|
Name |
Accession |
Description |
Interval |
E-value |
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
79-932 |
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: 1122.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 79 KDALVKQHAKVAEEAVSGWEKAEAEASALKLQLETVTLAKLAAEERAAHLDGALKECMKQVRTVKEEGEQKLHDVVFAKT 158
Cdd:pfam05911 1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 159 KQWEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGDLLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEIHVV 238
Cdd:pfam05911 81 KEWEKIKAELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEKEINSLKYELHVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 239 SKELEIRNEEKNMSVRSADVATKQHMEDVKKISKLEAECQRLRGLVRKKLPGPAALAQMKMEVESLGRDYGESRLRRSPA 318
Cdd:pfam05911 161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLVRKKLPGPAALAQMKLEVEMLGRDSGETRLRRSPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 319 KNSSFHrpmspMSPVPDYAFENLQHMQKENEFLTARLLSMEDETKMLKEALAKRNSELQTSRNMYAKTAGKLRGLEVQML 398
Cdd:pfam05911 241 KNSSPH-----LSPDPDFSEDSLQTPHKENEFLTERLLAMEEETKMLKEALAKRNSELQASRNMCAKTASKLSQLEAQLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 399 TGSQRkstsnpnmDIHFDGALSQNG-SNPPSMTSMSEDGVDDEGSCTESWANALVSELSHIKKEKG-AKSSVTEGSN-RL 475
Cdd:pfam05911 316 ELNQG--------QVSMELASSQNPaSNPPSLTSMSEDGSDDEVSCAESWASALISELEHFKKEKPkTKSSCKSVGNsDL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 476 ELMDDFLEMEKLACLS--SEANGHVSTVEkmkiddtEASLSGITERDGVKDSQSVLALPGTPSNKLQLSDSSPLLKLQSR 553
Cdd:pfam05911 388 ELMDDFLEMEKLACLSndKPSNGSHSSSK-------SSNNKKGEESDSEKDSSESTGKELVPVSSKDISLGKSLSWLQSR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 554 ISSLLDSESPQNNAGNILDSIRNILKDIEDE--------------ADSSNDSKTHHGDMVEVADNGSLM---KHSSSGSK 616
Cdd:pfam05911 461 ISVILESHVTQKSIGKILEDIRCALQDINDSlpeadsclssghpsTDASCDYITCKENSSVVEKEGSVSgddKSSEETSK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 617 HAMDQELVNAILKIQDFVKSLDQEVSKFQGQSSDCDGLCDKIQQFSALVEKALSNENVLNDIVMTLSLILSGTSEIKFMM 696
Cdd:pfam05911 541 QSIQQDLSKAISKIIDFVEGLSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSL 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 697 LKENTKEADNNNLDYVDKVTLLENKVqlepLKDSISGPCLPRSSSDPEI--EGPTDSG-CDVKTAVQICSSEEFEQLKSE 773
Cdd:pfam05911 621 LDVSSMEDEIKKHDCIDKVTLSENKV----AQVDNGCSEIDNLSSDPEIpsDGPLVSGsNDLKTEENKRLKEEFEQLKSE 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 774 KLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENEIKVLQSKIEV 853
Cdd:pfam05911 697 KENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEA 776
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002254057 854 LTAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVDEDADTKAKQEKEIAAAAEKLAECQETILILGRQLQSMRPP 932
Cdd:pfam05911 777 LEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGKQLKALASP 855
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-919 |
9.29e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLN------EKVKALNEDLSAAQSEITTKDaLVKQHAKVAE------EAVSGWEKAEAEASALKLQLETVT 115
Cdd:TIGR02168 195 LNELERQLKSLErqaekaERYKELKAELRELELALLVLR-LEELREELEElqeelkEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 116 LAKLAAEERAAHLDGALKECMKQVRTVkeEGEQKLHDvvfAKTKQWEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEE 195
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRL--EQQKQILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 196 RGDLLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKELE-IRNEEKNMSVRsadvatkqhmedvkkISKLE 274
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAsLNNEIERLEAR---------------LERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 275 AECQRLRGlvrkklpgpaalaqmkmEVESLGRDYGESRLRRSPaknssfhrpmspmspvpdyafENLQHMQKENEFLTAR 354
Cdd:TIGR02168 414 DRRERLQQ-----------------EIEELLKKLEEAELKELQ---------------------AELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 355 LLSMEDETKMLKEALAKRNSELQTSRNMYAKTAGKLRGLEVQMltgsQRKSTSNPNMDIHFDGALSQNGSNPPSMTSMse 434
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ----ENLEGFSEGVKALLKNQSGLSGILGVLSELI-- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 435 dgvddegSCTESWANALVSELShikkeKGAKSSVTEGSNRLELMDDFLEmeklaclsseanghvstvekmkiddtEASLS 514
Cdd:TIGR02168 530 -------SVDEGYEAAIEAALG-----GRLQAVVVENLNAAKKAIAFLK--------------------------QNELG 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 515 GITerdgvkdsqsVLALPGTPSNKLQLSDSSPLLKLQSRISSLLDSESPQNNAGNILDSIRNILKDIEDEADSSNDSKTH 594
Cdd:TIGR02168 572 RVT----------FLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 595 HGDMVEVADNGSLMkhSSSGSKHAMDQELVNAILKIQDFVKSLDQEVSKFQGQssdcdglCDKIQQfsALVEKALSNENV 674
Cdd:TIGR02168 642 RPGYRIVTLDGDLV--RPGGVITGGSAKTNSSILERRREIEELEEKIEELEEK-------IAELEK--ALAELRKELEEL 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 675 LNDIVMTLSLILSgtSEIKFMMLKENTKEADNNNLDYVDKVTLLEnkVQLEPLKDSISGPCLPRSSSDPEIEgptdSGCD 754
Cdd:TIGR02168 711 EEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQLS--KELTELEAEIEELEERLEEAEEELA----EAEA 782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 755 VKTAVQicssEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLE 834
Cdd:TIGR02168 783 EIEELE----AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 835 SRKAELENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNsmcvDEDADTKAKQEKeIAAAAEKLAE 914
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREK-LAQLELRLEG 933
|
....*
gi 1002254057 915 CQETI 919
Cdd:TIGR02168 934 LEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
765-928 |
3.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENEI 844
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 845 KVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMC--VDEDADTKAKQEKEIAAAAEKLAECQETILIL 922
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaeLAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
....*.
gi 1002254057 923 GRQLQS 928
Cdd:COG1196 406 EEAEEA 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
764-958 |
4.65e-09 |
|
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: 60.84 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENE 843
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIEvltaELDDERQNHQEDItryRDLEEKIERYENERNSMCVDEDADTKAKQEKEIAAAAEKLAECQETIlilg 923
Cdd:TIGR02168 402 IERLEARLE----RLEDRRERLQQEI---EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL---- 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002254057 924 RQLQSMRPPAESMGSSPNQR---MEDFLQDAAGTTEGV 958
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARldsLERLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-288 |
8.68e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 46 AHLTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKVAEEAVSGWEKAEAEASALKLQLETVTLAKLAAEERA 125
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 126 AHLDGALKEcmkqvrtvkEEGEQKLHDvvfAKTKQWEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGDLLMKIDE 205
Cdd:COG1196 319 EELEEELAE---------LEEELEELE---EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 206 EKARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKELEIRNEEKNMSVRSADVATKQHMEDVKKISKLEAECQRLRGLVR 285
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
...
gi 1002254057 286 KKL 288
Cdd:COG1196 467 ELL 469
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-232 |
2.98e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 43 ETYAHLTESEEQVKTLnEKVKALNEDLSAAQSEITTKDALVKQ-HAKVAEEAVsgwEKAEAEASALKLQLETVTLAKLAA 121
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlRLWFAQRRL---ELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 122 EERAAHLDGALKECMKQVRTV----KEEGEQKLhdvvfaktKQWEKIKAEFEAKLLEFEQELIRAGAENDA--------- 188
Cdd:COG4913 315 EARLDALREELDELEAQIRGNggdrLEQLEREI--------ERLERELEERERRRARLEALLAALGLPLPAsaeefaalr 386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002254057 189 --LSRSLEERGDLLMKIDEEKARAEAEIEVLKNTIQSGEREINSLK 232
Cdd:COG4913 387 aeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
763-963 |
1.64e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 763 SSEEFEQLKSEKLNLE--------------AELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAE 828
Cdd:TIGR02168 265 LEEKLEELRLEVSELEeeieelqkelyalaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 829 SYKSLESRKAELENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMcvdedadtkakqEKEIAAA 908
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL------------EARLERL 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002254057 909 AEKLAECQETILILGRQLQSMRPPAESMGSSPNQRMEDFLQDAAGTTEGVEYSQK 963
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
758-912 |
3.40e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.16 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 758 AVQICSSEEfeQLKSEKL-NLEAELSKCNEVIEetKFR-FKELEKSLEELTSKLV--ASEKSNSLAETQLKCMAESYKSL 833
Cdd:PRK05771 30 VVHIEDLKE--ELSNERLrKLRSLLTKLSEALD--KLRsYLPKLNPLREEKKKVSvkSLEELIKDVEEELEKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 834 ESRKAELENEIKVLQSKIEVLT----AELDDERQNHQEDITRY-----RDLEEKIERYENERNSMCVDEDAD-------T 897
Cdd:PRK05771 106 EEEISELENEIKELEQEIERLEpwgnFDLDLSLLLGFKYVSVFvgtvpEDKLEELKLESDVENVEYISTDKGyvyvvvvV 185
|
170
....*....|....*
gi 1002254057 898 KAKQEKEIAAAAEKL 912
Cdd:PRK05771 186 LKELSDEVEEELKKL 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
764-927 |
5.03e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKL-----NLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKA 838
Cdd:COG1196 219 KEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 839 ELENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNsmcvDEDADTKAKQEKEIAAAAEKLAECQET 918
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE----EAEEELEEAEAELAEAEEALLEAEAEL 374
|
....*....
gi 1002254057 919 ILILGRQLQ 927
Cdd:COG1196 375 AEAEEELEE 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
764-928 |
7.82e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENE 843
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERnsmcvDEDADTKAKQEKEIAAAAEKLAECQETILILG 923
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-----EEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
....*
gi 1002254057 924 RQLQS 928
Cdd:COG1196 470 EEAAL 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
763-918 |
2.26e-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: 51.99 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 763 SSEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSklvasEKSNSLAEtqlkcMAESYKSLES---RKAE 839
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-----EIDKLLAE-----IEELEREIEEerkRRDK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 840 LENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVDEDADTKAKQEK---------EIAAAAE 910
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlnaAIAGIEA 434
|
....*...
gi 1002254057 911 KLAECQET 918
Cdd:TIGR02169 435 KINELEEE 442
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
764-930 |
5.56e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENE 843
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVDEDADTKAKQEKEIAAAAEKLAECQETILILG 923
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
....*..
gi 1002254057 924 RQLQSMR 930
Cdd:COG1196 454 LEEEEEA 460
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
765-927 |
7.17e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENEI 844
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 845 KVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVDEDADTKAKQEKEIAAAAEKLAECQETILILGR 924
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
...
gi 1002254057 925 QLQ 927
Cdd:COG4372 205 AEK 207
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
765-923 |
1.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAE-----TQLKCMAESYKSLESRKAE 839
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 840 LENEIKVLQSKIEVLTAELDDERQNH-QEDITRYRDLEEKIERYENERNSmcVDEDADTKAKQ------EKEIAAAAEKL 912
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEE--AQEELEELEEEleqlenELEAAALEERL 245
|
170
....*....|.
gi 1002254057 913 AECQETILILG 923
Cdd:COG4717 246 KEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
773-914 |
1.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 773 EKLN-LEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMA--ESYKSLESRKAELEN---EIKV 846
Cdd:COG4913 610 AKLAaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaeREIAELEAELERLDAssdDLAA 689
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002254057 847 LQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVDEDADTKAKQEKEIAAAAEKLAE 914
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-310 |
2.10e-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: 48.91 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 49 TESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKVAEEAVSGWEKAEAEASALKLQLETVTLAKLAAEERAAHL 128
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 129 DGAL---KECMKQVRTVKEEGEQKLHDVVFA---------------KTKQWEKIKAE---FEAKLLEFEQELIRAGAEND 187
Cdd:TIGR02169 750 EQEIenvKSELKELEARIEELEEDLHKLEEAlndlearlshsripeIQAELSKLEEEvsrIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 188 ALSRSLEERGDLLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKEL-EIRNEEKNMsvrsadvatKQHMED 266
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgDLKKERDEL---------EAQLRE 900
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002254057 267 VK-KISKLEAECQRLRGLVRKKLpgpAALAQMKMEVESLGRDYGE 310
Cdd:TIGR02169 901 LErKIEELEAQIEKKRKRLSELK---AKLEALEEELSEIEDPKGE 942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
48-397 |
2.31e-05 |
|
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: 48.58 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLNEKVKALNEDLSAAQSEITTK-DALVKQHAKVAEEAVSGWE-----------KAEAEASALKLQLETVt 115
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRIEQLISEHEveitgltekasSARSQANSIQSQLEII- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 116 laklaaEERAAHLDGALkecMKQVRTVKEEGEQKLHDVVFAKTKQWEKIKaEFEAKLLEFEQELIRAGAENDALSRSLEE 195
Cdd:pfam15921 305 ------QEQARNQNSMY---MRQLSDLESTVSQLRSELREAKRMYEDKIE-ELEKQLVLANSELTEARTERDQFSQESGN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 196 RGDLLMKI--DEEKARAEAEIEVLKN------------TIQSGEREINSLKYEIHVVSKELEIRNEEKNMSVRSADVATK 261
Cdd:pfam15921 375 LDDQLQKLlaDLHKREKELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 262 QHMEDVKKISKLEAECQRLRGLVRKKLpgpAALAQMKMEVESLGRDYG------ESRLRRSPAKNSSFHRPMSPMspvpD 335
Cdd:pfam15921 455 GKNESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSdltaslQEKERAIEATNAEITKLRSRV----D 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002254057 336 YAFENLQHMQKENEFLTarllSMEDETKMLKEALAKRNSELQTSR----NM------YAKTAGKLRGLEVQM 397
Cdd:pfam15921 528 LKLQELQHLKNEGDHLR----NVQTECEALKLQMAEKDKVIEILRqqieNMtqlvgqHGRTAGAMQVEKAQL 595
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-276 |
2.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLNEKVKALNEDLSAAQSEIttkDALVKQHAKVAEEAvsgwEKAEAEASALKLQLETVTLAKLAAEERAAH 127
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEEL---AELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 128 LDGALKECMKQVRTVKEEGEQKLHDVVFAKTKQ---------WEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGD 198
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLeeleeaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002254057 199 LLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEIH-VVSKELEIRNEEKNMSVRSADVATKQHMEDVKKISKLEAE 276
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-296 |
4.02e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKVAEEAVSGWEKAEAEASALKLQLETVTLAKLAAEERAAH 127
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 128 LDGALKECMKQVRTVKEEGEQKLHDVVFAKTKQWEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGDLLMKIDEEK 207
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 208 ARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKELEIRNEEKNMSVRSADVATKQHMEDVKKISKLEAECQRLRGLVRKK 287
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
....*....
gi 1002254057 288 LPGPAALAQ 296
Cdd:COG1196 516 LAGLRGLAG 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
765-930 |
4.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLkcmaesyKSLESRKAELENEI 844
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL-------LEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 845 KVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERnsmcvDEDADTKAKQEKEIAAAAEKLAECQETILILGR 924
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-----EELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
....*.
gi 1002254057 925 QLQSMR 930
Cdd:COG1196 457 EEEALL 462
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
764-919 |
5.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEetkfRFKELEKSLEELTSKLVASEKSNSLAETQLKCMA-ESYKSLESRKAELE- 841
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEp 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 842 ------------NEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKI---------ERYENERNSMC--------VD 892
Cdd:PRK03918 600 fyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeelekkyseEEYEELREEYLelsrelagLR 679
|
170 180
....*....|....*....|....*..
gi 1002254057 893 EDADTKAKQEKEIAAAAEKLAECQETI 919
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEER 706
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
765-903 |
5.70e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEE---------LTSKLVASEKSNSLAETQLKCMAESYKSLES 835
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEE 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002254057 836 RKAELENEIKVLQSKIEVLTAELDDERQnhqeditryrDLEEKIERYENERNSMCVDEDADTKAKQEK 903
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELA----------ELEAELEELEAEREELAAKIPPELLALYER 182
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
765-958 |
8.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKL--VASEKSNSLAETQLKcmAESYKSLESRKAELEN 842
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeLEEERDDLLAEAGLD--DADAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 843 EIKVLQSkievltaELDDER---QNHQEDITRYRDLEEKIEryenERNsmcvdEDADTKAKQ-EKEIAAAAEKLAECQET 918
Cdd:PRK02224 322 RDEELRD-------RLEECRvaaQAHNEEAESLREDADDLE----ERA-----EELREEAAElESELEEAREAVEDRREE 385
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002254057 919 ILILGRQLQSMRppaESMGSSPNQR--MEDFLQDAAGTTEGV 958
Cdd:PRK02224 386 IEELEEEIEELR---ERFGDAPVDLgnAEDFLEELREERDEL 424
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
763-937 |
9.25e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 763 SSEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELEN 842
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 843 EIKVLQSKIEvltaELDDERQNHQEDItryRDLEEKIERYENERNSMcvDEDADTKAKQEKEIAAAAEKLAECQETILIL 922
Cdd:TIGR02169 869 ELEELEAALR----DLESRLGDLKKER---DELEAQLRELERKIEEL--EAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
170
....*....|....*
gi 1002254057 923 GRQLQSMRPPAESMG 937
Cdd:TIGR02169 940 KGEDEEIPEEELSLE 954
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
765-928 |
1.19e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENEI 844
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 845 KVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNsmcvdEDADTKAKQEKEIAAAAEKLAECQETILILGR 924
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
....
gi 1002254057 925 QLQS 928
Cdd:COG1196 422 ELEE 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
765-935 |
1.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEE---TKFRFKELEKSLEELTSKLVASEKSNSLAETQLKcmaesYKSLESRKAELE 841
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEleeLEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 842 NEIKVLQSKIEVLtAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVDEDADTKAKQEKEIAAAAEKLAECQETILI 921
Cdd:COG4717 146 ERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....
gi 1002254057 922 LGRQLQSMRPPAES 935
Cdd:COG4717 225 LEEELEQLENELEA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
763-940 |
1.50e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 763 SSEEFEQLKS-------EKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVAS------------EKSNSLAETQL 823
Cdd:TIGR02169 735 LKERLEELEEdlssleqEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelsklEEEVSRIEARL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 824 KCMAESYKSLESRKAELENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMC---------VDE- 893
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlgdlkkeRDEl 894
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002254057 894 DADTKAKQEK--EIAAAAEK----LAECQETILILGRQLQSMRPPAESMGSSP 940
Cdd:TIGR02169 895 EAQLRELERKieELEAQIEKkrkrLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
765-884 |
1.66e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKcmaeSYKSLESRKAELENEI 844
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS----EARSEERREIRKDREI 467
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1002254057 845 KVLQSKIEVLTAELDDERQnhqeditRYRDLEEKIERYEN 884
Cdd:COG2433 468 SRLDREIERLERELEEERE-------RIEELKRKLERLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
765-922 |
1.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKlvasEKSNSLAETQLKCMAESYKSLESRKAELENEI 844
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL----EKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 845 KVLQSKIEVLTA---------ELDDERQNHQEDItryRDLEEKIERYENERNSmcVDEDADTKAKQEKEIAAAAEKLAEC 915
Cdd:PRK03918 276 EELEEKVKELKElkekaeeyiKLSEFYEEYLDEL---REIEKRLSRLEEEING--IEERIKELEEKEERLEELKKKLKEL 350
|
....*..
gi 1002254057 916 QETILIL 922
Cdd:PRK03918 351 EKRLEEL 357
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
764-930 |
1.84e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLkcmaesyKSLESRKAELENE 843
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-------DELRAELTLLNEE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMcvdedADTKAKQEKEIAAAAEKLAECQETILILG 923
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL-----EELIEELESELEALLNERASLEEALALLR 893
|
....*..
gi 1002254057 924 RQLQSMR 930
Cdd:TIGR02168 894 SELEELS 900
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
760-861 |
1.97e-04 |
|
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: 44.15 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 760 QICSSEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKsnSLAETQlkcmaesyKSLESRKAE 839
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA--ELEEKK--------AELDEELAE 153
|
90 100
....*....|....*....|..
gi 1002254057 840 LENEIKVLQSKIEVLTAELDDE 861
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPE 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
771-927 |
1.99e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 771 KSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLE-------SRKAELENE 843
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveqleERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSmcvDEDADTKAKQE-----KEIAAAAEKLAECQET 918
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA---LREALDELRAEltllnEEAANLRERLESLERR 832
|
....*....
gi 1002254057 919 ILILGRQLQ 927
Cdd:TIGR02168 833 IAATERRLE 841
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-196 |
2.31e-04 |
|
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: 43.76 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 46 AHLTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQH---AKVAEEAVSGWEKAEaEASALKLQLETVTLAKLAAE 122
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002254057 123 ERAAHLDGALKECMKQVRTVKEEgeqklhdvVFAKTKQWEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEER 196
Cdd:COG1579 110 DEILELMERIEELEEELAELEAE--------LAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
776-942 |
2.75e-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: 44.37 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 776 NLEAELSKCNEVIEETKFRFKELEKSLEELTSK----LVASEKSNSLAETQLKCMAES----------YKSLESRKAELE 841
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEElaelLRALYRLGRQPPLALLLSPEDfldavrrlqyLKYLAPARREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 842 NEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMcVDEDADTKAKQEKEIAAAAEKLAECQETILI 921
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL-LARLEKELAELAAELAELQQEAEELEALIAR 231
|
170 180
....*....|....*....|.
gi 1002254057 922 LGRQLQSMRPPAESMGSSPNQ 942
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
764-930 |
2.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENE 843
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENErnsmcVDEDADTKAKQEKEIAAAAEKLAECQETILILG 923
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-----LEALLNERASLEEALALLRSELEELSEELRELE 907
|
....*..
gi 1002254057 924 RQLQSMR 930
Cdd:TIGR02168 908 SKRSELR 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
763-858 |
3.19e-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: 44.37 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 763 SSEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKcmaesykSLESRKAELEN 842
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAELAELEK 90
|
90
....*....|....*.
gi 1002254057 843 EIKVLQSKIEVLTAEL 858
Cdd:COG4942 91 EIAELRAELEAQKEEL 106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
766-917 |
3.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 766 EFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENEIK 845
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 846 VLQSKIEVLTA---------ELDDERQNHQEDITRYRD-LEEKIERYENERNSmcVDEDADTKAKQEKE-----IAAAAE 910
Cdd:PRK02224 590 SLERIRTLLAAiadaedeieRLREKREALAELNDERRErLAEKRERKRELEAE--FDEARIEEAREDKEraeeyLEQVEE 667
|
....*..
gi 1002254057 911 KLAECQE 917
Cdd:PRK02224 668 KLDELRE 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
764-914 |
3.32e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEEtkfrfkeLEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENE 843
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRR-------IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002254057 844 IKVLQSKIEVLTAELDD---ERQNHQEDITRYRDLEEKIERYENERNsmcVDEDADTKAKQEKEIAAAAEKLAE 914
Cdd:TIGR02169 746 LSSLEQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEARLSHSR---IPEIQAELSKLEEEVSRIEARLRE 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-304 |
3.90e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLNEKVKALNEDLSAAQSEitTKDALVKQHAKVAEEAVSGWEKAeAEASALKLQLETVTLAKLAAEERAAH 127
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREYEGYELL-KEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 128 LDGALKECMKQVrtvkEEGEQKLHDVVfaktkqwEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGDLLMKIDEEK 207
Cdd:TIGR02169 256 LTEEISELEKRL----EEIEQLLEELN-------KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 208 ARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKELEIRNEEKNMSV-RSADVATK------QHMEDVKKISKLEAECQRL 280
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRaELEEVDKEfaetrdELKDYREKLEKLKREINEL 404
|
250 260
....*....|....*....|....*...
gi 1002254057 281 RGLVRKKLP----GPAALAQMKMEVESL 304
Cdd:TIGR02169 405 KRELDRLQEelqrLSEELADLNAAIAGI 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
43-227 |
5.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 43 ETYAHLTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKV--AEEAVSGWEKAEAEASALKLQLEtvtlaklA 120
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLE-------E 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 121 AEERAAhldgALKECMKQVRTVKEEGEQKLhdvvfaktkqwEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGDLL 200
Cdd:COG4717 151 LEERLE----ELRELEEELEELEAELAELQ-----------EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180
....*....|....*....|....*..
gi 1002254057 201 MKIDEEKARAEAEIEVLKNTIQSGERE 227
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
52-215 |
5.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 52 EEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKV-------------------AEEAVSGWE--KAEAEAS----- 105
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvasAEREIAELEaeLERLDASsddla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 106 ALKLQLEtvtlaklAAEERAAHLDGALKECMKQVRTVKEEGEQKLHDVVFAKTKQWEKIKAEFEAKLLEFEQELIRAGAE 185
Cdd:COG4913 689 ALEEQLE-------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|..
gi 1002254057 186 N--DALSRSLEERGDllmKIDEEKARAEAEIE 215
Cdd:COG4913 762 AveRELRENLEERID---ALRARLNRAEEELE 790
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
765-916 |
6.00e-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: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNL--------------EAELSKCNEVIEETKFRF----KELEKSLEELTSKLVASEKSNSLAETQLKCM 826
Cdd:pfam12128 248 QEFNTLESAELRLshlhfgyksdetliASRQEERQETSAELNQLLrtldDQWKEKRDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 827 AESYKS-----LESRKAELENEIKVlQSKIEVLTAELDDERQNHQeditryrDLEEKIERYENERNSMCVDEDADTKAKQ 901
Cdd:pfam12128 328 EDQHGAfldadIETAAADQEQLPSW-QSELENLEERLKALTGKHQ-------DVTAKYNRRRSKIKEQNNRDIAGIKDKL 399
|
170
....*....|....*
gi 1002254057 902 EKEIAAAAEKLAECQ 916
Cdd:pfam12128 400 AKIREARDRQLAVAE 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
46-230 |
7.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 46 AHLTESEEQVKTLNEKVKALNEDLSAAQSEI-TTKDALVKQHAKVAE--EAVSGWEKAEAEASALKLQLETVTLAKLAAE 122
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIdKLQAEIAEAEAEIEErrEELGERARALYRSGGSVSYLDVLLGSESFSD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 123 --ERAAHLD---GALKECMKQVRTVKEEGEQKlhdvvfaktkqwekiKAEFEAKLLEFEQELIRAGAENDALSRSLEERG 197
Cdd:COG3883 117 flDRLSALSkiaDADADLLEELKADKAELEAK---------------KAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|...
gi 1002254057 198 DLLMKIDEEKARAEAEIEVLKNTIQSGEREINS 230
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
763-885 |
9.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 763 SSEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLvaSEKSNSLAETQLKCMAESYKSLESRKAELEN 842
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEK 687
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1002254057 843 EIKVLQSKIEVLTAELDDERQNHQE------DITRYRDLEEKIERYENE 885
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKEleklekALERVEELREKVKKYKAL 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-391 |
1.06e-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: 43.12 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 100 AEAEASALKLQ--LETVTLAKLAAEERAAHLDGALKECMKQVRTVKEEGEQKLHDVVFAKTK--QWEKIKAEFEAKLLEF 175
Cdd:TIGR02168 666 AKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 176 EQELIRAGAENDALSRSLEERGDLLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKELEIRNEE------K 249
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlreR 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 250 NMSVRSADVATKQHMED-VKKISKLEAECQRLRGLVRKKlpgPAALAQMKMEVESLGRDYGESRLRRSPAKnssfhrpms 328
Cdd:TIGR02168 826 LESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEEL---EELIEELESELEALLNERASLEEALALLR--------- 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002254057 329 pmspvpdyafENLQHMQKENEFLTARLLSMEDETKMLKEALAKRNSELQTSRNMYAKTAGKLR 391
Cdd:TIGR02168 894 ----------SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-287 |
1.20e-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: 43.12 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 23 QNSNQAEQDDKAPKYVQISPETYAHLTESEEQVKTLNEKVKALNEDLSAAQSEittkdalvkqhakvaeeavsgWEKAEA 102
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE---------------------LYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 103 EASALKLQLEtvtlaklAAEERAAHLDGALKEcmkqVRTVKEEGEQKLhDVVFAKTKQWEKIKAEFEAKLLEFEQELIRA 182
Cdd:TIGR02168 296 EISRLEQQKQ-------ILRERLANLERQLEE----LEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 183 GAENDALSRSLEERGDLLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEI---HVVSKELEIRNEEKNMSVRSADVA 259
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlQQEIEELLKKLEEAELKELQAELE 443
|
250 260 270
....*....|....*....|....*....|
gi 1002254057 260 TKQHMED--VKKISKLEAECQRLRGLVRKK 287
Cdd:TIGR02168 444 ELEEELEelQEELERLEEALEELREELEEA 473
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-217 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKVAEEAvsgwekAEAEASALKLQLETVtLAKLAAEERAAH 127
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA------EDLARLELRALLEER-FAAALGDAVERE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 128 LDGALKECMKQVRTVKEEGEQKLHDVVFAKTKQWEKIKA----------EFEAK--------LLEFEQELIRAGAENdal 189
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadleslpEYLALldrleedgLPEYEERFKELLNEN--- 843
|
170 180
....*....|....*....|....*...
gi 1002254057 190 srSLEERGDLLMKIDEEKARAEAEIEVL 217
Cdd:COG4913 844 --SIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
765-935 |
1.83e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEK-------SLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRK 837
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAelaeaeeELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 838 AELENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERnsmcvDEDADTKAKQEKEIAAAAEKLAECQE 917
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAA 491
|
170
....*....|....*...
gi 1002254057 918 TILILGRQLQSMRPPAES 935
Cdd:COG1196 492 RLLLLLEAEADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-223 |
1.86e-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: 42.35 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 23 QNSNQAEQDDKAPKYVQISPETYAHLTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVKQHAKVAEEAVSGWEKAEA 102
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 103 EASALKLQLETVTLAKLAAEERAAHLDGALKECMKQVRT----------VKEEGEQKLHDVVFAKTKQWEKIKaEFEAKL 172
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleallnERASLEEALALLRSELEELSEELR-ELESKR 910
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002254057 173 LEFEQELIRAGAENDALSRSLE--------------ERGDLLM--------KIDEEKARAEAEIEVLKNTIQS 223
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEglevridnlqerlsEEYSLTLeeaealenKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
764-926 |
1.90e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLvaseksNSLaETQLKCMAESYKSLESRKAELENE 843
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI------NEL-KRELDRLQEELQRLSEELADLNAA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 844 IKVLQSKIevltAELDDERQnhqeditryrDLEEKIERYENERNSMcvdedADTKAKQEKEIAAAAEKLAECQETILILG 923
Cdd:TIGR02169 429 IAGIEAKI----NELEEEKE----------DKALEIKKQEWKLEQL-----AADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
...
gi 1002254057 924 RQL 926
Cdd:TIGR02169 490 REL 492
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
764-885 |
1.92e-03 |
|
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: 42.31 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 764 SEEFEQLKSEKLNLEAElsKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENE 843
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1002254057 844 IKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENE 885
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
59-286 |
2.81e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 59 NEKVKALNEDLSAAQSEITTKDALVKQHAKVAEEAVSGWEKAEAEASALKLQLEtvtlaklAAEERAAHLDGALKECMKQ 138
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 139 VRTVKEEGEQKLHDVVFAKTKQWEKIKAEFEAKLLEFE--QELIRAGAENDALSRSLEERGDLLMKIDEEKARAEAEIEV 216
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 217 LKNTIQSGEREINSLKyeihvvsKELEIRNEEKNMSVRSADvatKQHMEDVKKISKLEAECQRLRGLVRK 286
Cdd:COG4942 172 ERAELEALLAELEEER-------AALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIAR 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
770-914 |
4.18e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 770 LKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKSLESRKAELENEIKVLQS 849
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002254057 850 KIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMC--VDEDADTKAKQEKEIAAAAEKLAE 914
Cdd:pfam01576 462 DVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQeqLEEEEEAKRNVERQLSTLQAQLSD 528
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
765-881 |
4.75e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSklvASEKSNSLAETQLKCMAESYKSLESRKAELENEI 844
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110
....*....|....*....|....*....|....*..
gi 1002254057 845 KVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIER 881
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
809-929 |
5.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 809 LVASEKSNSLAETQLKCMAESYKSLESRKAELENEIKVLQSKIEVLTAEldderqnhqeditrYRDLEEKIERYENErns 888
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE--------------YNELQAELEALQAE--- 66
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002254057 889 mcvdedadtKAKQEKEIAAAAEKLAECQEtilILGRQLQSM 929
Cdd:COG3883 67 ---------IDKLQAEIAEAEAEIEERRE---ELGERARAL 95
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
765-931 |
6.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTS-KLVASEKSNSLAETQLKCMAESY----KSLESRKAE 839
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELLEEYtaelKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 840 LENEIKVLQSKIEVLTAELDDERQnhqedITRYRDLEEKIERYENERNSMCVDEdadtKAKQEKEIAAAAEKLAECQETI 919
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESE-----LIKLKELAEQLKELEEKLKKYNLEE----LEKKAEEYEKLKEKLIKLKGEI 541
|
170
....*....|..
gi 1002254057 920 LILGRQLQSMRP 931
Cdd:PRK03918 542 KSLKKELEKLEE 553
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
765-928 |
7.76e-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: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 765 EEFEQLKSEKLNLEA-----ELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQLKCMAESYKslesrkAE 839
Cdd:TIGR02169 211 ERYQALLKEKREYEGyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK------DL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 840 LENEIKVLQSKIEVLTAELDDERQNHQEDITRYRDLEEKIERYENERNSMCVD-EDADTK-AKQEKEIAAAAEKLAECQE 917
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEiEELEREiEEERKRRDKLTEEYAELKE 364
|
170
....*....|.
gi 1002254057 918 TILILGRQLQS 928
Cdd:TIGR02169 365 ELEDLRAELEE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
768-1006 |
7.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 768 EQLKSEKLNLEAELSKCNEVIEETKFRFKELEKSLEELTSKLVASEKSNSLAETQL--------KCMAESYKS------- 832
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerreelgERARALYRSggsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 833 ---------------------LESRKAELENEIKVLQSKIEVLTAELDDERQNHQEDITRY----RDLEEKIERYENERN 887
Cdd:COG3883 106 dvllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELeaakAELEAQQAEQEALLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 888 SMCVDEDADTKAKQEKEIAAAAEKLAECQETILILGRQLQSMRPPAESMGSSPNQRMEDFLQDAAGTTEGVEYSQKPTGQ 967
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002254057 968 LDTDQEMHASGNESPVNGYKTHNAPSEADGSPFLSPNGS 1006
Cdd:COG3883 266 GAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSG 304
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
48-421 |
9.63e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 48 LTESEEQVKTLNEKVKALNEDLSAAQSEITTKDALVK------QHAKVAEEAVsgwEKAEAEASALKLQL---ETVTLAK 118
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelQHLKNEGDHL---RNVQTECEALKLQMaekDKVIEIL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 119 LAAEERAAHLDGALKECMKQVRTVKEEGEQKLHDVVFaKTKQWEKIKAEFEAKLLEFEQELIRAGAENDALSRSLEERGD 198
Cdd:pfam15921 568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL-ELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 199 LLMKIDEEKARAEAEIEVLKNTIQSGEREINSLKYEIHVVSKELEIRNEEKNMSVRSADVATKQHMEDVKKISKLEaecq 278
Cdd:pfam15921 647 AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD---- 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002254057 279 rlrglvrkklpGPAALAQMKMEveslgrdygesrlRRSPAKNSsfhrpmspmspvpdyafeNLQHMQKENEFLTARLLSM 358
Cdd:pfam15921 723 -----------GHAMKVAMGMQ-------------KQITAKRG------------------QIDALQSKIQFLEEAMTNA 760
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002254057 359 EDETKMLKEALAKRNSELQTSRNMYAKTAGKLRGLEVQmltgSQRKSTSNPNMDIHFDGALSQ 421
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ----ERRLKEKVANMEVALDKASLQ 819
|
|
| |
