 7 LAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAE----------LRNYQAfISQLDEAIAQQQQELAQAEAQVE 76
|
90
....*....|....*...
gi 755507765 513 PLQQHLQESQQEISSMQM 530
Cdd:pfam02050 77 KAREEWQEARQERKSLEK 94
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
368-549 |
1.23e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQ-----------RTS------EVQDLQDEVQRESINLQKLQAQKQQV 430
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELREELDElrkelaelnkaGGSidklrkEIERLEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 431 QELLGELDEQKAQLE--EQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGK 508
Cdd:COG1340 143 KELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQ 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 755507765 509 AQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSS 549
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
369-526 |
1.36e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKnnveqDLKEKEDTVKQRTSEVQdLQdEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQL 448
Cdd:pfam15905 152 KKMSSLSMELMKLRNKL-----EAKMKEVMAKQEGMEGK-LQ-VTQKN-----------------LEHSKGKVAQLEEKL 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITsqesQISSYEEELLKAREELsrlqqetAQLEESVESGKAQLEPLQQHLQESQQEIS 526
Cdd:pfam15905 208 VSTEKEKIEEKSETEKLLEYIT----ELSCVSEQVEKYKLDI-------AQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
354-542 |
1.41e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 354 KNITGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ----RESINLQKLQAQKQQ 429
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 430 VQELLGELDEQKAQ----------LEEQLQEVRKKCA--------EEAQL-------------ISSLKAEITSQESQISS 478
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 479 YEEELLKAREELSR-----------------LQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLE-MKDLETD 540
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNqLKDEQNK 264
|
..
gi 755507765 541 NN 542
Cdd:TIGR04523 265 IK 266
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
363-522 |
1.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 363 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqAQKQQVQELLGELDEQK 441
Cdd:COG4913 685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 442 AQL--EEQLQEVRKKCAEEaqlISSLKAEITSQESQI----SSY-----------------------------EEELLKA 486
Cdd:COG4913 756 AAAlgDAVERELRENLEER---IDALRARLNRAEEELeramRAFnrewpaetadldadleslpeylalldrleEDGLPEY 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755507765 487 REELSRLQQET---------AQLEESVESGKAQLEPLQQHLQESQ 522
Cdd:COG4913 833 EERFKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
369-542 |
1.47e-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: 47.30 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQrEKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklQAQKQQVQELLGELDeqKAQLEEQL 448
Cdd:pfam12795 17 KLLQDLQQALSLLD-KIDASKQRAAAYQKALDDAPAELRELRQELAALQ------AKAEAAPKEILASLS--LEELEQRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISsyeeellKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQ-EISS 527
Cdd:pfam12795 88 LQTSAQLQELQNQLAQLNSQLIELQTRPE-------RAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAA 160
|
170
....*....|....*
gi 755507765 528 MQMRLEMKDLETDNN 542
Cdd:pfam12795 161 LKAQIDMLEQELLSN 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
371-602 |
1.60e-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: 48.66 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 371 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQ 429
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 430 VQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE-ESVEsgk 508
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrERLE--- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 509 aQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGatdycslSTSSSETANFNEHAEGQNNLESE- 587
Cdd:pfam10174 469 -ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD-------SKLKSLEIAVEQKKEECSKLENQl 540
|
250
....*....|....*..
gi 755507765 588 -PTHQ-ESSVRSSPEIA 602
Cdd:pfam10174 541 kKAHNaEEAVRTNPEIN 557
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
368-525 |
1.94e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGEL---------- 437
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 -DEQK------AQLEEQLQEvRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQ 510
Cdd:COG1340 132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
170
....*....|....*
gi 755507765 511 LEPLQQHLQESQQEI 525
Cdd:COG1340 211 ADELHKEIVEAQEKA 225
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
368-536 |
2.05e-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: 48.43 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQK--------QQVQELLGELDE 439
Cdd:TIGR00618 713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtaalqtgAELSHLAAEIQF 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 440 QKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQhlq 519
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ--- 866
|
170
....*....|....*..
gi 755507765 520 eSQQEISSMQMRLEMKD 536
Cdd:TIGR00618 867 -EQAKIIQLSDKLNGIN 882
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
373-560 |
2.14e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.45 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 373 TLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqellGELDEQKAQLEEQLQEVR 452
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA-----------------ESSREQLQELEEQLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 453 kkcaeeaqlisSLKAEItsqESQISSYEEELLKAREELSR----LQQETAQLEESVESGKAQL----------------- 511
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLtsksqssssqselenrl 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755507765 512 ----EPL---QQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSSPqSVLVNGATD 560
Cdd:pfam09787 173 hqltETLiqkQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGT-SINMEGISD 227
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
436-538 |
2.15e-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: 47.54 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRkkcaeeaQLISSLKAEITSQESQISSYEEEL------LKARE-----EL------SRLQQETA 498
Cdd:pfam03148 255 ETEDAKNKLEWQLKKTL-------QEIAELEKNIEALEKAIRDKEAPLklaqtrLENRTyrpnvELcrdeaqYGLVDEVK 327
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 755507765 499 QLEESVESgkaqlepLQQHLQESQQEISSM---QMRLEmKDLE 538
Cdd:pfam03148 328 ELEETIEA-------LKQKLAEAEASLQALertRLRLE-EDIA 362
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-500 |
2.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 397 DTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQI 476
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 755507765 477 SSYEEELLKAREELSRLQQETAQL 500
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
388-507 |
2.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 388 VEQDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKA 467
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755507765 468 EITSQESQISSYEEELLKAREELSRLQQETAQLEESVESG 507
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-529 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEV------QRESINLQKLQAQKQQVQEL-LGELDEQ- 440
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltkkISSLKEKIEKLESEKKEKESkISDLEDEl 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 441 --------KAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQ-- 510
Cdd:TIGR04523 548 nkddfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEne 627
|
170 180
....*....|....*....|....
gi 755507765 511 -LEPLQQHLQES----QQEISSMQ 529
Cdd:TIGR04523 628 kLSSIIKNIKSKknklKQEVKQIK 651
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
370-504 |
2.88e-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: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEqdlKEKEDTVKQRtsevqdlqdevqresinlqklqaqkqqvqelLGELDEQKAQLEEQLQ 449
Cdd:COG0542 412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 450 EVRKKCAEEAQLIS---SLKAEITSQESQISSYEEELLKAREELSrlqQETAQLEESV 504
Cdd:COG0542 458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
53-189 |
3.60e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 44.40 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 53 LGKIWDLADTDGKGVLSKQEFfVALRLVACAQNGLEVslsslslavppprFHDSSSPLlTSGPSVAELPWAVKSEDKAKY 132
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSEA-------------DTDGDGRI-SREEFVAGMESLFEATVEPFA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 133 DAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAM 189
Cdd:COG5126 72 RAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
381-535 |
4.20e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 44.65 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 381 LQREKNNVEQDLKE------KEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqelLGEldEQKAQLEEQLQEVRKK 454
Cdd:pfam05672 25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 455 CAEEAQlisslkAEITSQESQISSYEEELLKAREELSRLQQETAqleesvesgkaqleplqQHLQESQQEISSMQMRLE- 533
Cdd:pfam05672 85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQERE-----------------KIMQQEEQERLERKKRIEe 141
|
...
gi 755507765 534 -MK 535
Cdd:pfam05672 142 iMK 144
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
371-523 |
4.82e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.56 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 371 LDTLNNEIVDLQREKNNVEQDLKEKedtvkqRTSEVQDLQDEVQREsinlqklqaqkqqvqellgeLDEQKAQLEEQLQE 450
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 451 VRKKCAEEAQLissLKAEItsqESQISSYEEELLKAREELSR----LQQETAQ-LEESVESGKAQLEP--------LQQH 517
Cdd:pfam01442 60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEklapYGEELRErLEQNVDALRARLAPyaeelrqkLAER 133
|
....*.
gi 755507765 518 LQESQQ 523
Cdd:pfam01442 134 LEELKE 139
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
380-540 |
5.15e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 380 DLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqKQQVQELlgELDEQKAQLEEQLQEVRKKCAEEa 459
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------------ALKSRKK--QMEKDNSELELKMEKVFQGTDEQ- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 460 qlissLKAEITSQESQISSYEEELLKAREELSRLQQETAQL-----EESVESGKAQL--EPLQQHLQESQQEISSMQMRL 532
Cdd:TIGR00606 303 -----LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektELLVEQGRLQLqaDRHQEHIRARDSLIQSLATRL 377
|
....*...
gi 755507765 533 EMKDLETD 540
Cdd:TIGR00606 378 ELDGFERG 385
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
366-554 |
5.31e-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: 46.89 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkQQVQELLGELDEQKAQLE 445
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----------EAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQL------QEVRKKCAEEAQLISSLKAEITS--QESQissyEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:TIGR00618 623 PEQdlqdvrLHLQQCSQELALKLTALHALQLTltQERV----REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
170 180 190
....*....|....*....|....*....|....*..
gi 755507765 518 LQESQQEISSMQMRLEMKDLETdNNQSNWSSSPQSVL 554
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREF-NEIENASSSLGSDL 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
370-523 |
6.13e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREknnveqDLKEKEDTVKQRTSEV-QDLQD-----EVQRESInlqklqaqkQQVQELLGELDEQKAQ 443
Cdd:PRK02224 303 GLDDADAEAVEARRE------ELEDRDEELRDRLEECrVAAQAhneeaESLREDA---------DDLEERAEELREEAAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 444 LEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQ 523
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
391-535 |
6.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 391 DLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLqaqkqqvqELLGELD-EQKAQLEEQLQEVRKKCAEEAQLiSSLKAEI 469
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIA--------ALLAEAGvEDEEELRAALEQAEEYQELKEEL-EELEEQL 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 470 TSQESQISSYEEELLKA--REELSRLQQETAQLEESVESGKAQLEPLQQHLQ--ESQQEISSMQMRLEMK 535
Cdd:COG4717 412 EELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEEL 481
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-544 |
9.03e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVD-------LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKA 442
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQ 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEEQLQEVRKKCAE-EAQLISSLKAEITSQESQISSYEEEL-LKARE-----ELSR----------LQQE-----TAQL 500
Cdd:pfam01576 942 QLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIAQLEEQLeQESRErqaanKLVRrtekklkevlLQVEderrhADQY 1021
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755507765 501 EESVESGKAQLEPLQQHLQESQQEISSMQM--RLEMKDLE--TDNNQS 544
Cdd:pfam01576 1022 KDQAEKGNSRMKQLKRQLEEAEEEASRANAarRKLQRELDdaTESNES 1069
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-543 |
9.53e-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: 46.21 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQ-------RTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQK 441
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 442 AQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQET-------AQLEESVESGKAQLEPL 514
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakiNELEEEKEDKALEIKKQ 453
|
170 180
....*....|....*....|....*....
gi 755507765 515 QQHLQESQQEISSMQMRLEmkDLETDNNQ 543
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELY--DLKEEYDR 480
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
471-543 |
1.02e-04 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 41.78 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755507765 471 SQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLemKDLETDNNQ 543
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKL--RKLQEENDE 71
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
326-525 |
1.06e-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: 44.94 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 326 NQKLIKGIDPPHSLTPEMIppsdRSSLQKN--ITGSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTVKQRT 403
Cdd:pfam15397 22 NLELIKAIQDTEDSTALKV----RKLLQQYekFGTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 404 SEVQDLQDEVQRES-------------InlqklqaqkqqvQELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEIT 470
Cdd:pfam15397 95 AKIQKTQEELNFLStykdkeypvkavqI------------ANLVRQLQQLKDSQQDELDELEEMRRMVLESLSRKIQKKK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 471 SQ------ESQISSYEEELL-KARE------ELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEI 525
Cdd:pfam15397 163 EKilsslaEKTLSPYQESLLqKTRDnqvmlkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
|
|
| DUF1090 |
pfam06476 |
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ... |
440-525 |
1.13e-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: 42.23 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 440 QKAQLEEQLQEVRKKCAEEaqlisSLKAEitsqesqissYEEELLKAREELSRLQQEtaqLEESVESGKAQL-EPLQQHL 518
Cdd:pfam06476 39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAEREAE---LAEAQAKGDADKiAKRQRKL 100
|
....*..
gi 755507765 519 QESQQEI 525
Cdd:pfam06476 101 AEARQEL 107
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
382-524 |
1.22e-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: 42.21 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 382 QREKNNVEQDLKEKEDTVKQRTSEVQDlqdevQRESINlqklqaqkqqvqellgELDEQ--KAQLEEQLQEVRKKCAEEA 459
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKAQEELEE-----SEETAE----------------ELEEErrQAEEEAERLEQKRQEAEEE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755507765 460 qlisslKAEItsQESQISSyEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQE 524
Cdd:pfam20492 64 ------KERL--EESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
363-534 |
1.45e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 363 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTVKQ-RTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQ 440
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 441 --------KAQLEE----QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEEL----------------LKAR--EEL 490
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELqslkkqkaslerqlaeTEERyeLQL 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755507765 491 SRLQQETAQLEESVESGKAQlepLQQHLQEsQQEISSMQMRLEM 534
Cdd:pfam00038 259 ADYQELISELEAELQETRQE---MARQLRE-YQELLNVKLALDI 298
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
481-530 |
1.70e-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: 40.65 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755507765 481 EELLKAREELSRLQQE---TAQLEESVESGKAQLEPLQQHLQESQQEIssMQM 530
Cdd:cd22248 27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
433-533 |
1.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 433 LLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVE--SGKAQ 510
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQ 126
|
90 100
....*....|....*....|...
gi 755507765 511 LEPLQQHLQESQQEISSMQMRLE 533
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLE 149
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
367-535 |
1.75e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.34 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIV-----DLQREKNNVEQDLKEkedtvkqRTSEVQDLQDE-VQREsinlqklqaqkqqvqELLGELDEQ 440
Cdd:pfam12072 43 AKKEAETKKKEALleakeEIHKLRAEAERELKE-------RRNELQRQERRlLQKE---------------ETLDRKDES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 441 KAQLEEQLQEVRKKCAEEAQLISSLKAEItsqESQISSYEEELlkarEELSRLQQETAqleesvesgKAQLepLQQHLQE 520
Cdd:pfam12072 101 LEKKEESLEKKEKELEAQQQQLEEKEEEL---EELIEEQRQEL----ERISGLTSEEA---------KEIL--LDEVEEE 162
|
170
....*....|....*
gi 755507765 521 SQQEISSMQMRLEMK 535
Cdd:pfam12072 163 LRHEAAVMIKEIEEE 177
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
473-534 |
1.85e-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: 41.83 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507765 473 ESQISSYEEELLKAREELSRLQQETAQLEEsvESGKAQLEplQQHLQESQQEISSMQMRLEM 534
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEE--ERRQAEEE--AERLEQKRQEAEEEKERLEE 69
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
377-538 |
1.87e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 377 EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQV----QELLGELDEQK------AQLEE 446
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpltRRMQRGEQTYAqletseEDVYH 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETaqlEESVESGKAQLEPLQQHLQESQQEIS 526
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT---EKLSEAEDMLACEQHALLRKLQPEQD 626
|
170
....*....|..
gi 755507765 527 SMQMRLEMKDLE 538
Cdd:TIGR00618 627 LQDVRLHLQQCS 638
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
434-545 |
1.90e-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: 45.06 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 434 LGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREE-------LSRLQQETAQLEESVES 506
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedLSSLEQEIENVKSELKE 762
|
90 100 110
....*....|....*....|....*....|....*....
gi 755507765 507 GKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSN 545
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
370-545 |
2.11e-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: 44.94 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTVKQRTSEVQDLQDEVqresinlqkLQAQKQQVQELLGELDEQKAQLEE 446
Cdd:COG3096 837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 QLQEVRKKCAEEAQL---ISSLKAEITSQESQISSYEEellkAREELSRLQQETAQLEESVE-------SGKAQL----- 511
Cdd:COG3096 908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983
|
170 180 190
....*....|....*....|....*....|....*..
gi 755507765 512 ---EPLQQHLQESQQEISsmQMRLEMKDLETDNNQSN 545
Cdd:COG3096 984 dlnEKLRARLEQAEEARR--EAREQLRQAQAQYSQYN 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-505 |
2.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTvKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDE-----QKA- 442
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755507765 443 QLEEQLQEVRKKCAEEAqlISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVE 505
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
442-532 |
2.34e-04 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 43.02 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 442 AQLEEQLQEVRKKCAEEAQLISSLKAEitsQESQISSYEEeLLKAREELSRLQ-QETAQLEESVESGKAQLEPLQQHLQE 520
Cdd:cd16855 4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
|
90
....*....|..
gi 755507765 521 SQQEISSMQMRL 532
Cdd:cd16855 80 KAQELLQLRMEL 91
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
369-532 |
2.36e-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: 44.83 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKE---------KEDTVKQRtsEVQDLQDEVQRESINLQKLQAQKQQVQELLgELDE 439
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagiKDKLAKIR--EARDRQLAVAEDDLQALESELREQLEAGKL-EFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 440 QKAQLEEQLQEVRKKCAEeAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 519
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQ-ATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
|
170
....*....|...
gi 755507765 520 ESQQEISSMQMRL 532
Cdd:pfam12128 517 ERQSALDELELQL 529
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-535 |
2.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 377 EIVDLQREKNNVEQDLkEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVR---- 452
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 453 ---KKCAEEAQL-----ISSLKAEITSQESQISSYEEELlkarEELSRLQQETAQLEESVESgkaqLEPLqqHLQESQQE 524
Cdd:PRK02224 652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVEA----LEAL--YDEAEELE 721
|
170
....*....|.
gi 755507765 525 ISSMQMRLEMK 535
Cdd:PRK02224 722 SMYGDLRAELR 732
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
374-524 |
2.63e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 374 LNNEIVD-----LQREKNNVEQ---DLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqvqeLLGELDEQKAQLE 445
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKCAEEAQ-LISSLKAEItsqesqissyeEELLKAREELSRLQQETAQLEESVESGKA---QLEPLQQHLQES 521
Cdd:PRK00409 562 EEEDKLLEEAEKEAQqAIKEAKKEA-----------DEIIKELRQLQKGGYASVKAHELIEARKRlnkANEKKEKKKKKQ 630
|
...
gi 755507765 522 QQE 524
Cdd:PRK00409 631 KEK 633
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
433-530 |
2.63e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 433 LLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQleesvesgkAQLE 512
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQE 213
|
90
....*....|....*...
gi 755507765 513 PLQQHLQESQQEISSMQM 530
Cdd:PRK11448 214 RKQKRKEITDQAAKRLEL 231
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
432-533 |
3.01e-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: 42.59 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKaeitsqesqissyeEELLKAREELSRLQQETAQLE---ESVESGK 508
Cdd:pfam13851 26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLT--------------EPLQKAQEEVEELRKQLENYEkdkQSLKNLK 91
|
90 100
....*....|....*....|....*
gi 755507765 509 AQLEPLQQHLQESQQEISSMQMRLE 533
Cdd:pfam13851 92 ARLKVLEKELKDLKWEHEVLEQRFE 116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
432-538 |
3.15e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLqevrKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE---ESVESGK 508
Cdd:PRK03918 169 EVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELE 244
|
90 100 110
....*....|....*....|....*....|
gi 755507765 509 AQLEPLQQHLQESQQEISSMQMRLEMKDLE 538
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKE 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
390-538 |
3.24e-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: 44.29 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 390 QDLKEKEDTVKQRTSEVQDLQDEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEqLQEVRKKCAE-EAQLIS----S 464
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-----------------LERLRREREKAER-YQALLKEKREyEGYELLkekeA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 465 LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPL--------QQHLQESQQEISSMQ-----MR 531
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLErsiaeKE 314
|
....*..
gi 755507765 532 LEMKDLE 538
Cdd:TIGR02169 315 RELEDAE 321
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
437-543 |
3.28e-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: 42.23 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDEQKAQLEEQLQEVRKKC-AEEAQLISSLKAEITSQESQISSYEEEL---LKAR-----------EELSRLQQET---- 497
Cdd:pfam08614 19 LEAENAKLQSEPESVLPSTsSSKLSKASPQSASIQSLEQLLAQLREELaelYRSRgelaqrlvdlnEELQELEKKLrede 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755507765 498 ----------AQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEM-----KDLETDNNQ 543
Cdd:pfam08614 99 rrlaaleaerAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMaeeklRKLEKENRE 159
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
369-504 |
3.38e-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: 44.24 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqellgELDEQKAQLEEQL 448
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE---------------------EKEKKISSLEKEL 619
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESV 504
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
436-509 |
3.92e-04 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 43.06 E-value: 3.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQ-----ESQISSYEEELLKAREELSRLQQETAQLEESVESGKA 509
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
369-532 |
3.96e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQrEKNNVEQDLKekedtvkqrtsevQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:PRK09039 53 SALDRLNSQIAELA-DLLSLERQGN-------------QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLisslkaeitSQEsqissyeeellkAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:PRK09039 119 GELAQELDSEKQV---------SAR------------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
....
gi 755507765 529 QMRL 532
Cdd:PRK09039 178 GRRL 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-502 |
4.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQreknNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkQQVQELLGELDE-QKAQLEE 446
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETE----------KRLEELRKELEElEKKYSEE 659
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755507765 447 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYE----------EELLKAREELSRLQQETAQLEE 502
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
373-540 |
4.46e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 373 TLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQ---DEVQRESINLQKLQAQKQQVQE----LLGELDEQK---- 441
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlSESERQRAELAEKLSKLQSELEsvssLLNEAEGKNikls 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 442 ---AQLEEQLQEVRKKCAEEAQL-------ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:pfam01576 461 kdvSSLESQLQDTQELLQEETRQklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540
|
170 180
....*....|....*....|....*....
gi 755507765 512 EPLQQHLQESQQEISSMQMRLEMKDLETD 540
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
381-536 |
4.52e-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: 41.74 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 381 LQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqkLQAQKQQVQELLGELDEQKAQLEEQLQEvrkkcaeeaq 460
Cdd:pfam16789 30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGT-----TSDKILQMKRYIKVVKERLKQEEKKVQD---------- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755507765 461 lisslkaeitsQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQ-EISSMQMRLEMKD 536
Cdd:pfam16789 95 -----------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQdEIGSALHLANQRK 160
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-532 |
4.65e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqELLGELDE-------QKA 442
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET--------------ELCAEAEEmrarlaaRKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 443 QLEE-----------------QLQEVRKKCAEEAQLISS-----------LKAEITSQESQISSYEEELLKAREELSRLQ 494
Cdd:pfam01576 72 ELEEilhelesrleeeeersqQLQNEKKKMQQHIQDLEEqldeeeaarqkLQLEKVTTEAKIKKLEEDILLLEDQNSKLS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755507765 495 QETAQLEESV---------ESGKAQLEPLQQHLQESQqeISSMQMRL 532
Cdd:pfam01576 152 KERKLLEERIseftsnlaeEEEKAKSLSKLKNKHEAM--ISDLEERL 196
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
434-540 |
4.72e-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: 40.67 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 434 LGELDEQKAQLEEQLQEvrkkcaeeaqlisslkaeitsQESQISSYEEELLKAREELSRLQQ-------ETAQLEESVES 506
Cdd:pfam20492 15 LKQYEEETKKAQEELEE---------------------SEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEM 73
|
90 100 110
....*....|....*....|....*....|....
gi 755507765 507 GKAQLEPLQQHLQESQQEISSMQMRLEMKDLETD 540
Cdd:pfam20492 74 EAEEKEQLEAELAEAQEEIARLEEEVERKEEEAR 107
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
309-608 |
4.89e-04 |
|
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: 43.79 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 309 GCGKLSKDQFALAFHLINQKLIKGiDPPHSLTPEMIPPSDRSSLQKNITGSSPVADFS-AIKELDTLNNEIVDLQ-REKN 386
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGSES-TLLEKAKEIINIEEALKGFQDPESELEDLAQTSdKLEKLVEQNTDLRLEKlGENA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 387 NVEQDLKEKEDTVKqrtSEVQDLQDEVqRESINLQKLQAQKQQVQELLGELdEQKAQLEEQLQEVRKKcaeeaqlISSLK 466
Cdd:COG5185 275 ESSKRLNENANNLI---KQFENTKEKI-AEYTKSIDIKKATESLEEQLAAA-EAEQELEESKRETETG-------IQNLT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 467 AEITSQESQISSYEEELLKARE------ELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEIS-------SMQMRlE 533
Cdd:COG5185 343 AEIEQGQESLTENLEAIKEEIEnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILatledtlKAADR-Q 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755507765 534 MKDLETDNNQSNWSSSPQSVLVNGATDycSLSTSSSETANfnehaEGQNNLESEPTHQESSVRSSPEIAPSDVTD 608
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELIS--ELNKVMREADE-----ESQSRLEEAYDEINRSVRSKKEDLNEELTQ 489
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
369-527 |
5.18e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTVKQRTSEVQDLQDEVQR----------ESINLQKLQAQKQQVQELLG 435
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKA---REELSRLQqetaQLEESVESGKAQLE 512
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLE----RLKEEIEKSSKQRA 656
|
170 180
....*....|....*....|..
gi 755507765 513 PL-------QQHLQESQQEISS 527
Cdd:TIGR00606 657 MLagatavySQFITQLTDENQS 678
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
436-540 |
5.23e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLE------ESVESGKA 509
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEkieryqEDLEELTE 361
|
90 100 110
....*....|....*....|....*....|.
gi 755507765 510 QLEPLQQHLQESQQEISSMQMRLEMKDLETD 540
Cdd:COG3096 362 RLEEQEEVVEEAAEQLAEAEARLEAAEEEVD 392
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
440-544 |
5.37e-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: 42.12 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 440 QKAQLEEQLqevRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVES-----------GK 508
Cdd:pfam06785 66 EKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdfaefrleSE 142
|
90 100 110
....*....|....*....|....*....|....*.
gi 755507765 509 AQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQS 544
Cdd:pfam06785 143 EQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLES 178
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
432-533 |
5.47e-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: 41.15 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLQEVRKkcaeeaqlissLKAEITSQESQIssyeeELLKAReeLSRLQQETAQLEESVESGKAQL 511
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRT-----------LEAEIERLQSKI-----ERLKTQ--LEDLERELALLQAKERQLEKKL 103
|
90 100
....*....|....*....|..
gi 755507765 512 EPLQQHLQESQQEISSMQMRLE 533
Cdd:pfam11559 104 KTLEQKLKNEKEELQRLKNALQ 125
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
476-544 |
5.71e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 5.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507765 476 ISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQS 544
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
380-516 |
6.05e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 40.26 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 380 DLQREKNNVE------QDLKEKEDTVKQRTSEVQDLQdevqresinlqklqaqkqqvqELLGELDEQKAQLEEqlqeVRK 453
Cdd:pfam18595 3 TLAEEKEELAelerkaRELQAKIDALQVVEKDLRSCI---------------------KLLEEIEAELAKLEE----AKK 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755507765 454 KCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQetaQLEESVESGKAQLEPLQQ 516
Cdd:pfam18595 58 KLKELRDALEEKEIELRELERREERLQRQLENAQEKLERLRE---QAEEKREAAQARLEELRE 117
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
370-536 |
6.60e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQ--RESINLQKLQAQKQQVQELLGELDEQKAQLEEQ 447
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 448 LQEVRKKCAEEAQLISS----------LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEfneqskklleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
170 180
....*....|....*....|
gi 755507765 518 LQESQQEISSMQMRLEM-KD 536
Cdd:PHA02562 395 KSELVKEKYHRGIVTDLlKD 414
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
438-533 |
6.83e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 40.74 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEI-TSQESQ---ISSYE---EELLKAREELSRLQQETAQLEESVESGKAQ 510
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaILEAEnskAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100
....*....|....*....|...
gi 755507765 511 LEPLQQHLQESQQEISSMQMRLE 533
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNS 104
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
385-530 |
7.70e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 41.68 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 385 KNNVEQDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqELLGELDEQKAQLEEQLQEVRKkcaEEAQLISS 464
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLKKE 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507765 465 LKA--EIT----SQESQISSYEEELLKAREELSRLQQETaqleesvesgKAQLEPLQQHLQESQQEISSMQM 530
Cdd:pfam14988 70 LQAlrPFAklkeSQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
436-538 |
8.12e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAE---ITSQESQISSYEEELLKAREELSRLQqetAQLEESVESGKAQLE 512
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQleqLRARIKELAARAPAWLAAQDALERLR---EQSGEALADSQEVTA 630
|
90 100
....*....|....*....|....*..
gi 755507765 513 PLQQHL-QESQQEISSMQMRLEMKDLE 538
Cdd:COG3096 631 AMQQLLeREREATVERDELAARKQALE 657
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
436-555 |
8.50e-04 |
|
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: 42.01 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQkaQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLK----AREE-LSRLQQETAQLEESVESgkaq 510
Cdd:pfam14992 9 EKDLQ--RLDEANQVLLLKIQEKEEEIQSLEREITLTRSLAEDEEREELNftimEKEDaLQELELETAKLEKKNEI---- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 755507765 511 lepLQQHLQESQQEISsmqmRLEMKDleTDNNQSNWSSSPQSVLV 555
Cdd:pfam14992 83 ---LVKSVMELQRKLS----RKSDKN--TGLEQETLKQMLEELKV 118
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
366-520 |
8.62e-04 |
|
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: 41.90 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 366 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDE 439
Cdd:pfam12795 48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 440 QKAQLEEQLQ--EVRKKCAEEAQLIsSLKAEITSQESQISSYEEELLKA--REELSRLQQETAQLEesvesgKAQLEPLQ 515
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLLTLR------IQRLEQQL 200
|
....*
gi 755507765 516 QHLQE 520
Cdd:pfam12795 201 QALQE 205
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
446-532 |
9.29e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.82 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 446 EQLQEVRKKCAEEAQLISSL-KAEITSQESQissYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQE 524
Cdd:pfam07111 484 EQLREERNRLDAELQLSAHLiQQEVGRAREQ---GEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEE 560
|
....*...
gi 755507765 525 ISSMQMRL 532
Cdd:pfam07111 561 AASLRQEL 568
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
368-533 |
9.58e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.53 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREK--NNVEQDLKEKEDTVKQRTSEVQDLQDEVQ-----RESinlqklqaqkQQVQELLGELDEQ 440
Cdd:COG3524 160 LAESEELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAFRNRNGildpeATA----------EALLQLIATLEGQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 441 KAQLEEQLQEVRKKCAEEAqlisslkAEITSQESQISSYEEELLKAREELSrlqqeTAQLEESVESGKAQLEPLQQHLQE 520
Cdd:COG3524 230 LAELEAELAALRSYLSPNS-------PQVRQLRRRIAALEKQIAAERARLT-----GASGGDSLASLLAEYERLELEREF 297
|
170
....*....|...
gi 755507765 521 SQQEISSMQMRLE 533
Cdd:COG3524 298 AEKAYTSALAALE 310
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
372-535 |
1.01e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 372 DTLNNEIVDL-QREKnnvEQDLKEKED------------TVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGEL- 437
Cdd:pfam15921 377 DQLQKLLADLhKREK---ELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMEVQR--------------LEALLKAMk 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 DEQKAQLEEQLQEVRKKcAEEAQLISSLKAeitsqesQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:pfam15921 440 SECQGQMERQMAAIQGK-NESLEKVSSLTA-------QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
170
....*....|....*...
gi 755507765 518 LQESQQEISSMQMRLEMK 535
Cdd:pfam15921 512 IEATNAEITKLRSRVDLK 529
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
385-552 |
1.07e-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: 41.20 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 385 KNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEEaqLISS 464
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 465 LKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPL---------QQHLQESQQEI---SSMQMRL 532
Cdd:pfam04012 88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkarlkaakaQEAVQTSLGSLstsSATDSFE 167
|
170 180
....*....|....*....|....
gi 755507765 533 EMK----DLETDNNQSNWSSSPQS 552
Cdd:pfam04012 168 RIEekieEREARADAAAELASAVD 191
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
370-533 |
1.08e-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: 42.57 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 370 ELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQResinlqklqaqkqqVQELLGELDEQKAQLE---E 446
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------------LTQKLTTAHRKEAENEallE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEEL------------------LKAREELSRLQQETAQLEESVESGK 508
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhqarlqaaqltlqladasLALREGRARWAQERETLQQSAEADK 317
|
170 180
....*....|....*....|....*...
gi 755507765 509 AQLEPLQ---QHLQESQQEISSMQMRLE 533
Cdd:pfam07888 318 DRIEKLSaelQRLEERLQEERMEREKLE 345
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
364-646 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 364 DFSAIKELDTLNNeivDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkqqvqellgelDEQKAQ 443
Cdd:PHA02562 161 DISVLSEMDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN--------------------GENIAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 444 LEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQL---EESVESG------KAQLEPL 514
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkvIKMYEKGgvcptcTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 515 QQHLQESQQEISSMQMRLEmkDLETDNNQSNwssspqsVLVNGATDycslsTSSSETANFNEHAEGQNNLESEpTHQESS 594
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLE--KLDTAIDELE-------EIMDEFNE-----QSKKLLELKNKISTNKQSLITL-VDKAKK 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 755507765 595 VRSSPEIAPSDVTDESEAVTVAGNEKVTPRFDDDKHSKEEDPFNVESSSLTD 646
Cdd:PHA02562 363 VKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
376-512 |
1.21e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 376 NEIVDLQREKNNVEQDLKEKEDtVKQRTSEVQDLQDEVQ--RESINLQKlqaqkqqvqELLGELDEQKAQLEEQLQEVRK 453
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEeiHKKIKELA---------EEAQELHEEMIELYKEADELRK 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 454 KcAEEA-QLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLE 512
Cdd:COG1340 210 E-ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
369-535 |
1.26e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEdtvkqrtSEVQDLQDEVQRESINLQKLQAQKQQVQEllgELDEQKAQLEEQL 448
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELE-------AQISELQEDLESERAARNKAEKQRRDLGE---ELEALKTELEDTL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 ------QEVR-KKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQES 521
Cdd:pfam01576 313 dttaaqQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392
|
170
....*....|....
gi 755507765 522 QQEISSMQMRLEMK 535
Cdd:pfam01576 393 LRTLQQAKQDSEHK 406
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
434-525 |
1.32e-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: 40.32 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 434 LGELDEQKAQLEEQL----QEVRKKCAEEAQ-LISSLKAEITSQESQISSYEEELLKA-REELSRLQQE-TAQLEESVES 506
Cdd:pfam01442 6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELQAKlGQNVEELRQRlEPYTEELRKR 85
|
90
....*....|....*....
gi 755507765 507 GKAQLEPLQQHLQESQQEI 525
Cdd:pfam01442 86 LNADAEELQEKLAPYGEEL 104
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
378-540 |
1.45e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 378 IVDLQREK-NNVEQDLKEKEDTVKQR-------TSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKaqlEEQLQ 449
Cdd:pfam05483 262 LLEESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 450 EVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELS----RLQQETAQLEE--------SVE------------ 505
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEmtkfknnkEVEleelkkilaede 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755507765 506 ---SGKAQLEPLQQHLQESQQ-----------EISSMQMRL------------EMKDLETD 540
Cdd:pfam05483 419 kllDEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLtaiktseehylkEVEDLKTE 479
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
376-539 |
1.50e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.89 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 376 NEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESinlqklqaqkQQVQELLGELDEQKAQLEEQLQEVRKKC 455
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA----------EEIQERLEELNQRWEELRELAEERRQRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 456 AEEAQL------ISSLKAEITSQESQISSYE-----EELLKAREELSRLQQETAQLEESVESgkaqLEPLQQHLQESQQE 524
Cdd:cd00176 103 EEALDLqqffrdADDLEQWLEEKEAALASEDlgkdlESVEELLKKHKELEEELEAHEPRLKS----LNELAEELLEEGHP 178
|
170
....*....|....*
gi 755507765 525 ISSMQMRLEMKDLET 539
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 ... |
369-533 |
1.50e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNE----IVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVqresinlqklqaqkqqvQELLGELDEQKAQL 444
Cdd:pfam01576 176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI-----------------AELQAQIAELRAQL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 445 ---EEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLE------PLQ 515
Cdd:pfam01576 239 akkEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQ 318
|
170
....*....|....*....
gi 755507765 516 QHLQ-ESQQEISSMQMRLE 533
Cdd:pfam01576 319 QELRsKREQEVTELKKALE 337
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
364-540 |
1.55e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 364 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTVKQRTSEVQDLQDEVQResinlqkLQAQKQQVQELLGE 436
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQ-------LEEKTKLQDENLKE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDEQKAQLEEQLQEVR----------KKCAEEAQLISSLKAEITSQ-ESQIssyeEELLKAREELSRLQQEtaqLEESVE 505
Cdd:pfam05483 287 LIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAHSFVVTE---FEATTC 359
|
170 180 190
....*....|....*....|....*....|....*
gi 755507765 506 SGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETD 540
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE 394
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-543 |
1.61e-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: 42.36 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 435 GELDEQKAQLEEQLQEVRKKCAEeaqlISSLKAEITSQESQISSYEEELLKAREELSRLQQ--------ETAQLEESVES 506
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIER----LDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellkEKEALERQKEA 241
|
90 100 110
....*....|....*....|....*....|....*....
gi 755507765 507 GKAQLEPLQQHLQESQQEISSMQMRLE--MKDLETDNNQ 543
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEeiEQLLEELNKK 280
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
371-538 |
1.62e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 371 LDTLNNEIVDLQREKNNvEQDLKEKEDTVKQRTSevQDLQDEVQREsinlqklqaqkqqvqELLGELDEQKAQLEEQLQE 450
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLG--KNLDDEDELE---------------QLQEELEARLESLSESVSE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 451 VRKKCAEEAQLISSLKAEITSQESQissyEEELLKAREELSRLQqetAQLEESVESGKAQLEPLQQHL-QESQQEISSMQ 529
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAAR----APAWLAAQDALARLR---EQSGEEFEDSQDVTEYMQQLLeRERELTVERDE 649
|
....*....
gi 755507765 530 MRLEMKDLE 538
Cdd:PRK04863 650 LAARKQALD 658
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
471-543 |
1.74e-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: 41.67 E-value: 1.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755507765 471 SQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQ 543
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
369-554 |
1.84e-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: 41.94 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQdlqdevqresinlqklqaqkqqvqellgELDEQKAQLEEQL 448
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----------------------------ELKEQNEELEKQY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 qEVRKKCAEEAQL----ISSLKAEITSQESQISSYEEELLKAR----EELSRLQQETAQLEESVESGKAQLEPLQQHLQE 520
Cdd:pfam05667 387 -KVKKKTLDLLPDaeenIAKLQALVDASAQRLVELAGQWEKHRvpliEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
170 180 190
....*....|....*....|....*....|....*..
gi 755507765 521 SQQEISS---MQMRLeMKDLETDNNQSNWSSSPQSVL 554
Cdd:pfam05667 466 VAEEAKQkeeLYKQL-VAEYERLPKDVSRSAYTRRIL 501
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
369-532 |
1.85e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 39.90 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQ-RTSEVQDLQDEVQresinlqklqaqkqqvqELLGELDEQKAQLEE- 446
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQEKLEQKEELGEGlTMIDFLQLQIENQ-----------------ALNEKIEERNKELKRl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 ---------QLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESveSG---------- 507
Cdd:pfam13870 69 klkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvpallhd 146
|
170 180
....*....|....*....|....*....
gi 755507765 508 ----KAQLEPLQQHLQESQQEISSMQMRL 532
Cdd:pfam13870 147 ydktKAEVEEKRKSVKKLRRKVKILEMRI 175
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
369-538 |
1.93e-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: 41.38 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTVKQ----RTSEVQ-DL-QDEVQRESINlqklqaqkqqVQELLGE--- 436
Cdd:pfam03148 64 KELEELDEEIELLLEEKRRLEKALEALEeplHIAQEcltlREKRQGiDLvHDEVEKELLK----------EVELIEGiqe 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 -LDEQKAQLEEQL---QEVRKKCA------EEAQLI----------S---SLKAEITSQESQISSYEE-------ELLKA 486
Cdd:pfam03148 134 lLQRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEwekftqdNIERA 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 487 REELsrlqQETAQLEESVESGKAQ--------------------------LEPLQQHLQESQQEISSMQMrlEMKDLE 538
Cdd:pfam03148 214 EKER----AASAQLRELIDSILEQtandlraqadavnfalrkrieetedaKNKLEWQLKKTLQEIAELEK--NIEALE 285
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
372-533 |
2.00e-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: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 372 DTLNNEIVDLQREknnVEQDLKEKEDTVKQRTSEVQ-DLQDEVQresinlqklqaqkqqvqELLGEL----DEQKAQLEE 446
Cdd:pfam01442 29 DRLEKETEALRER---LQKDLEEVRAKLEPYLEELQaKLGQNVE-----------------ELRQRLepytEELRKRLNA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 447 QLQEVRKKCA---EEAQliSSLKAEITSQESQISSYEEEL-LKAREELSRLQQetaQLEESVESGKAQLEPLQQHLQES- 521
Cdd:pfam01442 89 DAEELQEKLApygEELR--ERLEQNVDALRARLAPYAEELrQKLAERLEELKE---SLAPYAEEVQAQLSQRLQELREKl 163
|
170
....*....|..
gi 755507765 522 QQEISSMQMRLE 533
Cdd:pfam01442 164 EPQAEDLREKLD 175
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
365-545 |
2.10e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 365 FSAIKELDT-LNNEIVDLQREKNNVEQDLKEKEDTVKQRTS--EVQDLQD--EVQRESINLQKLQAQKQqVQELL----- 434
Cdd:COG5185 335 ETGIQNLTAeIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKDtiESTKESLDEIPQNQRGY-AQEILatled 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 435 --GELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEIT---------SQESQISSYEEELLKAREELSRLQQETAQLEES 503
Cdd:COG5185 414 tlKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkvmreadeeSQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755507765 504 VESGKAQLEPLQQHLQESQQEISSM--QMRLEMKDLETDNNQSN 545
Cdd:COG5185 494 VSTLKATLEKLRAKLERQLEGVRSKldQVAESLKDFMRARGYAH 537
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
352-497 |
2.38e-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: 40.77 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 352 LQKNITGSspVADFSAIKELDTLNNEIVDLQREKNNVeqdLKEKEDTVKQRTSEVQDL-QDEV--QRESInlqklqaqkq 428
Cdd:smart00787 149 LDENLEGL--KEDYKLLMKELELLNSIKPKLRDRKDA---LEEELRQLKQLEDELEDCdPTELdrAKEKL---------- 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 429 qvQELLGELDEQKAQLEEQLQEVRK---KCAEEAQLISSLKAEITSQES------QISSYEEELLKAReeLSRLQQET 497
Cdd:smart00787 214 --KKLLQEIMIKVKKLEELEEELQElesKIEDLTNKKSELNTEIAEAEKkleqcrGFTFKEIEKLKEQ--LKLLQSLT 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-538 |
2.43e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDtVKQRTSEVQDLQDEVQRESINLQKLQ------------AQKQQVQELLGE 436
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLTPEKLEKEleelekakeeieEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 437 LDEQKAQLEEQLQEVRK---KCA---------EEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETA------ 498
Cdd:PRK03918 417 LKKEIKELKKAIEELKKakgKCPvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseli 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755507765 499 -------QLE-----------ESVESGKAQLEPLQQHLQESQQEISSMQMRLE-MKDLE 538
Cdd:PRK03918 497 klkelaeQLKeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkLEELK 555
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
436-544 |
2.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELS------RLQQETAQLEESVESGKA 509
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEELEE 362
|
90 100 110
....*....|....*....|....*....|....*
gi 755507765 510 QLEPLQQHLQESQQEISSMQMRLEMKDLETDNNQS 544
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS 397
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
369-570 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKKCAEEAQLISSLKAEITS----------QESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 518
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTltqklttahrKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAEL 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 755507765 519 QESQQEISSMQMRLEMKDLETDNNQSNWSSSPQSVLVNGATDYCSLSTSSSE 570
Cdd:pfam07888 275 HQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAE 326
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
369-554 |
2.65e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQL 448
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 QEVRKK---CAEEAQLISSLKAEITSQESQI--------------SSYEEELLKAREELSRLQQETAQLEESVES-GKAQ 510
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYdeiteriaeqeiaySELQEELEEILKQLEEIEKEQEKLSEMLQGlRKDE 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755507765 511 LEpLQQHLQESQQEISSMQMRLEmkdletdnnQSNWSSSPQSVL 554
Cdd:PRK04778 414 LE-AREKLERYRNKLHEIKRYLE---------KSNLPGLPEDYL 447
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
381-591 |
2.65e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 381 LQREKNNVEQDLKEKEDTVKQRTSEVQDLqdEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCAEEAQ 460
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLM 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 461 LISSLKAEITSQESQISSyEEELLKAREELSRLQQETAQLEESVESGKAqlepLQQHLQESQQeissmqmrlemkDLETD 540
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRL-LQTLHSQEIHIRDAHEVATSIREISCQQHT----LTQHIHTLQQ------------QKTTL 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755507765 541 NNQSNWSSSPQSVLVNGAtdycslSTSSSETANFNE------HAEGQNNLESEPTHQ 591
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQ------ATIDTRTSAFRDlqgqlaHAKKQQELQQRYAEL 442
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
432-540 |
2.65e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
90 100 110
....*....|....*....|....*....|..
gi 755507765 512 EPLQQH---LQESQQEISSMQMRLEMKDLETD 540
Cdd:COG1340 102 AELNKAggsIDKLRKEIERLEWRQQTEVLSPE 133
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
380-533 |
2.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 380 DLQREKNNVEQDLK----EKEDT-----VKQRTSEVQDLQDEVQResinlqklqaqkqqvqellgeLDEQKAQLEEQL-- 448
Cdd:PRK02224 180 RVLSDQRGSLDQLKaqieEKEEKdlherLNGLESELAELDEEIER---------------------YEEQREQARETRde 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 449 -QEVRKKCAEEAQLISSLKAEITSQESQISSYE-------EELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQE 520
Cdd:PRK02224 239 aDEVLEEHEERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE 318
|
170
....*....|...
gi 755507765 521 SQQEISSMQMRLE 533
Cdd:PRK02224 319 LEDRDEELRDRLE 331
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
369-544 |
2.79e-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: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLqREKNNVE----QDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGE-------L 437
Cdd:pfam15921 510 RAIEATNAEITKL-RSRVDLKlqelQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaM 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 DEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEE---LLKAREELSR----LQQETAQLEESVESGKAQ 510
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvkLVNAGSERLRavkdIKQERDQLLNEVKTSRNE 668
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 755507765 511 LEPLQQHLQ---------ESQQEISSMQMRLEMKDLETDNNQS 544
Cdd:pfam15921 669 LNSLSEDYEvlkrnfrnkSEEMETTTNKLKMQLKSAQSELEQT 711
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
436-533 |
2.98e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSR-LQQETAQLEESVESGKAQLEPL 514
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeAQQAIKEAKKEADEIIKELRQL 596
|
90 100
....*....|....*....|.
gi 755507765 515 QQHLQESQ--QEISSMQMRLE 533
Cdd:PRK00409 597 QKGGYASVkaHELIEARKRLN 617
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
462-548 |
3.38e-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: 38.39 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 462 ISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVES-----GKA--QLEPLQQHLQESQQEISSMQMRLEM 534
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERelvlhAEDikALQALREELNELKAEIAELKAEAES 82
|
90
....*....|....
gi 755507765 535 KDLETDNNQSNWSS 548
Cdd:pfam07926 83 AKAELEESEESWEE 96
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
429-533 |
3.46e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 429 QVQELLGELDE------QKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEE 502
Cdd:COG3096 513 RLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 755507765 503 SVESGKAQ----------LEPLQQH----LQESQQEISSMQMRLE 533
Cdd:COG3096 593 RIKELAARapawlaaqdaLERLREQsgeaLADSQEVTAAMQQLLE 637
|
|
| End3 |
pfam12761 |
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ... |
359-494 |
3.53e-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: 39.59 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 359 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTVKQRTSEvqdlqdevqresiNLQKLQAQKQQVQELLGELD 438
Cdd:pfam12761 84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGG-------------NRDESSKPALVKREFEQLLD 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 755507765 439 EQKAQLEEQLQEVRKKCAEEaqlISSLKAEITSQESQISSYEEELLKAREELSRLQ 494
Cdd:pfam12761 148 YKERQLRELEEGSGKSKPIN---LKSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
352-531 |
3.66e-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: 40.86 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 352 LQKNITGSSPVADFSAIKELDTlnneivDLQREK-NNVEqdLKEKEDTV----KQRTSEVQDLQDEVQRESINLQKLQAQ 426
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKT------ELEKEKlKNIE--LTAHCDKLllenKELTQEASDMTLELKKHQEDIINCKKQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 427 KQQVQELLGELDEQKAQLEEQLQEVRKkcaEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLeesves 506
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL------ 599
|
170 180
....*....|....*....|....*
gi 755507765 507 gKAQLEPLQQHLQESQQEISSMQMR 531
Cdd:pfam05483 600 -KKQIENKNKNIEELHQENKALKKK 623
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
373-535 |
3.71e-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: 40.96 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 373 TLNNEIVDLQReknNVEQDLKEKEDTVKQRTSEVQDLQDeVQRESINLQKLQAQKQQVQELLG-----ELDEQKAQLEEQ 447
Cdd:pfam10174 551 RTNPEINDRIR---LLEQEVARYKEESGKAQAEVERLLG-ILREVENEKNDKDKKIAELESLTlrqmkEQNKKVANIKHG 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 448 LQEVRKKCAEEAQLISSLKAEIT--SQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEI 525
Cdd:pfam10174 627 QQEMKKKGAQLLEEARRREDNLAdnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEI 706
|
170
....*....|
gi 755507765 526 ssmqmrLEMK 535
Cdd:pfam10174 707 ------LEMK 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
384-661 |
3.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 384 EKNNVEQDLKEKED-TVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQ-KAQLEEQLQEVRKKC------ 455
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKiKAEELKKAEEEKKKVeqlkkk 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 456 -AEEAQLISSLKAE----ITSQESQISSYEEELLKArEELSRLQQETAQLEESV---ESGKAQLEPLQQHLQESQQEISS 527
Cdd:PTZ00121 1642 eAEEKKKAEELKKAeeenKIKAAEEAKKAEEDKKKA-EEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 528 MQMRLEMKDLETDN----NQSNWSSSPQSVLVNGATDYCSLSTSSSETANFNEHAEGQNNLESEPTHQESSVRSSPEIAP 603
Cdd:PTZ00121 1721 LKKAEEENKIKAEEakkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755507765 604 SDVTDESEaVTVAGNEKVTPRFDDDKHskeedpfnVESSSLTDAVADTNLDFFQSDPF 661
Cdd:PTZ00121 1801 KDIFDNFA-NIIEGGKEGNLVINDSKE--------MEDSAIKEVADSKNMQLEEADAF 1849
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
367-549 |
4.09e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 367 AIKELDTLNNEIV-DLQREK---NNVEQ---DLKEKEDTVKqrtSEVQDLQDE--VQREsinlqKLQAQKQQVQELLGEL 437
Cdd:pfam01576 265 KIRELEAQISELQeDLESERaarNKAEKqrrDLGEELEALK---TELEDTLDTtaAQQE-----LRSKREQEVTELKKAL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 438 DEQKAQLEEQLQEVRKKcaeEAQLISSLKAEI-------TSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQ 510
Cdd:pfam01576 337 EEETRSHEAQLQEMRQK---HTQALEELTEQLeqakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ 413
|
170 180 190
....*....|....*....|....*....|....*....
gi 755507765 511 LEPLQQHLQESQQEISSMQMRLEMKDLETDNNQSNWSSS 549
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
473-533 |
4.72e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.48 E-value: 4.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755507765 473 ESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLE 533
Cdd:pfam06005 10 ETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-528 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 377 EIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQEVRKKCA 456
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755507765 457 EEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEP----LQQHLQESQQEISSM 528
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdleeLERELERLEREIEAL 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
371-533 |
4.85e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 371 LDTLNNEIVDLQREKNNVEQDLKEKEdtvkqrtSEVQDLQDEVQresinlqKLQAQKqqvqellGELDEQKAQLEEQLQE 450
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALE-------SENAELQAELR-------TLQQAK-------QDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 451 VRKKC-------AEEAQLISSLKAEITSQESQISSYEEELLKAREELSR-----------LQQETAQ----------LEE 502
Cdd:pfam01576 417 LQARLseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSlesqlqdtqelLQEETRQklnlstrlrqLED 496
|
170 180 190
....*....|....*....|....*....|....*...
gi 755507765 503 SVESGKAQLEP-------LQQHLQESQQEISSMQMRLE 533
Cdd:pfam01576 497 ERNSLQEQLEEeeeakrnVERQLSTLQAQLSDMKKKLE 534
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
390-528 |
5.92e-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: 38.65 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 390 QDLKEKEDTVKQRTSEVQDLQDEVQresinlqklqaqkqqvqellgeldeqkaQLEEQLQEVRKkcaEEAQLISSLKAEI 469
Cdd:pfam06785 83 EGFKILEETLEELQSEEERLEEELS----------------------------QKEEELRRLTE---ENQQLQIQLQQIS 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 755507765 470 TSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSM 528
Cdd:pfam06785 132 QDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
432-533 |
6.10e-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: 39.62 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 432 ELLGELDEQKAQLEEQLQEVRKKCAEEAQLISSLKAEITS---QESQISSYEEELL-KAREELSRLQQE-------TAQL 500
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELdRAKEKLKKLLQEimikvkkLEEL 230
|
90 100 110
....*....|....*....|....*....|...
gi 755507765 501 EESVESGKAQLEPLQQHLQESQQEISSMQMRLE 533
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
368-543 |
6.22e-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: 40.42 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELD----- 438
Cdd:TIGR00606 743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdld 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 439 ---EQKAQLEEQLQEVRKKCAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:TIGR00606 822 rtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
170 180
....*....|....*....|....*...
gi 755507765 516 QHLQESQQEISSMQMRLEmkDLETDNNQ 543
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLE--KDQQEKEE 927
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-538 |
6.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRESINLQKLQAQKQQVQELLGELD---------- 438
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkgeikslk 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 439 -------EQK---AQLEEQLQEVRKKCAEEAQLISSLKAE-ITSQESQISSYEE------ELLKAREELSRLQQETAQLE 501
Cdd:PRK03918 546 kelekleELKkklAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPfyneylELKDAEKELEREEKELKKLE 625
|
170 180 190
....*....|....*....|....*....|....*..
gi 755507765 502 ESVESGKAQLEPLQQHLQESQQEISSMQMRLEMKDLE 538
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
436-523 |
6.86e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 39.42 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 436 ELDEQKAQLEEQLQEVRKKCA--EEAQlisSLKAEITSQesqissYEEELLKAREELSRLQQ-----ETAQLEESVESGK 508
Cdd:pfam17045 43 ELLSARNTLERKHKEIGLLRQqlEELE---KGKQELVAK------YEQQLQKLQEELSKLKRsyeklQRKQLKEAREEAK 113
|
90 100
....*....|....*....|.
gi 755507765 509 AQ------LEPLQQHLQESQQ 523
Cdd:pfam17045 114 SReedrseLSRLNGKLEEFRQ 134
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
369-516 |
6.99e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 369 KELDTLNNEIVDLQREKNNVEQDLKEKEDTVKqRTSEVQDLQ-----DEVQR-ESInlqklqaqkqqvQELLGELDEQKA 442
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLAAQLDAAF-RQGEHTGLQlilsgEESQRgERI------------LAYFGYLNQARQ 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507765 443 QLEEQLQEVRKKCAEEAQLISSLKAE----ITSQESQissyEEELLKAREElsrlQQET-AQLEESVESGKAQLEPLQQ 516
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQqktlLYEQQAQ----QQKLEQARNE----RKKTlTGLESSLQKDQQQLSELRA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
327-593 |
7.06e-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: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 327 QKLIKGIDPPHSLTPEMIPPSDRSSLQKNITGSSPVAdfsaIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTV---- 399
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifll 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 400 KQRTSEVQDLqdEVQRESINLQKLqaqkqqvqELLGELDEQKAQLE-EQLQ--EVRKKCAEEAQLISSLKAEITSQESQI 476
Cdd:pfam05483 446 QAREKEIHDL--EIQLTAIKTSEE--------HYLKEVEDLKTELEkEKLKniELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 477 SSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSmqmrlemkdlETDNNQSNWSSSPQSVLVN 556
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC----------KLDKSEENARSIEYEVLKK 585
|
250 260 270
....*....|....*....|....*....|....*..
gi 755507765 557 GAtdycSLSTSSSETANFNEHAEGQNNlESEPTHQES 593
Cdd:pfam05483 586 EK----QMKILENKCNNLKKQIENKNK-NIEELHQEN 617
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-522 |
7.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 386 NNVEQDL---KEKEDTVKQRTSEVQDLQdEVQREsinlqklqaqkqqvqelLGELDEQKAQLEEQLQEVRkkcaeeAQLI 462
Cdd:PRK04863 283 VHLEEALelrRELYTSRRQLAAEQYRLV-EMARE-----------------LAELNEAESDLEQDYQAAS------DHLN 338
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755507765 463 SSLKAEItsQESQISSYEEELLK--------------AREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQ 522
Cdd:PRK04863 339 LVQTALR--QQEKIERYQADLEEleerleeqnevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ 410
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
374-519 |
7.67e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 39.30 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 374 LNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQ---DEVQRESINLQKLQAQKQQVQELLGELDEQKAQLEEQLQE 450
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507765 451 vrkkcaeEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQQETAQ---LEESVESGKAQLEPLQQHLQ 519
Cdd:pfam15294 211 -------STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAyrnMKEMLTKKNEQIKELRKRLS 275
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
368-494 |
8.02e-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: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 368 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTVKQRTSEVQDLQDEVQRES-------INLQKLQAQKQQVQELLGELDEQ 440
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggISRESLVTAGALVAQAQANLLAT 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 755507765 441 KAQLEEQLQEVRkkcAEEAQLISSLKAEITSQESQISSYEEELLKAREELSRLQ 494
Cdd:pfam00529 161 VAQLDQIYVQIT---QSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
143-189 |
9.05e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 35.22 E-value: 9.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755507765 143 DGFLSGDKVKPVL--LNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAM 189
Cdd:cd00051 14 DGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
362-523 |
9.05e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 38.21 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 362 VADFSAIKEldTLNNEIVDLQREKNNVEQDLKEKEdtvkqRTSEVQDLQdevqresinlqklqaqkqqvqellgeldeQK 441
Cdd:pfam14988 73 LRPFAKLKE--SQEREIQDLEEEKEKVRAETAEKD-----REAHLQFLK-----------------------------EK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 442 AQLEEQLQE---------VRKKCAEEAQLISSLKAEITSQESQISSYEEELLkaREELSRLQQETAQLEEsvesGKAQLE 512
Cdd:pfam14988 117 ALLEKQLQElrilelgerATRELKRKAQALKLAAKQALSEFCRSIKRENRQL--QKELLQLIQETQALEA----IKSKLE 190
|
170
....*....|.
gi 755507765 513 PLQQHLQESQQ 523
Cdd:pfam14988 191 NRKQRLKEEQW 201
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
389-543 |
9.25e-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: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 389 EQDLKEKEDTVKQrtseVQDLQDEVQREsinlqklqaqkqqvqelLGELD-------EQKAQLEEQLQEVRKKCAEEAQL 461
Cdd:pfam01576 4 EEEMQAKEEELQK----VKERQQKAESE-----------------LKELEkkhqqlcEEKNALQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507765 462 ISSLKA------EI-TSQESQISSYEEELLKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQESQQEISSMQMRLEM 534
Cdd:pfam01576 63 RARLAArkqeleEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILL 142
|
....*....
gi 755507765 535 kdLETDNNQ 543
Cdd:pfam01576 143 --LEDQNSK 149
|
|
| |
