|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-832 |
1.40e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 517 NIQR---IIQE-NERLKQeiLEKSSRIKEQNDKISELIERNQRYVEQSNLmmekrnNSLQTATENTQARVLHAEQEKAKV 592
Cdd:COG1196 187 NLERledILGElERQLEP--LERQAEKAERYRELKEELKELEAELLLLKL------RELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELR 672
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 673 VTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLL-KKARVSTDQAAAEQLSLVQAE 751
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 752 LQTQWEAKCEQLLASAKnEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 831
Cdd:COG1196 419 LEEELEELEEALAELEE-EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
.
gi 1387290472 832 D 832
Cdd:COG1196 498 E 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
529-844 |
2.14e-17 |
|
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: 88.19 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 529 KQEILEKSSRIKEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLH 607
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 608 LKMTAHQKKETELQVQLTEsmketdlLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEK 687
Cdd:TIGR02168 754 KELTELEAEIEELEERLEE-------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 688 ESLEKNLsERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKArvstdQAAAEQLSLVQAELQTQWEAKCEQL--LA 765
Cdd:TIGR02168 827 ESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 766 SAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ-NAQHIKDLES-KAQTSGVEATAADPSEKVKKIMNQ 843
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENK 980
|
.
gi 1387290472 844 V 844
Cdd:TIGR02168 981 I 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
514-755 |
1.79e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARvLHAEQEKAKVT 593
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL-AELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKET----DLLRGQLAQLQAELSEVQETSQQVQSKLKSE---KQSR 666
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaeEELEELAEELLEALRAAAELAAQLEELEEAEealLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 667 RQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERcQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 746
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*....
gi 1387290472 747 LVQAELQTQ 755
Cdd:COG1196 496 LLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-799 |
2.50e-15 |
|
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: 81.26 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 517 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 596
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 597 AAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSL 676
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 677 EEELTDLRTEKESLEKNLSE----RKKKSAQ------ERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 746
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290472 747 LVQAELQ-TQWEAKCEQLLASAKNEH-------LQQYQEVCTQRDASQQQLLQLEEKCSAL 799
Cdd:TIGR02168 924 LAQLELRlEGLEVRIDNLQERLSEEYsltleeaEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
484-850 |
2.53e-15 |
|
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: 81.27 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 484 LMTKVEELQKHSagNSLLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLM 563
Cdd:TIGR02169 693 LQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 564 MEKRNNsLQTATENTQARVLHA-----EQEKAKVTEELAAATAQVSHLHLKMtahqKKETELQVQLTESMKEtdlLRGQL 638
Cdd:TIGR02169 771 EEDLHK-LEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKL----NRLTLEKEYLEKEIQE---LQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 639 AQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKsaqeRCQAEEEIDEIRKs 718
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRK- 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 719 HQEELDKLRQLLKKARVSTDQAAAEQLSLVQAE-----LQTQWEAKCEQL--LASAKNEHLQQYQEVctqrdasQQQLLQ 791
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledVQAELQRVEEEIraLEPVNMLAIQEYEEV-------LKRLDE 990
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 792 LEEKCSALQAQVTSLREQnaqhIKDLESKAQTSGVEATaadpsEKVKKIMNQVFQFLRG 850
Cdd:TIGR02169 991 LKEKRAKLEEERKAILER----IEEYEKKKREVFMEAF-----EAINENFNEIFAELSG 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
518-814 |
3.86e-15 |
|
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: 80.87 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 518 IQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELA 597
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL--------QKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 598 AATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLE 677
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 678 EELTDLRTEKESLEknlsERKKKSAQERCQAEEEIDEIRKS-HQEELDKLRQLLKKArVSTDQAAAEQLSLVQAELqtqw 756
Cdd:TIGR02168 400 NEIERLEARLERLE----DRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEEL-QEELERLEEALEELREEL---- 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 757 eAKCEQLLASAKNEhLQQYQevctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHI 814
Cdd:TIGR02168 471 -EEAEQALDAAERE-LAQLQ----ARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
574-818 |
8.78e-15 |
|
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: 79.72 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 574 ATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQ 653
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 654 QVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKK--SAQERCQA-EEEIDEIRKSHQEELDKLRQLL 730
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieQLKEELKAlREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 731 KKARVSTDQAAA-------------------EQLSLVQAELQTQWEAKCEQL--LASAKNEHLQQYQEVCTQRDASQQQL 789
Cdd:TIGR02168 824 ERLESLERRIAAterrledleeqieelsediESLAAEIEELEELIEELESELeaLLNERASLEEALALLRSELEELSEEL 903
|
250 260
....*....|....*....|....*....
gi 1387290472 790 LQLEEKCSALQAQVTSLREQNAQHIKDLE 818
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE 932
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
514-818 |
9.47e-15 |
|
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: 79.29 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILEkssrIKEQNDKISELIERNQryveqsnlmmeKRNNSLQTATENTQARVLHAEQEKAKVT 593
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQ-----------QEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKKETELQVQLTE--SMKETDLLRgqlaQLQAELSEVQETSQQVQSKLKSEKQSRRQLEL 671
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnNQKEQDWNK----ELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 672 RVTSLEEELTDLRTEKESLEKNLSERKKksaqercqaeeEIDEIRKSHQEELDKLRQLLKKARvstdqaAAEQLSLVQAE 751
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQN-----------EIEKLKKENQSYKQEIKNLESQIN------DLESKIQNQEK 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 752 LQTQWEAKCEQlLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL---REQNAQHIKDLE 818
Cdd:TIGR04523 406 LNQQKDEQIKK-LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntRESLETQLKVLS 474
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
510-820 |
3.18e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 510 ETSMIMSNIQRIIQENERLKQEILEKSSRI---KEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLhaE 586
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLnqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDL--N 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 587 QEKAKVTeelaaataqVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSR 666
Cdd:TIGR04523 302 NQKEQDW---------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 667 RQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQErcqaEEEIDEIRKSHqEELDKLRQLLKKARVS--------TD 738
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEK-ELLEKEIERLKETIIKnnseikdlTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 739 QAAAEQLSLVQAE-LQTQWEAKCEQLLASAKNEHlQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNA---QHI 814
Cdd:TIGR04523 448 QDSVKELIIKNLDnTRESLETQLKVLSRSINKIK-QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISslkEKI 526
|
....*.
gi 1387290472 815 KDLESK 820
Cdd:TIGR04523 527 EKLESE 532
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
460-883 |
4.45e-12 |
|
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: 70.52 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 460 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 534
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 535 KSSRIKE----QNDKISELIERNQRYVEQSNLMMEKRN-----NSLQtATENTQARVLHAEQEKAKVTEELAAATAQVSH 605
Cdd:pfam05483 389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQfekiaEELK-GKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 606 LHLKMTAHQKKETELQ-VQLTESMKETDLLRGQLAQLQAELSE-VQETSQQVQSKLKSEKQSRRQLElRVTSLEEELTDL 683
Cdd:pfam05483 468 HYLKEVEDLKTELEKEkLKNIELTAHCDKLLLENKELTQEASDmTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 684 RTEKESLEKnlsERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLK--------KARVSTDQAAAEQLSLVQAELQTQ 755
Cdd:pfam05483 547 RDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnlKKQIENKNKNIEELHQENKALKKK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 756 WEAKCEQL-------------LASAKN---EHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLReqnaqhiKDLES 819
Cdd:pfam05483 624 GSAENKQLnayeikvnkleleLASAKQkfeEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ-------KEIDK 696
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 820 KAQTSGVEATAAdpSEKVKKIMNQVFQFLRGEFEL-----EEFYSGRTVLGTIMNTIKMVTLRLLNQHE 883
Cdd:pfam05483 697 RCQHKIAEMVAL--MEKHKHQYDKIIEERDSELGLyknkeQEQSSAKAALEIELSNIKAELLSLKKQLE 763
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
623-822 |
1.25e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 623 QLTESMKEtdLLRGQLAQLQAELSEVQETSQQVQsKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSE-RKKKS 701
Cdd:COG4717 50 RLEKEADE--LFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 702 AQERCQAEEEIDEIRKSHQEELDKLRQllkkaRVSTDQAAAEQLSLVQAELQtQWEAKCEQLLASAKNEHLQQYQEVCTQ 781
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEE-----RLEELRELEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387290472 782 RDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQ 822
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
520-832 |
1.65e-11 |
|
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: 69.05 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 520 RIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARvLHAEQEKAKVTEELAAA 599
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAK-RKLEGESTDLQEQIAEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 600 TAQVSHLHLKMtahQKKETELQVQLTESMKETdllrGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEE 679
Cdd:pfam01576 228 QAQIAELRAQL---AKKEEELQAALARLEEET----AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 680 LTDLRTEKESL--------------EKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVS------TDQ 739
Cdd:pfam01576 301 LEALKTELEDTldttaaqqelrskrEQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNkanlekAKQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 740 AAAEQLSLVQAELQTQWEAKCEQLLASAKNEhlQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLreqnAQHIKDLES 819
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLE--GQLQELQARLSESERQRAELAEKLSKLQSELESV----SSLLNEAEG 454
|
330
....*....|...
gi 1387290472 820 KAQTSGVEATAAD 832
Cdd:pfam01576 455 KNIKLSKDVSSLE 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
488-751 |
3.47e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 488 VEELQKHSAGNSLLIPSMSVTMEtsmimSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKR 567
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 568 NNSLQTATE---NTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAE 644
Cdd:TIGR02169 321 EERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 645 LSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLserkKKSAQERCQAEEEIDEIRKSH---QE 721
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI----KKQEWKLEQLAADLSKYEQELydlKE 476
|
250 260 270
....*....|....*....|....*....|
gi 1387290472 722 ELDKLRQLLKKARVSTDQAAAEQLSLVQAE 751
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
612-812 |
3.77e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 612 AHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLE 691
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 692 KNLSERKKKSAQ---------------------------ERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTdQAAAEQ 744
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAEL-EAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 745 LSLVQAELQTQweakcEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQ 812
Cdd:COG4942 176 LEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
523-856 |
4.53e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 523 QEN-ERLkQEILEKssrIKEQNDKISELIERNQRYVEQSNlmmEKRNNSLQTATentqARVLHAEQEKAKVTEELAAAta 601
Cdd:TIGR02168 185 RENlDRL-EDILNE---LERQLKSLERQAEKAERYKELKA---ELRELELALLV----LRLEELREELEELQEELKEA-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 602 qvshlhlkmtahQKKETELQVQLTEsmketdlLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELT 681
Cdd:TIGR02168 252 ------------EEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 682 DLRTEKESLEKNL--SERKKKSAQERCQA-EEEIDEIrkshQEELDKLRQLLKKARvstdqAAAEQLSLVQAELQTQWEA 758
Cdd:TIGR02168 313 NLERQLEELEAQLeeLESKLDELAEELAElEEKLEEL----KEELESLEAELEELE-----AELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 759 kceqlLASAKNEHLQqyqevctQRDASQQQLLQLEEKCSALQAQvtslREQNAQHIKDLESKAQTSGVEATAADPSEKVK 838
Cdd:TIGR02168 384 -----LRSKVAQLEL-------QIASLNNEIERLEARLERLEDR----RERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
330
....*....|....*...
gi 1387290472 839 KIMNQVFQFLRGEFELEE 856
Cdd:TIGR02168 448 ELEELQEELERLEEALEE 465
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
522-872 |
6.69e-11 |
|
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: 66.52 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 522 IQENERLKQEILEKSSRIKEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARVLHAEQE--KAKV 592
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAataqvshlhlkmtahQKKETELQVQLTESMKETDllrGQLAQLQAELSEVQETSQQVQSKLKSEKqSRRQLELR 672
Cdd:COG5185 311 TESLEE---------------QLAAAEAEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEI-ENIVGEVE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 673 VTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLvQAEL 752
Cdd:COG5185 372 LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNEL-ISEL 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 753 QTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQA-----------QVTSLREQNAQHIKDLESKA 821
Cdd:COG5185 451 NKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAtleklraklerQLEGVRSKLDQVAESLKDFM 530
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1387290472 822 QTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEFYSGRTVLGTIMNTIK 872
Cdd:COG5185 531 RARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIE 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
577-816 |
1.05e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 577 NTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLR-------------------GQ 637
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiaeleaelerldassDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 638 LAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCqAEEEIDEIRK 717
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-AAALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 718 SHQEELDKLRQLLKKARvstdQAAAEQLSLVQAELQTQWEAKCEQLLASAknEHLQQYQEVCTQRDAS-----QQQLLQL 792
Cdd:COG4913 766 ELRENLEERIDALRARL----NRAEEELERAMRAFNREWPAETADLDADL--ESLPEYLALLDRLEEDglpeyEERFKEL 839
|
250 260
....*....|....*....|....*..
gi 1387290472 793 EEKCSalQAQVTSLR---EQNAQHIKD 816
Cdd:COG4913 840 LNENS--IEFVADLLsklRRAIREIKE 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
519-819 |
3.14e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 519 QRIIQENERLK------QEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 592
Cdd:COG4717 139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAATAQVSHLHLKMTAHQKKETELQ--------------VQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSK 658
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEarlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 659 LKSEKQSRRQLELRVTSLE-EELTDLRTE---KESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEE--LDKLRQLLKK 732
Cdd:COG4717 299 SLGKEAEELQALPALEELEeEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 733 ARVSTDQAAAEQLSLVQA--ELQTQWEAKCEQLLASAKNEH----LQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL 806
Cdd:COG4717 379 AGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEelleALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
330
....*....|...
gi 1387290472 807 ReqnaQHIKDLES 819
Cdd:COG4717 459 E----AELEQLEE 467
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
520-753 |
3.52e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 520 RIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAA 599
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDK----LQEELEQLREELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 600 TAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEE 679
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290472 680 LTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 753
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
518-820 |
4.15e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 518 IQRIIQENER---LKQEILEKSSRIKEQNDKISELIE---------------RNQRYVEQSNLMMEKRNNSLQTATENTQ 579
Cdd:TIGR04523 67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeqKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 580 ARVLHA--------------------------EQEKAKVTEELAAATAQVSHLHLKMTAHQKKE---TELQVQLTESMKE 630
Cdd:TIGR04523 147 IKKKEKeleklnnkyndlkkqkeelenelnllEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 631 TDLLRGQLAQLQAELSEVQETSQQVQSKLK-------------SEKQSR--------RQLELRVTSLEEELTDLRTEKES 689
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnkikkqlSEKQKEleqnnkkiKELEKQLNQLKSEISDLNNQKEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 690 -LEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLK--KARVSTDQAAAEQLSLVQAELQT---QWEAKCEQL 763
Cdd:TIGR04523 307 dWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKelTNSESENSEKQRELEEKQNEIEKlkkENQSYKQEI 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290472 764 --LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ---NAQHIKDLESK 820
Cdd:TIGR04523 387 knLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiikNNSEIKDLTNQ 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
615-831 |
5.16e-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: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 615 KKETELQvqLtESMKE-----TDL---LRGQLAQLQAElSEVQETSQQVQSKLKsekqsRRQLELRV----------TSL 676
Cdd:COG1196 174 KEEAERK--L-EATEEnlerlEDIlgeLERQLEPLERQ-AEKAERYRELKEELK-----ELEAELLLlklreleaelEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 677 EEELTDLRTEKESLEKNLSERKKKSAQERCQ---AEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 753
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 754 -TQWEAKCEQLLASAKnEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 831
Cdd:COG1196 325 lAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
526-839 |
7.32e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 526 ERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMME--KRNNSLQTATENTQARVLHAEQEKAKvTEELAAATAQV 603
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 604 SHLHLKMTAHQKKETElqVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRvtSLEEEltdl 683
Cdd:PTZ00121 1547 KADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEA---- 1618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 684 RTEKESLEKNLSERKKKSAQERCQAEE--EIDEIRKSHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAELQTQWEA--- 758
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEAlkk 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 759 ------KCEQLLASA-----KNEHLQQYQEVcTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVE 827
Cdd:PTZ00121 1697 eaeeakKAEELKKKEaeekkKAEELKKAEEE-NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
330
....*....|..
gi 1387290472 828 ATAADPSEKVKK 839
Cdd:PTZ00121 1776 EKEAVIEEELDE 1787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
514-752 |
9.73e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKqEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVT 593
Cdd:COG4913 223 TFEAADALVEHFDDLE-RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESmketDLlrGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRV 673
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGN----GG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 674 TSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLlkKARVST----DQAA----AEQL 745
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--ERRKSNiparLLALrdalAEAL 453
|
....*..
gi 1387290472 746 SLVQAEL 752
Cdd:COG4913 454 GLDEAEL 460
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
623-828 |
9.90e-10 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 63.01 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 623 QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSE-KQSRRQLELRvtSLEEELTDLRTEKESLEKNLSERKK-- 699
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtRETLSTLSLR--QLESRLAQTLDQLQNAQNDLAEYNSql 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 700 ---KSAQERCQAeeEIDEirksHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQtQWEAKCE---QLLASakNEHLQ 773
Cdd:PRK11281 152 vslQTQPERAQA--ALYA----NSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQA-LLNAQNDlqrKSLEG--NTQLQ 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290472 774 Q-YQEvctQRDASQQQLLQLEEKCSALQAQVTSLR-EQNAQHIKDLESKAQTSGVEA 828
Cdd:PRK11281 223 DlLQK---QRDYLTARIQRLEHQLQLLQEAINSKRlTLSEKTVQEAQSQDEAARIQA 276
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
526-817 |
2.31e-09 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 60.85 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 526 ERLKQEILEKSSRIKEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 602
Cdd:pfam15742 5 EKLKYQQQEEVQQLRQNLQRLQILctsAEKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 603 VSHLHLKMtahqkKETELQV-QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRrqlelrvtsleeeLT 681
Cdd:pfam15742 85 WKHCQQKI-----RELELEVlKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVC-------------LT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 682 DLRT-EKESLEKNLSERKKKSAQERCQAEEEiDEIRK---SHQEELDKLRQLLKKARVSTDQAAAEQLSLVQaelqtQWE 757
Cdd:pfam15742 147 DTCIlEKKQLEERIKEASENEAKLKQQYQEE-QQKRKlldQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQ-----QQE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290472 758 AKCEQLLA--SAKNEHLQQYQEvctqrdasqqqllqLEEKCSALQAQVTSLREQNAQHIKDL 817
Cdd:pfam15742 221 AQLKQLENekRKSDEHLKSNQE--------------LSEKLSSLQQEKEALQEELQQVLKQL 268
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
637-809 |
4.64e-09 |
|
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: 58.43 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 637 QLAQLQAELsevQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKEsleknlSERKKKSAQeRCQAEEEIDEIR 716
Cdd:pfam15397 64 QLQQAKAEL---QEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQ-IANLVRQLQQLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 717 KSHQEELDKLRQLLKKarvstdqaaaeqlslVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLL------ 790
Cdd:pfam15397 134 DSQQDELDELEEMRRM---------------VLESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVMLkeieqf 198
|
170 180
....*....|....*....|....
gi 1387290472 791 -----QLEEKCSALQAQVTSLREQ 809
Cdd:pfam15397 199 refidELEEEIPKLKAEVQQLQAQ 222
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
529-821 |
6.16e-09 |
|
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: 60.74 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 529 KQEILEKSSRIKEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATENtQARVLHAEQEKAKVTEELAAATAQVSHLHL 608
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 609 kmtahQKKETELQVQLTEsmKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQL---ELRVTSLEEELTDLRT 685
Cdd:COG3096 376 -----QLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 686 EKESLEKNLSERKKK---SAQERCQAEEEIDEIRK-----SHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAELqtqwe 757
Cdd:COG3096 449 KEQQATEEVLELEQKlsvADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYR--SQQALAQRLQQLRAQL----- 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 758 AKCEQLLASAKN--EHLQQYQ-----------EVCTQRDASQQQLLQLEEKCSALQAQVTSLR---EQNAQHIKDLESKA 821
Cdd:COG3096 522 AELEQRLRQQQNaeRLLEEFCqrigqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRqqlEQLRARIKELAARA 601
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
587-767 |
7.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 587 QEKAKVTEELAAATAQVSHLH--LKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQvqskLKSEKQ 664
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEeeLEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE----LEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 665 SRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQllKKARVSTDQAAAEQ 744
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--ELEELEEELEQLEN 234
|
170 180
....*....|....*....|...
gi 1387290472 745 LSLVQAELQTQWEAKCEQLLASA 767
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAA 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
516-732 |
1.24e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 516 SNIQRIIQENErlkQEILEKSSRIKEQNDKISELIERnQRYVEQSNLMMEKRNNSLqtatENTQARVLHAEQEKAKVTEE 595
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 596 LAAATAQVSHLHLKMTAHQKKETELQvQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLElrvtS 675
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----E 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 676 LEEELTDLRTEKESLEKNLSE---------------------RKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKK 732
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEEleerhelyeeakakkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
585-783 |
1.62e-08 |
|
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: 56.47 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 585 AEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKseKQ 664
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK--KY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 665 SRRQLELR----VTSLEEELTDLRTEKESLEKNLSErkkksAQERcqaEEEIDEIRKSHQEELDKLRQLLKKARVSTDQA 740
Cdd:COG1579 79 EEQLGNVRnnkeYEALQKEIESLKRRISDLEDEILE-----LMER---IEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387290472 741 AAEqlslVQAELQTQwEAKCEQLLASAKNEHLQQYQEVCTQRD 783
Cdd:COG1579 151 LAE----LEAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
516-820 |
1.71e-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: 58.88 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 516 SNIQRIIQENERLKQEILEKSSRIKEQNDKISEliernqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEE 595
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQN--------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 596 LAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELseVQETSQQvqSKLKSEKQsrrQLELRVTS 675
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL--KSKEKEL--KKLNEEKK---ELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 676 LEEELTDLRTEKESLEKNLSERKKKSAqercQAEEEIDEIrkshqeELDKLRQLLKKARVSTDQaAAEQLSLVQAELqtq 755
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKIS----DLEDELNKD------DFELKKENLEKEIDEKNK-EIEELKQTQKSL--- 580
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 756 wEAKCEQllasaKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQN---AQHIKDLESK 820
Cdd:TIGR04523 581 -KKKQEE-----KQELIDQKEK---EKKDLIKEIEEKEKKISSLEKELEKAKKENeklSSIIKNIKSK 639
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
606-811 |
1.83e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 57.24 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 606 LHLKMTAHQKKETELQVQLtESMKETDL--LRGQL-------AQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSL 676
Cdd:pfam00038 30 LETKISELRQKKGAEPSRL-YSLYEKEIedLRRQLdtltverARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 677 EEELTDLRTEKESLEKnlserkkksaqeRCQA-EEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQA--ELQ 753
Cdd:pfam00038 109 RKDLDEATLARVDLEA------------KIESlKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEIR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387290472 754 TQWEAKCEQLLASAKNEHLQQYQEVCTQRD-------ASQQQLLQLEEKCSALQAQVTSLREQNA 811
Cdd:pfam00038 177 AQYEEIAAKNREEAEEWYQSKLEELQQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
514-746 |
1.86e-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: 57.85 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVlhaEQEKAKVT 593
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKketelqvQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRV 673
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387290472 674 TSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEiRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 746
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
594-819 |
1.88e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLhLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELseVQETSQQVQSKLKSEKQSRRQLELRV 673
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 674 TSLEEELTDLRtekESLEKNLSERKKKSAQERCQAEEEIDEIrkshQEELDKLRQLLKKARVSTDQAAAEQLSLVQ--AE 751
Cdd:COG4913 319 DALREELDELE---AQIRGNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEEFAALRAeaAA 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 752 LQTQWEAKcEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLES 819
Cdd:COG4913 392 LLEALEEE-LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
519-823 |
2.28e-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: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 519 QRIIQENE--RLKQEILEKssriKEQNDKISELIERNQRYVEQSNlmmeKRNNSLQTATENTQARVLHAEQEKAKVTEEL 596
Cdd:TIGR04523 118 QKNKLEVElnKLEKQKKEN----KKNIDKFLTEIKKKEKELEKLN----NKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 597 AAATAQVSHLHLKMTAHQKKE---TELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLK------------- 660
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnkikkql 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 661 SEKQSR--------RQLELRVTSLEEELTDLRTEKES-LEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLK 731
Cdd:TIGR04523 270 SEKQKEleqnnkkiKELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 732 KARVSTDQaaaeqlslvQAELQTQWEAKcEQLLASAKNEHlQQYQevctqrdasqQQLLQLEEKCSALQAQVTSLREQNA 811
Cdd:TIGR04523 350 ELTNSESE---------NSEKQRELEEK-QNEIEKLKKEN-QSYK----------QEIKNLESQINDLESKIQNQEKLNQ 408
|
330
....*....|....*
gi 1387290472 812 Q---HIKDLESKAQT 823
Cdd:TIGR04523 409 QkdeQIKKLQQEKEL 423
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
526-837 |
2.63e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 526 ERLKQEILEKSS-----RIKEQNDKISELIERNQRYVEQSNLMMEKRNN--SLQTATENTQARVLHAEQEKAKVTEELAA 598
Cdd:PRK02224 190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEadEVLEEHEERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 599 ATAQVSHLHLKMTAHQKKETELQVQLTESMKETDL-------LRGQLAQLQAELSEVQETSQQVQ-------SKLKSEKQ 664
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRvaaqahnEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 665 SRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAqercQAEEEIDEIRKSHQ---EELDKLRQLLKKARvSTDQAA 741
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIE----ELEEEIEELRERFGdapVDLGNAEDFLEELR-EERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 742 AEQLSLVQAELQTQWE--AKCEQLLASAKNEHLQQYQE----VCTQRDASQQ------QLLQLEEKCSALQAQVTSLRE- 808
Cdd:PRK02224 425 REREAELEATLRTARErvEEAEALLEAGKCPECGQPVEgsphVETIEEDRERveeleaELEDLEEEVEEVEERLERAEDl 504
|
330 340 350
....*....|....*....|....*....|....*
gi 1387290472 809 -QNAQHIKDLESKAQTSG-----VEATAADPSEKV 837
Cdd:PRK02224 505 vEAEDRIERLEERREDLEeliaeRRETIEEKRERA 539
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
565-732 |
3.13e-08 |
|
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: 55.70 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 565 EKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMtahQKKETELQVqltesmketdlLRGQLAQLQAE 644
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEIEE-----------VEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 645 LSEV--QETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEE 722
Cdd:COG1579 82 LGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 1387290472 723 LDKLRQLLKK 732
Cdd:COG1579 162 EAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
576-795 |
3.39e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 576 ENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKE--TELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQ 653
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 654 QVQSKLKSEKQSRRQL--ELRVTSLEEELTDLRTEKESLEKNLSERkkksAQERCQAEEEIDEIRKSHQEELDKLRQLLK 731
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290472 732 KARvstdQAAAEQLSLVQAELQTQweakcEQLLASAkNEHLQQYQEVCTQRDASQQQLLQLEEK 795
Cdd:COG3206 320 AEL----EALQAREASLQAQLAQL-----EARLAEL-PELEAELRRLEREVEVARELYESLLQR 373
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
515-757 |
3.56e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.88 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 515 MSNIQRIIQENERL-KQEILEKSSRIKEQNDKISELIE---RNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKA 590
Cdd:pfam01576 329 VTELKKALEEETRShEAQLQEMRQKHTQALEELTEQLEqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 591 KvteelaaATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQ-------LQAELSEVQETSQQVQSKLKSEK 663
Cdd:pfam01576 409 K-------LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegknikLSKDVSSLESQLQDTQELLQEET 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 664 QSRRQLELRVTSLEEELTDLRTEKE--------------SLEKNLSERKKKsAQERCQAEEEIDEIRKSHQEELDKLRQL 729
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEeeeeakrnverqlsTLQAQLSDMKKK-LEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
250 260
....*....|....*....|....*...
gi 1387290472 730 LKKarvstDQAAAEQLSLVQAELQTQWE 757
Cdd:pfam01576 561 LEE-----KAAAYDKLEKTKNRLQQELD 583
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
517-800 |
4.06e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.61 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 517 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERN-----QRYVEQSNLMMEKRNNSLQTATENTQarvlhaeqekak 591
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ------------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 592 vtEELAAATAQVSHLHLK-------MTAHQKKETELQVQLTESMKETDLLRG-QLAQLQAELS------EVQETSQQVQS 657
Cdd:PRK11281 142 --NDLAEYNSQLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 658 KLKSEKQSRRQL-ELRVTSLEEELTDLRTEkesleknLSERKKKSAQERCQAEEEIDEIRKSH-----QEELDKLRQLLK 731
Cdd:PRK11281 220 QLQDLLQKQRDYlTARIQRLEHQLQLLQEA-------INSKRLTLSEKTVQEAQSQDEAARIQanplvAQELEINLQLSQ 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290472 732 KARVSTDQAAaeqlSLVQAELQTqweakceqllasaKN--EHLQQyqevcTQRDasqqqllqLEEKCSALQ 800
Cdd:PRK11281 293 RLLKATEKLN----TLTQQNLRV-------------KNwlDRLTQ-----SERN--------IKEQISVLK 333
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
522-844 |
6.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 522 IQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEqsnlmMEKRNNSLQTATEN--TQARVLHAEQEKAKVTEELAAA 599
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-----LEAELEELREELEKleKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 600 TAQVSHLHLKMTAHQKKET----------ELQVQLTESMKETDL-LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQ 668
Cdd:COG4717 145 PERLEELEERLEELRELEEeleeleaelaELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 669 LELRVTSLEEELTDLRtEKESLEKN-------------------------------------------LSERKKKSAQER 705
Cdd:COG4717 225 LEEELEQLENELEAAA-LEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 706 CQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQA--ELQTQW------------EAKCEQLLASAKNEH 771
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqELLREAeeleeelqleelEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290472 772 LQQYQEVCTQrdasQQQLLQLEEKCSALQAQVTSL---REQNAQHIKDLESKAQTSGVEATAADPSEKVKKIMNQV 844
Cdd:COG4717 384 EEELRAALEQ----AEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
637-839 |
1.21e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 637 QLAQLQAELSEVQETSQQVQSKLKSEKQSRRqlelrvtSLEEELTDLRTEKESLEKNLSERKKKSAQERCQ---AEEEID 713
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEK-------ALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 714 EIRKSHQEELDKLRQLLKKA----RVST--------------------------DQAAAEQLSLVQAELQTQWEAKCEQL 763
Cdd:COG4942 94 ELRAELEAQKEELAELLRALyrlgRQPPlalllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 764 --LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLrEQNAQHIKDLESKAQTSGVEATAADPSEKVKK 839
Cdd:COG4942 174 aeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
419-857 |
1.22e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 419 AYAYPQAPAVASQLQPVRPLYPAPLSQPPHFQGSGDVASFLMTEARqHNTEIRmavsKVADKMDHLMTKVEELQKHSAGN 498
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK-VVEGIL----KDTELTKLKESAKAKESGLRKGV 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 499 SLLIPSMSVTmETSMIMSNIQRIIQENERL--KQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE 576
Cdd:pfam02463 653 SLEEGLAEKS-EVKASLSELTKELLEIQELqeKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 577 NTQARVLHAEQEKAKVTEELAAATAQvshlhlkmtahqKKETELQVQLTESMKETDLlrgqlaqlqaelsEVQETSQQVQ 656
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRL------------KKEEKEEEKSELSLKEKEL-------------AEEREKTEKL 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 657 SKlksekqsRRQLELRVTSLEEELtdlrTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVS 736
Cdd:pfam02463 787 KV-------EEEKEEKLKAQEEEL----RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEE 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 737 TDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYQEvctqrdASQQQLLQLEEKCSALQAQVTSLREQNAQHI-- 814
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKEEAei 929
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1387290472 815 --KDLESKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEF 857
Cdd:pfam02463 930 llKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
592-851 |
1.27e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.53 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 592 VTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLEL 671
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 672 RVTSLEEELTDLRTEKESLEKNLSERKKKsaqercqaEEEIDEIRKSHQ-------------EELDKLRQLLKKARVSTD 738
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKL--------RKEIERLEWRQQtevlspeeekelvEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 739 Q--------AAAEQLSLVQAELQTQWEAKCEQLlasakNEHLQQYQEVCTQRDA--------------SQQQLLQLEEKC 796
Cdd:COG1340 158 KneklkelrAELKELRKEAEEIHKKIKELAEEA-----QELHEEMIELYKEADElrkeadelhkeiveAQEKADELHEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1387290472 797 SALQAQVTSLREQnaqhIKDLESKAQTSGVEATAADPSEKVKKIMNqvfQFLRGE 851
Cdd:COG1340 233 IELQKELRELRKE----LKKLRKKQRALKREKEKEELEEKAEEIFE---KLKKGE 280
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
591-858 |
2.13e-07 |
|
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: 55.36 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 591 KVTEELAAATAQVSHLHLKMTAhQKKETELQVQLTESMKET-----DLLRGQLAQLQAELSEVQETSQQVQSKLKS--EK 663
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAEL-LTLRSQLLTLCTPCMPDTyherkQVLEKELKHLREALQQTQQSHAYLTQKREAqeEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 664 QSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSA-QERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAA 742
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 743 EQLSL-VQAELQTQWEAKCeqllasaknEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQnaqhIKDLESKA 821
Cdd:TIGR00618 336 QQSSIeEQRRLLQTLHSQE---------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK----LQSLCKEL 402
|
250 260 270
....*....|....*....|....*....|....*..
gi 1387290472 822 QTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEFY 858
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
653-822 |
2.39e-07 |
|
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: 53.00 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 653 QQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQercqAEEEIDEIRkshqEELDKLRQLLKK 732
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVE----ARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 733 ARvstdqaAAEQLSLVQAELQTQweakceQLLASAKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQ 812
Cdd:COG1579 85 VR------NNKEYEALQKEIESL------KRRISDLEDEILELME---RIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170
....*....|
gi 1387290472 813 HIKDLESKAQ 822
Cdd:COG1579 150 ELAELEAELE 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
574-761 |
3.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 574 ATENTQARVLHAEQEKAKVTEELAAATAQVSHL--HLKMTAHQKKETE-LQVQLTESMKETDLLRGQLAQLQAELSEVQE 650
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELreELEKLEKEVKELEeLKEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 651 TSQQVQSKLKS-EKQSRRQLELR-------------------VTSLEEELTDLRTEKESLEKNLSERKKKSAQ------E 704
Cdd:PRK03918 267 RIEELKKEIEElEEKVKELKELKekaeeyiklsefyeeyldeLREIEKRLSRLEEEINGIEERIKELEEKEERleelkkK 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290472 705 RCQAEEEIDEIRKSHqEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCE 761
Cdd:PRK03918 347 LKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
515-852 |
3.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 515 MSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENT-------QARVLH 584
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELekrLEELEERHELYEEAKAKKEELERLKKRLTgltpeklEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 585 AEQEKAKVTEELAAATAQVSHL------------HLK------------MTAHQKKE--TELQVQLTESMKETDLLRGQL 638
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELkkeikelkkaieELKkakgkcpvcgreLTEEHRKEllEEYTAELKRIEKELKEIEEKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 639 AQLQAELSEVQ-------------ETSQQV-----------------------------------QSKLKSEKQSRRQLE 670
Cdd:PRK03918 476 RKLRKELRELEkvlkkeseliklkELAEQLkeleeklkkynleelekkaeeyeklkekliklkgeIKSLKKELEKLEELK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 671 LRVTSLEEELTDLRTEKESLEKNLSERKKKSAQErcqAEEEIDEIRKSHQE---------ELDKLRQLLKKARVSTDQAA 741
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAF 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 742 AEqLSLVQAELQtQWEAKCEQLLASAKNEhlqQYQEVctqrdasQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLES-K 820
Cdd:PRK03918 633 EE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKTLEKlK 700
|
410 420 430
....*....|....*....|....*....|..
gi 1387290472 821 AQTSGVEaTAADPSEKVKKIMNQVfQFLRGEF 852
Cdd:PRK03918 701 EELEERE-KAKKELEKLEKALERV-EELREKV 730
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
525-731 |
4.94e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 525 NErLKQEIlEKSSRIKEQNDKISELIERNQRYVEQ-----------------SNLMMEKRNNSLQTATENTQAR---VLH 584
Cdd:TIGR01612 1486 NE-LKEHI-DKSKGCKDEADKNAKAIEKNKELFEQykkdvtellnkysalaiKNKFAKTKKDSEIIIKEIKDAHkkfILE 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 585 AEQEKAKVTE--------ELAAATAQVSH-----LHLKMTAHQKKE---TELQVQLTESMKETDLLRGQLAQL-----QA 643
Cdd:TIGR01612 1564 AEKSEQKIKEikkekfriEDDAAKNDKSNkaaidIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFsidsqDT 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 644 ELSEVQETSQQVQSKLKSEKQSRRQLELRVTsleeELTDLRTEKESLEKNLSERKKKSaqeRCQAEEEIDEIRKSHQEEL 723
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLKDQKKNIEDKKK----ELDELDSEIEKIEIDVDQHKKNY---EIGIIEKIKEIAIANKEEI 1716
|
....*...
gi 1387290472 724 DKLRQLLK 731
Cdd:TIGR01612 1717 ESIKELIE 1724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
529-822 |
6.62e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 529 KQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHL-H 607
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELqH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 608 LKMTA----HQKKETE-LQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQ-SKLKSEKQ-SRRQLEL--------- 671
Cdd:pfam15921 536 LKNEGdhlrNVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELqefkilkdk 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 672 ---RVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQE--ELDKLRQLLKKarvsTDQAAAEQLS 746
Cdd:pfam15921 616 kdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNElnSLSEDYEVLKR----NFRNKSEEME 691
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290472 747 LVQAELQTQweakceqlLASAKNEhLQQYQEVCTQRDASQQQLLQLeekCSALQAQVTSLREQnaqhIKDLESKAQ 822
Cdd:pfam15921 692 TTTNKLKMQ--------LKSAQSE-LEQTRNTLKSMEGSDGHAMKV---AMGMQKQITAKRGQ----IDALQSKIQ 751
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
594-831 |
9.12e-07 |
|
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: 53.42 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQ---------------LQAELSEVQETSQQVQSK 658
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQanlladetladrleeLREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 659 -------------LKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDK 725
Cdd:COG3096 916 gkalaqleplvavLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNEKLRARLEQ 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 726 LRQLLKKARVSTDQAAAE--QLSLVQAELQTQWEAKCEQLlasakNEHLQQYQEVCTQRDAS------------QQQLLQ 791
Cdd:COG3096 996 AEEARREAREQLRQAQAQysQYNQVLASLKSSRDAKQQTL-----QELEQELEELGVQADAEaeerarirrdelHEELSQ 1070
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387290472 792 LEEKCSALQAQVTSLR---EQNAQHIKDLESKAQTSGVEATAA 831
Cdd:COG3096 1071 NRSRRSQLEKQLTRCEaemDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
524-932 |
1.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKR--NNSLQTATENTQARVLHAEQEKAKVTEEL---AA 598
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAkkkAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 599 ATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKqsRRQLELRVTsleE 678
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKA---E 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 679 ELtdlrteKESLEKNLSERKKKSAQERCQAE---EEIDEIRKSHQEELDKLRQLLKKARvsTDQAAAEQLSLVQAE--LQ 753
Cdd:PTZ00121 1556 EL------KKAEEKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMK--AEEAKKAEEAKIKAEelKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 754 TQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNaqhiKDLESKAQTSGVEATAADP 833
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE----EDEKKAAEALKKEAEEAKK 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 834 SEKVKKIMNQVFQflrgefELEEFYSGRTVlgtimNTIKMVTLRLLNQHEQEKGESSNEEEEEEDEAQARSPSGQSQAPL 913
Cdd:PTZ00121 1704 AEELKKKEAEEKK------KAEELKKAEEE-----NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
410
....*....|....*....
gi 1387290472 914 DRESQgpPAVLSEWVVQED 932
Cdd:PTZ00121 1773 IRKEK--EAVIEEELDEED 1789
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
535-856 |
1.07e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 535 KSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHq 614
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 615 KKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRrqlelrvtSLEEELtDLRTEKESLEKNL 694
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK--------KLQEEE-LKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 695 SERKKKsaqercQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEqLSLVQAELQTQWEAKCEQLLASAKNEHLQQ 774
Cdd:pfam02463 301 ELLKLE------RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-LKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 775 yqevctQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAADPSEKVKKIMNQVFQ-FLRGEFE 853
Cdd:pfam02463 374 ------ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIeLKQGKLT 447
|
...
gi 1387290472 854 LEE 856
Cdd:pfam02463 448 EEK 450
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
565-714 |
1.11e-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: 51.08 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 565 EKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTE--SMKETDLLRGQLAQLQ 642
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290472 643 AELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDE 714
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
524-839 |
1.20e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvTEELAAATAQV 603
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 604 SHL---------------HLKMTAHQKKETELQVQLTESMKETDLLR--GQLAQLQAELSEVQETSQQVQSKLKSEKQSR 666
Cdd:PTZ00121 1391 KKAdeakkkaeedkkkadELKKAAAAKKKADEAKKKAEEKKKADEAKkkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 667 RQLELRVTSLE----EELT----DLRTEKESLEKNLSERKK----KSAQERCQAEE--EIDEIRKShqEELDKLRQLLKK 732
Cdd:PTZ00121 1471 KADEAKKKAEEakkaDEAKkkaeEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEakKAEEAKKA--DEAKKAEEKKKA 1548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 733 ARVSTdqaaAEQLSLVQAELQTQWEAKCEQ--LLASAKNEHLQQYQEvctQRDASQQQLLQLEEKCSALQAQVTSLREQN 810
Cdd:PTZ00121 1549 DELKK----AEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
330 340
....*....|....*....|....*....
gi 1387290472 811 AQHIKDLESKAQTsgVEATAADPSEKVKK 839
Cdd:PTZ00121 1622 AEELKKAEEEKKK--VEQLKKKEAEEKKK 1648
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
611-818 |
1.49e-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: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 611 TAHQKKETELQVQLTESmkETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESL 690
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 691 EKNLSERKKKSAQERCQAEEEIDEIRKSHQEelDKLRQLLKKArvstdQAAAEQLSLVQAELqtqweAKCEQLLASAKNE 770
Cdd:COG1579 79 EEQLGNVRNNKEYEALQKEIESLKRRISDLE--DEILELMERI-----EELEEELAELEAEL-----AELEAELEEKKAE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387290472 771 hlqqyqevctqrdasqqqllqLEEKCSALQAQVTSLREQNAQHIKDLE 818
Cdd:COG1579 147 ---------------------LDEELAELEAELEELEAEREELAAKIP 173
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
612-812 |
1.76e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 50.38 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 612 AHQKKETELQVQLTESMKETDLLRGQLAQLQAelsevqetSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLE 691
Cdd:pfam12795 34 ASKQRAAAYQKALDDAPAELRELRQELAALQA--------KAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 692 KNLSERKKKSAQercqAEEEIDEIRKshqeELDKLRQLLKKARVSTDQAAAEQLSLVQAELQtqweakceqlLASAKNEH 771
Cdd:pfam12795 106 SQLIELQTRPER----AQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQAELA----------ALKAQIDM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387290472 772 LQQYQEVCT--------QRDASQQQLLQLEEKCSALQAQVTSLREQNAQ 812
Cdd:pfam12795 168 LEQELLSNNnrqdllkaRRDLLTLRIQRLEQQLQALQELLNEKRLQEAE 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
594-831 |
1.81e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRG---------------QLAQLQAELSEVQETSQQVQ-- 656
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRllprlnlladetladRVEEIREQLDEAEEAKRFVQqh 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 657 -----------SKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDK 725
Cdd:PRK04863 917 gnalaqlepivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 726 LRQLLKKARVSTDQAAAE--QLSLVQAELQTQWEAKcEQLLASAKNEhLQQY---------QEVCTQRDASQQQLLQLEE 794
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQlaQYNQVLASLKSSYDAK-RQMLQELKQE-LQDLgvpadsgaeERARARRDELHARLSANRS 1074
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1387290472 795 KCSALQAQVTS----LREQNAQhIKDLESKAQTSGVEATAA 831
Cdd:PRK04863 1075 RRNQLEKQLTFceaeMDNLTKK-LRKLERDYHEMREQVVNA 1114
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
506-768 |
2.19e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 506 SVTMETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA 585
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 586 EQEKAKVtEELAAATAQVSHLHLKMTAHQKKETELQ----VQLTESM---KETDLLRgQLAQLQAELSEVQEtSQQVQSK 658
Cdd:COG1340 85 EKLNELR-EELDELRKELAELNKAGGSIDKLRKEIErlewRQQTEVLspeEEKELVE-KIKELEKELEKAKK-ALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 659 LKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEE----------EIDEIRKSH---QEELDK 725
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhkeiveaqeKADELHEEIielQKELRE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387290472 726 LRQLLKKARvstDQAAAEQLSLVQAELQTQWEAKCEQLLASAK 768
Cdd:COG1340 242 LRKELKKLR---KKQRALKREKEKEELEEKAEEIFEKLKKGEK 281
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
515-759 |
2.38e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 515 MSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENTQArvlhAEQEKAK 591
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 592 VTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQ-----QVQSKLKSEKQSR 666
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 667 RQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 746
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|...
gi 1387290472 747 LVQAELQTQWEAK 759
Cdd:COG4372 273 TEEEELEIAALEL 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
524-839 |
2.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILE-KSSRIKEQNDKISELIERNQ--RYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvTEELAAAT 600
Cdd:PTZ00121 1221 EDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK-ADEAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 601 AQVSHLHLKMTAHQKKET-ELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRvTSLEEE 679
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKAdEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKK 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 680 LTDLRTEKESLEKNLSERKKKSAQERCQAEE-EIDEIRKSHQEELDKLRQLLKKARvSTDQAAAEQLSLVQAELQTQWEA 758
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAK 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 759 KCEQLLASA----KNEHLQQYQEvcTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGV-EATAADP 833
Cdd:PTZ00121 1458 KAEEAKKKAeeakKADEAKKKAE--EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKK 1535
|
....*.
gi 1387290472 834 SEKVKK 839
Cdd:PTZ00121 1536 ADEAKK 1541
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
642-852 |
2.83e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 642 QAELSEVQETSQQVQSKLKSEKQSRRQLELrvtsLE--EELTDLRTEkesLEKNLSERKKK-SAQERC--QAEEEIDEir 716
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEAL----LEakEEIHKLRNE---FEKELRERRNElQKLEKRllQKEENLDR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 717 ksHQEELDKLRQLLKKARvstdqaaaEQLSLVQAELQTQwEAKCEQLLAsaknEHLQQYQEVC--TQRDASQQQLLQLEE 794
Cdd:PRK12704 101 --KLELLEKREEELEKKE--------KELEQKQQELEKK-EEELEELIE----EQLQELERISglTAEEAKEILLEKVEE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 795 KcsalqaqvtsLREQNAQHIKDLESKAqtsgvEATAadpSEKVKKIMNQVFQFLRGEF 852
Cdd:PRK12704 166 E----------ARHEAAVLIKEIEEEA-----KEEA---DKKAKEILAQAIQRCAADH 205
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
570-823 |
3.34e-06 |
|
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: 51.18 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 570 SLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLK----MTAHQKKET---ELQVQLTESMKETDLLRGQLAQLQ 642
Cdd:pfam05667 255 QLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLtkgsRFTHTEKLQftnEAPAATSSPPTKVETEEELQQQRE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 643 AELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLsERKKKSAQERCQAEEEIdeirkshqee 722
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY-KVKKKTLDLLPDAEENI---------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 723 lDKLRQLLkkarvstdQAAAEQLslvqAELQTQWEAKCEQLLasaknEHLQQYQEVCT-QRDASQQQLLQLEEkcsalqa 801
Cdd:pfam05667 404 -AKLQALV--------DASAQRL----VELAGQWEKHRVPLI-----EEYRALKEAKSnKEDESQRKLEEIKE------- 458
|
250 260
....*....|....*....|..
gi 1387290472 802 qvtsLREQnaqhIKDLESKAQT 823
Cdd:pfam05667 459 ----LREK----IKEVAEEAKQ 472
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
510-818 |
3.40e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 510 ETSMIMSNIQRI---IQENERLKQEILEKSSrikeQNDKISELIERNQRYVeqSNLMMEKRNNslqtATENTQaRVLHAE 586
Cdd:PRK04863 224 ENSGVRKAFQDMeaaLRENRMTLEAIRVTQS----DRDLFKHLITESTNYV--AADYMRHANE----RRVHLE-EALELR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 587 QEKAKVTEELAAAtaqvshlhlkmtahqkketelQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLK-SEKQS 665
Cdd:PRK04863 293 RELYTSRRQLAAE---------------------QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRqQEKIE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 666 RRQLELrvtsleEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKS---HQEELDKLR----------QLLKK 732
Cdd:PRK04863 352 RYQADL------EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQALDVQQtraiqyqqavQALER 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 733 ARVSTDQA--AAEQLSLVQAELQTQWEAKCEQLLA---------SAKNEHLQQYQEVC-----TQRDASQQQLLQLEEKC 796
Cdd:PRK04863 426 AKQLCGLPdlTADNAEDWLEEFQAKEQEATEELLSleqklsvaqAAHSQFEQAYQLVRkiageVSRSEAWDVARELLRRL 505
|
330 340
....*....|....*....|..
gi 1387290472 797 SALQAQVTSLrEQNAQHIKDLE 818
Cdd:PRK04863 506 REQRHLAEQL-QQLRMRLSELE 526
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
609-754 |
3.49e-06 |
|
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: 49.13 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 609 KMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQvQSKlksEKQSRRQLELRVTSLEEELTDLRTEKE 688
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEK---DKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290472 689 SLEknlsERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKaRVstdQAAAEQLSLVQAELQT 754
Cdd:pfam13851 110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
620-824 |
3.51e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 620 LQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEkqsrrQLELRVTSLEEELTDLRTEKESLEKNLSErkk 699
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAE--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 700 ksaqercqAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQW----------EAKCEQLLASAKN 769
Cdd:COG3206 238 --------AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialRAQIAALRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387290472 770 EHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQhIKDLESKAQTS 824
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVA 363
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
514-697 |
4.74e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL----------IERNQRYVEQSNLMMEKRNNSLQTATENtqarvl 583
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteledlekeIKRLELEIEEVEARIKKYEEQLGNVRNN------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 584 haeqekakvtEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQEtsqqvqsklksek 663
Cdd:COG1579 89 ----------KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA------------- 145
|
170 180 190
....*....|....*....|....*....|....
gi 1387290472 664 qsrrQLELRVTSLEEELTDLRTEKESLEKNLSER 697
Cdd:COG1579 146 ----ELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
460-739 |
4.77e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 460 MTEARQHNTEIRMAVSKVA---------------DKMDHLMTKVEELQKH-----SAGNSLL--------IPSMSVTMET 511
Cdd:TIGR01612 1331 LLDAQKHNSDINLYLNEIAniynilklnkikkiiDEVKEYTKEIEENNKNikdelDKSEKLIkkikddinLEECKSKIES 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 512 SMIMSNIQRIIQENERLKQEILEKSSRI-------KEQNDKISELIERNQRYVEQSNLMME-KRNNSlqTATENTQARVL 583
Cdd:TIGR01612 1411 TLDDKDIDECIKKIKELKNHILSEESNIdtyfknaDENNENVLLLFKNIEMADNKSQHILKiKKDNA--TNDHDFNINEL 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 584 HAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKET----------ELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQ 653
Cdd:TIGR01612 1489 KEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVtellnkysalAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 654 QVQSKLKSEK---------------------QSRRQLE---LRVTSLEEELTDLRTEKESLEKNLS-------ERKKKSA 702
Cdd:TIGR01612 1569 QKIKEIKKEKfrieddaakndksnkaaidiqLSLENFEnkfLKISDIKKKINDCLKETESIEKKISsfsidsqDTELKEN 1648
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1387290472 703 QERCQAEEEIDEIRKSHQE-------ELDKLRQLLKKARVSTDQ 739
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKKniedkkkELDELDSEIEKIEIDVDQ 1692
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
258-446 |
4.85e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 50.92 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 258 SAAPSPIPPADSISADPVVSPSTSVPFRSGESalrsksnSLSEHLTVNTNPDTVKAKLISRMAKMgQPMLPILPPqldsn 337
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQS-------TAAPHTLIQQTPTLHPQRLPSPHPPL-QPMTQPPPP----- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 338 dseiedvnaPRGAGQPLATPSVQPSLQP-AHPVlpqmtsqapQPSVSRLQTPSAAlmQVASLDSHSAVSGNAQSFQPYAG 416
Cdd:pfam03154 259 ---------SQVSPQPLPQPSLHGQMPPmPHSL---------QTGPSHMQHPVPP--QPFPLTPQSSQSQVPPGPSPAAP 318
|
170 180 190
....*....|....*....|....*....|....*
gi 1387290472 417 VQAYAYPQAPAVASQLQP-----VRPLYPAPLSQP 446
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSqqpprEQPLPPAPLSMP 353
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
527-794 |
5.37e-06 |
|
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: 49.81 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 527 RLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAataqvshl 606
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 607 hlkmtahqkketeLQVQLTESMKETDLLRGQLAQ------LQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEL 680
Cdd:pfam15905 127 -------------LEKQLLELTRVNELLKAKFSEdgtqkkMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 681 TDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQ--EELDKLRQLLKKARVSTDQAAAEQLSLVQA------EL 752
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCvsEQVEKYKLDIAQLEELLKEKNDEIESLKQSleekeqEL 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1387290472 753 QTQWE---AKCeQLLASAKNEHLQQYQEVCTQRDASQQQL---LQLEE 794
Cdd:pfam15905 274 SKQIKdlnEKC-KLLESEKEELLREYEEKEQTLNAELEELkekLTLEE 320
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
601-773 |
6.61e-06 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 50.24 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 601 AQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRvtsLEEEl 680
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR---LKAE- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 681 tdlRTEKESLEKNLSERKKKSAQERCQAEE----------EIDEIRKSHQEELD-KLRQLLKKARVSTDQAAaeQLSLVQ 749
Cdd:pfam09726 478 ---QEARASAEKQLAEEKKRKKEEEATAARavalaaasrgECTESLKQRKRELEsEIKKLTHDIKLKEEQIR--ELEIKV 552
|
170 180 190
....*....|....*....|....*....|.
gi 1387290472 750 AELQTQWE-AKCEQLLASA------KNEHLQ 773
Cdd:pfam09726 553 QELRKYKEsEKDTEVLMSAlsamqdKNQHLE 583
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
514-689 |
6.85e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQ-ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE-NTQARVLHAEQEKAK 591
Cdd:COG5022 940 IDLEEGPSIEyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElSKQYGALQESTKQLK 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 592 VTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQaelseVQETSQQVQSKLKSEKQSRRQLEL 671
Cdd:COG5022 1020 ELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALK-----LRRENSLLDDKQLYQLESTENLLK 1094
|
170
....*....|....*...
gi 1387290472 672 RVTSLEEELTDLRTEKES 689
Cdd:COG5022 1095 TINVKDLEVTNRNLVKPA 1112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
448-853 |
7.04e-06 |
|
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: 50.50 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 448 HFQGSGDVASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEE-----LQKHSagnsllipsmsvtmetsmimSNIQRII 522
Cdd:pfam15921 214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQ--------------------DRIEQLI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 523 QENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELaaataq 602
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL------ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 603 vshlhlkmtahQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQL-------ELRVTS 675
Cdd:pfam15921 348 -----------EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnSITIDH 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 676 LEEELTDLRTEKESLEKNLserkkKSAQERCQAEEEideirkshqeeldklRQLlkkARVSTDQAAAEQLSLVQAELQTQ 755
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALL-----KAMKSECQGQME---------------RQM---AAIQGKNESLEKVSSLTAQLEST 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 756 WE---AKCEQLlaSAKNEHLQQYQEVCTQRDASQQqllQLEEKCSALQAQVTSLRE------QNAQHIKDLESKAQTSGV 826
Cdd:pfam15921 474 KEmlrKVVEEL--TAKKMTLESSERTVSDLTASLQ---EKERAIEATNAEITKLRSrvdlklQELQHLKNEGDHLRNVQT 548
|
410 420
....*....|....*....|....*..
gi 1387290472 827 EATAADPSEKVKkimNQVFQFLRGEFE 853
Cdd:pfam15921 549 ECEALKLQMAEK---DKVIEILRQQIE 572
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
462-761 |
8.41e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 462 EARQHNTEIRMAVSKVADKMDHLMTKVEELQK-----HSAGNSLLIPSMSVTMETSM-IMSNIQRIIQENERLKQEILEK 535
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEKELKEIEEK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 536 SSRIKEQNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARVLHAEQEKA-KVTEELAAATAQVSHLHLKMtahq 614
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKEL---- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 615 KKETELQVQLTESMKETDLLRGQLAQLQAELSE-----VQETSQQVQ----------------SKLKSEKQSRRQLELRV 673
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKelepfyneylelkdaeKELEREEKELKKLEEEL 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 674 TSLEEELTDLRTEKESLEKNLSERKKKSaqercqAEEEIDEIRKSHQE---ELDKLRQLLKKARVSTDQAAAEqLSLVQA 750
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKY------SEEEYEELREEYLElsrELAGLRAELEELEKRREEIKKT-LEKLKE 701
|
330
....*....|.
gi 1387290472 751 ELQTQWEAKCE 761
Cdd:PRK03918 702 ELEEREKAKKE 712
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
512-816 |
1.09e-05 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 48.83 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 512 SMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKR----NNSLQTAT-ENTqarVLHAE 586
Cdd:pfam14915 2 CMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTvfqyNGQLNVLKaENT---MLNSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 587 QEKAKVTEELAAATAQVSHLHLKMTAH-----QKKETELQVQLTESMKETDLLRGQLAqlqAELSEVQETSQQVQSKLkS 661
Cdd:pfam14915 79 LENEKQNKERLETEVESYRSRLAAAIQdheqsQTSKRDLELAFQRERDEWLRLQDKMN---FDVSNLRDENEILSQQL-S 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 662 EKQSRrqlelrVTSLEEELTDLR---TEK----ESLEKNLSerkkksaqercQAEEEIDEIRKSHQEELDKLRQLLKKar 734
Cdd:pfam14915 155 KAESK------ANSLENELHRTRdalREKtlllESVQRDLS-----------QAQCQKKELEHMYQNEQDKVNKYIGK-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 735 vstDQAAAEQLSLVQAE---LQTQWEAKCEQLLASAK---NEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLRE 808
Cdd:pfam14915 216 ---QESLEERLAQLQSEnmlLRQQLEDAQNKADAKEKtviDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKE 292
|
....*...
gi 1387290472 809 QNAQHIKD 816
Cdd:pfam14915 293 RLYQYEKE 300
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
390-744 |
2.07e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 390 AALMQVASLDSHSAVSGNAQSFQPYAG-----VQAYAYPQAPAVASQLQPVRPLYPAPLSQPPHFQGSGDVASFLMT--- 461
Cdd:PLN02939 1 AAAAESAALLSHGCGPIRSRAPFYLPSrrrlaVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENtsl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 462 ------------EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMETSMIMSN---------IQR 520
Cdd:PLN02939 81 rtvmelpqkstsSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNqarlqaledLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 521 IIQENERLKQEILEKSSRIKEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAT 600
Cdd:PLN02939 161 ILTEKEALQGKINILEMRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 601 AQVSHLHLKMTahQKKETELQVQLTEsmKETDLLRGQLAQLQAELSEVQETSQQVqSKLKSEK----------------- 663
Cdd:PLN02939 240 DDIQFLKAELI--EVAETEERVFKLE--KERSLLDASLRELESKFIVAQEDVSKL-SPLQYDCwwekvenlqdlldratn 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 664 ---------QSRRQLELRVTSLEEELTDLRTEKESLEK-NLSERKKKSAQERCQA-EEEIDEIRKSHQEELDKLRQLLKK 732
Cdd:PLN02939 315 qvekaalvlDQNQDLRDKVDKLEASLKEANVSKFSSYKvELLQQKLKLLEERLQAsDHEIHSYIQLYQESIKEFQDTLSK 394
|
410
....*....|..
gi 1387290472 733 ARVSTDQAAAEQ 744
Cdd:PLN02939 395 LKEESKKRSLEH 406
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
349-442 |
2.15e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 48.93 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 349 GAGQPLATPSVQPSLQPAHPVLPQMTSQ------APQPSVSRLQTPSAALMQVASLDSHSAVSGN-AQSFQPYAGVQAYA 421
Cdd:PRK10263 739 GPHEPLFTPIVEPVQQPQQPVAPQQQYQqpqqpvAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQYQ 818
|
90 100
....*....|....*....|...
gi 1387290472 422 YPQAPAVASQ--LQPVRPLYPAP 442
Cdd:PRK10263 819 QPQQPVAPQPqyQQPQQPVAPQP 841
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
481-744 |
2.20e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 481 MDHLMTKVEELQKHSAGNSLL--IPSMSVtmetsmimsnIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVE 558
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLlvVPRAEL----------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 559 QSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQvQLTESMKETDLLRgql 638
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 639 aqlQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKS 718
Cdd:pfam07888 149 ---ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA 225
|
250 260
....*....|....*....|....*.
gi 1387290472 719 HQEELDkLRQLLKKARVSTDQAAAEQ 744
Cdd:pfam07888 226 HRKEAE-NEALLEELRSLQERLNASE 250
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
484-856 |
2.22e-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: 48.81 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 484 LMTKVEELQKHSAGNSLLIPSMSVTMETSMIMSNIQRIIQenerLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLM 563
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ----IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 564 MEKRN---------NSLQTATENTQARVLHAEQEKAkVTEELAAATAQVSHLHLKMTAHQK---KETELQVQLTESMKET 631
Cdd:TIGR00618 341 EEQRRllqtlhsqeIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKeldILQREQATIDTRTSAF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 632 DLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELtDLRTEKESLEKNLSERKKKSAQERCQAEEE 711
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 712 IDEIRKSHQEELDKLRQLLKKARVS-TDQAAAEQLSLVQAELQTQWEAKCEQLlaSAKNEHLQQYQEVCTQRDASQQQLL 790
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDIDNPgPLTRRMQRGEQTYAQLETSEEDVYHQL--TSERKQRASLKEQMQEIQQSFSILT 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290472 791 QLEEKCSALQAQVTSLrEQNAQHIKDLESKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEE 856
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNI-TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
523-809 |
2.47e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 523 QENERLKQEILEKSSRIKEQNDKISELIERnqryVEQSNLMMEKRNNSLQTATENTQarvlhaeqekakvtEELAAATAQ 602
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQ--------------ELLQEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 603 VSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTD 682
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 683 LRTEKESLEKnlserkkksAQERCQaeEEIDEIrkshQEELDKLRQL---LKKARVSTDQAAAEQ--LSLVQAELQTQWE 757
Cdd:pfam01576 564 KAAAYDKLEK---------TKNRLQ--QELDDL----LVDLDHQRQLvsnLEKKQKKFDQMLAEEkaISARYAEERDRAE 628
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290472 758 AKCEQ------LLASAKNEHLQQYQEV--------------CTQRDASQQQLLQLEEKCSALQAQVTSLREQ 809
Cdd:pfam01576 629 AEAREketralSLARALEEALEAKEELertnkqlraemedlVSSKDDVGKNVHELERSKRALEQQVEEMKTQ 700
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
510-732 |
3.12e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 510 ETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEkrnnSLQTATENTQARVLHAEQEK 589
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELESELEALLNER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 590 AKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMK-----ETDL--LRGQLAQLQAELSEVQETSQQVQSKLKSE 662
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREklaqlELRLegLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 663 KQ-SRRQLELRVTSLEEELT----------------------------DLRTEKESLEknlserkkksaqercQAEEEID 713
Cdd:TIGR02168 963 IEdDEEEARRRLKRLENKIKelgpvnlaaieeyeelkerydfltaqkeDLTEAKETLE---------------EAIEEID 1027
|
250 260
....*....|....*....|
gi 1387290472 714 -EIRKSHQEELDKLRQLLKK 732
Cdd:TIGR02168 1028 rEARERFKDTFDQVNENFQR 1047
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
640-812 |
3.33e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 46.30 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 640 QLQAELSEVQETSQQVQSKLKSEKQS-RRQLELRvtslEEELTDLRTEKESLEkNLSERKKKSAQERCQAEEEIDEIRKS 718
Cdd:pfam14988 26 QYVQECEEIERRRQELASRYTQQTAElQTQLLQK----EKEQASLKKELQALR-PFAKLKESQEREIQDLEEEKEKVRAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 719 HQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLAS-AKNEHLQQYQEVCTQRDASQQQLLQLEEKCS 797
Cdd:pfam14988 101 TAEKDREAHLQFLKEKALLEKQLQELRILELGERATRELKRKAQALKLaAKQALSEFCRSIKRENRQLQKELLQLIQETQ 180
|
170
....*....|....*
gi 1387290472 798 ALQAQVTSLREQNAQ 812
Cdd:pfam14988 181 ALEAIKSKLENRKQR 195
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
586-840 |
3.98e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 586 EQEKAKVTEELAAAtaqvshlhlkmtahQKKETELQVQLTESMKETDLLRGQLAQ------LQAELSEVqETSQQVQSKL 659
Cdd:TIGR02169 169 DRKKEKALEELEEV--------------EENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREY-EGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 660 KSEKQsRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQ----AEEEIDEIRKSHQEELDKLRQLLKKARV 735
Cdd:TIGR02169 234 ALERQ-KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 736 STDQA--AAEQLSLVQAEL-------------QTQWEAKCEQL---LASAKNEH---LQQYQEVCTQRDASQQQLLQLEE 794
Cdd:TIGR02169 313 KERELedAEERLAKLEAEIdkllaeieelereIEEERKRRDKLteeYAELKEELedlRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387290472 795 KCSALQAQVTSLR--------------EQNAQHIKDLES-KAQTSGVEATAADPSEKVKKI 840
Cdd:TIGR02169 393 KLEKLKREINELKreldrlqeelqrlsEELADLNAAIAGiEAKINELEEEKEDKALEIKKQ 453
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
526-801 |
4.02e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 526 ERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMmEKRNNSL-------QTATENTQARVLHAEQ-----EKAKVT 593
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA-EEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARAL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATA-QVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQ-LQAELSEVQETS-----QQVQSKLKSEKQSR 666
Cdd:COG3096 429 CGLPDLTPeNAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKaYELVCKIAGEVErsqawQTARELLRRYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 667 RQLElRVTSLEEELTDLRTEKESLEK--NLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKA-------RVST 737
Cdd:COG3096 509 ALAQ-RLQQLRAQLAELEQRLRQQQNaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAveqrselRQQL 587
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 738 DQAAAEQLSLVQAE-----LQTQWEAKCEQLLASAKNEH---------LQQYQEVCTQRDASQQQLLQLEEKCSALQA 801
Cdd:COG3096 588 EQLRARIKELAARApawlaAQDALERLREQSGEALADSQevtaamqqlLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
508-855 |
4.28e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 508 TMETSMIMSNIQRIIQE----NERLKQEILEK--SSRIKEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQAr 581
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHqkavSERQQQEKFEKmeQERLRQEKEEKAREVERRRK--------LEEAEKARQAEMDRQAA- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 582 vLHAEQEKAKVTEElaaataqvSHLHLKMTAHQKKETElQVQLTESMKETDLLRgQLAQLQAELsevQETSQQVQSKLKS 661
Cdd:pfam17380 335 -IYAEQERMAMERE--------RELERIRQEERKRELE-RIRQEEIAMEISRMR-ELERLQMER---QQKNERVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 662 EKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQ--------LLKKA 733
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQqeeerkrkKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 734 RVSTDQAAAEQLS--LVQAELQTQWEAKCEQllaSAKNEHLQQYQEVCTQRDASQQQLLQLEEKcsalqaqvtSLREQNA 811
Cdd:pfam17380 481 KEKRDRKRAEEQRrkILEKELEERKQAMIEE---ERKRKLLEKEMEERQKAIYEEERRREAEEE---------RRKQQEM 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1387290472 812 QHIKDLESKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELE 855
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
514-715 |
4.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILEKS-SRIKEQNDKISELIERNQRYVEQSNlmMEKRNNSLQTATENTQARVLHAEQEKAKV 592
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD--AEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAATAQVSHLHLKMTAHQKKETElqvqltesmKETDLLRGQLAQLQAELSEVQETSQQVQS---KLKSEKQSRRQL 669
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEELR---------EEYLELSRELAGLRAELEELEKRREEIKKtleKLKEELEEREKA 709
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387290472 670 ELRVTSLEEELTDLRTEKESLeknlserKKKSAQERCQAEEEIDEI 715
Cdd:PRK03918 710 KKELEKLEKALERVEELREKV-------KKYKALLKERALSKVGEI 748
|
|
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
193-239 |
4.76e-05 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 43.34 E-value: 4.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1387290472 193 AVEVGDSLEVAYTSWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIK 239
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIP 46
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
579-727 |
5.59e-05 |
|
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: 44.92 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 579 QARVLHAEQEKakvteeLAAATAQVSHLHLKMTAHQKKETELQVQLTESmketdllrgQLAQLQAELSEVQETSQQVQSK 658
Cdd:pfam08614 15 RTALLEAENAK------LQSEPESVLPSTSSSKLSKASPQSASIQSLEQ---------LLAQLREELAELYRSRGELAQR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290472 659 LKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERkkksaqercqaEEEIDEIRKSH---QEELDKLR 727
Cdd:pfam08614 80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDR-----------EEELREKRKLNqdlQDELVALQ 140
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
596-817 |
6.01e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 596 LAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQL-------------AQLQAELS------EVQETSQQVQ 656
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLeeleaaalqpgeeEELEEERRrlsnaeKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 657 SKLKSE--------KQSRRQLElRVTSLEEELTDLRTEKESLEKNLSErkkkSAQE--RCQAEEEIDEIRKSHQEE-LDK 725
Cdd:COG0497 233 EALSGGeggaldllGQALRALE-RLAEYDPSLAELAERLESALIELEE----AASElrRYLDSLEFDPERLEEVEErLAL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 726 LRQLLKKARVSTDQAAAeqlslvqaeLQTQWEAKCEQLLASAknEHLQQYQEvctQRDASQQQLLQLEEKCSAL-QAQVT 804
Cdd:COG0497 308 LRRLARKYGVTVEELLA---------YAEELRAELAELENSD--ERLEELEA---ELAEAEAELLEAAEKLSAArKKAAK 373
|
250
....*....|...
gi 1387290472 805 SLREQNAQHIKDL 817
Cdd:COG0497 374 KLEKAVTAELADL 386
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
516-755 |
6.43e-05 |
|
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: 46.87 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 516 SNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRyveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEE 595
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKS---------SEELDSFKDTIESTKESLDEIPQNQRGYAQE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 596 LAAATAQvshlhlKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAEL--------SEVQETSQQVQSKLKSE-KQSR 666
Cdd:COG5185 407 ILATLED------TLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELnkvmreadEESQSRLEEAYDEINRSvRSKK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 667 RQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLS 746
Cdd:COG5185 481 EDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDG 560
|
....*....
gi 1387290472 747 LVQAELQTQ 755
Cdd:COG5185 561 QAANLRTAV 569
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
564-777 |
6.44e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 564 MEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQA 643
Cdd:PLN02939 168 LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 644 ELSEVQETSQQVqSKLKSE----KQSRRQLELRVTSLEEELTDLRTEK--------ESLEkNLSERKKKSAQERCQAEEE 711
Cdd:PLN02939 248 ELIEVAETEERV-FKLEKErsllDASLRELESKFIVAQEDVSKLSPLQydcwwekvENLQ-DLLDRATNQVEKAALVLDQ 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 712 IDEIRKshqeELDKLRQLLKKARVStdQAAAEQLSLVQAELQTQWE--AKCEQLLASakneHLQQYQE 777
Cdd:PLN02939 326 NQDLRD----KVDKLEASLKEANVS--KFSSYKVELLQQKLKLLEErlQASDHEIHS----YIQLYQE 383
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
623-831 |
6.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 623 QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKK--- 699
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 700 ---------------KSAQERCQAEEEIDEIRKSHQEELDKLRQLlkKARVSTDQAAAEQLSLVQAELQTQWEAKcEQLL 764
Cdd:COG3883 97 rsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKAD--KAELEAKKAELEAKLAELEALKAELEAA-KAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387290472 765 ASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 831
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
190-239 |
6.56e-05 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 43.25 E-value: 6.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1387290472 190 EGPAVEVGDSLEVAYTSWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIK 239
Cdd:COG0545 10 TGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIP 55
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
657-823 |
9.36e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 657 SKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKsHQEELDKLRQLLKKARVS 736
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 737 TDQaAAEQLSLVQAElqtqweakceqlLASAKNEHlQQYQEVCTQRDASQQQLLQLEEKcsaLQAQVTSLREQNA--QHI 814
Cdd:COG1340 80 RDE-LNEKLNELREE------------LDELRKEL-AELNKAGGSIDKLRKEIERLEWR---QQTEVLSPEEEKElvEKI 142
|
....*....
gi 1387290472 815 KDLESKAQT 823
Cdd:COG1340 143 KELEKELEK 151
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
506-732 |
1.00e-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: 46.55 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 506 SVTMETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL-------------------IERNQRYVEQsnlmMEK 566
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLedelnkddfelkkenlekeIDEKNKEIEE----LKQ 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 567 RNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHL--HLKMTAHQKKETELQVQLTESMKETdlLRGQLAQLQAE 644
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLekELEKAKKENEKLSSIIKNIKSKKNK--LKQEVKQIKET 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 645 LSEVQETSQQVQSKLKSEKqsrrqlelrvtSLEEELTDLrTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELD 724
Cdd:TIGR04523 654 IKEIRNKWPEIIKKIKESK-----------TKIDDIIEL-MKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELK 721
|
....*...
gi 1387290472 725 KLRQLLKK 732
Cdd:TIGR04523 722 KLDEFSKE 729
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
465-817 |
1.28e-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: 46.58 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 465 QHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMEtsMIMSNIQRIIQE-------NERLKQEILEKSS 537
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP--GRQSIIDLKEKEipelrnkLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 538 RIKEQNDKISEL----------------IERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLHAEQEKAKVTEELAAATA 601
Cdd:TIGR00606 766 DIEEQETLLGTImpeeesakvcltdvtiMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 602 QVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQlelrVTSLEEELT 681
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 682 DLRTEKESLEKNLSERKKKsaqercqAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQ---LSLVQAELQtqwea 758
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKK-------AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKeteLNTVNAQLE----- 987
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 759 KCEQLLASAKNEHLQQYQEVCTQRdaSQQQLLQLEEKCSALQAQVTSLREQNAQHIKDL 817
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRKRENELKEVEEELKQHLKEM 1044
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
531-705 |
1.44e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 46.21 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 531 EILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELAAAtaqvshlh 607
Cdd:pfam05911 664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlesTKSQLQESEQLIAELRSELASL-------- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 608 lkmtahQKKETELQVQLtESMKET-DLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTdlRTE 686
Cdd:pfam05911 736 ------KESNSLAETQL-KCMAESyEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNE 806
|
170 180
....*....|....*....|
gi 1387290472 687 KESLEKNL-SERKKKSAQER 705
Cdd:pfam05911 807 KKESSNCDaDQEDKKLQQEK 826
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
582-751 |
1.44e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 46.01 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 582 VLHAEQEKAKVTEELAAATAQVSHLHLKMTAhqkkETELQVQLTESMKETDLLRGQLAqLQAElSEVQETSQQVQSKLKS 661
Cdd:PRK00106 21 LISIKMKSAKEAAELTLLNAEQEAVNLRGKA----ERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 662 EKQSRRQLELRVT----SL---EEELTDLRTEKESLEKNLSErKKKSAQERcqaEEEIDEIRKSHQEELDKLRQLlkkar 734
Cdd:PRK00106 95 ERQELKQIESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL----- 165
|
170
....*....|....*..
gi 1387290472 735 vstDQAAAEQLSLVQAE 751
Cdd:PRK00106 166 ---SQAEAREIILAETE 179
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
616-793 |
1.52e-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: 46.19 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 616 KETELQVQLTESMKETDL-LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTS---LEEELTDLRTEKESLE 691
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimkLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 692 KNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEH 771
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEH 362
|
170 180
....*....|....*....|..
gi 1387290472 772 LQQYqEVCTQRDASQQQLLQLE 793
Cdd:TIGR00606 363 IRAR-DSLIQSLATRLELDGFE 383
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
579-755 |
1.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 579 QARVLHAEQEKAKVTEElAAATAQVshlhlkmtahQKKETELQVQlTESMKETDLLRGQLAQLQAELSEVQETSQQVQSK 658
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-AKKEAEA----------IKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 659 LKSEKQSrrqLELRVTSLEEELTDLRTEKESLEKnlserkkksaqercqAEEEIDEIRKSHQEELDKLRQLlkkarvSTD 738
Cdd:PRK12704 98 LDRKLEL---LEKREEELEKKEKELEQKQQELEK---------------KEEELEELIEEQLQELERISGL------TAE 153
|
170
....*....|....*..
gi 1387290472 739 QAAAEQLSLVQAELQTQ 755
Cdd:PRK12704 154 EAKEILLEKVEEEARHE 170
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
468-737 |
2.17e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 468 TEIRMAVSKVADKMDHLMTKVEEL-QKHSAGNSLlipsmsVTMEtsmimSNIQRIIQENERLKQEILEKSSRIKEQNDKI 546
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeERLERAEDL------VEAE-----DRIERLEERREDLEELIAERRETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 547 SELIERNQRYvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEEL-------------AAATAQVSHLHLKMTAH 613
Cdd:PRK02224 540 EELRERAAEL-EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIeslerirtllaaiADAEDEIERLREKREAL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 614 QKKETELQVQLTESMKETDLLRGQ-----LAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKE 688
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRE 698
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387290472 689 SLEknlserkkkSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVST 737
Cdd:PRK02224 699 RRE---------ALENRVEALEALYDEAEELESMYGDLRAELRQRNVET 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
518-816 |
2.34e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 518 IQRIIQENERLKQEILEKSSRIKEQNDKISEL--------IERNQRYVEQSNLmmEKRNNSLQTATENTQARVLHAEQEK 589
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELeseleearEAVEDRREEIEEL--EEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 590 AKVTEELAAATAQVSHLHLKMTAHQKKETELQvQLTESMK---------------ETDLLRGQLAQLQAELSEVQETSQQ 654
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAE-ALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 655 VQSKL-------KSEKQSRRQLELRVTSLE-------------EELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDE 714
Cdd:PRK02224 494 VEERLeraedlvEAEDRIERLEERREDLEEliaerretieekrERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 715 IRK--SHQEELDKLRQLLkkARVSTDQAAAEQLslvqaelqtqwEAKCEQLlasakNEHLQQYQEVCTQRdasQQQLLQL 792
Cdd:PRK02224 574 VAElnSKLAELKERIESL--ERIRTLLAAIADA-----------EDEIERL-----REKREALAELNDER---RERLAEK 632
|
330 340
....*....|....*....|....
gi 1387290472 793 EEKCSALQAQVTSLREQNAQHIKD 816
Cdd:PRK02224 633 RERKRELEAEFDEARIEEAREDKE 656
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
578-809 |
2.49e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 578 TQARVLHAEQEKAKVTEELAAATAQVSHLHLKMTahqkkETELqVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQS 657
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNL-----EAEL-LQLQEDLAASERARRQAQQERDELADEIASGASGKS 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 658 KLKSEKqsrRQLELRVTSLEEELTDLRTEKESleknLSERKKKSAQE---------------------RCQAEEEIDEIR 716
Cdd:pfam01576 879 ALQDEK---RRLEARIAQLEEELEEEQSNTEL----LNDRLRKSTLQveqlttelaaerstsqksesaRQQLERQNKELK 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 717 KSHQEELDKLRQLLKKArvstdqAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKC 796
Cdd:pfam01576 952 AKLQEMEGTVKSKFKSS------IAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQA 1025
|
250
....*....|...
gi 1387290472 797 SALQAQVTSLREQ 809
Cdd:pfam01576 1026 EKGNSRMKQLKRQ 1038
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
564-822 |
2.62e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 564 MEKRNNSLQTATENTQARV-------LHAEQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRG 636
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELknldknlNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 637 QLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKksaqERCQAEEEIDEIR 716
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK----EKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 717 -----------------KSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQaeLQTQWEAKCEQLLaSAKNEHlqqyQEVC 779
Cdd:TIGR04523 194 nkllklelllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINE--KTTEISNTQTQLN-QLKDEQ----NKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387290472 780 TQRDASQQQLLQLEEKCSALQAQVTSLREQnaqhIKDLESKAQ 822
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSE----ISDLNNQKE 305
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
524-802 |
3.12e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.17 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILEkssRIKEQNDKISELIERNQRYVEQ-SNLMMEKRNNSLQTATENTQARV-LHAEQEKAKVTEElaaata 601
Cdd:pfam09728 82 QNKKLKEESKK---LAKEEEEKRKELSEKFQSTLKDiQDKMEEKSEKNNKLREENEELREkLKSLIEQYELREL------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 602 qvsHLHlkmtaHQKKETELQVQLTES-MKETDLLRGQLAQlQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEl 680
Cdd:pfam09728 153 ---HFE-----KLLKTKELEVQLAEAkLQQATEEEEKKAQ-EKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEF- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 681 tdlrteKESLEKNlserkkksaqercqaEEEIDEIRKSHQEELDKLRQLLKKArvstdqaaaeqlslvqAELQTQWEaKC 760
Cdd:pfam09728 223 ------QDTLNKS---------------NEVFTTFKKEMEKMSKKIKKLEKEN----------------LTWKRKWE-KS 264
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387290472 761 EQLLASAKNEHLQQYQEVctqrDASQQQLLQLEEKCSALQAQ 802
Cdd:pfam09728 265 NKALLEMAEERQKLKEEL----EKLQKKLEKLENLCRALQAE 302
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
453-716 |
3.64e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 453 GDVASFLMTEARQHNTEI---RMAVSKVADKMDHLMTKVEELQKHSAgnSLLIPSMSVTMETSMIMSNIQRIIQENERLK 529
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIndrRLELQEFKILKDKKDAKIRELEARVS--DLELEKVKLVNAGSERLRAVKDIKQERDQLL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 530 QEIleKSSRikEQNDKISELIERNQRYVEQSNLMMEKRNNSL-------QTATENTQARVLHAEQEKAKVTEELAAATAQ 602
Cdd:pfam15921 660 NEV--KTSR--NELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 603 VSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTD 682
Cdd:pfam15921 736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
250 260 270
....*....|....*....|....*....|....
gi 1387290472 683 LRTEKESLEKNLSERKKKSAQERCQAEEEIDEIR 716
Cdd:pfam15921 816 ASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
624-857 |
3.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 624 LTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEK------NLSER 697
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 698 KKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTdqaaaeqlslvqaELqtQWEAKceqllasaknehlqQYQE 777
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-------------EL--KEKAE--------------EYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 778 VCTQRDASQQQLLQLEEKCSALQAQVTSLREQnaqhIKDLESKaqtsgveataadpSEKVKKIMNQVFQFLRGEFELEEF 857
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEK-------------EERLEELKKKLKELEKRLEELEER 360
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
528-670 |
3.85e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 528 LKQEILEKSSRIKEQNDKISELIERnqryveqsnLMMEKRNN-SLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHL 606
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADL---------LSLERQGNqDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290472 607 HLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKlksEKQSRRQLE 670
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKR---DRESQAKIA 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
608-819 |
3.93e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 608 LKMTAHQKKEteLQVQLTES----MKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDL 683
Cdd:pfam15921 80 LEEYSHQVKD--LQRRLNESnelhEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 684 RTEKESLEKNlserkkksaqercqAEEEIDEIRK---SHQEELDKLRQLLKKARVSTDQAAAEQ--------------LS 746
Cdd:pfam15921 158 KCLKEDMLED--------------SNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASGKKIYEHdsmstmhfrslgsaIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 747 LVQAELQTQW----------EAKCEQLLASAKNEH---LQQYQEVCTQRDASQQ-QLLQLEEKCSALQAQVTSL------ 806
Cdd:pfam15921 224 KILRELDTEIsylkgrifpvEDQLEALKSESQNKIellLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIqsqlei 303
|
250 260
....*....|....*....|.
gi 1387290472 807 -----REQNA---QHIKDLES 819
Cdd:pfam15921 304 iqeqaRNQNSmymRQLSDLES 324
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
526-802 |
4.36e-04 |
|
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: 44.43 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 526 ERLKQEILEKSSRIKEQNDKISELIERN---QRYVE---QSNLMMEKRNNSLQTATENTQARVLHAEQ---EKAK----V 592
Cdd:pfam10174 292 DQLKQELSKKESELLALQTKLETLTNQNsdcKQHIEvlkESLTAKEQRAAILQTEVDALRLRLEEKESflnKKTKqlqdL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAATAQVSHLHLKMTAHQKKETELQvqltesmKETDLLRGQLAQLQAELSEVQEtsqqvqsklksekqsrrqlelR 672
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKERKINVLQ-------KKIENLQEQLRDKDKQLAGLKE---------------------R 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 673 VTSLEEELTDLRTEKESLEKNLSErkKKSAQERCQaeEEIDEIRKSHQEELDKLRQLLKKARvstdqaaaEQLSLVQAEL 752
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSE--KERIIERLK--EQREREDRERLEELESLKKENKDLK--------EKVSALQPEL 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1387290472 753 QTQweakcEQLLASAKnEHLQQYQEVCTQRDASQQQL----LQLEEKCSALQAQ 802
Cdd:pfam10174 492 TEK-----ESSLIDLK-EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQ 539
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
462-808 |
4.40e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 462 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSA---GNSLlIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSSR 538
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlnGQSV-CPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 539 IKEQNDKISELIERNQRyveqsnLMMEKRNNSLqtaTENTQARVLHAEQEKAKVTEelaaatAQVSHLHLKMTAHQKKET 618
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEY------LESEEINKSI---NEYNKIESARADLEDIKIKI------NELKDKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 619 ELQVQLTESmKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSekqsrrqLELRVTSLEEELTDLRTEKESL------EK 692
Cdd:PRK01156 557 SLKLEDLDS-KRTSWLNALAVISLIDIETNRSRSNEIKKQLND-------LESRLQEIEIGFPDDKSYIDKSireienEA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 693 NLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQwEAKCEQLLASAKNEHL 772
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-DAKANRARLESTIEIL 707
|
330 340 350
....*....|....*....|....*....|....*.
gi 1387290472 773 QQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLRE 808
Cdd:PRK01156 708 RTRINELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
524-839 |
5.79e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILEKSSRIKEQNDkisELIERNQRYVEQSNLMMEKRNNSLQTATENTqARVLHAEQEKAkVTEELAAATAQV 603
Cdd:NF041483 503 ESERVRTEAIERATTLRRQAE---ETLERTRAEAERLRAEAEEQAEEVRAAAERA-ARELREETERA-IAARQAEAAEEL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 604 SHLHlkmTAHQKKETELQVQLTESMKETDLLRGQLAQLQAEL-SEVQETSQQVQSKLKSEKQSRRqlelrvTSLEEELTD 682
Cdd:NF041483 578 TRLH---TEAEERLTAAEEALADARAEAERIRREAAEETERLrTEAAERIRTLQAQAEQEAERLR------TEAAADASA 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 683 LRTEKESLEKNLserkkksaqeRCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQwEAKCEQ 762
Cdd:NF041483 649 ARAEGENVAVRL----------RSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARR-RREAEE 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 763 LLASAKNEHLQQYQEVCTQR-----------DASQQQLLQLEEKCSALQAQVTSLREQNAQHIKD----LESKAQ--TSG 825
Cdd:NF041483 718 TLGSARAEADQERERAREQSeellasarkrvEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEeeIAG 797
|
330
....*....|....
gi 1387290472 826 VEATAADPSEKVKK 839
Cdd:NF041483 798 LRSAAEHAAERTRT 811
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
517-709 |
6.01e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 517 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRyVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 596
Cdd:COG2268 175 AITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETE-IAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 597 AAATAQvshlhlkmtahQKKETELQVQLTESMKEtdllrgQLAQLQAELSEVQetsQQVQSKLKSEKQSRRQLelrvtsl 676
Cdd:COG2268 254 RREAET-----------ARAEAEAAYEIAEANAE------REVQRQLEIAERE---REIELQEKEAEREEAEL------- 306
|
170 180 190
....*....|....*....|....*....|...
gi 1387290472 677 eeeltdlrtEKESLEKNLSERKKKSAQERCQAE 709
Cdd:COG2268 307 ---------EADVRKPAEAEKQAAEAEAEAEAE 330
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
691-809 |
6.14e-04 |
|
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: 41.09 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 691 EKNLSERKKKSAQERcqaEEEIDEIRKSHQEELDKLRQLLKKARVSTDQ------AAAEQLSLVQAELQtQWEAKCEQLL 764
Cdd:pfam07926 2 ELSSLQSEIKRLKEE---AADAEAQLQKLQEDLEKQAEIAREAQQNYERelvlhaEDIKALQALREELN-ELKAEIAELK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1387290472 765 A---SAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQ 809
Cdd:pfam07926 78 AeaeSAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
671-804 |
6.41e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 671 LRVTSLEEELTDLRTEKESLEKnlserkkksaqERCQAEEEIDEirkSHQEELDKLRQLLKKARvstdqaaaEQLslvqA 750
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290472 751 ELQTQWEAKCEQL--LASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVT 804
Cdd:COG0542 458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
614-735 |
6.63e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 614 QKKETELQVQLTESMKETDLLRGQ-LAQLQAELSEVQETSQQVQSKLKSEKQsrrqLELRVTSLEEELTDLRTEKESLEK 692
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 693 NLSERKKKSAQERCQAEEEIDE--------------IRKSHQEELDKLRQL---LKKaRV 735
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
259-454 |
6.67e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 259 AAPSPIPPadsiSADPVVSPSTSVPFRSGESALRS--KSNSLSEHLTVNTNPDTVKAKLISRMAKMGQPMLPILPPQLDS 336
Cdd:PHA03247 2825 AGPLPPPT----SAQPTAPPPPPGPPPPSLPLGGSvaPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL 2900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 337 NDSEIEDVNAPRGAGQPLATPSVQPSLQPAHPVLPQMTSQAPQPSvsrlqtpsaalmqvaslDSHSAVSGNAQSFQPYAG 416
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP-----------------TTDPAGAGEPSGAVPQPW 2963
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387290472 417 VQAYAYPQAPAVASQLQPVRPLYPAPLSQPPHFQGSGD 454
Cdd:PHA03247 2964 LGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSL 3001
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
518-831 |
6.76e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 518 IQRIIQENERLKQEI-------LEKSSRIKEQNDKISEL-IERNQRYVEQSNLM-------MEKRNNSLQTATENTQARV 582
Cdd:pfam07111 68 ISRQLQELRRLEEEVrllretsLQQKMRLEAQAMELDALaVAEKAGQAEAEGLRaalagaeMVRKNLEEGSQRELEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 583 LHAEQEKAKVT---EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLA----QLQAELSEVQETSQQV 655
Cdd:pfam07111 148 LHQEQLSSLTQaheEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSktqeELEAQVTLVESLRKYV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 656 QSKLKSEKQSrRQLELRVTSLEEELTDLRTEKESLEKNLserkkKSAQERCQAeeeIDEIRKSHQEELDKLRQLLKKarv 735
Cdd:pfam07111 228 GEQVPPEVHS-QTWELERQELLDTMQHLQEDRADLQATV-----ELLQVRVQS---LTHMLALQEEELTRKIQPSDS--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 736 stdqaaaeqlslvqaeLQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIK 815
Cdd:pfam07111 296 ----------------LEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR 359
|
330
....*....|....*.
gi 1387290472 816 DLESKAQTSGVEATAA 831
Cdd:pfam07111 360 ALQDKAAEVEVERMSA 375
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
589-730 |
6.97e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 589 KAKVTEELAAATAQVSHLhLKMTAHQKKETELQV-----QLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEK 663
Cdd:PRK09039 51 KDSALDRLNSQIAELADL-LSLERQGNQDLQDSVanlraSLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 664 Q----SRRQLELrvtsLEEELTDLRTEKESLEKNL--SERKKKSAQERCQA---------EEEIDEIRKSHQEELDKLRQ 728
Cdd:PRK09039 130 QvsarALAQVEL----LNQQIAALRRQLAALEAALdaSEKRDRESQAKIADlgrrlnvalAQRVQELNRYRSEFFGRLRE 205
|
..
gi 1387290472 729 LL 730
Cdd:PRK09039 206 IL 207
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
517-824 |
7.37e-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: 44.06 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 517 NIQRIIQENERLKQEILE----KSSRIKEQNDKISELIERnQRYVEQSNL---------MMEKRNNSLQ----------- 572
Cdd:pfam12128 369 KHQDVTAKYNRRRSKIKEqnnrDIAGIKDKLAKIREARDR-QLAVAEDDLqaleselreQLEAGKLEFNeeeyrlksrlg 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 573 ---------TATEN--TQARVLHAEQEKAKvtEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQL 641
Cdd:pfam12128 448 elklrlnqaTATPEllLQLENFDERIERAR--EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 642 QAEL------------SEVQETSQQVQSKLKSEKQSRRQL--ELRVTSLEEELT---------------------DLRTE 686
Cdd:pfam12128 526 ELQLfpqagtllhflrKEAPDWEQSIGKVISPELLHRTDLdpEVWDGSVGGELNlygvkldlkridvpewaaseeELRER 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 687 KESLEKNL-SERKKKSAQER--CQAEEEIDEIRKshqeELDKLRQLLKKARVS----TDQAAAEQLSLVQA--------- 750
Cdd:pfam12128 606 LDKAEEALqSAREKQAAAEEqlVQANGELEKASR----EETFARTALKNARLDlrrlFDEKQSEKDKKNKAlaerkdsan 681
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 751 ELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEE----KCSALQAQVTSLREQNAQHIKDLESKAQTS 824
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
514-859 |
7.66e-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: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILE----------KSSRIKEQNDKISELIERNQRYVEQSNLmmeKRNNSLQTATENTQARVL 583
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTEllveqgrlqlQADRHQEHIRARDSLIQSLATRLELDGF---ERGPFSERQIKNFHTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 584 HAEQEKAKVTEELaaataqVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKS-- 661
Cdd:TIGR00606 401 ERQEDEAKTAAQL------CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRil 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 662 EKQSRRQLELRVTSLEEELTDLRTEKESlEKNLSERKKKSAQERCQAEEEIDEirKSHQEELDKLRQLLKKARVSTDQAA 741
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKKE-VKSLQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 742 AEQLSLVQAELQTQ-----WEAKCEQLLASAKNE----------------HLQQYQ-EVCTQRDASQQQLLQLEEK---- 795
Cdd:TIGR00606 552 RKIKSRHSDELTSLlgyfpNKKQLEDWLHSKSKEinqtrdrlaklnkelaSLEQNKnHINNELESKEEQLSSYEDKlfdv 631
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 796 --CSALQAQVTSLREQNAQHIKDLESKAQTSGVEAT----AADPSEKVKKIMNQVFQflrGEFELEEFYS 859
Cdd:TIGR00606 632 cgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQfitqLTDENQSCCPVCQRVFQ---TEAELQEFIS 698
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
518-836 |
8.04e-04 |
|
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: 43.66 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 518 IQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYV---EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE 594
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELtekESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 595 ELAAATAQVSHLHlkmtahqkkETELQVQLTESMKEtdllrgQLAQLQAELSEVQETSQQVQSKlksekqsrrqlelrVT 674
Cdd:pfam10174 532 ECSKLENQLKKAH---------NAEEAVRTNPEIND------RIRLLEQEVARYKEESGKAQAE--------------VE 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 675 SLEEELTDLRTEKESLEKNLSE-RKKKSAQERCQAeEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 753
Cdd:pfam10174 583 RLLGILREVENEKNDKDKKIAElESLTLRQMKEQN-KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 754 TQWEaKCEQLLASAKnehlqqyqevctQRDASQQQllQLEEKcsalQAQVTSLREQNAQHIKD-LESKAqtsgvEATAAD 832
Cdd:pfam10174 662 GALE-KTRQELDATK------------ARLSSTQQ--SLAEK----DGHLTNLRAERRKQLEEiLEMKQ-----EALLAA 717
|
....
gi 1387290472 833 PSEK 836
Cdd:pfam10174 718 ISEK 721
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
522-661 |
8.94e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 41.42 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 522 IQENERLKQEILEKS-SRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE---NTQARVLHAEQEKAK-VTEEL 596
Cdd:pfam10368 27 LVELEKKEQELYEEIiELGMDEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEefkKIKEIIEEIEDEELKkEAEEL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387290472 597 AAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLlrgQLAQLQAELSEVQETSQQVQSKLKS 661
Cdd:pfam10368 107 IDAMEERYEAYDELYDAYKKALELDKELYEMLKDEDL---TLEELQEQIEKINESYEEVKEANEQ 168
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
510-774 |
9.07e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 510 ETSMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRN----NSLQTATENTQARVLHA 585
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIleylKEKAEREEEREAEREEI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 586 EQEKAKVTEELAAATAQvshlhlkmtAHQKKEtelqvqltesmkETDLLRGQLAQLQAELSEVQETSQQVQSKLKSE--- 662
Cdd:pfam13868 179 EEEKEREIARLRAQQEK---------AQDEKA------------ERDELRAKLYQEEQERKERQKEREEAEKKARQRqel 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 663 KQSRR-QLELRVTSLEEEltdLRTEKESLEKNLSERKKKSAQERCQAEEEIdEIRKSHQEELDKLRQLLKKARvstdqAA 741
Cdd:pfam13868 238 QQAREeQIELKERRLAEE---AEREEEEFERMLRKQAEDEEIEQEEAEKRR-MKRLEHRRELEKQIEEREEQR-----AA 308
|
250 260 270
....*....|....*....|....*....|...
gi 1387290472 742 AEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQ 774
Cdd:pfam13868 309 EREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
594-777 |
9.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLqAELSEVQETSQQVQSKLKSEKQSRRQLELRV 673
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 674 TSLEEELTDLrtEKESLEKNLSERKKKSAQercqAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 753
Cdd:COG4717 416 GELEELLEAL--DEEELEEELEELEEELEE----LEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|....
gi 1387290472 754 TQWEAKceQLLASAKNEHLQQYQE 777
Cdd:COG4717 490 EEWAAL--KLALELLEEAREEYRE 511
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
683-856 |
9.42e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 683 LRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLL-----KKARVSTDQAAAE---------QLSLV 748
Cdd:PRK00106 26 MKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELlleakEEARKYREEIEQEfkserqelkQIESR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 749 QAELQTQWEAKCEQLlaSAKNEHLQQYQEVCTQR----DASQQQLLQLEEKCSALQAQVTSLREQNAQHI------KDL- 817
Cdd:PRK00106 106 LTERATSLDRKDENL--SSKEKTLESKEQSLTDKskhiDEREEQVEKLEEQKKAELERVAALSQAEAREIilaeteNKLt 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387290472 818 -ESKAQTSGVEATAADPSEKV-KKIMNQVFQFLRGEFELEE 856
Cdd:PRK00106 184 hEIATRIREAEREVKDRSDKMaKDLLAQAMQRLAGEYVTEQ 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
661-856 |
9.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 661 SEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAqercqaEEEIDEIRKSHQEELDKLRQLLKKARVSTDQA 740
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG------LVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 741 AAeQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSLREQNAQHIKDL--E 818
Cdd:COG3206 239 EA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlaS 317
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387290472 819 SKAQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEE 856
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
577-743 |
1.03e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 577 NTQAR---VLHAEQEKAKVTEELAAATAQvshlhlkMTAHQKKEtelqvQLTESMKETDLLRGQLAQLQAELSEVQETSQ 653
Cdd:COG3524 171 SERARedaVRFAEEEVERAEERLRDAREA-------LLAFRNRN-----GILDPEATAEALLQLIATLEGQLAELEAELA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 654 QVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEirkshqeeldklrQLLKKA 733
Cdd:COG3524 239 ALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLLAEYERLELEREFAE-------------KAYTSA 305
|
170
....*....|
gi 1387290472 734 RVSTDQAAAE 743
Cdd:COG3524 306 LAALEQARIE 315
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
594-794 |
1.03e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAA-ATAQVSHLHLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQ---SRRQL 669
Cdd:pfam05701 264 AELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAelaSLRQR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 670 E----LRVTSLEEELTDLRTEKESL---EKNLSERKKKSAQERCQAEEEIDEIRKSHQeeldKLRQLLKKARVSTDQAAA 742
Cdd:pfam05701 344 EgmasIAVSSLEAELNRTKSEIALVqakEKEAREKMVELPKQLQQAAQEAEEAKSLAQ----AAREELRKAKEEAEQAKA 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 743 EqLSLVQAELQ-TQWE---AKCEQLLASAKNEHLQQYQ---EVCTQRDASQQQLLQLEE 794
Cdd:pfam05701 420 A-ASTVESRLEaVLKEieaAKASEKLALAAIKALQESEssaESTNQEDSPRGVTLSLEE 477
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
647-795 |
1.03e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 647 EVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEltdLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKL 726
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEE---IRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 727 RQL-LKKARVSTDQAAAEQLSlvQAELQTQWEAKCEQLLASAKNEHLQQYQEvctQRDASQQQLLQLEEK 795
Cdd:pfam15709 433 QELqRKKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEERLEYQRQ---KQEAEEKARLEAEER 497
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
588-825 |
1.05e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 588 EKAKVTEELAAATAQVshlhlkmTAHQKKETE-LQVQLT--ESMKETdLLRGQlaQLQAELSEVQETSQQVQSKLKSEKQ 664
Cdd:PRK10929 24 DEKQITQELEQAKAAK-------TPAQAEIVEaLQSALNwlEERKGS-LERAK--QYQQVIDNFPKLSAELRQQLNNERD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 665 SRRQLELRVTSLEEELTDLRTEKESLEKNlserkKKSAQERCQAEEEIDEIRKSHQEELDKLRQL------LKKARVSTD 738
Cdd:PRK10929 94 EPRSVPPNMSTDALEQEILQVSSQLLEKS-----RQAQQEQDRAREISDSLSQLPQQQTEARRQLneierrLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 739 QAAAEQLSLVQAELQTQwEAKCEQL-LA--SAKNEhlqqyQEVCTQR-DASQQQLLQLEEKCSALQAQVTSLREQNA-QH 813
Cdd:PRK10929 169 PLAQAQLTALQAESAAL-KALVDELeLAqlSANNR-----QELARLRsELAKKRSQQLDAYLQALRNQLNSQRQREAeRA 242
|
250
....*....|..
gi 1387290472 814 IKDLESKAQTSG 825
Cdd:PRK10929 243 LESTELLAEQSG 254
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
582-774 |
1.12e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 582 VLHAEQEKAKVTE--ELAAATAQVSHLHLKmtahqKKETELQVQLTE-SMKETDLLRGQLAQLQAELSEVQEtsQQVQSK 658
Cdd:pfam09731 235 VEKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 659 LKSEKQSRRQLElrvtSLEEELTDLRTE-KESLEKNLSERKKksaQERCQAEEEIDEIRKSHQEeldKLRQLLKKARVST 737
Cdd:pfam09731 308 KREEKHIERALE----KQKEELDKLAEElSARLEEVRAADEA---QLRLEFEREREEIRESYEE---KLRTELERQAEAH 377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387290472 738 DQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQ 774
Cdd:pfam09731 378 EEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
614-733 |
1.26e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 41.59 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 614 QKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQsrrQLELRVTSLEEELTDL----RTEKES 689
Cdd:pfam05010 28 KAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKD---QALADLNSVEKSFSDLfkryEKQKEV 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 690 LE--KNLSERKKKSAQERC----------------------QAEEEIDEIRKSHQEELDKLRQLLKKA 733
Cdd:pfam05010 105 ISgyKKNEESLKKCAQDYLarikkeeqryqalkahaeekldQANEEIAQVRSKAKAETAALQASLRKE 172
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
677-831 |
1.29e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 41.19 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 677 EEELTDLRTEKEslEKNLSERKKKSAQERCQAEEEiDEIRKshqEELDKLRQLLKKARvstdqAAAEQLSLVqAELQTQW 756
Cdd:pfam15927 5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 757 E--AKCEQL--LASAK--NEHLQQYQEVcTQRDASQ-----QQLLQLEEKCSAL------QAQVTSLREQNAQHIKDLES 819
Cdd:pfam15927 73 EryMRCDGLpdPRDEQeiNTFISLWREE-EEEDIDEvmetcTLVLELIEELEELlldtppEELAEKYVEQYKEVILVLRE 151
|
170
....*....|..
gi 1387290472 820 KAQTSGVEATAA 831
Cdd:pfam15927 152 LINKKIDEATAH 163
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
632-734 |
1.51e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 632 DLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSR-RQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEE 710
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100
....*....|....*....|....*.
gi 1387290472 711 EIDEIRK--SHQEELDKLRQLLKKAR 734
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEER 485
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
621-806 |
1.53e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 621 QVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKL-----KSEKQSRrQLELRVTSLEEELTDL-------RTEKE 688
Cdd:pfam12128 589 RIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangELEKASR-EETFARTALKNARLDLrrlfdekQSEKD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 689 SLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEqlslVQAELQTQwEAKCEQLLASAK 768
Cdd:pfam12128 668 KKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV----VEGALDAQ-LALLKAAIAARR 742
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387290472 769 NEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL 806
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTL 780
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
530-824 |
1.60e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 530 QEILEKSSRIKEQNDKISElIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLHLk 609
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLAC-IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRV- 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 610 mtahQKKETELQvQLTESMKETDLLRGQLAQLQAELSEV---QETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTE 686
Cdd:COG5022 878 ----ELAERQLQ-ELKIDVKSISSLKLVNLELESEIIELkksLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVK 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 687 KESLEKNLSERK--KKSAQERC----QAEEEIDEIRKShQEELDKLRQLLK-----KARVSTDQAAAEQLSLVQAELQT- 754
Cdd:COG5022 953 LPELNKLHEVESklKETSEEYEdllkKSTILVREGNKA-NSELKNFKKELAelskqYGALQESTKQLKELPVEVAELQSa 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 755 --------------QWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQleekCSALQAQVTSLREQNAqhiKDLESK 820
Cdd:COG5022 1032 skiissestelsilKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ----LYQLESTENLLKTINV---KDLEVT 1104
|
....
gi 1387290472 821 AQTS 824
Cdd:COG5022 1105 NRNL 1108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
477-736 |
1.62e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 477 VADKMDHLMTKVEELQK-HSAGNSLLIPSMSVTMET--SMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKISELIERN 553
Cdd:PRK04863 798 LAERYATLSFDVQKLQRlHQAFSRFIGSHLAVAFEAdpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 554 QRYVEQSNLMMEkrnNSLQTATENTQARVLHAEQEKAKVTEELAAATA---QVSHL--------HLKMTAHQKKETELQV 622
Cdd:PRK04863 878 NRLLPRLNLLAD---ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQlepIVSVLqsdpeqfeQLKQDYQQAQQTQRDA 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 623 Q------------------------LTESMKETDLLRGQLAQLQAELSEVQE---TSQ-------QVQSKLKSEKQSRRQ 668
Cdd:PRK04863 955 KqqafaltevvqrrahfsyedaaemLAKNSDLNEKLRQRLEQAEQERTRAREqlrQAQaqlaqynQVLASLKSSYDAKRQ 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 669 LelrVTSLEEELTDL------------RTEKESLEKNLSE-RKKKSAQERCQA--EEEIDEIRK---SHQEELDKLRQLL 730
Cdd:PRK04863 1035 M---LQELKQELQDLgvpadsgaeeraRARRDELHARLSAnRSRRNQLEKQLTfcEAEMDNLTKklrKLERDYHEMREQV 1111
|
....*.
gi 1387290472 731 KKARVS 736
Cdd:PRK04863 1112 VNAKAG 1117
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
254-447 |
1.70e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 254 SSRDSAAPSPIPPADSISADPVVSPSTsvpfrSGESALRSKSNSLSEHLTVNTNPDTVKAKLISRMAKMGQPMLPILPPQ 333
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSP-----AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 334 ldsndseiedvnAPRgagQPLATPSVQPSLQPAHPVLPQMTSQ-APQPSVSRLQTPSAALMQVASLDSHSAVSGnaqsfq 412
Cdd:PHA03247 2682 ------------RPR---RRAARPTVGSLTSLADPPPPPPTPEpAPHALVSATPLPPGPAAARQASPALPAAPA------ 2740
|
170 180 190
....*....|....*....|....*....|....*.
gi 1387290472 413 PYAGVQAYAYPQAPA-VASQLQPVRPLYPAPLSQPP 447
Cdd:PHA03247 2741 PPAVPAGPATPGGPArPARPPTTAGPPAPAPPAAPA 2776
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
586-806 |
1.73e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 586 EQEKAKVTEeLAAATAQVSHLHLKMTAHQKketelqvQLTESMKE-TDLLRGQLAQLQAELSEVQETSQQvqSKLKSEKQ 664
Cdd:PRK10246 191 EQHKSARTE-LEKLQAQASGVALLTPEQVQ-------SLTASLQVlTDEEKQLLTAQQQQQQSLNWLTRL--DELQQEAS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 665 SRRQLELRVtslEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQAAAEQ 744
Cdd:PRK10246 261 RRQQALQQA---LAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQ 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290472 745 LSLVQAELQT--QWEAKCEQLlaSAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL 806
Cdd:PRK10246 338 SAELQAQQQSlnTWLAEHDRF--RQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAL 399
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
515-833 |
1.77e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 515 MSNIQRIIQENERLKQEILEKSSRIKEQNDKISE-LIERNQRYVEQSNLMMEkrnnsLQTATENtQARVLHAEQEKAKV- 592
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAaLNEMRQRYKEKTQQLAD-----VKTICEQ-EARIKDLEAQRAQLq 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 ----------TEELAAATAQVshlhLKMTAHQKKETELQVQLTESMKETDLLRGQL----AQLQAELSEVQETSQQVQSk 658
Cdd:PRK10246 502 agqpcplcgsTSHPAVEAYQA----LEPGVNQSRLDALEKEVKKLGEEGAALRGQLdaltKQLQRDESEAQSLRQEEQA- 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 659 LKSEKQSRRQlELRVT-SLEEELTDLRTEKESLEKNL---SERKKKSAQERCQAEEEIdeirkSHQEELDKLRQLLkkar 734
Cdd:PRK10246 577 LTQQWQAVCA-SLNITlQPQDDIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQQII-----QYQQQIEQRQQQL---- 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 735 vsTDQAAAEQLSLVQAELQTQWeakceqllASAKNEHLQQYQEVCTQRDASQQQLLQLE--------------------- 793
Cdd:PRK10246 647 --LTALAGYALTLPQEDEEASW--------LATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetval 716
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1387290472 794 -------EKCSALQAQVTSLREQNAQHIKDLeSKAQTSGVEATAADP 833
Cdd:PRK10246 717 dnwrqvhEQCLSLHSQLQTLQQQDVLEAQRL-QKAQAQFDTALQASV 762
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
524-751 |
1.88e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQV 603
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 604 SHLHLKMTAHQKKETELQVQLTESMKETDLLRGQlaQLQAELSEVQeTSQQVQSKLKSEKQSRRQLELRVTSLEEELTDL 683
Cdd:TIGR00618 732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFN--NNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 684 RTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKShQEELDKLRQLLKKARVSTDQAAAEQLSLVQAE 751
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT-LGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
468-738 |
2.05e-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: 42.19 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 468 TEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLIPSMSVTMETSMIMS--NIQRIiQENERLKQEILEKSSRIKEQNDK 545
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaaHEARI-RELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 546 ISELIER--NQRYVEQSnlmmEKRNnsLQTATENTQA--RVLHAEQEKAKVTEELAAATAQ-----VSHLHLKMTAHQKK 616
Cdd:pfam07888 155 MKERAKKagAQRKEEEA----ERKQ--LQAKLQQTEEelRSLSKEFQELRNSLAQRDTQVLqlqdtITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 617 ETE----------LQVQLTESMKETDLLRGQLAQL------------QAELSEVQETSQQVQSKLK---------SEKQS 665
Cdd:pfam07888 229 EAEnealleelrsLQERLNASERKVEGLGEELSSMaaqrdrtqaelhQARLQAAQLTLQLADASLAlregrarwaQERET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 666 RRQ-----------LELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKS--------------HQ 720
Cdd:pfam07888 309 LQQsaeadkdriekLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvaqkekeqlqaeKQ 388
|
330
....*....|....*...
gi 1387290472 721 EELDKLRQLLKKARVSTD 738
Cdd:pfam07888 389 ELLEYIRQLEQRLETVAD 406
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
523-754 |
2.13e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 523 QENERLKQEILEKSSRIKEQNDKISELIERN----QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAA 598
Cdd:PTZ00440 560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 599 ATAQVSHLHLKMTA--HQKKETE-LQVQLTESMKETDLLR--------GQLAQLQAELSEVQETSQQVQSKL-----KSE 662
Cdd:PTZ00440 640 LLDELSHFLDDHKYlyHEAKSKEdLQTLLNTSKNEYEKLEfmksdnidNIIKNLKKELQNLLSLKENIIKKQlnnieQDI 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 663 KQSRRQLELRVTSLEEELTDLRTEKESLE---KNLSERKKKSAQERCQAEEEIDEIRKSHQEELDKLRQLLKKARVSTDQ 739
Cdd:PTZ00440 720 SNSLNQYTIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISND 799
|
250
....*....|....*..
gi 1387290472 740 AAA--EQLSLVQAELQT 754
Cdd:PTZ00440 800 INIlkENKKNNQDLLNS 816
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
462-700 |
2.47e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 462 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNsllipsmsVTMETSMIMSN---IQRIIQENERLKQEILEKSSR 538
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEN--------IARKQNKYDELveeAKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 539 IKEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTATENtqarvLHAEQEK-AKVTEELAAATAQVShlhlK 609
Cdd:PHA02562 250 IEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIKDKLKELQHSLE----K 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 610 MTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKsekqsrrQLELRVTSLEEELTDLRTEKES 689
Cdd:PHA02562 318 LDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE-------ELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|.
gi 1387290472 690 LEKNLSERKKK 700
Cdd:PHA02562 391 IVKTKSELVKE 401
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
640-763 |
2.54e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.60 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 640 QLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSErkKKSAQERCQA-EEEIDEIRKS 718
Cdd:pfam12718 18 ELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTN--NENLTRKIQLlEEELEESDKR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1387290472 719 HQEELDKLRQllkkarvsTDQAAAEQLSLVQAELQT--QWEAKCEQL 763
Cdd:pfam12718 96 LKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
626-731 |
2.61e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.25 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 626 ESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQER 705
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEV 211
|
90 100
....*....|....*....|....*.
gi 1387290472 706 CQAEEEIDEIrksHQEELDKLRQLLK 731
Cdd:COG4026 212 FSLEELWKEL---FPEELPEEDFIYF 234
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
658-817 |
2.69e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 658 KLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIR--------------KSHQEEL 723
Cdd:pfam12128 245 KLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRdelngelsaadaavAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 724 DKLRQLLK---KARVSTDQAAAEQLSLVQAELQTQ-------------WEAKCEQLLASAKNEHLQQYQEVCTQRDASQQ 787
Cdd:pfam12128 325 EALEDQHGaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIRE 404
|
170 180 190
....*....|....*....|....*....|.
gi 1387290472 788 QL-LQLEEKCSALQAQVTSLREQNAQHIKDL 817
Cdd:pfam12128 405 ARdRQLAVAEDDLQALESELREQLEAGKLEF 435
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
618-732 |
2.72e-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: 41.16 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 618 TELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQsKLKSEKQS-------RRQLELRVTSLE-----EELTDLRT 685
Cdd:smart00787 154 EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK-QLEDELEDcdpteldRAKEKLKKLLQEimikvKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387290472 686 EKESLEKNLSERKKKSA---QERCQAEEEIDEIRKSHQEELDKLRQLLKK 732
Cdd:smart00787 233 ELQELESKIEDLTNKKSelnTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
524-753 |
2.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 524 ENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaeqEKAKVT--EELAAATA 601
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL----AEAGVEdeEELRAALE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 602 QVSHLHlkmtAHQKKETELQVQLTESMKE--TDLLRGQLAQLQAELSEVQETSQQVQSKLKSekqsrrqlelrvtsLEEE 679
Cdd:COG4717 393 QAEEYQ----ELKEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEELEE--------------LREE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387290472 680 LTDLRTEKESLEKnlserkkksaqercqaEEEIDEIRKSHQEELDKLRQLLKKARVstDQAAAEQLSLVQAELQ 753
Cdd:COG4717 455 LAELEAELEQLEE----------------DGELAELLQELEELKAELRELAEEWAA--LKLALELLEEAREEYR 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
518-694 |
2.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 518 IQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQRYVEQSNL-MMEKRNNSLQTATENTQAR----------VLHAE 586
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYsWDEIDVASAEREIAELEAElerldassddLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 587 QEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTEsmketdlLRGQLAqlQAELSEVQETSQQVQSKLKSEKQSR 666
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-------LQDRLE--AAEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*...
gi 1387290472 667 RQLELRvTSLEEELTDLRTEKESLEKNL 694
Cdd:COG4913 763 VERELR-ENLEERIDALRARLNRAEEEL 789
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
626-732 |
3.17e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.22 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 626 ESMKETDL-LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEEltdLRTEKESLEKNlserKKKSAQE 704
Cdd:pfam11559 55 ESLNETIRtLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQK---LKNEKEELQRL----KNALQQI 127
|
90 100
....*....|....*....|....*...
gi 1387290472 705 RCQAEEEIdeirKSHQEELDKLRQLLKK 732
Cdd:pfam11559 128 KTQFAHEV----KKRDREIEKLKERLAQ 151
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
479-871 |
3.27e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 479 DKMDHLMTKVEELQKHSAGNSLLIPSMSVTMETSMIMS----NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNq 554
Cdd:PTZ00440 481 DSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNnnfkNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDE- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 555 ryvEQSNLMMEKRNNSLQTATENTQARvlhaeQEKAKVTEELAAATAQVSHLHLKMTAHQKKETELQVQLTESMKE--TD 632
Cdd:PTZ00440 560 ---KLKRSMKNDIKNKIKYIEENVDHI-----KDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYilNK 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 633 LLRGQLAQLQAELSEVQETsqqvQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEI 712
Cdd:PTZ00440 632 FYKGDLQELLDELSHFLDD----HKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENI 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 713 -----DEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLvqAELQTQWEAKCEQLLASAKN--EHLQQYQEVCTQRDAS 785
Cdd:PTZ00440 708 ikkqlNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKL--EVYKHQIINRKNEFILHLYEndKDLPDGKNTYEEFLQY 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 786 QQQLLQLEEKCSalqAQVTSLREqNAQHIKDLESKAQT--SGVEATAADPSEKVKKIMN----QVFQFLRGEFElEEFYS 859
Cdd:PTZ00440 786 KDTILNKENKIS---NDINILKE-NKKNNQDLLNSYNIliQKLEAHTEKNDEELKQLLQkfptEDENLNLKELE-KEFNE 860
|
410
....*....|..
gi 1387290472 860 GRTVLGTIMNTI 871
Cdd:PTZ00440 861 NNQIVDNIIKDI 872
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
519-693 |
3.53e-03 |
|
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: 40.90 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 519 QRIIQENERLKQEILEKSSRIKEQNDKISELI------ERNQRYVEQSNLMMEKRNnsLQTATENTQArvlHAEQEKAKV 592
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLEleelrqERDLLREEIQKLRGQIQQ--LRTELQELEA---QQQEEAESS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAATAQVShlhLKMTAHQKKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQ---SRRQL 669
Cdd:pfam09787 92 REQLQELEEQLA---TERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQsssSQSEL 168
|
170 180
....*....|....*....|....*.
gi 1387290472 670 ELRVTSLEEELTDLRTEKESL--EKN 693
Cdd:pfam09787 169 ENRLHQLTETLIQKQTMLEALstEKN 194
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
619-727 |
3.97e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 38.73 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 619 ELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSrrqlelrvtsLEEELTDLRTEKESLEKnlsERK 698
Cdd:pfam17675 13 ELDKQLEDAEKERDAYISFLKKLEKETPEELEELEKELEKLEKEEEE----------LLQELEELEKEREELDA---ELE 79
|
90 100
....*....|....*....|....*....
gi 1387290472 699 KKSAQERCQAEEEIDEIRKSHQEELDKLR 727
Cdd:pfam17675 80 ALEEELEALDEEEEEFWREYNALQLQLLE 108
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
635-762 |
4.33e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 635 RGQLAQLQAELSEvqetsqqvQSKLKSEKQSRRQLELRVTSLEEEltdlRTEKESLEKNLSERKKKSAQERCQ-AEEEID 713
Cdd:pfam05672 19 KRRQAREQREREE--------QERLEKEEEERLRKEELRRRAEEE----RARREEEARRLEEERRREEEERQRkAEEEAE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1387290472 714 EIRKSHQEELDKLRQLLKKARVSTdQAAAEQLSLVQAELQTQWEAKCEQ 762
Cdd:pfam05672 87 EREQREQEEQERLQKQKEEAEAKA-REEAERQRQEREKIMQQEEQERLE 134
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
639-753 |
4.65e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 639 AQLQAE------LSEVQETSQQVQSKLKSEKQSRR----QLELRVTSLEEELtDLRTEK-ESLEKNLSERKKKSAQERC- 706
Cdd:pfam12072 43 AKKEAEtkkkeaLLEAKEEIHKLRAEAERELKERRnelqRQERRLLQKEETL-DRKDESlEKKEESLEKKEKELEAQQQq 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1387290472 707 --QAEEEIDEIRKSHQEELDKLRQLlkkarvSTDQAAAEQLSLVQAELQ 753
Cdd:pfam12072 122 leEKEEELEELIEEQRQELERISGL------TSEEAKEILLDEVEEELR 164
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
614-735 |
4.68e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 614 QKKETELQVQLtESMKEtdllrgQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKN 693
Cdd:pfam20492 5 EREKQELEERL-KQYEE------ETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1387290472 694 lserKKKSAQERCQAEEEIDEI---RKSHQEELDKLRQLLKKARV 735
Cdd:pfam20492 78 ----KEQLEAELAEAQEEIARLeeeVERKEEEARRLQEELEEARE 118
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
522-918 |
5.09e-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: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 522 IQENERLKQEILEKSSrikeQNDKISELIERNQRYVeQSNLMM---EKRNNSlqtatentqARVLHAEQEKAKVTEELAA 598
Cdd:COG3096 238 LRENRMTLEAIRVTQS----DRDLFKHLITEATNYV-AADYMRhanERRELS---------ERALELRRELFGARRQLAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 599 AtaqvshlhlkmtahqkketelQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLK-SEKQSRRQLELrvtsle 677
Cdd:COG3096 304 E---------------------QYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqQEKIERYQEDL------ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 678 EELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKS---HQEELDKL----------RQLLKKARVSTDQA--AA 742
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQqtraiqyqqaVQALEKARALCGLPdlTP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 743 EQLSLVQAELQTQWEAKCEQLLA---------SAKNEHLQQYQEVC-----TQRDASQQQLLQLEEKCSALQAQVTSLrE 808
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLEleqklsvadAARRQFEKAYELVCkiageVERSQAWQTARELLRRYRSQQALAQRL-Q 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 809 QNAQHIKDLESK-AQTSGVEATAADPSEKVKKIMNQVFQFLRGEFELEEfysgrtvlgtimntikmvTLRLLNQHEQEKG 887
Cdd:COG3096 516 QLRAQLAELEQRlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEA------------------QLEELEEQAAEAV 577
|
410 420 430
....*....|....*....|....*....|.
gi 1387290472 888 ESSNEEEEEEDEAQARSPSGQSQAPLDRESQ 918
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAWLAAQ 608
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
720-831 |
5.32e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 720 QEELDKLRQLLKKARVSTDQAAAEQLSLVQ-AELQTQWEAKcEQLLASAKNEhLQQYQEVCTQRDASQQQLLQLEEKCSA 798
Cdd:COG1566 82 QAALAQAEAQLAAAEAQLARLEAELGAEAEiAAAEAQLAAA-QAQLDLAQRE-LERYQALYKKGAVSQQELDEARAALDA 159
|
90 100 110
....*....|....*....|....*....|...
gi 1387290472 799 LQAQVTSLREQNAQHIKDLESKAQTSGVEATAA 831
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
465-696 |
5.66e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 465 QHNTEIRMAVSKVAdkMDHLMTKVEELQKHSAGNSllipsmsvtmetsmimSNIQRIIQENERLKQEILEKSSRIKEQND 544
Cdd:pfam06008 35 ENAHKIQIEILEKE--LSSLAQETEELQKKATQTL----------------AKAQQVNAESERTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 545 KISELIERNQRY-VEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAkvTEELAAATAQVSHLhlkmtahQKKETEL 620
Cdd:pfam06008 97 NIKEINEKVATLgENDFALPSSDLSRMLAEAQrmlGEIRSRDFGTQLQNA--EAELKAAQDLLSRI-------QTWFQSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387290472 621 QVQlTESMKETdlLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSE 696
Cdd:pfam06008 168 QEE-NKALANA--LRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
620-753 |
6.38e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 620 LQVQLTESMKETDLLRGQLAQLQAELSevqetsqqvqsklkSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSErkk 699
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLS--------------LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAE--- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 700 kSAQERCQAEEEIDEIRKshqeELDKLRQLLKKAR----VSTDQAAA--EQLSLVQAELQ 753
Cdd:PRK09039 107 -LAGAGAAAEGRAGELAQ----ELDSEKQVSARALaqveLLNQQIAAlrRQLAALEAALD 161
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
512-749 |
6.41e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 512 SMIMSNIQRIIQENERLKQEILEKSSRIKEQNDKI-------SELIERNQRYVEQSNLMM---EKRNNSLQTATENTQAR 581
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIeilekelSSLAQETEELQKKATQTLakaQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 582 VLHAEQEKAKVTEelaaATAQVSHLHLKmtAHQKKETELQVQLTESMKETDLLRG-----QLAQLQAELSEVQETSQQVQ 656
Cdd:pfam06008 88 AEAIKNLIDNIKE----INEKVATLGEN--DFALPSSDLSRMLAEAQRMLGEIRSrdfgtQLQNAEAELKAAQDLLSRIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 657 SKLKSEKQSRRQLELRVTSL----EEELTDLRtekESLEKnlSERKKKSAQERCQAEEEIDEIRKSHQEELDKLR----Q 728
Cdd:pfam06008 162 TWFQSPQEENKALANALRDSlaeyEAKLSDLR---ELLRE--AAAKTRDANRLNLANQANLREFQRKKEEVSEQKnqleE 236
|
250 260
....*....|....*....|.
gi 1387290472 729 LLKKARVSTDQAAAeQLSLVQ 749
Cdd:pfam06008 237 TLKTARDSLDAANL-LLQEID 256
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
594-728 |
6.48e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 594 EELAAATAQVS--HLHLKMTAHQKKEtelqvqLTESMKEtdlLRGQLAQL------------QAELSEVQETSQQVQSKL 659
Cdd:pfam00038 142 EEVRELQAQVSdtQVNVEMDAARKLD------LTSALAE---IRAQYEEIaaknreeaeewyQSKLEELQQAAARNGDAL 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 660 KSEKQSRRQLELRVTSLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIrkshQEELDKLRQ 728
Cdd:pfam00038 213 RSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISEL----EAELQETRQ 277
|
|
| Sds3 |
pfam08598 |
Sds3-like; Repression of gene transcription is mediated by histone deacetylases containing ... |
633-784 |
6.89e-03 |
|
Sds3-like; Repression of gene transcription is mediated by histone deacetylases containing repressor-co-repressor complexes, which are recruited to promoters of target genes via interactions with sequence-specific transcription factors. The co-repressor complex contains a core of at least seven proteins. This family represents the conserved region found in Sds3, Dep1 and BRMS1-homolog p40 proteins.
Pssm-ID: 430099 Cd Length: 218 Bit Score: 39.26 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 633 LLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELtdlrtEKESLEKNLSERKKKSAQERcqaEEEI 712
Cdd:pfam08598 19 LYRNKLTALQTELQLLHQGSHPELLQYYRDLEEERDAELKRLRLREEY-----QLKRIDIETKADRTAAHQEF---KKLV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387290472 713 DEIRKSHQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYqEVCTQRDA 784
Cdd:pfam08598 91 KLLKEKLYDETTQKIYRLNEERRLLDLANTNSYLVDYKKTRSHTLAGLLNPNFTSRNNPVDPG-ELVTDRRS 161
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
615-762 |
8.07e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 615 KKETELQVQlteSMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLE-------EELTDLRTEK 687
Cdd:pfam15709 375 REELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQElqrkkqqEEAERAEAEK 451
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387290472 688 E---SLEKNLSERKKKSAQercQAEEEIDEIRKSHQEELDKLRQLLKKARvstdQAAAEQLSLVQAELQTQWEAKCEQ 762
Cdd:pfam15709 452 QrqkELEMQLAEEQKRLME---MAEEERLEYQRQKQEAEEKARLEAEERR----QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
514-844 |
8.61e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 514 IMSNIQRIIQENERLKQEILEKSSRIKEQNDKISEL-IERNQRYVEQSNLMMEKrnnsLQTATENTQARVLHAEQEKAKV 592
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEE----LQEELERLEEALEELREELEEA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 593 TEELAAATAQVSHLHLKMTAHQKKETELQ------VQLTESMKETDLLRGQLAQ-------------------LQAELSE 647
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSElisvdegyeaaieaalggrLQAVVVE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 648 VQETSQQVQSKLKSEKQSRRQ-LELR------------------------------------------------VTSLEE 678
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTfLPLDsikgteiqgndreilkniegflgvakdlvkfdpklrkalsyllggvlvVDDLDN 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 679 ELTDLR---------------------------------TEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDK 725
Cdd:TIGR02168 634 ALELAKklrpgyrivtldgdlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 726 LRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEQLLASAKNEHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTS 805
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1387290472 806 LREQNAQHIKDLES-KAQTSGVEATAADPSEKVKKIMNQV 844
Cdd:TIGR02168 794 LKEELKALREALDElRAELTLLNEEAANLRERLESLERRI 833
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
523-679 |
8.65e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.93 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 523 QENERLKQEILEKSSRIKEqndkisELIERNQRYVEQSNLMMEKRNNS--LQTATENTQARVLHAEQEKAKVTEElaaat 600
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMRE------ELELEQQRRFEEIRLRKQRLEEErqRQEEEERKQRLQLQAAQERARQQQE----- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 601 aqvsHLHLKMTAHQKKETELQVQLTESMKE-TDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEE 679
Cdd:pfam15709 427 ----EFRRKLQELQRKKQQEEAERAEAEKQrQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEE 502
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
615-753 |
8.87e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.05 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 615 KKETELQVQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQLELRVTSLEEELTDLRTEKEslekNL 694
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLV----TL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387290472 695 SERKKKSAQERCQAEEEIDEIRKSHqEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 753
Cdd:pfam10473 79 RSEKENLTKELQKKQERVSELESLN-SSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
525-725 |
8.95e-03 |
|
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: 39.79 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 525 NERLKQEILEKSSRiKEQNDKISELIE-RNQRYVEQSNLM-----MEKRNNSLQTATENTQARVLHAEqEKAKVTEelaa 598
Cdd:pfam15905 138 NELLKAKFSEDGTQ-KKMSSLSMELMKlRNKLEAKMKEVMakqegMEGKLQVTQKNLEHSKGKVAQLE-EKLVSTE---- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 599 ataqvshlhlKMTAHQKKETElqvQLTESMKETDLLRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQ----LELRVT 674
Cdd:pfam15905 212 ----------KEKIEEKSETE---KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEkeqeLSKQIK 278
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387290472 675 SLEEELTDLRTEKESLEKNLSERKKKSAQERCQAEEEIDEIRKSHQEELDK 725
Cdd:pfam15905 279 DLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-822 |
9.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 666 RRQLELRVTSLEEELTDLRTEKESLEKnlserkkksAQERCQAEEEIDEIRKSHQE---ELDKLRQLLKKARVSTDQAAA 742
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 743 EQLSLVQAELQTQWEakceqllasaknEHLQQYQEVCTQRDASQQQLLQLEEKCSALQ-AQVTSLREQNAQHIKDLESKA 821
Cdd:COG4913 291 ELLEAELEELRAELA------------RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERE 358
|
.
gi 1387290472 822 Q 822
Cdd:COG4913 359 R 359
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
517-813 |
9.14e-03 |
|
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: 40.11 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 517 NIQRIIQENERLKQEILEKSSRIKEQNDKISELIERNQ---RYVEQSNLMMEKRNNSLQTATE-----NTQARVLHAEQE 588
Cdd:pfam05557 42 QLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRlkkKYLEALNKKLNEKESQLADAREvisclKNELSELRRQIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 589 KAKV-----TEELAAATAQVSHLHLKMTAHQKKETELQVQLTES------MKETDllrgQLAQLQAELSEVQETSQQVQS 657
Cdd:pfam05557 122 RAELelqstNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLaeaeqrIKELE----FEIQSQEQDSEIVKNSKSELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 658 KL-KSEKQSRRQLE----LRVTS-----LEEELTDLRTEKESLEKnlserkkksaqerCQAEEEIDEIRKSH-QEELdkl 726
Cdd:pfam05557 198 RIpELEKELERLREhnkhLNENIenkllLKEEVEDLKRKLEREEK-------------YREEAATLELEKEKlEQEL--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 727 rqllkKARVSTDQAAAeqLSLVQAELQTqweAKCEQLLASAKNeHLQQYQEVCTQRDASQQQLLQLEEKCSALQAQVTSL 806
Cdd:pfam05557 262 -----QSWVKLAQDTG--LNLRSPEDLS---RRIEQLQQREIV-LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDL 330
|
....*..
gi 1387290472 807 REQNAQH 813
Cdd:pfam05557 331 NKKLKRH 337
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
634-853 |
9.84e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 634 LRGQLAQLQAELSEVQETSQQVQSKLKSEKQSRRQ-----LELRVTSLEEELTD-------LRTEKES-----LEKNLSE 696
Cdd:NF041483 96 LRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQqldqeLAERRQTVESHVNEnvawaeqLRARTESqarrlLDESRAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 697 RKKKSAQERCQAEEEIDEIRKSHQEELDKLR----QLLKKARvstdqAAAEQLsLVQAELQTQwEAK--CEQLLASAKNE 770
Cdd:NF041483 176 AEQALAAARAEAERLAEEARQRLGSEAESARaeaeAILRRAR-----KDAERL-LNAASTQAQ-EATdhAEQLRSSTAAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 771 HLQQYQEVCTQRDASQQQLLQLEEKCSALQAQ----VTSLREQNAQHIKDLES---------KAQTSGVEATAADPSEKV 837
Cdd:NF041483 249 SDQARRQAAELSRAAEQRMQEAEEALREARAEaekvVAEAKEAAAKQLASAESaneqrtrtaKEEIARLVGEATKEAEAL 328
|
250
....*....|....*.
gi 1387290472 838 KKIMNQVFQFLRGEFE 853
Cdd:NF041483 329 KAEAEQALADARAEAE 344
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
490-757 |
9.86e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 490 ELQKHSAGNSLLIPSMSVTMETSMIMsniQRIIQENERLkqeiLEKSSRIKEQNDKISE----LIERNQRYVEQSNLM-- 563
Cdd:PRK10929 83 ELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQL----LEKSRQAQQEQDRAREisdsLSQLPQQQTEARRQLne 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 564 MEKRNNSLQTAT---ENTQARVLHAEQ--EKAKVTE-ELAAATA----QVSHLHLKMtaHQKKETELQVQL--------- 624
Cdd:PRK10929 156 IERRLQTLGTPNtplAQAQLTALQAESaaLKALVDElELAQLSAnnrqELARLRSEL--AKKRSQQLDAYLqalrnqlns 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 625 ------------TESMKET--DLLRGQLAQLQA--ELSevQETSQQVQS-KLKSEKQsrRQLELRVTSLEEELTDLRTEK 687
Cdd:PRK10929 234 qrqreaeralesTELLAEQsgDLPKSIVAQFKInrELS--QALNQQAQRmDLIASQQ--RQAASQTLQVRQALNTLREQS 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387290472 688 ----------ESLEKNLSERKKKSAQErcQAEEEIDEIR--KSHQEE-LDKLRQLLKKARVSTDQAAAEQLSLVQAELQT 754
Cdd:PRK10929 310 qwlgvsnalgEALRAQVARLPEMPKPQ--QLDTEMAQLRvqRLRYEDlLNKQPQLRQIRQADGQPLTAEQNRILDAQLRT 387
|
...
gi 1387290472 755 QWE 757
Cdd:PRK10929 388 QRE 390
|
|
| |
