|
Name |
Accession |
Description |
Interval |
E-value |
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
132-957 |
0e+00 |
|
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: 998.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 132 KEALVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKT 211
Cdd:pfam05911 1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 212 KQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV 291
Cdd:pfam05911 81 KEWEKIKAELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEKEINSLKYELHVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 292 SKELEIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPV 371
Cdd:pfam05911 161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLVRKKLPGPAALAQMKLEVEMLGRDSGETRLRRSPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 372 KVSSPCKSPggysstGSEFSLDNAQKFQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQL 451
Cdd:pfam05911 241 KNSSPHLSP------DPDFSEDSLQTPHKENEFLTERLLAMEEETKMLKEALAKRNSELQASRNMCAKTASKLSQLEAQL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 452 QQNNSQKSSLEVCPNLNTSNPSSSISV-SEDGNDDSGSCSGSLST---NPSQQIKKEKDMAALERVESVNSHVELMDDFL 527
Cdd:pfam05911 315 EELNQGQVSMELASSQNPASNPPSLTSmSEDGSDDEVSCAESWASaliSELEHFKKEKPKTKSSCKSVGNSDLELMDDFL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 528 EMEKLACLPNLSSSNGSIDSKDGSGDQK----------SEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADI 597
Cdd:pfam05911 395 EMEKLACLSNDKPSNGSHSSSKSSNNKKgeesdsekdsSESTGKELVPVSSKDISLGKSLSWLQSRISVILESHVTQKSI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 598 QKIVGDIKCILQDVNACMDQEKPSEVHVHPEE----VSDLCPEQNLV---------EDCHLAEQKLQSIHQDLKNAVSRI 664
Cdd:pfam05911 475 GKILEDIRCALQDINDSLPEADSCLSSGHPSTdascDYITCKENSSVvekegsvsgDDKSSEETSKQSIQQDLSKAISKI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 665 HDFVLLLRNEVKAGQDTSIEGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGLASSEVETLSPD 744
Cdd:pfam05911 555 IDFVEGLSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSLLDVSSMEDEIKKHD 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 745 CIDKVALPESKVVDKDSSqeIYQNGCVHNEPGVPCDENRVSGY------ESDSKLQEIEELRSEKEKMAVD-------IE 811
Cdd:pfam05911 635 CIDKVTLSENKVAQVDNG--CSEIDNLSSDPEIPSDGPLVSGSndlkteENKRLKEEFEQLKSEKENLEVElasctenLE 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 812 GLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAI 891
Cdd:pfam05911 713 STKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELE 792
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012 892 LRCHELEEHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETIFVLGKQLKSFR-PQPEQ 957
Cdd:pfam05911 793 AKCLELQEQLERNEKKESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGKQLKALAsPQDAS 859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-953 |
3.67e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 150 WEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVaLSKTKQIEKMTMEFEKrmcdYE 229
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQI----LR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 230 QELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVhvvsKELEIRNEEKNMCIRSA 309
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 310 ESANKQHLEgvkKIAKLEAECQRLRSLvrkklpgpaaLAQMKLEVENLGRDSGDARQKRSPVKVSspckspggysstgsE 389
Cdd:TIGR02168 385 RSKVAQLEL---QIASLNNEIERLEAR----------LERLEDRRERLQQEIEELLKKLEEAELK--------------E 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 390 FSLDNAQKfQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQlqQNNSQKSSLEVCPNLNt 469
Cdd:TIGR02168 438 LQAELEEL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLK- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 470 snpsssisVSEDGNDDSGSCSGSLSTnpsqqikKEKDMAALERVESvnshvELMDDflemeklACLPNLSSSNGSIDSKD 549
Cdd:TIGR02168 514 --------NQSGLSGILGVLSELISV-------DEGYEAAIEAALG-----GRLQA-------VVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 550 GSGDQKSEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADIQKIV----GDIKCI--LQDVNACMDQEKPSEV 623
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllGGVLVVddLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 624 HVHPE-----------------EVSDLCPEQ---NLVEDCHLAEQKLQSIHQDLKNAVSRIHDFVLLLRNEVKAGQDTSI 683
Cdd:TIGR02168 647 IVTLDgdlvrpggvitggsaktNSSILERRReieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 684 EGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGL---ASSEVETLSPDCIDKVALPESKVVDKD 760
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 761 SSQEIYQ--NGCVHNEpgvpcdENRVSGYESD--SKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQR 836
Cdd:TIGR02168 807 ELRAELTllNEEAANL------RERLESLERRiaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 837 SNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIqrhrntSLVAEDDEE 916
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLE 954
|
810 820 830
....*....|....*....|....*....|....*..
gi 15221012 917 ADIKSKQERELSaaaekLAECQETIFVLGKQLKSFRP 953
Cdd:TIGR02168 955 EAEALENKIEDD-----EEEARRRLKRLENKIKELGP 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-357 |
1.82e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 84 EEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSGWEKADAEALALKNT 163
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 164 LESvtlskltAEDRAAHLDGALKECMRQIRNLKKDHEvklhdVALSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALS 243
Cdd:TIGR02168 763 IEE-------LEERLEEAEEELAEAEAEIEELEAQIE-----QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 244 RTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSKELEIRNEEKNMCIRSAESANKQHLEGVKKI 323
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270
....*....|....*....|....*....|....*
gi 15221012 324 AKLEAECQRLR-SLVRKKLpgpaALAQMKLEVENL 357
Cdd:TIGR02168 911 SELRRELEELReKLAQLEL----RLEGLEVRIDNL 941
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
55-284 |
3.45e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSKVAEDAvsgwEKADAEALALKNTlesvtlSKLTAEDRAAHLDGALKECMRQIRNLKKDhevklhdvalskTKQI 214
Cdd:COG4942 105 ELAELLRALYRL----GRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARREQAEELRAD------------LAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 215 EKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSL 284
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
794-959 |
7.08e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 874 QKLENELEDEKCNHQEAILRCHELEEHIQR-----HRNTSLVAEDDEEADIKSKQERELSAAA----EKLAECQETIFVL 944
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEEleaqiEQLKEELKALREALDELRAELTLLNEEAanlrERLESLERRIAAT 836
|
170
....*....|....*
gi 15221012 945 GKQLKSFRPQPEQMR 959
Cdd:TIGR02168 837 ERRLEDLEEQIEELS 851
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-374 |
2.53e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYdvqvktyenQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:COG1196 218 LKEELKELEAELLLL---------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKTKQI 214
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 215 EKmtmefEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSKE 294
Cdd:COG1196 369 EA-----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 295 LEIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPVKVS 374
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-366 |
2.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKL-------NEDVEDLNEKLSVANE 127
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 128 EIVTKEALVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEvklhdVA 207
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----EL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 208 LSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYE 287
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 288 VHVVSKELEIRNEEKNMcIRSAESANKQHLEGVKKIAKLEAECQRLRSL-----VRKKLPGPAALAQMKLEVENLGRDSG 362
Cdd:COG1196 479 LAELLEELAEAAARLLL-LLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligVEAAYEAALEAALAAALQNIVVEDDE 557
|
....
gi 15221012 363 DARQ 366
Cdd:COG1196 558 VAAA 561
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
70-267 |
4.89e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 70 DVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSG 149
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 150 WEKADAEALALKNTLESVT----LSKLTAEDRAAHLDGALkecMRQIRNLKKDHEVKLHDVAlSKTKQIEKMTMEFEKRM 225
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESfsdfLDRLSALSKIADADADL---LEELKADKAELEAKKAELE-AKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15221012 226 CDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEI 267
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-334 |
1.79e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSkvaedavSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVAL------ 208
Cdd:TIGR02168 790 QIEQLK-------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeie 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 209 SKTKQIEKMTMEFE---KRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLk 285
Cdd:TIGR02168 863 ELEELIEELESELEallNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL- 941
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15221012 286 yevhvvskeLEIRNEEKNMcirSAESANKQHLEGVKKIAKLEAECQRLR 334
Cdd:TIGR02168 942 ---------QERLSEEYSL---TLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
788-941 |
2.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 788 ESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVN 867
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012 868 QLKEKIQKLENELEDEKCNHQEAILRCHELE---EHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETI 941
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-340 |
4.09e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 56 EEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVtkeal 135
Cdd:TIGR02169 208 EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK----- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 136 vkqhskvaedavsgwEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLkkdhEVKLHDVaLSKTKQIE 215
Cdd:TIGR02169 283 ---------------DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL----EAEIDKL-LAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 216 KMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEvhvvSKEL 295
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE----LQRL 418
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15221012 296 EIRNEEKNMCIRSAESANKQHLEGVK-KIAKLEAECQRLRSLVRKK 340
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAADL 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-282 |
4.89e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEvKLHDVALSKTKQI 214
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN-ELEEEKEDKALEI 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221012 215 EKMTMEFE---KRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIK 282
Cdd:TIGR02169 451 KKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
54-301 |
6.77e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 54 GLEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKdfeEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIvtke 133
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI---- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 134 alvkqhskvaEDAVSGWEKADAEALALKNTLESvtlskLTAEDRAAHLDGALKECMRQIrnlkKDHEVKLHDVAlSKTKQ 213
Cdd:PHA02562 251 ----------EDPSAALNKLNTAAAKIKSKIEQ-----FQKVIKMYEKGGVCPTCTQQI----SEGPDRITKIK-DKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 214 IEKmtmEFEKRMCDYEQellrsaadsdalsrtLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSK 293
Cdd:PHA02562 311 LQH---SLEKLDTAIDE---------------LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
....*...
gi 15221012 294 ELEIRNEE 301
Cdd:PHA02562 373 EFVDNAEE 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-285 |
2.27e-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: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESvtlskltAEDRAAHLDGALKECMRQIR-NLKKDHEVKLHDVAlSKTKQ 213
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEeLLKKLEEAELKELQ-AELEE 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221012 214 IEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNmlvKVSEEKSRADAeIETLKSNLEMCEREIKSLK 285
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQLQARLDS-LERLQENLEGFSEGVKALL 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-329 |
3.73e-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: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 72 QVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEAlvkqhSKVaEDAVSGWE 151
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL-----SKL-EEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 152 KADAEalaLKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVA--LSKTKQIEKMTMEFEKRMCDYE 229
Cdd:TIGR02169 812 ARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEelEEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 230 QELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV-----------SKELEIR 298
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaelqRVEEEIR 968
|
250 260 270
....*....|....*....|....*....|...
gi 15221012 299 N-EEKNM-CIRSAESANKQHLEGVKKIAKLEAE 329
Cdd:TIGR02169 969 AlEPVNMlAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
788-966 |
5.16e-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: 47.36 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 788 ESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVN 867
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 868 QLKEKIQKLENELEDEKCNH-------QEAILRCHELEEHIQRHRNtSLVAEDDEEADIKSKQER---ELSAAAEKLAEC 937
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELeeleaelEELESRLEELEEQLETLRS-KVAQLELQIASLNNEIERleaRLERLEDRRERL 419
|
170 180
....*....|....*....|....*....
gi 15221012 938 QETIFVLGKQLKSFRPQPEQMRSPQTRNE 966
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEE 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-337 |
2.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 103 EYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAV-------SGWEKADAEALALKNTLE------SVTL 169
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeieKEIEQLEQEEEKLKERLEeleedlSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 170 SKLTAEDRA-AHLDGALKECMRQIRNLKKDHEVKLHDVALSKTKQI-------EKMTMEFEKRMCDYEQELLRSAADSDA 241
Cdd:TIGR02169 751 QEIENVKSElKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqaelsklEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 242 LSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSKEL-EIRNEEKNMcirsaesanKQHLEGV 320
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgDLKKERDEL---------EAQLREL 901
|
250
....*....|....*...
gi 15221012 321 K-KIAKLEAECQRLRSLV 337
Cdd:TIGR02169 902 ErKIEELEAQIEKKRKRL 919
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
794-941 |
2.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQ------------LRCMTESYRSLESRAAD 861
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelerldassddLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 862 LEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNTSL------VAEDDEEADIKSKQERELSAAAEKLA 935
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerfaaALGDAVERELRENLEERIDALRARLN 783
|
....*.
gi 15221012 936 ECQETI 941
Cdd:COG4913 784 RAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-325 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESVT---------LSKLTAEDRaaHLDGALKECMRQIRNLKKDHEvKLHD 205
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQkelkskekeLKKLNEEKK--ELEEKVKDLTKKISSLKEKIE-KLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 206 VALSKTKQIEKMTMEFEKRMCDYEQELLRSAADS--DALSRTLQERSNMLVKVSEEKSRAD---AEIETLKSNLEMCERE 280
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEELKQTQKSLKKKQEEKQELIDqkeKEKKDLIKEIEEKEKK 611
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15221012 281 IKSLKYEVHVVSKELEIRNEEKnMCIRSAESANKQHLEGVKKIAK 325
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSII-KNIKSKKNKLKQEVKQIKETIK 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
798-941 |
2.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 798 ELRSEKEKmaVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLE 877
Cdd:COG1196 217 ELKEELKE--LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221012 878 NELEDEKCNHQEAILRCHELEEHIQR--HRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETI 941
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEEleEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
34-462 |
3.01e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 34 EAIKKPKYVQISVEQYTHFTGLEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQI----DAYDEKVHEYEEQVQ 109
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqnSMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 110 KLNED-----------VEDLNEKLSVANEEIV---TKEALVKQHSKVAEDAVS-------------GWEKADAEALALKN 162
Cdd:pfam15921 328 QLRSElreakrmyedkIEELEKQLVLANSELTearTERDQFSQESGNLDDQLQklladlhkrekelSLEKEQNKRLWDRD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 163 TLESVTLSKLTAE--DR---AAHLDGALK----ECM----RQIRNLKKDHEvKLHDVAlSKTKQIEKmTMEFEKRMCdye 229
Cdd:pfam15921 408 TGNSITIDHLRREldDRnmeVQRLEALLKamksECQgqmeRQMAAIQGKNE-SLEKVS-SLTAQLES-TKEMLRKVV--- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 230 QELLRSAADSDALSRTLQERSNMLvkvsEEKSRA----DAEIETLKSNLEMCEREIKSLKYE------VHVVSKELEIRN 299
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASL----QEKERAieatNAEITKLRSRVDLKLQELQHLKNEgdhlrnVQTECEALKLQM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 300 EEKNMCIRSAesanKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPVKVSSPCKS 379
Cdd:pfam15921 558 AEKDKVIEIL----RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 380 PGGYSSTGSEfSLDNAQKFQKE-----NEFLTER--LLAMEEETKMLKEALAKRNSELLESRNlcaQSTSKLQSLEAQLQ 452
Cdd:pfam15921 634 KVKLVNAGSE-RLRAVKDIKQErdqllNEVKTSRneLNSLSEDYEVLKRNFRNKSEEMETTTN---KLKMQLKSAQSELE 709
|
490
....*....|
gi 15221012 453 QNNSQKSSLE 462
Cdd:pfam15921 710 QTRNTLKSME 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
794-884 |
3.85e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 794 QEIEELRSEKEKmavdiegLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:COG4942 20 DAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90
....*....|.
gi 15221012 874 QKLENELEDEK 884
Cdd:COG4942 93 AELRAELEAQK 103
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-463 |
4.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 33 KEAIKKPKYVQISVEQYTHFTGLEEQIKSYDVQIKgydVQVKTYENQVESYEEQVKDFEEQidayDEKVHEYEEQVQKLN 112
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 113 EDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVsgwEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQI 192
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEELERLKKRLTGLTP---EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 193 RNLKK--------------DHEVKLHDVALSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERS-------- 250
Cdd:PRK03918 429 EELKKakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlkel 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 251 -NMLVKVSEEKSRADA-EIETLKSNLEMCEREIKSLKYEVHVVsKELEIRNEEKNMCIRSAESANKQHL-----EGVKKI 323
Cdd:PRK03918 509 eEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLkeleeLGFESV 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 324 AKLEAECQRLRSLVRKKL---PGPAALAQMKLEVENLGRDSGDARQKRSPVKvsspckspggysstgSEFSLDNAQKFQK 400
Cdd:PRK03918 588 EELEERLKELEPFYNEYLelkDAEKELEREEKELKKLEEELDKAFEELAETE---------------KRLEELRKELEEL 652
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221012 401 ENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQLQQNNSQKSSLEV 463
Cdd:PRK03918 653 EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-451 |
5.06e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 54 GLEEQIKSYD---VQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNE--DVEDLNEKLSVANEE 128
Cdd:PRK03918 225 KLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 129 IVTKEALVKQHSKVAEDAVSGWEKADAEALALKNTLESvtlskltaedraahLDGALKECMRQIRNLKKDHEvkLHDVAL 208
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--------------LKKKLKELEKRLEELEERHE--LYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 209 SKTKQIEKMtmefEKRMCDYEQELLrsAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEmcerEIKSLKYEV 288
Cdd:PRK03918 369 AKKEELERL----KKRLTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKC 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 289 HVVSKELEirNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLgrdsgdaRQKR 368
Cdd:PRK03918 439 PVCGRELT--EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQL-------KELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 369 SPVKvsspckspggysstgsEFSLDNAQKFQKENEFLTERLLAMEEETKMLKEALAKRnsELLESRNlcAQSTSKLQSLE 448
Cdd:PRK03918 510 EKLK----------------KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL--EELKKKL--AELEKKLDELE 569
|
...
gi 15221012 449 AQL 451
Cdd:PRK03918 570 EEL 572
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-335 |
7.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 74 KTYENQVESYEEQVK---DFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEivtKEALVKQHSKVAEdavsgw 150
Cdd:PRK03918 172 KEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKEEIEE------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 151 ekADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKTK-QIEKMTMEFEKRMCDYE 229
Cdd:PRK03918 243 --LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 230 QELlrsaadsDALSRTLQERSNM---LVKVSEEKSRADAEIETLKSNLEMCErEIKSLKYEVHVVSKELEIRNEEKnmCI 306
Cdd:PRK03918 321 EEI-------NGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEK--LE 390
|
250 260
....*....|....*....|....*....
gi 15221012 307 RSAESANKQHLEGVKKIAKLEAECQRLRS 335
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
780-906 |
1.19e-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: 42.05 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 780 DENRVSGYESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEqllADIRSQFDSAQRSNRLADTQLrcmtesyRSLESRA 859
Cdd:pfam09787 40 DSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQL-------ATERSAR 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15221012 860 ADLEIDVNQLKEKIQKLENELEDEKCNHQEailRCHELEEHIQRHRN 906
Cdd:pfam09787 110 REAEAELERLQEELRYLEEELRRSKATLQS---RIKDREAEIEKLRN 153
|
|
| V_ATPase_I |
pfam01496 |
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase ... |
855-945 |
1.40e-03 |
|
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal. It has roles in proton transport and assembly of the V-type ATPase complex. This subunit is encoded by two homologous gene in yeast VPH1 and STV1.
Pssm-ID: 460232 [Multi-domain] Cd Length: 748 Bit Score: 42.85 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 855 LESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNTS-LVAEDDEEADIKSKQERELSAAAEK 933
Cdd:pfam01496 60 LETPEAPSPREIDELEEKLEKLENELRELNENYETLKRNYNELTELRHVLRKAQeFFDRASGEQEEIRAASSDQEEDNAL 139
|
90
....*....|..
gi 15221012 934 LAECQETIFVLG 945
Cdd:pfam01496 140 LLDDVELGFVAG 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
792-939 |
1.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 792 KLQEIEELRsEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKE 871
Cdd:COG1196 217 ELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 872 KIQKLENELEDEKCNHQEAILRCHELEEHIQR--HRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQE 939
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAEleEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
56-269 |
1.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 56 EEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIvtKEAL 135
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 136 VKQ--------------HSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKEcmrqIRNLKKDHEV 201
Cdd:COG3883 93 RALyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221012 202 KLHDVAlSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIET 269
Cdd:COG3883 169 AKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-282 |
1.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQID--AYDEKVHEYEEQVQKL---NEDVEDLNEKLSVANEEI 129
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLdasSDDLAALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 130 VT----KEALVKQHSKVA---EDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVK 202
Cdd:COG4913 702 EEleeeLDELKGEIGRLEkelEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 203 LHDvalsKTKQIEKMTMEFEKRMCDYEQEL---LRSAADSDALSRTLQERSnmLVKVSEE-----KSRADAEIETLKSNL 274
Cdd:COG4913 782 LNR----AEEELERAMRAFNREWPAETADLdadLESLPEYLALLDRLEEDG--LPEYEERfkellNENSIEFVADLLSKL 855
|
....*...
gi 15221012 275 EMCEREIK 282
Cdd:COG4913 856 RRAIREIK 863
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
788-956 |
2.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 788 ESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVN 867
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 868 QLKEKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETIFVLGKQ 947
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205
|
....*....
gi 15221012 948 LKSFRPQPE 956
Cdd:COG4372 206 EKLIESLPR 214
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
792-956 |
2.31e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 792 KLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRC--MTESYRSLESRAADLEIDVNQL 869
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 870 KEKIQKLEnELEDEKCNHQEAIlrcHELEEHIQRHRNTSLVAEDDEEADIK---SKQERELSAAAEKLAECQETIFVLGK 946
Cdd:COG4717 152 EERLEELR-ELEEELEELEAEL---AELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|
gi 15221012 947 QLKSFRPQPE 956
Cdd:COG4717 228 ELEQLENELE 237
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
55-325 |
2.65e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELET 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 135 LVKQHSK---------VAEDAVSGWEKA--DAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNlkKDHEVKL 203
Cdd:pfam19220 203 QLDATRArlralegqlAAEQAERERAEAqlEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRD--RDEAIRA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 204 HDVALSKTkQIEKMTmeFEKRMCDYEQELLRSA---ADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEmcERe 280
Cdd:pfam19220 281 AERRLKEA-SIERDT--LERRLAGLEADLERRTqqfQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLS--DR- 354
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15221012 281 IKSLKYEVHVVSKELEIRNEEKNMCIRsAESANKQHLEGVKKIAK 325
Cdd:pfam19220 355 IAELTKRFEVERAALEQANRRLKEELQ-RERAERALAQGALEIAR 398
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
794-941 |
3.32e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRsnrladtQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA-------QLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 874 QKLENEL--------EDEKCNHQEAIL-----RCHELEEHIQRHRNTSLVAEDDEEadIKSKQERELSAAAEKLAECQET 940
Cdd:TIGR02169 927 EALEEELseiedpkgEDEEIPEEELSLedvqaELQRVEEEIRALEPVNMLAIQEYE--EVLKRLDELKEKRAKLEEERKA 1004
|
.
gi 15221012 941 I 941
Cdd:TIGR02169 1005 I 1005
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-275 |
4.34e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 85 EQVKDFEEQIDAYDEKVHEYEEQVQKLNEdvedLNEKLSVANEEIVTKEALVKQHSKV--AEDAVSGWEKADAEALALKN 162
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 163 TLESvtlskltAEDRAAhldgALKECMRQIRNLKKDHEVKLhdvalsktkqiEKMTMEFEKRMCDYEQELLRSAADSDAL 242
Cdd:COG4717 147 RLEE-------LEERLE----ELRELEEELEELEAELAELQ-----------EELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190
....*....|....*....|....*....|...
gi 15221012 243 SRTLQERSNMLVKVSEEKSRADAEIETLKSNLE 275
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
71-369 |
4.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 71 VQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSGW 150
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 151 EKADAEALALKNTLESVTLSKLTAEDR---AAHLDGALK--ECMRQIRnlkkdhEVKLHDVALSKTKQIEKMTMEFEkrm 225
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERveeAEALLEAGKcpECGQPVE------GSPHVETIEEDRERVEELEAELE--- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 226 cDYEQELLRSAADSDALSrTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVhvvsKELEIRNEEKNmc 305
Cdd:PRK02224 486 -DLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA----AELEAEAEEKR-- 557
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221012 306 irsaESANKQHLEGVKKIAKLeAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRS 369
Cdd:PRK02224 558 ----EAAAEAEEEAEEAREEV-AELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE 616
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
213-291 |
4.97e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 39.18 E-value: 4.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221012 213 QIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV 291
Cdd:pfam05266 106 KLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELEFEAT 184
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
81-444 |
6.25e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 81 ESYEEQVKDFEEQ-IDAYdEKVHEYeeQVQKLNEDVEDLNEKLS----VANEEIV----TKEALVKQHSKVAEDAVSGWE 151
Cdd:PTZ00108 976 SDALDILKEFYLVrLDLY-KKRKEY--LLGKLERELARLSNKVRfikhVINGELVitnaKKKDLVKELKKLGYVRFKDII 1052
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 152 KADAEALALKNTLESVTLSKLTAEDRAAHLDGAL--------------KEcmrQIRNLKKDHEVKLHDVALSKTKQIEKM 217
Cdd:PTZ00108 1053 KKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVsydyllsmpiwsltKE---KVEKLNAELEKKEKELEKLKNTTPKDM 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 218 TME----FEKRMCDYEQELLRSAADsdalSRTLQERSNMLVKVSEEKSRADAEiETLKSNLEMCEREIKSLKYEVHVVSK 293
Cdd:PTZ00108 1130 WLEdldkFEEALEEQEEVEEKEIAK----EQRLKSKTKGKASKLRKPKLKKKE-KKKKKSSADKSKKASVVGNSKRVDSD 1204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 294 ELeIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPVKV 373
Cdd:PTZ00108 1205 EK-RKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQY 1283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221012 374 SS--PCKSPGGYSSTGSEFSLDNAQKFQKeneFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKL 444
Cdd:PTZ00108 1284 SPppPSKRPDGESNGGSKPSSPTKKKVKK---RLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLL 1353
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
794-936 |
6.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221012 874 QKLENELEDEKCNHQEAILRCHELEEHIQRHRNTSLVAEDDE------EADIKSKQERELSAAAEKLAE 936
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLeeleeaEEALLERLERLEEELEELEEA 429
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
57-200 |
6.86e-03 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 38.11 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 57 EQIKSYDVQIKGYDV---QVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEqvqkLNEDVEDLNEKLSVANEEIVTKE 133
Cdd:pfam06810 1 EQADKVMEAENGKDIpkaKFDEVNTERDTLKEQLATRDKQLKDLKKVAKDNEE----LQKQIDELQAKNKDAEADYEAKI 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012 134 ALVKQHSKVaEDAVSGWEKADAEALALKNTLESVTLSKltaedraahlDGALKECMRQIRNLKKDHE 200
Cdd:pfam06810 77 ADLKFDNAI-KLALKGAKAKNEKAVKALLDKDKLKLKD----------DGTLIGLDEQIEGLKESDK 132
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-362 |
6.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 112 NEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSGWEKADAEALALKNTLEsvtlsklTAEDRAAHLDGALKECMRQ 191
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 192 IRNLKKDHEVKLHDVA-----LSKTKQIEKMTMEFEKrmcDYEQELLRSAADSDALSRTLQERSNMLVKVSEEksradae 266
Cdd:COG4942 92 IAELRAELEAQKEELAellraLYRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAEELRADLAE------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 267 IETLKSNLEMCEREIKSLKYEVHVVSKELEIRNEEKNMCIRSAESANKQHLegvKKIAKLEAECQRLRSLVrKKLPGPAA 346
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALI-ARLEAEAA 237
|
250
....*....|....*.
gi 15221012 347 LAQMKLEVENLGRDSG 362
Cdd:COG4942 238 AAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-275 |
8.17e-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: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 84 EEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANeeivtkealvkQHSKVAEDAVSgWEKADAEALALKNT 163
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----------RLAEYSWDEID-VASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 164 LESVTLSKL---TAEDRAAHLDGALKECMRQIRNLKKD---HEVKLHDvALSKTKQIEKMTMEFEKRMCDYEQELL---R 234
Cdd:COG4913 677 LERLDASSDdlaALEEQLEELEAELEELEEELDELKGEigrLEKELEQ-AEEELDELQDRLEAAEDLARLELRALLeerF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15221012 235 SAADSDALSRTLQERsnmlvkVSEEKSRADAEIETLKSNLE 275
Cdd:COG4913 756 AAALGDAVERELREN------LEERIDALRARLNRAEEELE 790
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
791-936 |
8.22e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 791 SKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEidvnqlk 870
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE------- 743
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221012 871 EKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNtslvAEDDEEADIKSKQERELSAAAEKLAE 936
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE----ALNDLEARLSHSRIPEIQAELSKLEE 805
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
55-303 |
8.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLS-------VANE 127
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKelkeerdELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 128 EIVT-KEALVKQHSKVAEDAVSGWEKADAEAL--ALKNTLESVTLSKltAEDRAahLDGALKECMRQIRNLKKDHEVKlh 204
Cdd:COG1340 86 KLNElREELDELRKELAELNKAGGSIDKLRKEieRLEWRQQTEVLSP--EEEKE--LVEKIKELEKELEKAKKALEKN-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012 205 dvalSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSL 284
Cdd:COG1340 160 ----EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250
....*....|....*....
gi 15221012 285 KYEVHVVSKELEIRNEEKN 303
Cdd:COG1340 236 QKELRELRKELKKLRKKQR 254
|
|
|