|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-1162 |
0e+00 |
|
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: 932.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYGnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGsKGEPPAKYAEV 83
Cdd:TIGR02169 1 YIERIELENFKSFG-KKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNG-KNGQSGNEAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 AMYFNNEDRGFPiDEDEVVIKRRVYPDGR-STYWLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKMSPIERRL 162
Cdd:TIGR02169 79 TVTFKNDDGKFP-DELEVVRRLKVTDDGKySYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 163 IIDEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEK 242
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 243 FIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEI 322
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 323 EESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEA 402
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 403 KKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRE 482
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 483 LQKVESELAKAREELIKAEAQR-----EVRGNRAVEFLKSQRIEGLYGTLGELISVpKSEYALAVEVALGGNYDNVVVED 557
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKASIQGVHGTVAQLGSV-GERYATAIEVAAGNRLNNVVVED 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 558 DRVAEKAIKLLKEKKLGRLTFLPLNKIK-----PRSMREKPKLGIpAMDVVSYDPRFRNAVAYALGDTLIVNDMDEAREV 632
Cdd:TIGR02169 557 DAVAKEAIELLKRRKAGRATFLPLNKMRderrdLSILSEDGVIGF-AVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 633 GiGKVRMVTLGGELLERSGAITGGHYKPRGKLGVNVDEiRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSE 712
Cdd:TIGR02169 636 M-GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 713 LSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKI 792
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 793 REVEAEISKLKEELSRVESKLESLDSRINeELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEEN 872
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLN-RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 873 VKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPAlVRSIKEIPLEV- 951
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP-KGEDEEIPEEEl 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 952 --EKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLNAIAKNF 1029
Cdd:TIGR02169 952 slEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENF 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1030 SELFAKLSpGGEAKLILENPEDPFSGGLEIEAKPAGKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLD 1109
Cdd:TIGR02169 1032 NEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLD 1110
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....
gi 57159276 1110 DANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIGVSM-RNGVSKVVSLSL 1162
Cdd:TIGR02169 1111 GVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMrRNGESQVFGLKL 1164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-1162 |
0e+00 |
|
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: 626.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYGNKkVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGSKGEPPAKYAEV 83
Cdd:TIGR02168 1 RLKKLELAGFKSFADP-TTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 AMYFNNEDRGFPIDE-DEVVIKRRVYPDGRSTYWLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKMSPIERRL 162
Cdd:TIGR02168 80 ELVFDNSDGLLPGADySEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 163 IIDEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEK 242
Cdd:TIGR02168 160 IFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 243 FIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENAQKEI 322
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-LYALANEISRLEQQKQILRERLANLERQL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 323 EESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEA 402
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 403 KKALYMKESEISKFEEEISRAKARITQfnARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRE 482
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 483 LQKVESELAKAREEL-----IKAEAQREVRGNRAVeFLKSQRIEGLYGTLGELISVPkSEYALAVEVALGGNYDNVVVED 557
Cdd:TIGR02168 477 LDAAERELAQLQARLdslerLQENLEGFSEGVKAL-LKNQSGLSGILGVLSELISVD-EGYEAAIEAALGGRLQAVVVEN 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 558 DRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIP--------AMDVVSYDPRFRNAVAYALGDTLIVNDMDEA 629
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgvAKDLVKFDPKLRKALSYLLGGVLVVDDLDNA 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 630 REVGI---GKVRMVTLGGELLERSGAITGGHYKPRGKL---GVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENEL 703
Cdd:TIGR02168 635 LELAKklrPGYRIVTLDGDLVRPGGVITGGSAKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 704 FELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENP 783
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 784 EAR--ELNSKIREVEAEISKLKEELSRVESKLESLDSRI------NEELLPRKADLEEEIEGLVNKINALNAYIEENKNA 855
Cdd:TIGR02168 795 KEElkALREALDELRAELTLLNEEAANLRERLESLERRIaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 856 ITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKH 935
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 936 FDPALVRsikEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQKR 1015
Cdd:TIGR02168 955 EAEALEN---KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1016 QVFLQTLNAIAKNFSELFAKLSPGGEAKLILENPEDPFSGGLEIEAKPAGKDVKRIEAMSGGEKAIIALAFVFAIQRYKP 1095
Cdd:TIGR02168 1032 ERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKP 1111
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 1096 APFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIGVSMRN-GVSKVVSLSL 1162
Cdd:TIGR02168 1112 APFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEkGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-1171 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 614.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYGnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGSKGEPPAKYAEV 83
Cdd:COG1196 2 RLKRLELAGFKSFA-DPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 AMYFNNEDRGFPIDEDEVVIKRRVYPDGRSTYWLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKMSPIERRLI 163
Cdd:COG1196 81 SLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 164 IDEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKF 243
Cdd:COG1196 161 IEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 244 IEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENAQKEIE 323
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEERLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 324 ESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAK 403
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 404 KALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTREL 483
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 484 QKVESELAKAREE---LIKAEAQREVRGNRAVEFLKSQRIEGLYGTLGELISVPKsEYALAVEVALGGNYDNVVVEDDRV 560
Cdd:COG1196 480 AELLEELAEAAARlllLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA-AYEAALEAALAAALQNIVVEDDEV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 561 AEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGI---PAMDVVSYDPRFRNAVAYALGDTLIVNDMDEAREvGIGKV 637
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGaigAAVDLVASDLREADARYYVLGDTLLGRTLVAARL-EAALR 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 638 RMVTLGGELLERSGAITGGhykprgklgvnvdeirkrvealegrkealeaqvnalkvevkglenelfelrmkkselskdv 717
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGG------------------------------------------------------------- 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 718 qviqkeldsylaedrslkeeieenerliselekrieESKGEMAKLRGRIERLEKKREKIKKALEnpearelnskirevea 797
Cdd:COG1196 657 ------------------------------------SAGGSLTGGSRRELLAALLEAEAELEEL---------------- 684
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 798 eisklkeelsrvesklesldsrineellprkadleeeieglvnkinalnayieenknaitelekeleelktaeenvKDEL 877
Cdd:COG1196 685 ----------------------------------------------------------------------------AERL 688
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 878 KELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQD 957
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 958 IEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLNAIAKNFSELFAKLS 1037
Cdd:COG1196 769 LERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLF 848
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1038 PGGEAKLILENPEDPFSGGLEIEAKPAGKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVA 1117
Cdd:COG1196 849 GGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFA 928
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 57159276 1118 DLIKEASQNSQFIVITHRDVMMAQADRIIGVSMRN-GVSKVVSLSLEKARKILEE 1171
Cdd:COG1196 929 ELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEpGVSRVVSVDLEEAEELAEA 983
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-1156 |
4.40e-142 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 459.82 E-value: 4.40e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYGnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFagSKGEPPAKYAEV 83
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 AMYFNNEDRGFPIDEDEVVIKRRVYPDGRSTYWLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKMSPIERRLI 163
Cdd:pfam02463 78 EITFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 164 IDEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKF 243
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 244 IEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIE 323
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 324 ESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAK 403
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 404 KALYMKESEISkfeEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTR-- 481
Cdd:pfam02463 398 ELKSEEEKEAQ---LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDll 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 482 -ELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRIEGLYGTLGELISVPKSEYALAVEVALGGNYDNVVVEDDRV 560
Cdd:pfam02463 475 kETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 561 AEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAMDVVSYDPRFRnavAYALGDTLIVNDMDEAREVGIGKVRMV 640
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN---LAQLDKATLEADEDDKRAKVVEGILKD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 641 TLGGELLERSGAITGGHYKP---------RGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKS 711
Cdd:pfam02463 632 TELTKLKESAKAKESGLRKGvsleeglaeKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 712 ELSKDVQVIQKELDSYLAEDRSLKEEIEENE----RLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARE 787
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKqkidEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 788 LNSKIREVEAEISKLKEELSRVESKLESLDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELK 867
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 868 TAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEI 947
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 948 PLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLNAIAK 1027
Cdd:pfam02463 952 ENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINK 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1028 NFSELFAKLSPGGEAKLILENPEDPFSGGLEIEAKPAGKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAH 1107
Cdd:pfam02463 1032 GWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAA 1111
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 57159276 1108 LDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIGVSM-RNGVSK 1156
Cdd:pfam02463 1112 LDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMvENGVST 1161
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1041-1156 |
9.37e-50 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 174.96 E-value: 9.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1041 EAKLILENPEDPFS----GGLE--IEAKpaGKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVK 1114
Cdd:cd03278 77 EVTLTFDNSDGRYSiisqGDVSeiIEAP--GKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVE 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 57159276 1115 RVADLIKEASQNSQFIVITHRDVMMAQADRIIGVSMRN-GVSK 1156
Cdd:cd03278 155 RFARLLKEFSKETQFIVITHRKGTMEAADRLYGVTMQEsGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
5-96 |
1.86e-39 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 145.30 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGSKGEPPAKYAEVA 84
Cdd:cd03278 1 LKKLELKGFKSFA-DKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVT 79
|
90
....*....|..
gi 57159276 85 MYFNNEDRGFPI 96
Cdd:cd03278 80 LTFDNSDGRYSI 91
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
521-632 |
7.46e-37 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 135.05 E-value: 7.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 521 EGLYGTLGELISVPKsEYALAVEVALGGNYDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGI--- 597
Cdd:smart00968 1 PGVLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLREAllp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 57159276 598 ------PAMDVVSYDPRFRNAVAYALGDTLIVNDMDEAREV 632
Cdd:smart00968 80 epgfvgPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
520-632 |
6.40e-35 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 129.30 E-value: 6.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 520 IEGLYGTLGELISVPKsEYALAVEVALGGNYDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKL---G 596
Cdd:pfam06470 1 LKGVLGRLADLIEVDE-GYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLkggA 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 57159276 597 IPAMDVVSYDPRFRNAVAYALGDTLIVNDMDEAREV 632
Cdd:pfam06470 80 GPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALEL 115
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
4-169 |
9.31e-32 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 125.10 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYGNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGskGEPPAKYAEV 83
Cdd:cd03273 2 HIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKR--GQAGITKASV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 AMYFNNEDR-GFPI---DEDEVVIKRRVYPDGRSTYWLNGKRATRSEIIDLLSAAMISPEGYN-LVLQGDITKFIKMSPI 158
Cdd:cd03273 80 TIVFDNSDKsQSPIgfeNYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHfLIMQGRITKVLNMGGV 159
|
170
....*....|.
gi 57159276 159 ERRLIIdEISG 169
Cdd:cd03273 160 WKESLT-ELSG 169
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1067-1156 |
2.30e-29 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 115.48 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1067 DVKRIeaMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQN-SQFIVITHRDVMMAQADRI 1145
Cdd:cd03239 90 KVEQI--LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKL 167
|
90
....*....|.
gi 57159276 1146 IGVSMRNGVSK 1156
Cdd:cd03239 168 IGVLFVHGVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1053-1162 |
1.36e-27 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 112.67 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1053 FSGGLEIEA--KPAGKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKE-ASQNSQF 1129
Cdd:cd03275 133 FQGDVESIAskNPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREqAGPNFQF 212
|
90 100 110
....*....|....*....|....*....|....*.
gi 57159276 1130 IVITHRDVMMAQADRIIGVsMRN---GVSKVVSLSL 1162
Cdd:cd03275 213 IVISLKEEFFSKADALVGV-YRDqecNSSKVLTLDL 247
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1065-1157 |
2.27e-27 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 111.97 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1065 GKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADR 1144
Cdd:cd03272 150 QDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADK 229
|
90
....*....|...
gi 57159276 1145 IIGVSMRNGVSKV 1157
Cdd:cd03272 230 FYGVKFRNKVSTI 242
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1058-1158 |
6.84e-25 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 103.91 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1058 EIE--AKPAGKDVKRIEAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHR 1135
Cdd:cd03274 110 EVEqiAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLR 189
|
90 100
....*....|....*....|...
gi 57159276 1136 DVMMAQADRIIGVSMRNGVSKVV 1158
Cdd:cd03274 190 NNMFELADRLVGIYKTNNCTKSV 212
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
5-169 |
7.39e-25 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 104.96 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKKVVVPLARgFTAIVGANGSGKSNIGDAVLFVLgGLSAKAMRASRISDLIFAGSKGEPPAKYAEVA 84
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVL-GEKSSHLRSKNLKDLIYRARVGKPDSNSAYVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEdrgfpiDEDEVVIKRRVYPdGRSTYWLNGKRATRSEIIDLLSAAMISPEGYN-LVLQGDI-TKFIKMSPIERRL 162
Cdd:cd03275 79 AVYEDD------DGEEKTFRRIITG-GSSSYRINGKVVSLKEYNEELEKINILVKARNfLVFQGDVeSIASKNPPGKRFR 151
|
....*..
gi 57159276 163 IIDEISG 169
Cdd:cd03275 152 DMDNLSG 158
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
252-1043 |
4.69e-23 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 106.54 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 252 EEIEGQIKSLEdRLKEIAKEIVAKEKELAEIErqlEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRK 331
Cdd:COG4913 245 EDAREQIELLE-PIRELAERYAAARERLAELE---YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 332 SKEELKHVSEEIEKSKGAikrwgkRREQLLVQIKERETVRNELviklgeidkrfSEAREEFDKVVAELEEAKkalymkES 411
Cdd:COG4913 321 LREELDELEAQIRGNGGD------RLEQLEREIERLERELEER-----------ERRRARLEALLAALGLPL------PA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 412 EISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRkaekeleektrelqKVESELA 491
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS--------------NIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 492 KAREELIKAEAQREVrgnrAVEFlksqrieglygtLGELISVPKSEYA--LAVEVALGGNYDNVVVEDDRVAEkAIKLLK 569
Cdd:COG4913 444 ALRDALAEALGLDEA----ELPF------------VGELIEVRPEEERwrGAIERVLGGFALTLLVPPEHYAA-ALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 570 EKKL-GRLTFLPLNKIKPRSMREKPKLG-IPAmdVVSYDP-RFRNAVAYALG---DTLIVNDMDEAREV--GIGKVRMVT 641
Cdd:COG4913 507 RLHLrGRLVYERVRTGLPDPERPRLDPDsLAG--KLDFKPhPFRAWLEAELGrrfDYVCVDSPEELRRHprAITRAGQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 642 LGGELLERsgaitGGHYKPRGK--LGVNVdeiRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQV 719
Cdd:COG4913 585 GNGTRHEK-----DDRRRIRSRyvLGFDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 720 IQKELDSylaedRSLKEEIEENERLISELEKrieeSKGEMAKLRGRIERLEKKREKIKKALEnpearELNSKIREVEAEI 799
Cdd:COG4913 657 SWDEIDV-----ASAEREIAELEAELERLDA----SSDDLAALEEQLEELEAELEELEEELD-----ELKGEIGRLEKEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 800 SKLKEELSRVESKLESLDSRINEELLprkADLEEEIEGLvnkinalnayieenknaiteleKELEELKTAEENVKDELKE 879
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELR---ALLEERFAAA----------------------LGDAVERELRENLEERIDA 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 880 LREGREQIRVEIAELRKE-KDELTSKLQELR--IEANT--LKVRLAQVETTLQEKRAELKHfdpALVRSIKEiplEVEKL 954
Cdd:COG4913 778 LRARLNRAEEELERAMRAfNREWPAETADLDadLESLPeyLALLDRLEEDGLPEYEERFKE---LLNENSIE---FVADL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 955 RQDIEKMEEEIRS-LEPVNmKAIEDFEVVERRYLELSSKREQVlaekESIEEFIQEIEGQKRQVFLQTLNAIAKNFS--- 1030
Cdd:COG4913 852 LSKLRRAIREIKErIDPLN-DSLKRIPFGPGRYLRLEARPRPD----PEVREFRQELRAVTSGASLFDEELSEARFAalk 926
|
810
....*....|...
gi 57159276 1031 ELFAKLSPGGEAK 1043
Cdd:COG4913 927 RLIERLRSEEEES 939
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
5-169 |
5.78e-23 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 99.26 E-value: 5.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKaMRASRISDLIFAGSKgePPAKYAEVA 84
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTH-LREEQRQALLHEGSG--PSVMSAYVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEDRGFPIDEDEVVIKRRVypdG--RSTYWLNGKRATRSEIIDLLSAAMISPEG-YNLVLQGDITKFIKMSPIERR 161
Cdd:cd03272 78 IIFDNSDNRFPIDKEEVRLRRTI---GlkKDEYFLDKKNVTKNDVMNLLESAGFSRSNpYYIVPQGKINSLTNMKQDEQQ 154
|
....*...
gi 57159276 162 LiIDEISG 169
Cdd:cd03272 155 E-MQQLSG 161
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
5-89 |
7.56e-21 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 92.36 E-value: 7.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLgGLSAKAMRASRISDLIFAgSKGEPPAKYAEVA 84
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVF-GFRASKMRQKKLSDLIHN-SAGHPNLDSCSVE 80
|
....*
gi 57159276 85 MYFNN 89
Cdd:cd03274 81 VHFQE 85
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1074-1157 |
5.18e-20 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 90.82 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1074 MSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIGVSMRNG 1153
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVDG 246
|
....
gi 57159276 1154 VSKV 1157
Cdd:cd03273 247 TSTV 250
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1074-1156 |
9.55e-20 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 87.42 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1074 MSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQN-SQFIVITHRDVMMAQADRIIGVSMRN 1152
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKVI 157
|
....*
gi 57159276 1153 -GVSK 1156
Cdd:cd03227 158 tGVYK 162
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
5-934 |
4.89e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.18 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGnkKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGlsAKAMrASRISDLIFAGskgeppAKYAEVA 84
Cdd:PRK02224 3 FDRVRLENFKCYA--DADLRLEDGVTVIHGVNGSGKSSLLEACFFALYG--SKAL-DDTLDDVITIG------AEEAEIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEDRGFPIDE------DEVVIKRRVYPDGRSTYwlNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKMSPI 158
Cdd:PRK02224 72 LWFEHAGGEYHIERrvrlsgDRATTAKCVLETPEGTI--DGARDVREEVTELLRMDAEAFVNCAYVRQGEVNKLINATPS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 159 ERRLIIDeisgiaeydakkekalkelkqteenlarvDLLirevkaQLDKLEKERndalryldlkEKLEKARVTlllaeIK 238
Cdd:PRK02224 150 DRQDMID-----------------------------DLL------QLGKLEEYR----------ERASDARLG-----VE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 239 RLEkfieeggsreeeiEGQIKSLEDRLKEIAKEivaKEKELAEIERQLEEKsgdgILEITRKISEVKSKIEVAKRNIENA 318
Cdd:PRK02224 180 RVL-------------SDQRGSLDQLKAQIEEK---EEKDLHERLNGLESE----LAELDEEIERYEEQREQARETRDEA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 319 QKEIEESQARLrkskEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEI----------DKRFSEA 388
Cdd:PRK02224 240 DEVLEEHEERR----EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEAR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 389 REEFDKvvaELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESR 468
Cdd:PRK02224 316 REELED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 469 HRKAEKELEEKTRELQKVESELAKAREELikaeaqrevrgnraveflksqriEGLYGTLGELISVPKSEyalavevalgg 548
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREER-----------------------DELREREAELEATLRTA----------- 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 549 nydnvvveDDRVAEkAIKLLKEKKLgrltflplnkikprsmrekPKLGIPamdvvsydprfrnavayaLGDTLIVNDMDE 628
Cdd:PRK02224 439 --------RERVEE-AEALLEAGKC-------------------PECGQP------------------VEGSPHVETIEE 472
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 629 AREvgigkvrmvtlggellersgaitgghykprgklgvNVDEIRKRVEALEGRKEALEAQVNALKvEVKGLENELFELRM 708
Cdd:PRK02224 473 DRE-----------------------------------RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEE 516
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 709 KKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEarel 788
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE---- 592
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 789 nsKIREVEAEISKLKEELSRVESKLESLDSRINE------ELLPRKADLEEEIEGlvnkinalnayieenkNAITELEKE 862
Cdd:PRK02224 593 --RIRTLLAAIADAEDEIERLREKREALAELNDErrerlaEKRERKRELEAEFDE----------------ARIEEARED 654
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 863 LEELKTAEENVKDELKELREGREQIRVEI----------AELRKEKDELTSKLQELRieanTLKVRLAQVETTLQEKRAE 932
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREERDDLQAEIgaveneleelEELRERREALENRVEALE----ALYDEAEELESMYGDLRAE 730
|
..
gi 57159276 933 LK 934
Cdd:PRK02224 731 LR 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-1162 |
1.31e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.58 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 405 ALYMKESEISKF------EEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEgkisKVESRHRKAEKELEE 478
Cdd:PRK03918 129 AIYIRQGEIDAIlesdesREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 479 KTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRieglygtlgELISVPKSEYALAVEVALGGNYDNVVVEDD 558
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK---------ELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 559 RVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAMDVVSYDPRFRNAVAYALGDTLIVNDMDEAREVGIGKVR 638
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 639 MVTLGGELLERSGAITGGHYKPRGKL-GVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSK-- 715
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKak 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 716 -DVQVIQKELD---------SYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRgRIERLEKKREKIKKALENPEA 785
Cdd:PRK03918 436 gKCPVCGRELTeehrkelleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 786 RELnSKIREVEAEISKLKEELSRVESKLESLDSRIN--EELLPRKADLEEEIEGLVNKINALNAYIEEnknaitelekel 863
Cdd:PRK03918 515 YNL-EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEklEELKKKLAELEKKLDELEEELAELLKELEE------------ 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 864 eELKTAEENVKDELKELregrEQIRVEIAELRKEKDELTSKLQELRIEANTLKV---RLAQVETTLQEKRAEL----KHF 936
Cdd:PRK03918 582 -LGFESVEELEERLKEL----EPFYNEYLELKDAEKELEREEKELKKLEEELDKafeELAETEKRLEELRKELeeleKKY 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 937 DPALVRSIKEiplEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQV-LAEK--ESIEEFIQEIEGQ 1013
Cdd:PRK03918 657 SEEEYEELRE---EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELeKLEKalERVEELREKVKKY 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1014 KRQVFLQTLNAIAKNFSELFAKLSPGGEAKLILENPEDPFSGGLEIEAKPAGkdvkrIEAMSGGEKAIIALAFVFAIQRY 1093
Cdd:PRK03918 734 KALLKERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVKLFVVYQGKERP-----LTFLSGGERIALGLAFRLALSLY 808
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1094 KPA--PFYLLDEIDAHLDDANVKRVADLIKEASQN-SQFIVITHRDVMMAQADRIIGVSMRNGVSKVVSLSL 1162
Cdd:PRK03918 809 LAGniPLLILDEPTPFLDEERRRKLVDIMERYLRKiPQVIIVSHDEELKDAADYVIRVSLEGGVSKVEVVSL 880
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5-799 |
3.26e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYgnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGSKGeppakyAEVA 84
Cdd:PRK03918 3 IEELKIKNFRSH--KSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSG------TEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEDRGFPIDEDEVVIKRRVYPDGRSTYWLNGKRATRSEIIDLLSAAMISPEGYnlVLQGDITKFIKmSPIERRLII 164
Cdd:PRK03918 75 LKFEKNGRKYRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLNAIY--IRQGEIDAILE-SDESREKVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 165 DEISGIAEYDAKKEKALKELKQTEENLARVDLLIR---EVKAQLDKLEKERNDALRYLDLKEKLE---KARVTLLLAEIK 238
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELpelREELEKLEKEVK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 239 RLEKF---IEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEE-KSGDGILEITRKISEVKSKIEVAKRN 314
Cdd:PRK03918 232 ELEELkeeIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELRE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 315 IENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRnELVIKLGEIDKRFSEarEEFDK 394
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTG--LTPEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 395 VVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEK-----IAEAKASLEAKRSELSQVEGKISKVESRH 469
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKEL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 470 RKAEKELEEKTRELQKVESELAKAREELikaeAQREVrgnraVEFLKSQRiEGLYGTLGELISVPKSEYALAVEVALGGN 549
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELI----KLKEL-----AEQLKELE-EKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 550 YDNVVVEDDrvAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAMDVVSydprfrnavayalgdtlivNDMDEA 629
Cdd:PRK03918 539 GEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-------------------ERLKEL 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 630 REVGIGKVRMVTLGGELLERSgaitgghyKPRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKglENELFELRMK 709
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREE--------KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 710 KSELSKDVqviqKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKaLENPEARELN 789
Cdd:PRK03918 668 YLELSREL----AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKK-YKALLKERAL 742
|
810
....*....|
gi 57159276 790 SKIREVEAEI 799
Cdd:PRK03918 743 SKVGEIASEI 752
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
5-89 |
2.49e-16 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 78.12 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKkVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRisdLIFAGSKGEPPAKYAEVA 84
Cdd:cd03239 1 IKQITLKNFKSYRDE-TVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSL---LFLAGGGVKAGINSASVE 76
|
....*
gi 57159276 85 MYFNN 89
Cdd:cd03239 77 ITFDK 81
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
668-1148 |
6.28e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVqviqKELDsylAEDRSLKEEIEENERLI-- 745
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE----AELE---ATLRTARERVEEAEALLea 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 746 ------------SELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEArelnskIREVEAEISKLKEELSRVESKL 813
Cdd:PRK02224 452 gkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED------LVEAEDRIERLEERREDLEELI 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 814 ESLDSRINE------ELLPRKADLE--------------EEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENv 873
Cdd:PRK02224 526 AERRETIEEkreraeELRERAAELEaeaeekreaaaeaeEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA- 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 874 KDELKELREGREQI-------RVEIAELRKEKDELTSKLQELRIEantlkvrlaqvetTLQEKRAELKHFDPALVRSIKE 946
Cdd:PRK02224 605 EDEIERLREKREALaelnderRERLAEKRERKRELEAEFDEARIE-------------EAREDKERAEEYLEQVEEKLDE 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 947 IPLEVEKLRQDIEKMEEEIRSLEPVNmkaiEDFEVVERRYLELSSKREQVlaekESIEEFIQEIEGQKRQVFLQTLNAIA 1026
Cdd:PRK02224 672 LREERDDLQAEIGAVENELEELEELR----ERREALENRVEALEALYDEA----EELESMYGDLRAELRQRNVETLERML 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1027 KNFSEL------FAKLSPGGEAKLIL----ENPEDPfsggleieakpagkdvkriEAMSGGEKAIIALAFVFAIQRY--- 1093
Cdd:PRK02224 744 NETFDLvyqndaYSHIELDGEYELTVyqkdGEPLEP-------------------EQLSGGERALFNLSLRCAIYRLlae 804
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1094 -----KPAPFYLLDEIDAHLDDANVKRVADLIKEASQN--SQFIVITHRDVMMAQADRIIGV 1148
Cdd:PRK02224 805 giegdAPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLgvEQIVVVSHDDELVGAADDLVRV 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
668-1016 |
8.32e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEAL-------EAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEE 740
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 741 NERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEAR--ELNSKIREVEAEISKLKEELSRVESKLESLDS 818
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgNAEDFLEELREERDELREREAELEATLRTARE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 819 RI--NEELLP-------------------------RKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEe 871
Cdd:PRK02224 441 RVeeAEALLEagkcpecgqpvegsphvetieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE- 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 872 NVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVR---LAQVETTLQEKRAELKHFDPALVRsIKEIP 948
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEaeeAREEVAELNSKLAELKERIESLER-IRTLL 598
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 949 LEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKR-----EQVLAEKESIEEFIQEIEGQKRQ 1016
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFdeariEEAREDKERAEEYLEQVEEKLDE 671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
209-973 |
4.47e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 209 EKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEivAKEKELAEIERQLEE 288
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 289 KSGDGIL----EITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQI 364
Cdd:PTZ00121 1301 KKKADEAkkkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 365 KERETvRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKA--LYMKESEISKFEEEISRAKARitqfnARRNLLKEKIA 442
Cdd:PTZ00121 1381 DAAKK-KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAEEA-----KKADEAKKKAE 1454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 443 EAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRIEG 522
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 523 LYGTLGELISVPKSEYALAVEvalggnyDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAMDV 602
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 603 VSydprfrnavayalgdtlivndmDEAREVGIGKVRMVTLGGELLERsgaitgghyKPRGKLGVNVDEIRKRVEALegRK 682
Cdd:PTZ00121 1608 KA----------------------EEAKKAEEAKIKAEELKKAEEEK---------KKVEQLKKKEAEEKKKAEEL--KK 1654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 683 EALEAQVNALKVEVKGLENElfelrmKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKL 762
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDK------KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 763 RGRIERLEKKREKIK-KALENPEARELNSKIREVEAEISKLKEELSR-----VESKLESLDSRINEELLPRKADLEEEIE 836
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 837 GLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEI----AELRKEKDELTSKLQELRIEA 912
Cdd:PTZ00121 1809 NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDgnkeADFNKEKDLKEDDEEEIEEAD 1888
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57159276 913 NTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEiplevEKLRQDIEKMEEEIRSLEPVNM 973
Cdd:PTZ00121 1889 EIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD-----EYIKRDAEETREEIIKISKKDM 1944
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
298-1030 |
4.50e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 298 TRKISEVKSKIEVAKRNieNAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQllvQIKERETVRNELVIK 377
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKT--ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE---DAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 378 LGEIDKRFSEAREefdkvvaeLEEAKKALYMKESEISKFEEEISRAKAritqfnARRNLLKEKIAEAKASLEAKRSELSQ 457
Cdd:PTZ00121 1165 KAEEARKAEDAKK--------AEAARKAEEVRKAEELRKAEDARKAEA------ARKAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 458 VEGKISKVESRHRKAEKE-LEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRieglygtlgeliSVPKS 536
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD------------EAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 537 EYALAVEvalggnydnvvvEDDRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAMDVVSYDPRFRNAVAYA 616
Cdd:PTZ00121 1299 EEKKKAD------------EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 617 LGDTLIVNDMDEAREVGIGKVRMVTLGGELLERS--GAITGGHYKPRGKLGVNVDEIRKRVE----ALEGRKEALEAQvN 690
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAeeDKKKADELKKAAAAKKKADEAKKKAEekkkADEAKKKAEEAK-K 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 691 ALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRsLKEEIEENERLISELEKRiEESKGEMAKLRGRIERle 770
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE-AKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEA-- 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 771 KKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEE---LLPRKADLEEEIEGlVNKINALNA 847
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknMALRKAEEAKKAEE-ARIEEVMKL 1600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 848 YIEENKNAITELEKELEELKTAEENVKDE-------------------LKELREGREQIRVEIAELRKEKDELTSKLQEL 908
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEeekkkveqlkkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 909 RIEANTLKVRLAQVETTLQEKRA--ELKHFDPALVRSIKEIPLEVE----KLRQDIEKMEEEIRSLEPVNMKAIEDFEVV 982
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 57159276 983 ERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLNAIAKNFS 1030
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
667-1023 |
1.11e-14 |
|
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: 78.91 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 667 NVDEIRKRVEALEGRKEA-----LEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEEN 741
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 742 ERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKalenpEARELNSKIREVEAEISKLKEELSRVESKLESLDSRIn 821
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-----LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 822 EELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDEL 901
Cdd:TIGR04523 443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 902 TSKLQELRIEANTLKVRLAQVETTLQEKRAELKHfdpalvrsiKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEV 981
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFELKK---------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 57159276 982 VERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLN 1023
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
4-161 |
8.63e-14 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 74.42 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYgnKKVVVPLARGFTAIVGANGSGKSNIGDAVlFVLGglSAKAMRASRISDLIFAGskgeppAKYAEV 83
Cdd:COG1195 1 RLKRLSLTNFRNY--ESLELEFSPGINVLVGPNGQGKTNLLEAI-YLLA--TGRSFRTARDAELIRFG------ADGFRV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 84 AMYFNNEDRGFPIdedEVVIKRrvypDGRSTYWLNGKRATR-SEIIDLLSAAMISPEGYNLVlqgditkfiKMSPIERR 161
Cdd:COG1195 70 RAEVERDGREVRL---GLGLSR----GGKKRVRINGKPVRRlSDLAGLLPVVLFSPEDLRLV---------KGGPSERR 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
250-967 |
1.16e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 250 REEEIEGQIKSLEDRLKEIAKEIV--AKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVakRNIENAQKEIEESQA 327
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAeeAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDA--RKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 328 RLRKSKEELKHV-----SEEIEKSKGAIKRWGKRREQLLVQIKE----RETVRNELVIKLGEI----DKRFSEAREEFDK 394
Cdd:PTZ00121 1155 EIARKAEDARKAeearkAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEArkaeDAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 395 VVAELEEAKKALYMKESE-ISKFEE----EISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRH 469
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEeIRKFEEarmaHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 470 RKAEkELEEKTRELQKVESELAK-AREELIKAEAQREVRGNRAVEFLKSQRIEglygtlgELISVPKSEYALAVEVAlgg 548
Cdd:PTZ00121 1315 KKAD-EAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEAEAAADEAEAAEEKA-------EAAEKKKEEAKKKADAA--- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 549 nydNVVVEDDRVAEKAIKLLKE--KKLGRLTFLPLNKIKPRSMREKPKLGIPAMDVVSYDPRFRNAvayalgdtlivndm 626
Cdd:PTZ00121 1384 ---KKKAEEKKKADEAKKKAEEdkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-------------- 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 627 DEAREVGIGKVRMVTLGGELLERSGAitgGHYKPRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKV--EVKGLENELF 704
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKK 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 705 ELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIER-LEKKR---------- 773
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARieevmklyee 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 774 ------EKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLdSRINEELLPRKADLEEEIEGLVNKINALNA 847
Cdd:PTZ00121 1604 ekkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 848 YIEENKNAITELEKELEELKTAEENVKDELKE------LREGREQIRVEIAELRKEKDELTSKLQELRIEANTlKVRLAQ 921
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAH 1761
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 57159276 922 VETTLQEKRAELKHFDPALVRsiKEIPLEVEKLRQDIEKMEEEIRS 967
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
189-900 |
1.86e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.06 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 189 ENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKarvtLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEI 268
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNID----KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 269 AKEIVAKEKELAEIERQLE---------EKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHV 339
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 340 SEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKrfsEAREEFDKVVaeleeakkalymkESEISKFEEE 419
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKEQDWNKEL-------------KSELKNQEKK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 420 ISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIK 499
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 500 AEAQREvrgnravefLKSQRIEGLygtlgelisvpKSEYalavevalggnydnvvveddRVAEKAIKLLKEKKLgrltfl 579
Cdd:TIGR04523 403 QEKLNQ---------QKDEQIKKL-----------QQEK--------------------ELLEKEIERLKETII------ 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 580 pLNKIKPRSMREKpklgipamdvvsydprfrnavAYALgdTLIVNDMDEAREVGIGKVRMVTLGGELLERSGAITGGHYK 659
Cdd:TIGR04523 437 -KNNSEIKDLTNQ---------------------DSVK--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 660 PRGKlgvNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLaedrsLKEEIE 739
Cdd:TIGR04523 493 SKEK---ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN-----LEKEID 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 740 ENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEAR--ELNSKIREVEAEISKLKEELSRVESKLESLD 817
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKisSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 818 ---SRINEELLP---RKADLEEEIEGLVNKINALNAYIEENKN--------AITELEKELEELKTAE--ENVKDELKELR 881
Cdd:TIGR04523 645 qevKQIKETIKEirnKWPEIIKKIKESKTKIDDIIELMKDWLKelslhykkYITRMIRIKDLPKLEEkyKEIEKELKKLD 724
|
730
....*....|....*....
gi 57159276 882 EGREQIRVEIAELRKEKDE 900
Cdd:TIGR04523 725 EFSKELENIIKNFNKKFDD 743
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-1014 |
2.27e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 383 KRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKI 462
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 463 SKVESRHRKAEKELEEKTRELQKVeselaKAREELIKAEAQREVRGNRAVEflksqrieglygtlgeliSVPKSEYALAV 542
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEV-----RKAEELRKAEDARKAEAARKAE------------------EERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 543 EvalggnyDNVVVEDDRVAEKAIKLLKEKKlgrltflplnkikpRSMREKPKLGIPAMDVVSYDPRFRNAVAYALGDTLI 622
Cdd:PTZ00121 1221 E-------DAKKAEAVKKAEEAKKDAEEAK--------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 623 VNDMDEAREVGIGKvrmvtlggELLERSGAITGGHYKPRGKLGVNVDEIRKRVEALEGRKEALE--AQVNALKVEVKGLE 700
Cdd:PTZ00121 1280 ADELKKAEEKKKAD--------EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAKKAAEAAKAE 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 701 NELFELRMKKSELSKDVQVIQKELDSYLAEdrSLKEEIEEnERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKAL 780
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKAD--AAKKKAEE-KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 781 ENPEARELNSKIREVEA--EISKLKEELSRVESKLESLDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITE 858
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 859 LEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELtSKLQELRIEANTLKV---RLAQVETTLQEKRAE-LK 934
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELKKAEEKKKAeeaKKAEEDKNMALRKAEeAK 1587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 935 HFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRslepVNMKAIEDFEVVERRYLELSSKREQvlaEKESIEEFIQEIEGQK 1014
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK----IKAEELKKAEEEKKKVEQLKKKEAE---EKKKAEELKKAEEENK 1660
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
5-1013 |
2.39e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.01 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSY-GNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGlsaKAMRASRISDLIFAGSKGEPPAKYAEV 83
Cdd:TIGR00618 3 PLRLTLKNFGSYkGTHTIDFTALGPIFLICGKTGAGKTTLLDAITYALYG---KLPRRSEVIRSLNSLYAAPSEAAFAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 AMYFNNEDRGFPID--------EDEVVIKRRVYPDGRSTYWLN-GKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIK 154
Cdd:TIGR00618 80 EFSLGTKIYRVHRTlrctrshrKTEQPEQLYLEQKKGRGRILAaKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 155 MSPIERRLIIDEISGIAEYdakkekalkelkqtEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLL 234
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQY--------------TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 235 AEIKRLEKFIEEGGSREEEIEGQIKSLE--DRLKEIAKEIVAKEKELAEIERQLEEKSGDgiLEITRKISEVKSKIEVAK 312
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKREAQEeqLKKQQLLKQLRARIEELRAQEAVLEETQER--INRARKAAPLAAHIKAVT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 313 RNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRwgKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEF 392
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ--RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 393 DKVVAELEEAKKALYMKESEISKFEEEISRAKARitqfNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKA 472
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTR----TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 473 EKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRieglygtlgeliSVPKSEYALAVEVALGGNYDN 552
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC------------PLCGSCIHPNPARQDIDNPGP 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 553 VVVEDDRVAEKAIKLLK--EKKLGRLTflplnkikprSMREKPKlgipamdvvsydpRFRNAVAYALGDTLIVNDMDEAR 630
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETseEDVYHQLT----------SERKQRA-------------SLKEQMQEIQQSFSILTQCDNRS 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 631 EVGIGKVRMVTlggellersgaitgghykprgklgvnvDEIRKRVEALEGRKEALEAQVNALKVEvKGLENELFELRMKK 710
Cdd:TIGR00618 583 KEDIPNLQNIT---------------------------VRLQDLTEKLSEAEDMLACEQHALLRK-LQPEQDLQDVRLHL 634
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 711 SELSKDVQVIQKELDSYLAEdrSLKEEIEENERLISELEKRIEESK-GEMAKLRGRIERLEKKREKIKKALENPEAREln 789
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLT--LTQERVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEMLAQCQTLLRELE-- 710
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 790 skirEVEAEISKLKEELSRVESKlesldsrineellpRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTA 869
Cdd:TIGR00618 711 ----THIEEYDREFNEIENASSS--------------LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA 772
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 870 EENVKDELKEL-------REGREQIRVEIAELRKE-KDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALv 941
Cdd:TIGR00618 773 ALQTGAELSHLaaeiqffNRLREEDTHLLKTLEAEiGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL- 851
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 942 RSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQ 1013
Cdd:TIGR00618 852 LKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADS 923
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
259-1011 |
2.98e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 259 KSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKH 338
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 339 VSEEIEKSKGAIKRWGKrreqllvQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEE 418
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEK-------QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 419 EISRAKARITQFNARRNLLKEKIAEAKasleakrselsQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELI 498
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKNK-----------SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 499 KAEAQRevrgNRAVEFLKSQRIEglygtlgelisvpkseyalavevalggnydnvvveddrvAEKAIKLLKEKKLGrltf 578
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKE---------------------------------------LEQNNKKIKELEKQ---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 579 lpLNKIKPRsmrekpklgipamdvvsydprfrnavayalgdtliVNDMDEAREVGIGKvrmvtlggellersgaitgghy 658
Cdd:TIGR04523 290 --LNQLKSE-----------------------------------ISDLNNQKEQDWNK---------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 659 kprgKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEI 738
Cdd:TIGR04523 311 ----ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 739 EENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENpeareLNSKIREVEAEISKLKEELSRVESKLESLDS 818
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-----LKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 819 RINEellprkadLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEK 898
Cdd:TIGR04523 462 TRES--------LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 899 DELTSKLQELRIEANTLKVRL--AQVETTLQEKR---AELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNM 973
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELkkENLEKEIDEKNkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
730 740 750
....*....|....*....|....*....|....*...
gi 57159276 974 KAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIE 1011
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
658-1135 |
4.12e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 658 YKPRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSY--LAEDRSLK 735
Cdd:COG4717 59 FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 736 EEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENP-------------EARELNSKIREVEAEISKL 802
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeelqdlaeELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 803 KEELSRVESKLESLDSRINEE----------------------------------------------------LLPRKAD 830
Cdd:COG4717 219 QEELEELEEELEQLENELEAAaleerlkearlllliaaallallglggsllsliltiagvlflvlgllallflLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 831 LEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAE--------ENVKDELKELREGREQIRVEIAELRKEK---- 898
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllelldriEELQELLREAEELEEELQLEELEQEIAAllae 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 899 ------DELTSKLQELRiEANTLKVRLAQVETTLQEK----RAELKHFDPALVRS-IKEIPLEVEKLRQDIEKMEEEIRS 967
Cdd:COG4717 379 agvedeEELRAALEQAE-EYQELKEELEELEEQLEELlgelEELLEALDEEELEEeLEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 968 LEpVNMKAIEDFEVVERRYLELSSKREQV--LAEK--------ESIEEFIQEIEGQKRQVFLQTLnaiaknfSELFAKLS 1037
Cdd:COG4717 458 LE-AELEQLEEDGELAELLQELEELKAELreLAEEwaalklalELLEEAREEYREERLPPVLERA-------SEYFSRLT 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1038 PGGEAKLILEnpedpfsGGLEIEAKPAGKDVKRIEAMSGGEKAIIALAFVFA-IQRYKPAPF-YLLDEIDAHLDDANVKR 1115
Cdd:COG4717 530 DGRYRLIRID-------EDLSLKVDTEDGRTRPVEELSRGTREQLYLALRLAlAELLAGEPLpLILDDAFVNFDDERLRA 602
|
570 580
....*....|....*....|
gi 57159276 1116 VADLIKEASQNSQFIVITHR 1135
Cdd:COG4717 603 ALELLAELAKGRQVIYFTCH 622
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
685-911 |
4.80e-13 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 73.12 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 685 LEAQVNALKVEVKGLENELFELRMKKSElskDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRG 764
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGE---NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 765 RIERLEKKREKIKKAL----ENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEEllprkADLEEEIEGLVN 840
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL-----EEIMDEFNEQSK 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57159276 841 KINALNAYIEENKNAITELEKELEElktaeenVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIE 911
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKK-------VKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
4-221 |
5.19e-13 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 72.11 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYgnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFvlggLS-AKAMRASRISDLIFAGskgeppAKYAE 82
Cdd:PRK00064 2 YLTRLSLTDFRNY--EELDLELSPGVNVLVGENGQGKTNLLEAIYL----LApGRSHRTARDKELIRFG------AEAAV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 83 VAMYFNNEDRGFPIdedEVVIKRrvypDGRSTYWLNGKRATR-SEIIDLLSAAMISPEGYNLVlqgditkfiKMSPIERR 161
Cdd:PRK00064 70 IHGRVEKGGRELPL---GLEIDK----KGGRKVRINGEPQRKlAELAGLLNVVLFTPEDLRLV---------KGGPSERR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 162 LIIDEISGiaeydakkekalkelkQTEENLARvdllireVKAQLDKLEKERNDALRYLDL 221
Cdd:PRK00064 134 RFLDRLLF----------------QIEPVYAS-------ALSQYERALKQRNALLKQADY 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
389-1160 |
2.56e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 71.47 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 389 REEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKR---SELSQVEGKISKV 465
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNryeSEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 466 ESRHRKAeKELEEKTRELqkVESELAKAREELIKAEAQREVRGNraveflKSQRIEGLYGtlgeliSVPKSEYALAVEVA 545
Cdd:PRK01156 269 LEKNNYY-KELEERHMKI--INDPVYKNRNYINDYFKYKNDIEN------KKQILSNIDA------EINKYHAIIKKLSV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 546 LGGNYDNVVVEDDRVAE--KAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAMDVVSYDPRFRNAVAYALGDTLI- 622
Cdd:PRK01156 334 LQKDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNe 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 623 --VNDMDEAREVGIGKVRMVTLGGEL--LERSGAITGGHYK-PRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVK 697
Cdd:PRK01156 414 inVKLQDISSKVSSLNQRIRALRENLdeLSRNMEMLNGQSVcPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 698 GLENELFELRMKKSELSKdvqviqKELDSYLAEDRSLK------EEIEENERLISELEKRIEESKGEMAKLRgrIERLEK 771
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLES------EEINKSINEYNKIEsaradlEDIKIKINELKDKHDKYEEIKNRYKSLK--LEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 772 KREKIKKAL---ENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELlprkADLEEEIEGLVNKINAlnay 848
Cdd:PRK01156 566 KRTSWLNALaviSLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI----REIENEANNLNNKYNE---- 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 849 IEENKNAItelekeleelktaeenvkdelKELREGREQIRVEIAElrkeKDELTSKLQELRIEANTLKVRLAQVETTLQE 928
Cdd:PRK01156 638 IQENKILI---------------------EKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDD 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 929 ---KRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIrslepvnmKAIEDFevveRRYLELSSKREQVLAEKESIEE 1005
Cdd:PRK01156 693 akaNRARLESTIEILRTRINELSDRINDINETLESMKKIK--------KAIGDL----KRLREAFDKSGVPAMIRKSASQ 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1006 FIQEIEGQKRQVFLQTLNAIAKNfSELFAKLSPGGEaklilenpedpfsggleieakpagkdVKRIEAMSGGEKAIIALA 1085
Cdd:PRK01156 761 AMTSLTRKYLFEFNLDFDDIDVD-QDFNITVSRGGM--------------------------VEGIDSLSGGEKTAVAFA 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1086 FVFAIQRY--KPAPFYLLDEIDAHLDDANVKRVADLI----KEASQNSQFIVITHRDVMMAQADRIIGVSMRNGVSKVVS 1159
Cdd:PRK01156 814 LRVAVAQFlnNDKSLLIMDEPTAFLDEDRRTNLKDIIeyslKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVIP 893
|
.
gi 57159276 1160 L 1160
Cdd:PRK01156 894 L 894
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-208 |
2.70e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 66.96 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKkVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKamRASRISDLIFAGSKGeppakyAEVA 84
Cdd:COG0419 2 LLRLRLENFRSYRDT-ETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSEE------ASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEDRgfpidedEVVIKRRvypdgrstywlngkratrseiidllsaamispegynlvlQGDITKFIKMSPIERRLII 164
Cdd:COG0419 73 LEFEHGGK-------RYRIERR---------------------------------------QGEFAEFLEAKPSERKEAL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57159276 165 DEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKL 208
Cdd:COG0419 107 KRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQL 150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
699-932 |
4.71e-12 |
|
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: 69.02 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 699 LENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKK 778
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 779 ALenpeARELNSKIRevEAEISKLKEELSRVESKLESLDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNAIte 858
Cdd:COG4942 105 EL----AELLRALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL-- 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 859 lekeleelKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAE 932
Cdd:COG4942 177 --------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
200-523 |
6.64e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 200 EVKAQLDKLEKERNDALRYLDLKEKLEKARvtlllAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKEL 279
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAK-----KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 280 AEIERQLEEKSGDGilEITRKISEVKSKIEVAKRNIENAQKEIEEsqarlRKSKEELKHVSEEIEKSKGAIKRWGKRREQ 359
Cdd:PTZ00121 1374 EEAKKKADAAKKKA--EEKKKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 360 LLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKES--EISKFEEEISRAKARITQFNARRNLL 437
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 438 KEKIAEAKASLEAKRSELSQVEGKISKVESRhRKAE--KELEEKTRELQKVESELAKArEELIKAEAQREVRGNRAVEFL 515
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEEL-KKAEekKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEE 1604
|
....*...
gi 57159276 516 KSQRIEGL 523
Cdd:PTZ00121 1605 KKMKAEEA 1612
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
745-966 |
9.78e-12 |
|
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: 68.25 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 745 ISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALEnpearELNSKIREVEAEISKLKEELSRVESKLESLDSRInEEL 824
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIRALEQELAALEAELAELEKEI-AEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 825 LPRKADLEEEIEGLVNKINALNAYIEE----NKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDE 900
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 901 LTSKLQELRIEANTLKVRLAQVETTLQEKRAELKhfdpALVRSIKEIPLEVEKLRQDIEKMEEEIR 966
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELA----ELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
5-856 |
1.02e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 69.55 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKKVVvpLARGFTAIVGANGSGKSNIGDAVLFVLGGlsakAMRASRISDLIFAGskgeppAKYAEVA 84
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFALFT----DKRTEKIEDMIKKG------KNNLEVE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEDRGFPIDEDevVIKRRVYPDGRSTYWLNGKRATR--SEIIDLLSAAMISPE-----GYNLVLQGDITKFIKMSP 157
Cdd:PRK01156 71 LEFRIGGHVYQIRRS--IERRGKGSRREAYIKKDGSIIAEgfDDTTKYIEKNILGISkdvflNSIFVGQGEMDSLISGDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 158 IERRLIIDEISGIaeydakkekalkelkqteENLARVDLLIREVkaqLDKLEKERNDalrYLDLKEKLEKARVtlllaEI 237
Cdd:PRK01156 149 AQRKKILDEILEI------------------NSLERNYDKLKDV---IDMLRAEISN---IDYLEEKLKSSNL-----EL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 238 KRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKsgdgileitRKISEVKSKIEVAKRNIEN 317
Cdd:PRK01156 200 ENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK---------NRYESEIKTAESDLSMELE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 318 AQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEArEEFDKVVA 397
Cdd:PRK01156 271 KNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDY-IKKKSRYD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 398 ELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSqvegkiskvesrhrkaeKELE 477
Cdd:PRK01156 350 DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK-----------------KELN 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 478 EKTRELQKVESELAKAREElIKAEAQREVRGNRAVEFLKSQRIEGLYGT-LGElisvPKSEYAlaveVALGGNYDNVVVE 556
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQR-IRALRENLDELSRNMEMLNGQSVCPVCGTtLGE----EKSNHI----INHYNEKKSRLEE 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 557 DDRVAEKAIKLLKEKKlgrltfLPLNKIKPRSMREKPKlgipamDVVSYDPRFRNAVAYALGDTLIVNDMDEARevgigk 636
Cdd:PRK01156 484 KIREIEIEVKDIDEKI------VDLKKRKEYLESEEIN------KSINEYNKIESARADLEDIKIKINELKDKH------ 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 637 vrmvTLGGELLERSGAITGGHYKPRGKLGVNVDEIRKR--VEALEGRKEALEAQVNALkveVKGLENELFELRMKKSELS 714
Cdd:PRK01156 546 ----DKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLidIETNRSRSNEIKKQLNDL---ESRLQEIEIGFPDDKSYID 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 715 KDVQVIQKELDSYlaedRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERlekkrekikKALENPEARELNSKIRE 794
Cdd:PRK01156 619 KSIREIENEANNL----NNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPD---------LKEITSRINDIEDNLKK 685
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 795 VEAEISKLKEELSRVESKLESLDSRINeELLPRKADLEEEIEGLvNKINALNAYIEENKNAI 856
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRIN-ELSDRINDINETLESM-KKIKKAIGDLKRLREAF 745
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1075-1153 |
1.18e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 69.02 E-value: 1.18e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 1075 SGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIgvSMRNG 1153
Cdd:COG4988 475 SGGQAQRLALARAL----LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRIL--VLDDG 547
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
19-501 |
1.46e-11 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 68.56 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 19 KKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGlsakamRASriSDLIFAGskgeppAKYAEVAMYFNN--------- 89
Cdd:COG0497 14 DELELEFGPGLTVLTGETGAGKSILLDALGLLLGG------RAD--ASLVRHG------ADKAEVEAVFDLsddpplaaw 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 90 -EDRGFPIDEDEVVIKRRVYPDGRSTYWLNGKRATRSeiidLLSAAMispegynlvlqgditkfikmspieRRLIidEIS 168
Cdd:COG0497 80 lEENGLDLDDGELILRREISADGRSRAFINGRPVTLS----QLRELG------------------------ELLV--DIH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 169 GiaeydakkekalkelkQTEenlarvDLLIREVKAQLDKLekernDAlrYLDLKEKLEKarVTLLLAEIKRLEKfieegg 248
Cdd:COG0497 130 G----------------QHE------HQSLLDPDAQRELL-----DA--FAGLEELLEE--YREAYRAWRALKK------ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 249 sreeeiegqiksledRLKEIAKEIVAKEKELAEIERQLEEksgdgileitrkisevkskievakrnIENAQKEIEEsQAR 328
Cdd:COG0497 173 ---------------ELEELRADEAERARELDLLRFQLEE--------------------------LEAAALQPGE-EEE 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 329 LRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKEretVRNELViKLGEIDKRFSEAREEFDKVVAELEEAkkalym 408
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEALEALSGGEGGALDLLGQ---ALRALE-RLAEYDPSLAELAERLESALIELEEA------ 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 409 kESEISKFEEEISRAKARITQFNARRNLLK----------EKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEE 478
Cdd:COG0497 281 -ASELRRYLDSLEFDPERLEEVEERLALLRrlarkygvtvEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLE 359
|
490 500
....*....|....*....|...
gi 57159276 479 KTRELQKVESELAKAREELIKAE 501
Cdd:COG0497 360 AAEKLSAARKKAAKKLEKAVTAE 382
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1072-1153 |
1.48e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 68.64 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1072 EAMSGGEKAIIALAFVFAiqryKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIgvSMR 1151
Cdd:COG4987 470 RRLSGGERRRLALARALL----RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL--VLE 543
|
..
gi 57159276 1152 NG 1153
Cdd:COG4987 544 DG 545
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-510 |
1.61e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 257 QIKSLEDRLKEIAKEIVAKEKELAEIERQLEEksgdgileITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEEL 336
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA--------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 337 KHVSEEIEKSKGAIKrwgkrrEQLLVQIKERETVRNELVIKlgeidkrfSEAREEFDKVVAELEEAKKALYMKESEISKF 416
Cdd:COG4942 93 AELRAELEAQKEELA------ELLRALYRLGRQPPLALLLS--------PEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 417 EEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREE 496
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....
gi 57159276 497 LIKAEAQREVRGNR 510
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-507 |
1.82e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 273 VAKEKELAEIERQLEEksgdgileITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKR 352
Cdd:COG4942 16 AAQADAAAEAEAELEQ--------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 353 WGKRREQLLVQIKERETVRNELVIKLgeidkrFSEAREEFDKVVAELEEAKKAL----YMKE--SEISKFEEEISRAKAR 426
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRAL------YRLGRQPPLALLLSPEDFLDAVrrlqYLKYlaPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 427 ITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREV 506
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
.
gi 57159276 507 R 507
Cdd:COG4942 242 R 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
669-1005 |
2.68e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 669 DEIRKRVEALEGRKeaLEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSY---LAEDRSLKEEIEENERLI 745
Cdd:PRK02224 190 DQLKAQIEEKEEKD--LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 746 SELEKRIEESKGEMAKLRGRIERLEKKREKI--KKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRInEE 823
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA-ES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 824 LLPRKADLEEEIEGLVNKINALNAYIEENKNAITELekeleelktaeenvKDELKELREGREQIRVEIAELRKEKDELTS 903
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDR--------------REEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 904 KLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPAL-----------------VRSIKEIPLEVEKLRQDIEKMEEEIR 966
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 57159276 967 SLEPvNMKAIEDFEVVERRYLELSSKRE---QVLAEKESIEE 1005
Cdd:PRK02224 493 EVEE-RLERAEDLVEAEDRIERLEERREdleELIAERRETIE 533
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
712-1134 |
2.88e-11 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 67.84 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 712 ELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEM-------AKLRGRIERLEKKREKIKKALENpE 784
Cdd:COG4694 103 ELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDlkklfasSGRNYRKANLEKKLSALKSSSED-E 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 785 ARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELLPR-KADLEEEIEGLVNK--INALNAYIEENKNAI----- 856
Cdd:COG4694 182 LKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVSSaIEELAALIQNPGNSdwVEQGLAYHKEEEDDTcpfcq 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 857 --TELEKELEELKTAEENVKDELKELREGREQIRVEIAELRK-----EKDELTSKLQELRIEANTLKVRLAQVETTLQEK 929
Cdd:COG4694 262 qeLAAERIEALEAYFDDEYEKLLAALKDLLEELESAINALSAllleiLRTLLPSAKEDLKAALEALNALLETLLAALEEK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 930 RAEL-KHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLElsskrEQVLAEKESIEEFIQ 1008
Cdd:COG4694 342 IANPsTSIDLDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHELAELK-----EDLSRYKAEVEELIE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1009 EIEGQKRqvFLQTLNAIAKNFSELFAKLSPGGE-AKLILENPEDPFSGGLEIEAKPAGKDVKRI-----------EAMSG 1076
Cdd:COG4694 417 ELKTIKA--LKKALEDLKTEISELEAELSSVDEaADEINEELKALGFDEFSLEAVEDGRSSYRLkrngendakpaKTLSE 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 1077 GEKAIIALAFVFA-----IQRYKPAPFYLLDEIDAhLDDANVKRVADLIK-EASQNSQFIVITH 1134
Cdd:COG4694 495 GEKTAIALAYFLAelegdENDLKKKIVVIDDPVSS-LDSNHRFAVASLLKeLSKKAKQVIVLTH 557
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
669-825 |
2.91e-11 |
|
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: 64.95 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 669 DEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSY---LAEDRSLKE------EIE 739
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqLGNVRNNKEyealqkEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 740 ENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKalenpearELNSKIREVEAEISKLKEELSRVESKLESLDSR 819
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEA--------ELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
....*.
gi 57159276 820 INEELL 825
Cdd:COG1579 172 IPPELL 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1074-1153 |
3.22e-11 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 62.65 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1074 MSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKE-ASQNSQFIVITHR-DVMMAQADRIIGvsMR 1151
Cdd:cd00267 81 LSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDpELAELAADRVIV--LK 154
|
..
gi 57159276 1152 NG 1153
Cdd:cd00267 155 DG 156
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
209-1014 |
3.25e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 209 EKERNDALRYLDLKEKLEKARvtllLAEIKRL--EKFIEEGGSREEEIEgqiKSLEDRLKEIAKEIVAKEKelAEIERQL 286
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDAR----KAEEARKaeDAKKAEAARKAEEVR---KAEELRKAEDARKAEAARK--AEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 287 EEKSGdgiLEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKE-ELKHVSEEIEKSKGAIKRWGKRREQLLVQIK 365
Cdd:PTZ00121 1215 EEARK---AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEaRMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 366 ERETVRNELVIKLGEIDKRFSEAREEfDKVVAELEEAKKAL--YMKESEISKFEEEISRAKARITQFNARRNLLKEKIAE 443
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKAdaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 444 AKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQR--EVRGNRAVEFLKSQRIE 521
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 522 glygtlgelisvPKSEYALAVEVALGGnydnvvVEDDRVAEKAIKLLKEKKLGRLTflplnKIKPRSMREKPKLGIPAMD 601
Cdd:PTZ00121 1451 ------------KKAEEAKKAEEAKKK------AEEAKKADEAKKKAEEAKKADEA-----KKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 602 VVSYDPRFRNAVAYALGDTLivNDMDEAREVGIGKVRMVTLGGELLERSGAITGGHYKPRGKLGVNVDEIR----KRVEA 677
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmalRKAEE 1585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 678 LEGRKEALEAQVNALKVEVKGLENElfELRMKKSELSKDVQVIQKELDSYLAEdrSLKEEIEENERLISELEKRIEESKG 757
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELKKAEEEKKKVE--QLKKKEAEEKKKAEELKKAEEENKI 1661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 758 EMAKLRgrierlEKKREKIKKAlenPEARELNSKIREVEAEISKLKEELSRVES--KLESLDSRINEELlpRKADLEEEI 835
Cdd:PTZ00121 1662 KAAEEA------KKAEEDKKKA---EEAKKAEEDEKKAAEALKKEAEEAKKAEElkKKEAEEKKKAEEL--KKAEEENKI 1730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 836 eglvnKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEanTL 915
Cdd:PTZ00121 1731 -----KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK--DI 1803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 916 KVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAiedfevverrylelSSKREQ 995
Cdd:PTZ00121 1804 FDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED--------------GNKEAD 1869
|
810
....*....|....*....
gi 57159276 996 VLAEKESIEEFIQEIEGQK 1014
Cdd:PTZ00121 1870 FNKEKDLKEDDEEEIEEAD 1888
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
673-963 |
6.30e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 66.46 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 673 KRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEkri 752
Cdd:pfam07888 59 KEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE--- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 753 EESKGEMAKLRGRIERLEKKREKIKKAL-----ENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEellpr 827
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAGaqrkeEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ----- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 828 kadLEEEIEGLVNKINALNAYIEENknaitelekeleelktaeENVKDELKELRE-------GREQIRVEIAELRKEKDE 900
Cdd:pfam07888 211 ---LQDTITTLTQKLTTAHRKEAEN------------------EALLEELRSLQErlnaserKVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 901 LTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEE 963
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1059-1146 |
1.00e-10 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 65.77 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1059 IEAKPAGKDVK---RIEAMSGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHR 1135
Cdd:TIGR02857 441 VAALPQGLDTPigeGGAGLSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHR 516
|
90
....*....|.
gi 57159276 1136 DVMMAQADRII 1146
Cdd:TIGR02857 517 LALAALADRIV 527
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
210-1011 |
1.62e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 210 KERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKE-------IVAKEKELAEI 282
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEikndkeqKNKLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 283 ERQLEEKSGDGILEITRkISEVKSKIEVAKRNIENAQKEIEEsqarLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLV 362
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTE-IKKKEKELEKLNNKYNDLKKQKEE----LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 363 QIKERETVRNELVIKLGEIDKRFSEAREEFDKvvaeleeakkalymKESEISKFEEEISRAKARITQfnarrnlLKEKIA 442
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEK--------------KQQEINEKTTEISNTQTQLNQ-------LKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 443 EAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRE-----LQKVESELAKAREELIKAEAQReVRGNRAVEFLKS 517
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQI-SQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 518 QrIEGLYGTLGELISVPKSeyalavevalggnydnvvvEDDRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLgi 597
Cdd:TIGR04523 343 Q-ISQLKKELTNSESENSE-------------------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 598 pamdvvsydprfrnavayalgdtlivndmDEAREVgigkvrmvtlggellersgaitgghykpRGKLGVNVDEIRKRVEA 677
Cdd:TIGR04523 401 -----------------------------QNQEKL----------------------------NQQKDEQIKKLQQEKEL 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 678 LEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKG 757
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 758 EMAKLRGRIERLEKKREkikkalenpearELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELlprkadLEEEIEG 837
Cdd:TIGR04523 504 EKKELEEKVKDLTKKIS------------SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN------LEKEIDE 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 838 LVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKV 917
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 918 RLAQVETTLQEKRAELkhfdPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEP---VNMKAIEDFEVVERRYLELSSKRE 994
Cdd:TIGR04523 646 EVKQIKETIKEIRNKW----PEIIKKIKESKTKIDDIIELMKDWLKELSLHYKkyiTRMIRIKDLPKLEEKYKEIEKELK 721
|
810
....*....|....*..
gi 57159276 995 QVLAEKESIEEFIQEIE 1011
Cdd:TIGR04523 722 KLDEFSKELENIIKNFN 738
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
5-105 |
2.05e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 64.18 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYgnKKVVVPLARgFTAIVGANGSGKSNIGDAVLF----VLGGLSAKAMRASRISDLIFAGSKGEPPAky 80
Cdd:COG4637 2 ITRIRIKNFKSL--RDLELPLGP-LTVLIGANGSGKSNLLDALRFlsdaARGGLQDALARRGGLEELLWRGPRTITEP-- 76
|
90 100 110
....*....|....*....|....*....|....
gi 57159276 81 AEVAMYFNNEDR---------GFPIDEDEVVIKR 105
Cdd:COG4637 77 IRLELEFAEEDErdlryelelGLPEPGGRPEVKE 110
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
663-1015 |
2.44e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 663 KLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKeldsYLAEDRSLKEEIEENE 742
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK----KIQKNKSLESQISELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 743 RLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENpEARELNSKIREVE---AEISKLKEELSRVESKLESLDSR 819
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 820 INEELLprkADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKD 899
Cdd:TIGR04523 304 KEQDWN---KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 900 ELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIplevEKLRQDIEKMEEEIRSLEpvnmkaiEDF 979
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI----ERLKETIIKNNSEIKDLT-------NQD 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 57159276 980 EVVERRYLELSSKREQvlaEKESIEEFIQEIEGQKR 1015
Cdd:TIGR04523 450 SVKELIIKNLDNTRES---LETQLKVLSRSINKIKQ 482
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1075-1146 |
2.80e-10 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 60.47 E-value: 2.80e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1075 SGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:cd03228 98 SGGQRQRIAIARAL----LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
200-521 |
2.92e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 200 EVKAQLDKLEKERNDALRYLDLKEKLEkarvtlllaEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKEL 279
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAE---------EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 280 AEIERQLEEKSGDGilEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHvSEEIEKSKGAIKRWGKRR-- 357
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEKKKad 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 358 ------------EQLLVQIKERETVRNELVIKLGEIDKRFSEAREEfdKVVAELEEAKKalyMKESEISKFEEEISRAKA 425
Cdd:PTZ00121 1550 elkkaeelkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKK---MKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 426 RITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRhRKAEKElEEKTRELQKVESELAKAREELIKAEAQR- 504
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEED-KKKAEEAKKAEEDEKKAAEALKKEAEEAk 1702
|
330 340
....*....|....*....|
gi 57159276 505 ---EVRGNRAVEFLKSQRIE 521
Cdd:PTZ00121 1703 kaeELKKKEAEEKKKAEELK 1722
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
255-493 |
5.85e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 255 EGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEksgdgileITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKE 334
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEE--------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 335 ELKHVSEEIEKSKGAIKRWgkrreQLLVQIKERETV--RNELVIKLGEIDKrfsEAREEFDKVVAELEEAKKALYMKESE 412
Cdd:COG3883 87 ELGERARALYRSGGSVSYL-----DVLLGSESFSDFldRLSALSKIADADA---DLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 413 ISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAK 492
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
.
gi 57159276 493 A 493
Cdd:COG3883 239 A 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-1015 |
6.08e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 679 EGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYlaedrslKEEIEENERLISELEKRIEESKGE 758
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND-------KEQKNKLEVELNKLEKQKKENKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 759 MAKLRGRIERLEKKREKIkkaleNPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRIN---------EELLPRKA 829
Cdd:TIGR04523 140 IDKFLTEIKKKEKELEKL-----NNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLklelllsnlKKKIQKNK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 830 DLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELR 909
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 910 IEANTLKVRLAQ-----VETTLQEKRAELKHFDPALVRSIKEIplevEKLRQDIEKMEEEIRSLEPVNMKAIEDFEvver 984
Cdd:TIGR04523 295 SEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKII----SQLNEQISQLKKELTNSESENSEKQRELE---- 366
|
330 340 350
....*....|....*....|....*....|.
gi 57159276 985 rylELSSKREQVLAEKESIEEFIQEIEGQKR 1015
Cdd:TIGR04523 367 ---EKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
200-511 |
1.21e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 200 EVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEiegqiKSLEDRLKEIAKEIVAKEKEL 279
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEAKKKADEA 1502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 280 AEIERQLEEKSGDGILEITRKISEVKSKIEvaKRNIENAQKEIEESQARLRKSKEELKHVSE----EIEKSKGAIKRWGK 355
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAEEKKKADELKKAEELKKAEEkkkaEEAKKAEEDKNMAL 1580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 356 RREQLLVQIKERetvRNELVIKLGEIDKRF--SEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNAR 433
Cdd:PTZ00121 1581 RKAEEAKKAEEA---RIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 434 RNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRA 511
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
669-913 |
1.54e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 669 DEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELdsylaedRSLKEEIEENERLISEL 748
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-------AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 749 EKRIEESKGEMAKLRGRIERLEkKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDsRINEELLPRK 828
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-ALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 829 ADLEEEIEGLVNKINALNAYIEENKNAITelekeleELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQEL 908
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLA-------RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*
gi 57159276 909 RIEAN 913
Cdd:COG4942 247 GFAAL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
233-409 |
1.67e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 233 LLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAK 312
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 313 --RNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLlvqIKERETVRNELVIKLGEIDKRFSEARE 390
Cdd:COG1579 87 nnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL---EAELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|....*....
gi 57159276 391 EFDKVVAELEEAKKALYMK 409
Cdd:COG1579 164 EREELAAKIPPELLALYER 182
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
666-962 |
1.74e-09 |
|
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: 62.44 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 666 VNVDEIRKRVEALEGRKEALEAQVNALKVEVKG-LENELFELRMKKSELSKdVQVIQKELDSYLAEDRSLKEEI------ 738
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGqMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELtakkmt 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 739 -EENERLISEL-------EKRIEESKGEMAKLRGRIERLEKKREKIKKALENpearelnskIREVEAEISKLKEELSRVE 810
Cdd:pfam15921 491 lESSERTVSDLtaslqekERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH---------LRNVQTECEALKLQMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 811 SKLESLDSRINE-------------ELLPRKADLEEEIEGLVNKINALNAyIEENKNAITELEKELEELKTAEEnvkdeL 877
Cdd:pfam15921 562 KVIEILRQQIENmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKI-LKDKKDAKIRELEARVSDLELEK-----V 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 878 KELREGREQIRVeIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQD 957
Cdd:pfam15921 636 KLVNAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
....*
gi 57159276 958 IEKME 962
Cdd:pfam15921 715 LKSME 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-928 |
1.78e-09 |
|
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: 62.44 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 189 ENLARVDLLIREVKAQLDkLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEggsrEEEIEGQIKSLEDRLKEI 268
Cdd:pfam15921 125 ERDAMADIRRRESQSQED-LRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 269 AKEIVAKEKELAEIE-RQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKE--------IEESQARLRK--SKEELK 337
Cdd:pfam15921 200 SGKKIYEHDSMSTMHfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSEsqnkiellLQQHQDRIEQliSEHEVE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 338 hVSEEIEKSKGAIKRWGKRREQLLVqIKERETVRNELVIK-LGEIDKRFSEAReefdkvvAELEEAKKalyMKESEISKF 416
Cdd:pfam15921 280 -ITGLTEKASSARSQANSIQSQLEI-IQEQARNQNSMYMRqLSDLESTVSQLR-------SELREAKR---MYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 417 EEEISRAKARIT-------QFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHR-------KAEKELEEKTRE 482
Cdd:pfam15921 348 EKQLVLANSELTearterdQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 483 LQKVESELakareELIKAEAQREVRGNRAVEFLKSQRIEGLYGTLGELISVpkSEYALAVEVALGGNYDNVVVEDDRVAE 562
Cdd:pfam15921 428 VQRLEALL-----KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKKMTLESSERTVSD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 563 KAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLgipaMDVVSYDPRFRNAVAYALGDTLIVNDMDEAREVGIGKVRMVTl 642
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMT- 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 643 ggELLERSGAITGGHYKPRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQK 722
Cdd:pfam15921 576 --QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 723 ELDSYLAEDRSLKeeieenerliSELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEArelnskireveaeiskl 802
Cdd:pfam15921 654 ERDQLLNEVKTSR----------NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS----------------- 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 803 keELSRVESKLESLDSRiNEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITelekeleelktaeeNVKDELKELRE 882
Cdd:pfam15921 707 --ELEQTRNTLKSMEGS-DGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------------NANKEKHFLKE 769
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 57159276 883 GREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQE 928
Cdd:pfam15921 770 EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
186-499 |
1.98e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 61.79 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKL-EKERNDALRYLDLKEKLEKARVTLLlaeiKRLEKFieegGSREEEIEGQIKSLEDR 264
Cdd:pfam06160 90 EIEELLDDIEEDIKQILEELDELlESEEKNREEVEELKDKYRELRKTLL----ANRFSY----GPAIDELEKQLAEIEEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 265 LKEI-----------AKEIVAK-EKELAEIERQLEEKSG---DGILEITRKISEVKS---KIEVAKRNIE--NAQKEIEE 324
Cdd:pfam06160 162 FSQFeeltesgdyleAREVLEKlEEETDALEELMEDIPPlyeELKTELPDQLEELKEgyrEMEEEGYALEhlNVDKEIQQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 325 SQARLRKSKE-----ELKHVSEEIEKSKGAIkrwgkrreQLLVQIKERE-TVRNELVIKLGEIDKRFSEAREEFDKVVAE 398
Cdd:pfam06160 242 LEEQLEENLAllenlELDEAEEALEEIEERI--------DQLYDLLEKEvDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 399 LEEAKKALYMKESEISKFEEeisrAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHrkaeKELEE 478
Cdd:pfam06160 314 LERVQQSYTLNENELERVRG----LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQ----EEFKE 385
|
330 340
....*....|....*....|.
gi 57159276 479 KTRELQKVESElakAREELIK 499
Cdd:pfam06160 386 SLQSLRKDELE---AREKLDE 403
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
359-522 |
3.18e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.78 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 359 QLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKAR------------ 426
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 427 ----ITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKA-- 500
Cdd:COG1579 94 lqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKip 173
|
170 180
....*....|....*....|....*....
gi 57159276 501 -------EAQREVRGNRAVEFLKSQRIEG 522
Cdd:COG1579 174 pellalyERIRKRKNGLAVVPVEGGACGG 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
747-969 |
3.29e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 747 ELEKRIEESKGEMAKLRGRIERLEKKREKIKkALEnpEARELNSKIREVEAEISKLKEELSRV-----ESKLESLDSRIn 821
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIE-LLE--PIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAEL- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 822 EELLPRKADLEEEIEGLVNKINALNAYIEENKNAItelekeleelktaEENVKDELKELREgreqirvEIAELRKEKDEL 901
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQI-------------RGNGGDRLEQLER-------EIERLERELEER 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 902 TSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLE 969
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
198-405 |
3.43e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 198 IREVKAQLDKLEKERNDALRYLDLKEKLEKArvtlLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEK 277
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 278 ELAEIERQLEEK-----------------SGDGILEITRKISEVKSKIEVAKRNIE---NAQKEIEESQARLRKSKEELK 337
Cdd:COG4942 98 ELEAQKEELAELlralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 338 HVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKA 405
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1062-1152 |
3.47e-09 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 57.99 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1062 KPAGKDVKrieAMSGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVAD-LIKEA--SQNSQFIVITHRDV- 1137
Cdd:cd03276 101 KAAVRDVK---TLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDlLVKEAkkQPGRQFIFITPQDIs 177
|
90
....*....|....*
gi 57159276 1138 MMAQADRIIGVSMRN 1152
Cdd:cd03276 178 GLASSDDVKVFRMKD 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
313-803 |
4.56e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 313 RNIENAQKEIEESQARLRKSKEELKHVSEEIEKskgaIKRWGKRREQLLVQIKERETVRNEL--VIKLGEIDKRFSEARE 390
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 391 EfdkvVAELEEAKKALYMKESEISKFEEEISRAKARITQfnarrnlLKEKIAEAKASL-EAKRSELSQVEGKISKVESRH 469
Cdd:COG4717 140 E----LAELPERLEELEERLEELRELEEELEELEAELAE-------LQEELEELLEQLsLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 470 RKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRIEGLYGTLGELISVPKSEYALAVEVALGGN 549
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 550 YdnvvveddrvaekAIKLLKEKKLGRLTFLPLNKIKPRS-------MREKPKLGIPAMDVVSYDPRFRNAVAYAlgDTLI 622
Cdd:COG4717 289 L-------------FLLLAREKASLGKEAEELQALPALEeleeeelEELLAALGLPPDLSPEELLELLDRIEEL--QELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 623 VNDMDEAREVGIGKVRmvTLGGELLERSGAitgghykprgklgVNVDEIRKRVEALEgRKEALEAQVNALKVEVKGLENE 702
Cdd:COG4717 354 REAEELEEELQLEELE--QEIAALLAEAGV-------------EDEEELRAALEQAE-EYQELKEELEELEEQLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 703 LFELrmkkselskdvqviqkeldSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREkIKKALEn 782
Cdd:COG4717 418 LEEL-------------------LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-LAELLQ- 476
|
490 500
....*....|....*....|.
gi 57159276 783 pEARELNSKIREVEAEISKLK 803
Cdd:COG4717 477 -ELEELKAELRELAEEWAALK 496
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
253-415 |
7.83e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.63 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 253 EIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENAQKEIEESqarlrKS 332
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 333 KEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESE 412
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
...
gi 57159276 413 ISK 415
Cdd:COG1579 168 LAA 170
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
5-217 |
9.97e-09 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 57.69 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKKVvvPLARGFTAIVGANGSGKSNIGDAVLFVLGGlsaKAMRASRISDLIFAGskgeppAKYAEVA 84
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISLLATG---KSHRTSRDKELIRWG------AEEAKIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNNEDRGFPIdedEVVIKrrvyPDGRSTYWLNG-KRATRSEIIDLLSAAMISPEGYNLVlqgditkfiKMSPIERRLI 163
Cdd:cd03242 70 AVLERQGGELAL---ELTIR----SGGGRKARLNGiKVRRLSDLLGVLNAVWFAPEDLELV---------KGSPADRRRF 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57159276 164 IDEIsgiaeydakkekalkelkqteenLARVDLLIREVKAQLDKLEKERNDALR 217
Cdd:cd03242 134 LDRL-----------------------LGQLEPAYAHVLSEYQKALRQRNALLK 164
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
410-1017 |
1.14e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 410 ESEISKFEEEISRAKARITQFNARRNLLKEkiaEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKvesE 489
Cdd:pfam15921 277 EVEITGLTEKASSARSQANSIQSQLEIIQE---QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK---Q 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 490 LAKAREELIKAEAQREvrgnravEFlkSQRIEGLYGTLGELIS-VPKSEYALAVEvalggnydnvvveddrvaEKAIKLL 568
Cdd:pfam15921 351 LVLANSELTEARTERD-------QF--SQESGNLDDQLQKLLAdLHKREKELSLE------------------KEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 569 KEKKLGrltflplNKIKPRSMREkpKLGIPAMDVVSYDPRFRNAVAYALGdtlivnDMDEAREVGIGKvrmvtlgGELLE 648
Cdd:pfam15921 404 WDRDTG-------NSITIDHLRR--ELDDRNMEVQRLEALLKAMKSECQG------QMERQMAAIQGK-------NESLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 649 RSGAITgghykprGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKdvqvIQKELDSYL 728
Cdd:pfam15921 462 KVSSLT-------AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK----LRSRVDLKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 729 AEDRSLKEEIEEnerlISELEKRIEESKGEMAKLRGRIERLEKKREKIKKAL--ENPEARELNSKIREVEAEISKLKEEL 806
Cdd:pfam15921 531 QELQHLKNEGDH----LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqHGRTAGAMQVEKAQLEKEINDRRLEL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 807 SRVESKLESLDSRInEELLPRKADLEEEIEGLVNKINalnayieENKNAITELEKELEELKTAEENVKDELKELREGREQ 886
Cdd:pfam15921 607 QEFKILKDKKDAKI-RELEARVSDLELEKVKLVNAGS-------ERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 887 IrveiaelrkeKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIK---EIPLEVEKLRQDIEKMEE 963
Cdd:pfam15921 679 L----------KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvamGMQKQITAKRGQIDALQS 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 57159276 964 EIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQV 1017
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1006-1172 |
1.33e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1006 FIQEIEGQKRQVFLQTLNAIAKNFSELFAKLSPGGEAKLILENP--EDPFSGgleieakpagkdvkriEAMSGGEKAIIA 1083
Cdd:COG4637 205 TLRETHPERFERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKglDRPFPA----------------RELSDGTLRFLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1084 LAFvfAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQ--ADRIIGVSMRN-GVSKVVSL 1160
Cdd:COG4637 269 LLA--ALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDAlePEEVLVLEREDdGETRIRRL 346
|
170
....*....|..
gi 57159276 1161 SLEKARKILEEI 1172
Cdd:COG4637 347 SDLELPEWLEGY 358
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
671-913 |
1.36e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 671 IRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSkdvqviqkeldsylaedrsLKEEIEENERLISELEK 750
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-------------------LSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 751 RIEESKGEMAKLRGRIERLEKK----REKIKKALENPEARELNSKIREVEAEISKLKEELS-------RVESKLESLDSR 819
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQlgsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 820 INEELLPRKADLEEEIEGLVNKINALNAYIEENKNAItelekeleelktaeenvkDELKELREGREQIRVEIAELRKEKD 899
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARL------------------AELPELEAELRRLEREVEVARELYE 368
|
250
....*....|....
gi 57159276 900 ELTSKLQELRIEAN 913
Cdd:COG3206 369 SLLQRLEEARLAEA 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-505 |
1.55e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 164 IDEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKF 243
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 244 IEEGGSREEEIEGQIKSLEDRLK-EIAKEIVAKEKELAEIERQLEEKsgdgileitRKISEVKSKIEVAKRNIENAQKEI 322
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKaDELKKAAAAKKKADEAKKKAEEK---------KKADEAKKKAEEAKKADEAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 323 EESQARLRKSKEELKHVSEEIEKskgaiKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAE---- 398
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKK-----KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeakk 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 399 LEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKisKVESRHRKAEKELEE 478
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA--RIEEVMKLYEEEKKM 1607
|
330 340
....*....|....*....|....*..
gi 57159276 479 KTRELQKVESELAKArEELIKAEAQRE 505
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKA-EELKKAEEEKK 1633
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
271-554 |
1.58e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 271 EIVAKEKELAEIERQLEEksgdgileITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAI 350
Cdd:COG3883 17 QIQAKQKELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 351 KRWgkrreqlLVQIKERETVRNELVIKLGeiDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQF 430
Cdd:COG3883 89 GER-------ARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 431 NARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNR 510
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 57159276 511 AVEFLKSQRIEGLYGTLGELISVPKSEYALAVEVALGGNYDNVV 554
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
730-933 |
1.90e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 730 EDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALEnpearELNSKIREVEAEISKLKEELS-R 808
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-----KLQAEIAEAEAEIEERREELGeR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 809 VESKLESLDSRINEELLprkadLE-EEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQI 887
Cdd:COG3883 92 ARALYRSGGSVSYLDVL-----LGsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 57159276 888 RVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAEL 933
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
699-851 |
1.96e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 699 LENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKRE--KI 776
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57159276 777 KKALENPEAR--ELNSKIREVEAEISKLKEELSRVESKLESLDSRINEEllprKADLEEEIEGLVNKINALNAYIEE 851
Cdd:COG1579 95 QKEIESLKRRisDLEDEILELMERIEELEEELAELEAELAELEAELEEK----KAELDEELAELEAELEELEAEREE 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
748-932 |
3.64e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 748 LEKRIEESKGEMAKLRGR-----IERLEKKREKIKKALENPEA-RELNSKIREVEAEISKLKEELSRVESKLESLDSRI- 820
Cdd:COG4717 47 LLERLEKEADELFKPQGRkpelnLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELEKLEKLLq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 821 NEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKEL----REGREQIRVEIAELRK 896
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*.
gi 57159276 897 EKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAE 932
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
7-62 |
4.30e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 4.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 7 KIEMKGFKSYGNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRAS 62
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
25-132 |
4.35e-08 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 56.06 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 25 LARGFTAIVGANGSGKSNIGDAVLFVLGG-LSAKAMRASRISDLI---FAGSKgEPPAKYAEVAMYFnnedrgfpIDEDE 100
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGrASADLIRSGAEKAVVegvFDISD-EEEAKALLLELGI--------EDDDD 89
|
90 100 110
....*....|....*....|....*....|..
gi 57159276 101 VVIKRRVYPDGRSTYWLNGKRATRSEIIDLLS 132
Cdd:cd03241 90 LIIRREISRKGRSRYFINGQSVTLKLLRELGS 121
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-503 |
6.89e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 187 TEENLA-------RVDLLIREVKAQLDKLEKERNDALRYLDlKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIK 259
Cdd:TIGR04523 150 KEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNID-KIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 260 SLEDRLKEIAKEIVAKEKELAEIERQLE--------------------EKSGDGILEITRKISEVKSKIEV--------- 310
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnkikkqlsekqkelEQNNKKIKELEKQLNQLKSEISDlnnqkeqdw 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 311 ---AKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRW----GKRREQLLVQIKERETVRNELVIKLGEIDK 383
Cdd:TIGR04523 309 nkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 384 ---RFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEG 460
Cdd:TIGR04523 389 lesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 57159276 461 KISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQ 503
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-345 |
6.96e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.56 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 6 EKIEMKGFKSYGNKKVVVPLAR-GFTAIVGANGSGKSNIGDAVLFVLGGlsaKAMRASRISDLIFAGSKgeppaKYAEVA 84
Cdd:PHA02562 5 KKIRYKNILSVGNQPIEIQLDKvKKTLITGKNGAGKSTMLEALTFALFG---KPFRDIKKGQLINSINK-----KDLLVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 85 MYFNnedrgfpIDEDEVVIKRRVYPDGRSTyWLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDI--------TKFIKMS 156
Cdd:PHA02562 77 LWFE-------YGEKEYYIKRGIKPNVFEI-YCNGKLLDESASSKDFQKYFEQMLGMNYKSFKQIvvlgtagyVPFMQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 157 PIERRLIID---EISGIAEYDAKKEKALKELKQTEENL-ARVDLLIREVKAQ------LDKLEKERNDALR--YLDLKEK 224
Cdd:PHA02562 149 APARRKLVEdllDISVLSEMDKLNKDKIRELNQQIQTLdMKIDHIQQQIKTYnknieeQRKKNGENIARKQnkYDELVEE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 225 LE--KARVTLLLAEI-------------------------------KRLEKFIEEGG------SREEEIEGQIKSLEDRL 265
Cdd:PHA02562 229 AKtiKAEIEELTDELlnlvmdiedpsaalnklntaaakikskieqfQKVIKMYEKGGvcptctQQISEGPDRITKIKDKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 266 KEIAKEIvakekELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIEN-------AQKEIEESQARLRKSKEELKH 338
Cdd:PHA02562 309 KELQHSL-----EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITlvdkakkVKAAIEELQAEFVDNAEELAK 383
|
....*..
gi 57159276 339 VSEEIEK 345
Cdd:PHA02562 384 LQDELDK 390
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1075-1158 |
9.66e-08 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 56.38 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1075 SGGEKAIIALAfvfaiqR--YKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIgvSMRN 1152
Cdd:COG2274 613 SGGQRQRLAIA------RalLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII--VLDK 684
|
....*.
gi 57159276 1153 GvsKVV 1158
Cdd:COG2274 685 G--RIV 688
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
667-935 |
1.03e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 667 NVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLIS 746
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 747 ELEKRIEESKGEMAKLRGRIERLEKKR---EKIKKALENPEARELNSKI-----REVEAEISKLKEELSRVESKLEslds 818
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLspeeeKELVEKIKELEKELEKAKKALE---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 819 rINEELLprkaDLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEK 898
Cdd:COG1340 158 -KNEKLK----ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 57159276 899 DELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKH 935
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
668-840 |
1.03e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.18 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYlaEDRSLKEEIEENerlISE 747
Cdd:PHA02562 222 YDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY--EKGGVCPTCTQQ---ISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 748 LEKRIEESKGEMAKLRGRIERLEKKREKIKKALEnpEARELNSKIREVEAEISKLKEELSRVESKLESLDSRInEELLPR 827
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMD--EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI-EELQAE 373
|
170
....*....|...
gi 57159276 828 KADLEEEIEGLVN 840
Cdd:PHA02562 374 FVDNAEELAKLQD 386
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
189-814 |
1.21e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 189 ENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKE- 267
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 268 --------IAKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIeesQARLRKSKEELKHV 339
Cdd:pfam05483 151 natrhlcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEM---HFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 340 SEEIEKSkgaIKRWGKRREQLLVQIKERETVRNELVIKLGEI--------------DKRFSEAREEFDKVVAELEEAKKA 405
Cdd:pfam05483 228 EEEYKKE---INDKEKQVSLLLIQITEKENKMKDLTFLLEESrdkanqleektklqDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 406 LYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELS----QVEGKISKVESRHRKAEKELEEKTR 481
Cdd:pfam05483 305 LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEattcSLEELLRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 482 ELQKVESELAKAR----------EEL--IKAEAQREVRGNRAVEFL------KSQRIEGLYGTLGE----------LISV 533
Cdd:pfam05483 385 ELQKKSSELEEMTkfknnkevelEELkkILAEDEKLLDEKKQFEKIaeelkgKEQELIFLLQAREKeihdleiqltAIKT 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 534 PKSEYALAVE-------------VALGGNYDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPLNKIKPRSMREKPKLGIPAM 600
Cdd:pfam05483 465 SEEHYLKEVEdlktelekeklknIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 601 DVvsydprfRNAVAYALGDTLIVND-----MDEAREVGIGKVRMVTLGGELLERSGAITGGHYKPRGKLGVNVDEIRKRV 675
Cdd:pfam05483 545 NL-------RDELESVREEFIQKGDevkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 676 EALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELS----KDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKR 751
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIdnyqKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKR 697
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 752 IEESKGEMAKLrgrierLEKKREKIKKALENPEA---------RELNSKIREVEAEISKLKEELSRVESKLE 814
Cdd:pfam05483 698 CQHKIAEMVAL------MEKHKHQYDKIIEERDSelglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLE 763
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
292-505 |
1.34e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 292 DGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKrwgkrreqllvqikeretvr 371
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 372 nelviklgeidkrfsEAREEFDKVVAELEEAKKALYMKESEISK---------FEEEISRAKARITQFNARRNLL----- 437
Cdd:COG3883 76 ---------------EAEAEIEERREELGERARALYRSGGSVSYldvllgsesFSDFLDRLSALSKIADADADLLeelka 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 438 -KEKIAEAKASLEAKRSELSQvegKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQRE 505
Cdd:COG3883 141 dKAELEAKKAELEAKLAELEA---LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
705-916 |
2.14e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 705 ELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENpe 784
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 785 arelnskiREVEAEISKLKEELSRVESKLESLDSRIneellprkadleEEIEGLVNKINALNAYIEENKNAITELEKELE 864
Cdd:COG4717 128 --------LPLYQELEALEAELAELPERLEELEERL------------EELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57159276 865 ELKTAE-ENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLK 916
Cdd:COG4717 188 LATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
28-217 |
2.17e-07 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 54.41 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 28 GFTAIVGANGSGKSNIGDAVLFVLGGLsakaMRASRISDLIFAGSkgEPPAKYAEVamyfnneDRGFPIDEDEVVIKRrv 107
Cdd:PRK14079 24 GVTAVVGENAAGKTNLLEAIYLALTGE----LPNGRLADLVRFGE--GEAWVHAEV-------ETGGGLSRLEVGLGP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 108 ypdGRSTYWLNGKRATRSEIIDLLSAAMISPEGYNLVLQgditkfikmSPIERRLIIDEIsgiaeydakkekalkelkqt 187
Cdd:PRK14079 89 ---GRRELKLDGVRVSLRELARLPGAVLIRPEDLELVLG---------PPEGRRAYLDRL-------------------- 136
|
170 180 190
....*....|....*....|....*....|
gi 57159276 188 eenLARVDLLIREVKAQLDKLEKERNDALR 217
Cdd:PRK14079 137 ---LSRLSARYAALLSAYERAVQQRNAALK 163
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
188-503 |
2.55e-07 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 55.07 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 188 EENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTL--LLAEIKRLEKFIEEGGSR---------EEEIEG 256
Cdd:pfam13166 109 EEKLDAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSALSEALngFKYEANFKSRLLREIEKDnfnagvllsDEDRKA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 257 QIKSLEDR-LKEIAK-EIVAKEKELAEIERQLEEKSGDGILEITRKISE------VKSKIEVAKRNIENA---QKEIEES 325
Cdd:pfam13166 189 ALATVFSDnKPEIAPlTFNVIDFDALEKAEILIQKVIGKSSAIEELIKNpdladwVEQGLELHKAHLDTCpfcGQPLPAE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 326 QarlrksKEELK-----HVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVI---KLGEIDKRFSEAREEFDKVVA 397
Cdd:pfam13166 269 R------KAALEahfddEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAfelDVEDIESEAEVLNSQLDGLRR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 398 ELEEAKKALYM------KESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEakRSELSQVEGKISKVESRHRK 471
Cdd:pfam13166 343 ALEAKRKDPFKsieldsVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLR--LHLVEEFKSEIDEYKDKYAG 420
|
330 340 350
....*....|....*....|....*....|..
gi 57159276 472 AEKELEEKTRELQKVESELAKAREELIKAEAQ 503
Cdd:pfam13166 421 LEKAINSLEKEIKNLEAEIKKLREEIKELEAQ 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-827 |
3.53e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 198 IREVKAQLDKLEKERNDALR-YLDLKEKLEK----ARVTLLLAEIKRlEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEi 272
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRmYEDKIEELEKqlvlANSELTEARTER-DQFSQESGNLDDQLQKLLADLHKREKELSLE- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 273 vaKEKElaeiERQLEEKSGDGIleitrkisevksKIEVAKRNIENAQKEIEESQARLRKSKEELKHvseEIEKSKGAIKr 352
Cdd:pfam15921 397 --KEQN----KRLWDRDTGNSI------------TIDHLRRELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQ- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 353 wGKrreqllvqikeretvrNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISkfeeeisrakaritqfna 432
Cdd:pfam15921 455 -GK----------------NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS------------------ 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 433 rrnllkekiaEAKASLEAKRSELSQVEGKISKVESRhrkaekeLEEKTRELQKVESELAKAREELIKAEAQR--EVRGNR 510
Cdd:pfam15921 500 ----------DLTASLQEKERAIEATNAEITKLRSR-------VDLKLQELQHLKNEGDHLRNVQTECEALKlqMAEKDK 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 511 AVEFLKsQRIEGLYGTLGELisvPKSEYALAVEVALGGNYDNvvveDDRVAEKAIKLLKEKK-------LGRLTFLPLNK 583
Cdd:pfam15921 563 VIEILR-QQIENMTQLVGQH---GRTAGAMQVEKAQLEKEIN----DRRLELQEFKILKDKKdakirelEARVSDLELEK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 584 IKPRSMREKPKLGIPamDVVSYDPRFRNAVAYALGDtliVNDMDEAREVGIGKVRMVTlggELLERSgaitgghykpRGK 663
Cdd:pfam15921 635 VKLVNAGSERLRAVK--DIKQERDQLLNEVKTSRNE---LNSLSEDYEVLKRNFRNKS---EEMETT----------TNK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 664 LGVNVDEIRKRVEALEGRKEALE-AQVNALKVEVkGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENE 742
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAM-GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 743 RLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEAR--ELNSKIREVEAEISKLKEELSRVESKLESLDSRI 820
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTS 855
|
....*..
gi 57159276 821 NEELLPR 827
Cdd:pfam15921 856 NSSMKPR 862
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1069-1153 |
3.73e-07 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 52.08 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1069 KRIEAMSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKE-ASQNSQFIVITHR-DVMMAQADRII 1146
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDlDLLLELADRVI 205
|
....*..
gi 57159276 1147 gvSMRNG 1153
Cdd:cd03225 206 --VLEDG 210
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
997-1173 |
4.19e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.47 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 997 LAEKESIEEFIQEIEgQKRQVFLQTLNAIAKNFSELFAKLSPGGEAKLILENPE-DPFSGGLEIEAKpAGKDVkRIEAMS 1075
Cdd:COG3593 88 LLKEEDKEELEEALE-ELNEELKEALKALNELLSEYLKELLDGLDLELELSLDElEDLLKSLSLRIE-DGKEL-PLDRLG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1076 GGEKAIIALAFVFAI---QRYKPAPFYLLDEIDAHLDDANVKRVADLIKE-ASQNSQFIVITHRDVMMAQA--DRIIGVS 1149
Cdd:COG3593 165 SGFQRLILLALLSALaelKRAPANPILLIEEPEAHLHPQAQRRLLKLLKElSEKPNQVIITTHSPHLLSEVplENIRRLR 244
|
170 180
....*....|....*....|....*..
gi 57159276 1150 MRNG---VSKVVSLSLEKARKILEEIR 1173
Cdd:COG3593 245 RDSGgttSTKLIDLDDEDLRKLLRYLG 271
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
226-851 |
5.70e-07 |
|
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: 54.07 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 226 EKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDGILEITR---KIS 302
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAadaAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 303 EVKSKIEVAKRNIENAQKEIEES----QARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKERetvrneLVIKL 378
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIETaaadQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ------NNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 379 GEIDKRFSEAREEFDKVVAELEEAKKAL-----YMKESEISKFEEEISRAKARIT--------------------QFNAR 433
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQALeselrEQLEAGKLEFNEEEYRLKSRLGelklrlnqatatpelllqleNFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 434 RNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIkaeaqrevrgnravE 513
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL--------------H 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 514 FLKSQrIEGLYGTLGELISvpkseyalaveVALGGNYDNVVVEDDrvaekaikllkEKKLGRLTFLPLnkikprsmrekp 593
Cdd:pfam12128 539 FLRKE-APDWEQSIGKVIS-----------PELLHRTDLDPEVWD-----------GSVGGELNLYGV------------ 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 594 KLGIPAMDVVSYdprfrnavaYALGDTL------IVNDMDEAREV-GIGKVRMVTLGGELLERSGAIT-------GGHYK 659
Cdd:pfam12128 584 KLDLKRIDVPEW---------AASEEELrerldkAEEALQSAREKqAAAEEQLVQANGELEKASREETfartalkNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 660 PRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENEL-----------FELRMKKSELSKDV---------QV 719
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkeqkREARTEKQAYWQVVegaldaqlaLL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 720 IQKELDSYLAEDRSLKEEIEENERLISEL---EKRIEESKGEMAKLRGRIERLEKKREKIKKALE------NPEARELNS 790
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwLQRRPRLAT 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 791 KIREVEAEISKLKEELSRVESKLESLDSRINEEllpRKA--DLEEEIEGLVNKINALNAYIEE 851
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEME---RKAseKQQVRLSENLRGLRCEMSKLAT 874
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1071-1156 |
6.66e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1071 IEAMSGGEKAIIALAFVFAIQRYKPA--PFYLLDEIDAHLDDANV-KRVADLIKEASQ--NSQFIVITHRDVMMAQADRI 1145
Cdd:cd03240 113 RGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERKSqkNFQLIVITHDEELVDAADHI 192
|
90
....*....|..
gi 57159276 1146 IGVSMR-NGVSK 1156
Cdd:cd03240 193 YRVEKDgRQKSR 204
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
191-351 |
6.75e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 191 LARVDLLIREVKAQLDKLEKERNdalrylDLKEKLEKARvtlllAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEI-- 268
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELA------ALEARLEAAK-----TELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 269 AKEIVAKEKELAEIERQLEEKSgDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKG 348
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
...
gi 57159276 349 AIK 351
Cdd:COG1579 167 ELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
186-518 |
7.01e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLE--KARVTLLLAEIKRLEKFIE--EGGSREEEIEGQIKSL 261
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELREELEKLEKLLQllPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 262 EDRLKEI---AKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKH 338
Cdd:COG4717 145 PERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 339 VSEEIEKSKGaiKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEE 418
Cdd:COG4717 225 LEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 419 EISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEE-KTRELQKVESEL-----AK 492
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALlaeagVE 382
|
330 340
....*....|....*....|....*...
gi 57159276 493 AREELIKA--EAQREVRGNRAVEFLKSQ 518
Cdd:COG4717 383 DEEELRAAleQAEEYQELKEELEELEEQ 410
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
678-1013 |
9.34e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 678 LEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQK--------------ELDSYLAEDRS-LKEEIEENE 742
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqarnqnsmymrqlsDLESTVSQLRSeLREAKRMYE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 743 RLISELEKRIEESKGEMAKLRGRIERLEK-----------------KREKiKKALENPEAREL------NS-KIREVEAE 798
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQesgnlddqlqklladlhKREK-ELSLEKEQNKRLwdrdtgNSiTIDHLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 799 ISKLKEELSRVESKLESLDSRINEELLPRKADLEEEIEGLvNKINALNAYIEENK----NAITELEKELEELKTAEENVK 874
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL-EKVSSLTAQLESTKemlrKVVEELTAKKMTLESSERTVS 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 875 DELKELREGREQIRVEIAELRKEKDELTSKLQELRieantlkvRLAQVETTLQEKRAELKhfdpALVRSIKEIPLEVEKL 954
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ--------HLKNEGDHLRNVQTECE----ALKLQMAEKDKVIEIL 567
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 955 RQDIEKMEEEI----RSLEPVNMKAIEDFEVVERRYLELssKREQVLAEKESIEefIQEIEGQ 1013
Cdd:pfam15921 568 RQQIENMTQLVgqhgRTAGAMQVEKAQLEKEINDRRLEL--QEFKILKDKKDAK--IRELEAR 626
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
840-1016 |
1.21e-06 |
|
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: 52.07 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 840 NKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREgreqirvEIAELRKEKDELTSKLQELRIEANTLKVRL 919
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 920 AQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAE 999
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170
....*....|....*..
gi 57159276 1000 KESIEEFIQEIEGQKRQ 1016
Cdd:COG4942 173 RAELEALLAELEEERAA 189
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
197-491 |
1.27e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 52.71 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 197 LIREVKAQLDKLEKERNDAL---------RYLDLKEKLEKARVTLLLAEIKR-----LEKFIEEGGSREEEIEGQIKSLE 262
Cdd:NF033838 70 ILSEIQKSLDKRKHTQNVALnkklsdiktEYLYELNVLKEKSEAELTSKTKKeldaaFEQFKKDTLEPGKKVAEATKKVE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 263 DRLK--EIAKE--------IVAKEKELAEIERQLEEKSGD-GILEITRKISEVKSKIEVAKRNIENAQKEIeesqARLRK 331
Cdd:NF033838 150 EAEKkaKDQKEedrrnyptNTYKTLELEIAESDVEVKKAElELVKEEAKEPRDEEKIKQAKAKVESKKAEA----TRLEK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 332 SKEELKHVSEEIEKSKGA-IKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAR-------EEF--------DKV 395
Cdd:NF033838 226 IKTDREKAEEEAKRRADAkLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKssdssvgEETlpspslkpEKK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 396 VAE----LEEAKKALYMK----------------ESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSEL 455
Cdd:NF033838 306 VAEaekkVEEAKKKAKDQkeedrrnyptntyktlELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEA 385
|
330 340 350
....*....|....*....|....*....|....*.
gi 57159276 456 SQVEgkisKVESRHRKAEKELEEKTRELQKVESELA 491
Cdd:NF033838 386 TRLE----KIKTDRKKAEEEAKRKAAEEDKVKEKPA 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
668-855 |
1.39e-06 |
|
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: 52.07 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSL------------- 734
Cdd:COG4942 43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqppl 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 735 -----KEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKalenpEARELNSKIREVEAEISKLKEELSRV 809
Cdd:COG4942 123 alllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA-----ERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 57159276 810 ESKLESLDSRInEELLPRKADLEEEIEGLVNKINALNAYIEENKNA 855
Cdd:COG4942 198 QKLLARLEKEL-AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
679-871 |
1.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 679 EGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSylaedrsLKEEIEENERLISELEKRIEESKGE 758
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 759 MAK-LR-------------------------GRIERLEKKREKIKKALENPEA--RELNSKIREVEAEISKLKEELSRVE 810
Cdd:COG3883 88 LGErARalyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKAdkAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57159276 811 SKLESLDSRInEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEE 871
Cdd:COG3883 168 AAKAELEAQQ-AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
198-420 |
1.68e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 52.24 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 198 IREVKAQLDKLEKerndALRYL-DLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKE 276
Cdd:PRK05771 45 LRKLRSLLTKLSE----ALDKLrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 277 KELAEIE---------------------------RQLEEKSGDGILEITRKISEVKSK----IEVAKRNIENAQKEIEE- 324
Cdd:PRK05771 121 QEIERLEpwgnfdldlslllgfkyvsvfvgtvpeDKLEELKLESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKl 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 325 ------------SQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKER---ETVRNELVIKLGEIDKRFS-EA 388
Cdd:PRK05771 201 gferleleeegtPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleiELERAEALSKFLKTDKTFAiEG 280
|
250 260 270
....*....|....*....|....*....|....*.
gi 57159276 389 ---REEFDKVVAELEEA-KKALYMKESEISKFEEEI 420
Cdd:PRK05771 281 wvpEDRVKKLKELIDKAtGGSAYVEFVEPDEEEEEV 316
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
297-499 |
1.69e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 297 ITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKhvsEEIEKSKGAIKRwgkRREQLLVQIKERETVRNELVi 376
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELV---EEAKTIKAEIEE---LTDELLNLVMDIEDPSAALN- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 377 KLGEIDKRFSEAREEFDKVVAELEE------AKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEK---IAEAKAS 447
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEImdeFNEQSKK 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57159276 448 LEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIK 499
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
4-53 |
2.00e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.54 E-value: 2.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYGNkkVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGG 53
Cdd:COG3593 2 KLEKIKIKNFRSIKD--LSIELSDDLTVLVGENNSGKSSILEALRLLLGP 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
236-482 |
2.63e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 236 EIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEksgdgileitrkisevkskievakrni 315
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 316 enAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGK-----------RREQLLVQIKEREtvrNELVIKLGEIDKR 384
Cdd:COG3883 70 --LQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAD---ADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 385 FSEAREEFDKVVAELEEAKKALymkESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISK 464
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAEL---EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250
....*....|....*...
gi 57159276 465 VESRHRKAEKELEEKTRE 482
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
709-931 |
2.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 709 KKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENpEAREL 788
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE-RARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 789 NSKireveaeisklkeelSRVESKLES-LDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELK 867
Cdd:COG3883 96 YRS---------------GGSVSYLDVlLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 868 TAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRA 931
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
5-91 |
2.65e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYgNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVL-GGLSAKAMRASRISDLIFAGSKGeppakyAEV 83
Cdd:cd03240 1 IDKLSIRNIRSF-HERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEVR------AQV 73
|
....*...
gi 57159276 84 AMYFNNED 91
Cdd:cd03240 74 KLAFENAN 81
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
670-1022 |
2.70e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 670 EIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRmkkselskDVQVIQKELDSYLAEDRSLKEEIEENERLISELE 749
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR--------EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 750 KRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRvesklesldsrineELLPRKA 829
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK--------------LLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 830 DLEEEIEGLVNKINALNAYIEENKNAItelekeleelktaEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELR 909
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRD-------------AHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 910 IEANTLKVRLAQVETTLQEKRAELKHfdpaLVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLEL 989
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
330 340 350
....*....|....*....|....*....|....*.
gi 57159276 990 SSKR---EQVLAEKESIEEFIQEIEGQKRQVFLQTL 1022
Cdd:TIGR00618 476 QTKEqihLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1075-1154 |
3.18e-06 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 48.75 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1075 SGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEAS-QNSQFIVITHRDVMMAQADRIIgvSMRNG 1153
Cdd:cd03246 98 SGGQRQRLGLARAL----YGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRIL--VLEDG 171
|
.
gi 57159276 1154 V 1154
Cdd:cd03246 172 R 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
805-965 |
3.47e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 805 ELSRVESKLESLDSRInEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGR 884
Cdd:COG1579 11 DLQELDSELDRLEHRL-KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 885 E--QIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKME 962
Cdd:COG1579 90 EyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
...
gi 57159276 963 EEI 965
Cdd:COG1579 170 AKI 172
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
150-968 |
3.49e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 150 TKFIKMSPIERRLIIDEISGIAEYDAKKEKALKELKQTEEnlarvdlLIREVKAQLDKLEKERNDALRYLD----LKEKL 225
Cdd:TIGR00606 182 TRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACE-------IRDQITSKEAQLESSREIVKSYENeldpLKNRL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 226 EKarVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEI---------------AKEIVAKEKELAEIERQLEEKS 290
Cdd:TIGR00606 255 KE--IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdeqlndlyhnhQRTVREKERELVDCQRELEKLN 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 291 GDGIL------EITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRRE-----Q 359
Cdd:TIGR00606 333 KERRLlnqektELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 360 LLVQIKERETVR----NELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKES---EISKFEEEISRAKARITQfna 432
Cdd:TIGR00606 413 LCADLQSKERLKqeqaDEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSK--- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 433 rrnllkekiAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAV 512
Cdd:TIGR00606 490 ---------AEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 513 E-------FLKSQRIEGLYGTLGELISVPKSEYA-LAVEVA-LGGNYDNVVVEDDRVAEKAIKLlkEKKLGRLTFLPLNK 583
Cdd:TIGR00606 561 EltsllgyFPNKKQLEDWLHSKSKEINQTRDRLAkLNKELAsLEQNKNHINNELESKEEQLSSY--EDKLFDVCGSQDEE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 584 IKPRSMREKPKlgipamdvVSYDPRFRNAVAYALGDTLIVNDMDEAREVGIGKVRMVTLGGELLERSGAITGGHYKPRGK 663
Cdd:TIGR00606 639 SDLERLKEEIE--------KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDK 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 664 LgvnvDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVI-------QKELDSYLAEDRS--- 733
Cdd:TIGR00606 711 L----KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLkndieeqETLLGTIMPEEESakv 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 734 ----------LKEEIEENERLISELEKRIEESKGEMA--KLRGRIERLEKKREKIKKALE---------NPEARELNSKI 792
Cdd:TIGR00606 787 cltdvtimerFQMELKDVERKIAQQAAKLQGSDLDRTvqQVNQEKQEKQHELDTVVSKIElnrkliqdqQEQIQHLKSKT 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 793 REVEAEISKLKEELSRVESKLESLDSRINE-------------ELLP---RKADLEEEIEGLVNKINALNAYIEENKNAI 856
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEvqslireikdakeQDSPletFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 857 TELEKELEELKTAEEN-----VKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKV--RLAQVETTLQEK 929
Cdd:TIGR00606 947 KEKVKNIHGYMKDIENkiqdgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIqeRWLQDNLTLRKR 1026
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 57159276 930 RAELKHFDPALVRSIKEI-PLEVEKLRQDIEKMEEEIRSL 968
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLI 1066
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1075-1173 |
3.77e-06 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 49.89 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1075 SGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIIGVSMRNGV 1154
Cdd:cd03241 172 SGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVEG 251
|
90 100
....*....|....*....|.
gi 57159276 1155 SKVVSL--SLEKARKILEEIR 1173
Cdd:cd03241 252 GRTVTKvrELDKEERVEEIAR 272
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
186-523 |
3.80e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVtlLLAEIKRLEKFIEEGGSREEEIEGQI---KSLE 262
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELPERLEELEERLeelRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 263 DRLKEIAKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEE 342
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 343 IEKSKGAI-----------------------------------------------KRWGKRREQLLVQIKERETVRNELV 375
Cdd:COG4717 243 ERLKEARLllliaaallallglggsllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 376 IKLGEIDKRFSEAREEFDKVVAELEEAKKAL-----YMKESEISKFEEEISR------------AKARITQFNARRNLlK 438
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLreaeeLEEELQLEELEQEIAAllaeagvedeeeLRAALEQAEEYQEL-K 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 439 EKIAEAKASLEAKRSELSQVEGKISK--VESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLK 516
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
....*..
gi 57159276 517 SQRIEGL 523
Cdd:COG4717 482 KAELREL 488
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
251-503 |
3.92e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 251 EEEIEGQIKSLEDRLKEIAKEIVAKE-KELAEIERQLEEKSgDGILEITRKisEVKSKIEVAKrNIENAQKEIEESQARL 329
Cdd:PRK04778 251 HLDIEKEIQDLKEQIDENLALLEELDlDEAEEKNEEIQERI-DQLYDILER--EVKARKYVEK-NSDTLPDFLEHAKEQN 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 330 RKSKEELKHVSEEIEKSKGAIKRwgkrREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKalymk 409
Cdd:PRK04778 327 KELKEEIDRVKQSYTLNESELES----VRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK----- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 410 esEISKFEEEIsrAKARITQFNARRNL--LKEKIAEAKASLEAkrselSQVEGKISKVESRHRKAEKELEEKTRELQKVE 487
Cdd:PRK04778 398 --EQEKLSEML--QGLRKDELEAREKLerYRNKLHEIKRYLEK-----SNLPGLPEDYLEMFFEVSDEIEALAEELEEKP 468
|
250
....*....|....*.
gi 57159276 488 SELAKAREELIKAEAQ 503
Cdd:PRK04778 469 INMEAVNRLLEEATED 484
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
879-1140 |
4.45e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 50.08 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 879 ELREGREQIRVEIAELRKEKDELTSKLqELRIEANTLKVRLAQVETTLQEK--RAELKHFDPALVRSIKEIPLEVEKLRQ 956
Cdd:pfam13304 48 LLNGIDPKEPIEFEISEFLEDGVRYRY-GLDLEREDVEEKLSSKPTLLEKRllLREDSEEREPKFPPEAEELRLGLDVEE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 957 DIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLNAIAKNFSELFAKL 1036
Cdd:pfam13304 127 RIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1037 spggeaKLILENPEDPFSGGLEIEAKPAGKDVkRIEAMSGGEKAIIALAFVFAIQRyKPAPFYLLDEIDAHLDDANVKRV 1116
Cdd:pfam13304 207 ------EKSLLVDDRLRERGLILLENGGGGEL-PAFELSDGTKRLLALLAALLSAL-PKGGLLLIDEPESGLHPKLLRRL 278
|
250 260
....*....|....*....|....*
gi 57159276 1117 ADLIKEASQN-SQFIVITHRDVMMA 1140
Cdd:pfam13304 279 LELLKELSRNgAQLILTTHSPLLLD 303
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1075-1133 |
5.75e-06 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 48.75 E-value: 5.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1075 SGGEKAIIALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVAD-LIKEASQN--SQFIVIT 1133
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDmLVETACKEgtSQYFLIT 189
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-75 |
7.14e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.23 E-value: 7.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 4 YIEKIEMKGFKSYGNKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGSKGE 75
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
8-191 |
7.78e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 47.88 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 8 IEMKGFKSYGNkkVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASR--ISDLIFAGSKGEPPAKYAEVAM 85
Cdd:pfam13476 1 LTIENFRSFRD--QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGggFVKGDIRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 86 YFNNEDRGFPIDEDEVVIKRRVYPDGRSTYWLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKMSPIERRLIID 165
Cdd:pfam13476 79 ENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELE 158
|
170 180
....*....|....*....|....*.
gi 57159276 166 EISGIAEYDAKKEKALKELKQTEENL 191
Cdd:pfam13476 159 KALEEKEDEKKLLEKLLQLKEKKKEL 184
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
695-934 |
8.39e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 695 EVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLeKKRE 774
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI-NSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 775 KIKKALENPEARELNS---KIREVEAEISKLKEELSRVESKLESLDSRINeELLPRKADLEEEIEGLVNKINALNAYIEE 851
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKlekQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 852 NKNAITELEKELEELKTAEENVK---DELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQE 928
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKsleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
....*.
gi 57159276 929 KRAELK 934
Cdd:TIGR04523 272 KQKELE 277
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
672-966 |
9.49e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 672 RKRVEALEGRKEALEAQVNALKVEvKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEeNERLISELEKR 751
Cdd:COG5022 761 RRRYLQALKRIKKIQVIQHGFRLR-RLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIK-REKKLRETEEV 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 752 --------IEESKGEMAKLRGRIERLEKK--------------REKIKKALENPEARELNSKIREVEAEISKLKEELSRV 809
Cdd:COG5022 839 efslkaevLIQKFGRSLKAKKRFSLLKKEtiylqsaqrvelaeRQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSD 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 810 ES-KLESLDSRI-NEELLPRKADLEEEIEGLVNKINALNAYIEENKNaitelekeleeLKTAEENVKDELKELREGREQI 887
Cdd:COG5022 919 LIeNLEFKTELIaRLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESK-----------LKETSEEYEDLLKKSTILVREG 987
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 888 RVEIAELRKEKDELTSKLQELRIEANTLKvRLAQVETTLQEKRAELKHfdPALVRSIKEIPLEVEKLRQDIEKMEEEIR 966
Cdd:COG5022 988 NKANSELKNFKKELAELSKQYGALQESTK-QLKELPVEVAELQSASKI--ISSESTELSILKPLQKLKGLLLLENNQLQ 1063
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
758-947 |
1.07e-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: 48.00 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 758 EMAKLRGRIERLEKKREKIKKALENPEAR--ELNSKIREVEAEISKLKEELSRVESKLESLDSRI--NEELLPRKADLEE 833
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDElaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 834 eieglvnkINALNAYIEenknaitelekeleELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEAN 913
Cdd:COG1579 91 --------YEALQKEIE--------------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180 190
....*....|....*....|....*....|....*
gi 57159276 914 TLKVRLAQVETTLQEKRAEL-KHFDPALVRSIKEI 947
Cdd:COG1579 149 EELAELEAELEELEAEREELaAKIPPELLALYERI 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
661-1013 |
1.27e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 661 RGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEI-- 738
Cdd:pfam01576 63 RARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIll 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 739 --EENERLISE---LEKRIEESKGEMAK---------------------LRGRIERLEKKR---EKIKKALENpEARELN 789
Cdd:pfam01576 143 leDQNSKLSKErklLEERISEFTSNLAEeeekakslsklknkheamisdLEERLKKEEKGRqelEKAKRKLEG-ESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 790 SKIREVEAEISKLKEELSRVESKLESLDSRINEELLpRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTA 869
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETA-QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 870 EENVKDEL----------KELREGREQirvEIAELRKEKDELT----SKLQELRIEANTLKVRLAQVETTLQEKRAELKH 935
Cdd:pfam01576 301 LEALKTELedtldttaaqQELRSKREQ---EVTELKKALEEETrsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 936 FDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEEFIQEIEGQ 1013
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK 455
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
670-981 |
1.36e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 670 EIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENerlISELE 749
Cdd:COG5185 212 TGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN---ANNLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 750 KRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELlpRKA 829
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI--ENI 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 830 DLEEEIEGLVNKINALNAYIEENKNAI-----TELEKELEELKTAEENVK---DELKELREGREQIRVEIAELRKEKDEL 901
Cdd:COG5185 367 VGEVELSKSSEELDSFKDTIESTKESLdeipqNQRGYAQEILATLEDTLKaadRQIEELQRQIEQATSSNEEVSKLLNEL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 902 TSKLQELRIEANTLKV-----RLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAI 976
Cdd:COG5185 447 ISELNKVMREADEESQsrleeAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESL 526
|
....*
gi 57159276 977 EDFEV 981
Cdd:COG5185 527 KDFMR 531
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
186-504 |
1.41e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLlAEIKRLEKFIEEGGSREEEIEGQIKSLEDRL 265
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLL-DEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 266 KEIAKEIVAKEKELAEIERQLEEKSGDgiLEiTRKISEVKSKIEVAKRNIENAQKEIEESQARLrkskeELKHVSEEIEK 345
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTE--LE-KEKLKNIELTAHCDKLLLENKELTQEASDMTL-----ELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 346 SKGAIKRWGKRREQLL---VQIK-ERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEIS 421
Cdd:pfam05483 525 CKKQEERMLKQIENLEekeMNLRdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 422 RAKARITQFNARRNLLKEKIAeakasleAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKvESELAKAREELIKAE 501
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGS-------AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLLEE 676
|
...
gi 57159276 502 AQR 504
Cdd:pfam05483 677 VEK 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
827-1036 |
1.43e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 827 RKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQ 906
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 907 ELRIEANTLkVRLAQVETTLQEKRAELKHFDPA-LVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERR 985
Cdd:COG4942 101 AQKEELAEL-LRALYRLGRQPPLALLLSPEDFLdAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57159276 986 YLELSSKREQVLAEKESIEEFIQEIEGQKR--QVFLQTLNAIAKNFSELFAKL 1036
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAelAAELAELQQEAEELEALIARL 232
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
257-820 |
1.56e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 257 QIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKiEVAKRNIENAQKEIEESQARLRKSKEEL 336
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ-LSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 337 KHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKF 416
Cdd:TIGR00606 663 AVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 417 EEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVE------GKISKVESRHRKAEKELEEKTRELQKVESEL 490
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKLQGSDLDR 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 491 AKAREELIKAEAQREVRG-------NRAVEFLKSQRIEGLYGTLGELISvpkSEYALAVEVALGGNYDNVVVEDDRVAEK 563
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTvvskielNRKLIQDQQEQIQHLKSKTNELKS---EKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 564 AIKLLKEKklgRLTFLPLNKIKPRSMREKPKLgipamdVVSYDPRFRNAvayalgdTLIVNDMDEAREVGIGkvRMVTLG 643
Cdd:TIGR00606 900 LIREIKDA---KEQDSPLETFLEKDQQEKEEL------ISSKETSNKKA-------QDKVNDIKEKVKNIHG--YMKDIE 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 644 GELLERSGAITGGHYKPRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELfeLRMKKSELSKDVQVIQKE 723
Cdd:TIGR00606 962 NKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL--TLRKRENELKEVEEELKQ 1039
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 724 LDSYLAEDRSLKEEIEENErliseLEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKIREVEAEISKLK 803
Cdd:TIGR00606 1040 HLKEMGQMQVLQMKQEHQK-----LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTE 1114
|
570
....*....|....*..
gi 57159276 804 EELSRVESKLESLDSRI 820
Cdd:TIGR00606 1115 LVNKDLDIYYKTLDQAI 1131
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
766-1143 |
1.60e-05 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 48.96 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 766 IERLEKKREKIKKALEnpEARELNSKIREVEAEISKLKEELSRVES-KLESLDSRINEELLPRKADLEEEIEGLVNKINA 844
Cdd:TIGR00634 160 VKAYRELYQAWLKARQ--QLKDRQQKEQELAQRLDFLQFQLEELEEaDLQPGEDEALEAEQQRLSNLEKLRELSQNALAA 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 845 LNAYIEENKNAITELEKELEELKTAEENVKdeLKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVET 924
Cdd:TIGR00634 238 LRGDVDVQEGSLLEGLGEAQLALASVIDGS--LRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 925 tLQEKRAelkhfdpalvRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVlAEKesie 1004
Cdd:TIGR00634 316 -LKRKYG----------ASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKA-AER---- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1005 eFIQEIEGQKRQVFLQTlnaiAKNFSELFAKLSPGGEAKLI---LENPEDPFSGGLEIEAKPAGKdvkrieAMSGGEKAI 1081
Cdd:TIGR00634 380 -LAKRVEQELKALAMEK----AEFTVEIKTSLPSGAKARAGaygADQVEFLFSANTGEPVKPLAK------VASGGELSR 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1082 IALAFVFAIQRYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQAD 1143
Cdd:TIGR00634 449 VMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
681-921 |
1.72e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 681 RKEALEAQVNALKVEVKGLENeLFELRMKkselSKDVQVIQKELDSYLAE--DRSLKEEIEENERLISELEKRIEEskge 758
Cdd:COG3206 116 REAAIERLRKNLTVEPVKGSN-VIEISYT----SPDPELAAAVANALAEAylEQNLELRREEARKALEFLEEQLPE---- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 759 makLRGRIERLEKKREKIKKA--LENPEARE--LNSKIREVEAEISKLKEELSRVESKLESLDSRINEELLPRKADLE-E 833
Cdd:COG3206 187 ---LRKELEEAEAALEEFRQKngLVDLSEEAklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQsP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 834 EIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELK-ELREGREQIRVEIAELRKEKDELTSKLQELRIEA 912
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
....*....
gi 57159276 913 NTLKVRLAQ 921
Cdd:COG3206 344 AELPELEAE 352
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
411-524 |
1.94e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 411 SEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESEL 490
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 57159276 491 AKAREELIK--AEAQREVRGNRAVEFLKSQRIEGLY 524
Cdd:COG4942 100 EAQKEELAEllRALYRLGRQPPLALLLSPEDFLDAV 135
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1074-1146 |
1.95e-05 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 47.20 E-value: 1.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 1074 MSGGEKAIIALAFVFAIQRykpaPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:cd03245 141 LSGGQRQAVALARALLNDP----PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRII 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-432 |
2.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLK-------------EKLEKARVTLLLA--EIKRLEKFIEEGGSR 250
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaereiAELEAELERLDASsdDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 251 EEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKI---EVAKRNIENAQKEIEESQA 327
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRA 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 328 RLRKSKEELkhvseeIEKSKGAIKRWGKRREQLLVQIKERETVRNELViKLGEIDkrFSEAREEFDKVVAELEEAKKALY 407
Cdd:COG4913 781 RLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALLD-RLEEDG--LPEYEERFKELLNENSIEFVADL 851
|
250 260
....*....|....*....|....*
gi 57159276 408 mkeseISKFEEEISRAKARITQFNA 432
Cdd:COG4913 852 -----LSKLRRAIREIKERIDPLND 871
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-503 |
2.72e-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: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 192 ARVDLLIREVKAQLDKLEKERN-----DALRyLDLKEKleKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLE---- 262
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDHLRNvqtecEALK-LQMAEK--DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEkein 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 263 DRLKEIAKEIVAKEKELAEIeRQLEEKSGDGILEITRKISEVKSKIevakRNIENAQKEIEESQARLRKSKEELKHVSEE 342
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKI-RELEARVSDLELEKVKLVNAGSERL----RAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 343 IEkskgAIKRWGKRREQllvqikERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKK-ALYMkeseiskfEEEIS 421
Cdd:pfam15921 676 YE----VLKRNFRNKSE------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvAMGM--------QKQIT 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 422 RAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAE 501
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
..
gi 57159276 502 AQ 503
Cdd:pfam15921 818 LQ 819
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1075-1146 |
2.96e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.28 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1075 SGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:PRK11160 477 SGGEQRRLGIARAL----LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1069-1153 |
3.04e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1069 KRIEAMSGGEKAIIALafvfaIQRYKPAP-FYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVI--THRDVMMAQADRI 1145
Cdd:PRK10247 133 KNIAELSGGEKQRISL-----IRNLQFMPkVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKV 207
|
....*...
gi 57159276 1146 IGVSMRNG 1153
Cdd:PRK10247 208 ITLQPHAG 215
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
186-511 |
5.13e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKERNdalRYLDLKEKLEKaRVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRL 265
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKE---RYKRDREQWER-QRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 266 KEIAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENA-------QKEIEESQARLRKSKEELKH 338
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEED-IKTLTQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 339 VSEEIEKSKGAIKRWGKRREQL---LVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISK 415
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLqdtITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 416 FEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQV----EGKISKVESRHRKAEKELEEKTRELQKVESELA 491
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340
....*....|....*....|..
gi 57159276 492 KARE--ELIKAEAQREVRGNRA 511
Cdd:pfam07888 350 REKDcnRVQLSESRRELQELKA 371
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
747-1036 |
5.57e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 747 ELEKRIEESKGEmaklrgRIERLEKKREKIKKALenpearelnSKIREVEAEISKLKEELSRVE-SKLESLDSRINEELL 825
Cdd:PRK05771 32 HIEDLKEELSNE------RLRKLRSLLTKLSEAL---------DKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 826 prkaDLEEEIEGLVNKINALNAYIEENKNAITELEKEleelktaeENVKDELKELREGrEQIRVEIAELRKEKDELTSkl 905
Cdd:PRK05771 97 ----KIEKEIKELEEEISELENEIKELEQEIERLEPW--------GNFDLDLSLLLGF-KYVSVFVGTVPEDKLEELK-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 906 qelrieantlkvrlAQVETTLQEKRAELKHFDPALVRSIKEipleveklrqDIEKMEEEIRSLEPVNMKaIEDFEVVERR 985
Cdd:PRK05771 162 --------------LESDVENVEYISTDKGYVYVVVVVLKE----------LSDEVEEELKKLGFERLE-LEEEGTPSEL 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 57159276 986 YLELSSKREQVLAEKESIEEFIQEI--EGQKRQVFLQTLNAIAKNFSELFAKL 1036
Cdd:PRK05771 217 IREIKEELEEIEKERESLLEELKELakKYLEELLALYEYLEIELERAEALSKF 269
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
206-1008 |
5.61e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 206 DKLEKERNDALRYLDlKEKLEKARVTLL-LAEIK-RLEKFIEEGGSREEEIE--GQIKSLEDRLKEIAKEIVAKEKELAE 281
Cdd:TIGR01612 1058 DEIEKEIGKNIELLN-KEILEEAEINITnFNEIKeKLKHYNFDDFGKEENIKyaDEINKIKDDIKNLDQKIDHHIKALEE 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 282 IERqleeKSGDGILEITRKISEVK--SKIEVAKRNIENAQKEIEESQARLRKSK---EELKHVSEEI----------EKS 346
Cdd:TIGR01612 1137 IKK----KSENYIDEIKAQINDLEdvADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIaeiekdktslEEV 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 347 KGAIKRWGKRREQLLVQIKERETVRNELVIK--------LGEIDKRFSEAREEFD---KVVAELE------EAKKALYMK 409
Cdd:TIGR01612 1213 KGINLSYGKNLGKLFLEKIDEEKKKSEHMIKameayiedLDEIKEKSPEIENEMGiemDIKAEMEtfnishDDDKDHHII 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 410 ESEISKFEEEISRAKARITQFNARR---NLLKEKIAEAKASLEAKRSELSQVEGKISKVES-----RHRKAEKELEEKTR 481
Cdd:TIGR01612 1293 SKKHDENISDIREKSLKIIEDFSEEsdiNDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilklnKIKKIIDEVKEYTK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 482 ELQK----VESELAKArEELIKaeaqrEVRGNRAVEFLKSQrieglygtlgelisvpkseyalaVEVALggnydnvvveD 557
Cdd:TIGR01612 1373 EIEEnnknIKDELDKS-EKLIK-----KIKDDINLEECKSK-----------------------IESTL----------D 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 558 DRVAEKAIKLLKEKKLGRLTflplnkikprsmrekpklgipamDVVSYDPRFRNAVAYALGDTLIVNDMDEAREvgigKV 637
Cdd:TIGR01612 1414 DKDIDECIKKIKELKNHILS-----------------------EESNIDTYFKNADENNENVLLLFKNIEMADN----KS 1466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 638 RMVTLggelLERSGAITGGHYkprgklgvNVDEIRKRVEALEGRKEalEAQVNALKVE-----VKGLENELFELRMKKSE 712
Cdd:TIGR01612 1467 QHILK----IKKDNATNDHDF--------NINELKEHIDKSKGCKD--EADKNAKAIEknkelFEQYKKDVTELLNKYSA 1532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 713 LSKDVQVIQKELDSylaeDRSLKEEIEENERLISELEKRiEESKGEMAKLRGRIERLEKKREKIKKA-------LENPEA 785
Cdd:TIGR01612 1533 LAIKNKFAKTKKDS----EIIIKEIKDAHKKFILEAEKS-EQKIKEIKKEKFRIEDDAAKNDKSNKAaidiqlsLENFEN 1607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 786 RELnsKIREVEAEISKLKEELSRVESKLESLDsrINEEllprkadlEEEIEGLVNKINALNAYIEENKNAitelekelee 865
Cdd:TIGR01612 1608 KFL--KISDIKKKINDCLKETESIEKKISSFS--IDSQ--------DTELKENGDNLNSLQEFLESLKDQ---------- 1665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 866 lktaEENVKDELKELregreqirveiaelrkekDELTSKLQELRIEANTLKvrlaqvettlqekraelKHFDPALVRSIK 945
Cdd:TIGR01612 1666 ----KKNIEDKKKEL------------------DELDSEIEKIEIDVDQHK-----------------KNYEIGIIEKIK 1706
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 946 EIPleveklRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESI-EEFIQ 1008
Cdd:TIGR01612 1707 EIA------IANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIyEEFIE 1764
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-489 |
6.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 196 LLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEiEGQIKSLEDRLKEIAKEIVAK 275
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAAEEAKKAEEDKKKAE 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 276 EKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQAR---LRKSKEELKHVSEEIEKSKGAIKR 352
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaeeAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 353 WGKRREQLLVQIKERETVRnELVIKlGEIDKRFSEAREEFDKVVAELEE---------AKKALYMKESEiskfEEEISRA 423
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEK-EAVIE-EELDEEDEKRRMEVDKKIKDIFDnfaniieggKEGNLVINDSK----EMEDSAI 1832
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 424 KARITQFNARRNLLKEkIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEkTRELQKVESE 489
Cdd:PTZ00121 1833 KEVADSKNMQLEEADA-FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE-ADEIEKIDKD 1896
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
192-454 |
7.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 192 ARVDLLIREVKAQLDKLEKERNDALRYLD-LKEKLEKARvtlllAEIKRLEKFIEEggsreeeIEGQIKSLEDRLKEIAK 270
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDaLQAELEELN-----EEYNELQAELEA-------LQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 271 EIVAKEKELAEIERQLEEKSGD-GILEI---TRKISEVKSKIEVAKRNIENAQKEIEEsqarLRKSKEELKHVSEEIEKs 346
Cdd:COG3883 80 EIEERREELGERARALYRSGGSvSYLDVllgSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 347 kgaikrwgkrreqllvQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKAR 426
Cdd:COG3883 155 ----------------KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250 260
....*....|....*....|....*...
gi 57159276 427 ITQFNARRNLLKEKIAEAKASLEAKRSE 454
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
207-571 |
7.45e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 207 KLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEE-------GGSREEEIEGQIKSLEDRLKEIAKEIVAKEKEL 279
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 280 AEIERQL-----EEKSGDGIL--------------EITRKISEVKSKIEVA--KRNIENAQKEIEESQARLRK---SKEE 335
Cdd:TIGR00606 768 EEQETLLgtimpEEESAKVCLtdvtimerfqmelkDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTvvsKIEL 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 336 LKHVSEE----IEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKES 411
Cdd:TIGR00606 848 NRKLIQDqqeqIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 412 EISKFEEEISRA-------KARITQFNARRNLLKEKIAEAKAS-LEAKRSELSQVEGKISKVESRHRKAEKELEEKTREL 483
Cdd:TIGR00606 928 LISSKETSNKKAqdkvndiKEKVKNIHGYMKDIENKIQDGKDDyLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 484 qkvesELAKAREELIKAEAQREVRGNRAVEfLKSQRIEGLYGTLGELISVPKSEY-ALAVEVALGGNYDNVVVEDDRVAE 562
Cdd:TIGR00606 1008 -----DTQKIQERWLQDNLTLRKRENELKE-VEEELKQHLKEMGQMQVLQMKQEHqKLEENIDLIKRNHVLALGRQKGYE 1081
|
....*....
gi 57159276 563 KAIKLLKEK 571
Cdd:TIGR00606 1082 KEIKHFKKE 1090
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
253-965 |
7.64e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 253 EIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSGDGIlEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKS 332
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 333 KEELKHVSEEIEK---SKGAIKRWGKRREQLLVQIK---ERETVRNE-----LVIKLGEIDKRFSEAREEFDKVVAELEE 401
Cdd:pfam01576 298 GEELEALKTELEDtldTTAAQQELRSKREQEVTELKkalEEETRSHEaqlqeMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 402 AKKALYMKESEIS------------------KFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGK-- 461
Cdd:pfam01576 378 AKQALESENAELQaelrtlqqakqdsehkrkKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKni 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 462 -----ISKVESRHRKAEKELEEKTRE-------LQKVESELAKAREELIKAEAQREvRGNRAVEFLKSQ------RIEGL 523
Cdd:pfam01576 458 klskdVSSLESQLQDTQELLQEETRQklnlstrLRQLEDERNSLQEQLEEEEEAKR-NVERQLSTLQAQlsdmkkKLEED 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 524 YGTLgELISVPKSEYALAVEVA--------------------LGGNYDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPLNK 583
Cdd:pfam01576 537 AGTL-EALEEGKKRLQRELEALtqqleekaaaydklektknrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 584 IKPRSMREKpklgipamDVVSYDPRFRNAVAYALGDTLivNDMDEAREVGIGKVRMVTLGGELLERSGaitgghykprgk 663
Cdd:pfam01576 616 ISARYAEER--------DRAEAEAREKETRALSLARAL--EEALEAKEELERTNKQLRAEMEDLVSSK------------ 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 664 lgvnvDEIRKRVEALEGRKEALEAQVNALKVEVKGLENEL---------FELRM--------------------KKSELS 714
Cdd:pfam01576 674 -----DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELqatedaklrLEVNMqalkaqferdlqardeqgeeKRRQLV 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 715 KDVQVIQKELDS-------YLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALEN--PEA 785
Cdd:pfam01576 749 KQVRELEAELEDerkqraqAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEilAQS 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 786 RELNSKIREVEAEISKLKEELS---RVESKLESLDSRINEEL---LPRKADLEEEIEGLVNKINALNAYIEENKNAITEL 859
Cdd:pfam01576 829 KESEKKLKNLEAELLQLQEDLAaseRARRQAQQERDELADEIasgASGKSALQDEKRRLEARIAQLEEELEEEQSNTELL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 860 EKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQEL--------RIEANTLKVRLAQVETTLQEKRA 931
Cdd:pfam01576 909 NDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMegtvkskfKSSIAALEAKIAQLEEQLEQESR 988
|
810 820 830
....*....|....*....|....*....|....*..
gi 57159276 932 ELKHFDPALVRS---IKEIPLEVEKLRQDIEKMEEEI 965
Cdd:pfam01576 989 ERQAANKLVRRTekkLKEVLLQVEDERRHADQYKDQA 1025
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
659-776 |
7.67e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 659 KPRGKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEI 738
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 57159276 739 EENERLISELE---KRIEESKGEMAKLRgRIERLEKKREKI 776
Cdd:COG2433 472 REIERLERELEeerERIEELKRKLERLK-ELWKLEHSGELV 511
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
746-1036 |
8.02e-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: 47.04 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 746 SELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENP-------EARELNSKIREVEAEISKLKEELSRVESKLESLDS 818
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 819 R---INEELLPRKADLEEEIEGLVNKINALNAYIEEnknaitelekeleelktAEENVKDELKELREGREQIRVEIAELR 895
Cdd:pfam15921 300 QleiIQEQARNQNSMYMRQLSDLESTVSQLRSELRE-----------------AKRMYEDKIEELEKQLVLANSELTEAR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 896 KEKDELTSKLQELRIEANTLKVRLAQVETTLQ-EKRAELKHFD---------PALVRSIKEIPLEVEKLRQDIEKMEEEI 965
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLLADLHKREKELSlEKEQNKRLWDrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSEC 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 966 RSLEPVNMKAIE-DFEVVERryleLSSKREQVLAEKESIEEFIQEIEGQKrqvflQTLNAIAKNFSELFAKL 1036
Cdd:pfam15921 443 QGQMERQMAAIQgKNESLEK----VSSLTAQLESTKEMLRKVVEELTAKK-----MTLESSERTVSDLTASL 505
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1045-1146 |
8.30e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 43.98 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1045 ILENPEDPFSGglEIEAKPAGKdVKRIEAMSGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEas 1124
Cdd:cd03221 45 LIAGELEPDEG--IVTWGSTVK-IGYFEQLSGGEKMRLALAKLL----LENPNLLLLDEPTNHLDLESIEALEEALKE-- 115
|
90 100
....*....|....*....|...
gi 57159276 1125 QNSQFIVITH-RDVMMAQADRII 1146
Cdd:cd03221 116 YPGTVILVSHdRYFLDQVATKII 138
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
5-90 |
8.50e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 44.90 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGNKKVvvPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGskgeppAKYAEVA 84
Cdd:cd03276 1 IESITLKNFMCHRHLQI--EFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDG------ESSAKIT 72
|
....*.
gi 57159276 85 MYFNNE 90
Cdd:cd03276 73 VTLKNQ 78
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
265-429 |
8.56e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 265 LKEIAKEIVAKEKELA-----EIERQLEEKSGDGILEITRKISEVKSKIEvakRNIENAQKEIEESQARLRKSKEELKHV 339
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAkrileEAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 340 SEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFS-----EAREE-FDKVVAELeEAKKALYMKESEI 413
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAKEIlLEKVEEEA-RHEAAVLIKEIEE 180
|
170
....*....|....*.
gi 57159276 414 SKFEEEISRAKARITQ 429
Cdd:PRK12704 181 EAKEEADKKAKEILAQ 196
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
170-456 |
9.59e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 170 IAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKErnDALRYLDLKEKLEKARVTLllAEIKRLEKFIEEGGS 249
Cdd:PRK01156 471 INHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE--EINKSINEYNKIESARADL--EDIKIKINELKDKHD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 250 REEEIEGQIKSL---------EDRLKEIAK----EIVAKEKELAEIERQLEEKSgDGILEITRKISEVKS-------KIE 309
Cdd:PRK01156 547 KYEEIKNRYKSLkledldskrTSWLNALAVisliDIETNRSRSNEIKKQLNDLE-SRLQEIEIGFPDDKSyidksirEIE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 310 VAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRwgkrreqllvqikeretvRNELVIKLGEIDKRFSEAR 389
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPD------------------LKEITSRINDIEDNLKKSR 687
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57159276 390 EEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQfnarrnllKEKIAEAKASLEAKRSELS 456
Cdd:PRK01156 688 KALDDAKANRARLESTIEILRTRINELSDRINDINETLES--------MKKIKKAIGDLKRLREAFD 746
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
233-513 |
1.16e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 233 LLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIER-----QLEEKSGDGileitrKISEVKSK 307
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAarqklQLEKVTTEA------KIKKLEED 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 308 IEVAKRNIENAQKEIEESQARLrksKEELKHVSEEIEKSKGAIKRWGKRR---EQLLVQIKERETVRNELVIKLGEIDKR 384
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERI---SEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEKGRQELEKAKRKLEGE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 385 FSEAREEFDKVVAELEEAKKALymkeseiSKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISK 464
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQL-------AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNK 289
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 57159276 465 VESRHRKAEKELEEKTRELQkveselakarEELIKAEAQREVRGNRAVE 513
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELE----------DTLDTTAAQQELRSKREQE 328
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
208-449 |
1.33e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 208 LEKERNDALRYL---------DLKEKLEKARVTLLLAEIKRLEKFI--------EEGGSREEEIEGQIKSLEDRLKEIak 270
Cdd:PRK05771 14 LKSYKDEVLEALhelgvvhieDLKEELSNERLRKLRSLLTKLSEALdklrsylpKLNPLREEKKKVSVKSLEELIKDV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 271 eivakEKELAEIERQLEEKsgdgileiTRKISEVKSKIevakrnienaqKEIEESQARLrkskEELKHVSEEIEK---SK 347
Cdd:PRK05771 92 -----EEELEKIEKEIKEL--------EEEISELENEI-----------KELEQEIERL----EPWGNFDLDLSLllgFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 348 GAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRF-----SEAREEFDKVVAELEEAKKALymkeSEISKFEEEISR 422
Cdd:PRK05771 144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVvvvvlKELSDEVEEELKKLGFERLEL----EEEGTPSELIRE 219
|
250 260
....*....|....*....|....*..
gi 57159276 423 AKARITQFNARRNLLKEKIAEAKASLE 449
Cdd:PRK05771 220 IKEELEEIEKERESLLEELKELAKKYL 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
668-766 |
1.41e-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: 45.53 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISE 747
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
90 100
....*....|....*....|....
gi 57159276 748 LEKRIEESKGEM-----AKLRGRI 766
Cdd:COG4942 232 LEAEAAAAAERTpaagfAALKGKL 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
234-1009 |
1.43e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 234 LAEIKRLEKFIEEGGSREEEIEGQiksleDRLKEIAKEIVAKEKElAEIERQLEEKSGDGILEITRKISEVKSKIEVAKR 313
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKAL-----ETLRQVRQTQGQKVQE-HQMELKYLKQYKEKACEIRDQITSKEAQLESSRE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 314 ----------NIENAQKEIEESQARLRKSKEELKhvseEIEKSKGAIKRWGKRREQLLVQIKE-RETVRNELVIKLGEID 382
Cdd:TIGR00606 239 ivksyeneldPLKNRLKEIEHNLSKIMKLDNEIK----ALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDLYHNHQRTV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 383 KRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGK- 461
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKn 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 462 -----ISKVESRHRKAEK---ELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRIEGLYGTLGELISV 533
Cdd:TIGR00606 395 fhtlvIERQEDEAKTAAQlcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 534 PKSEYALAVEVALGGNYDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPL-NKIKPRSMREKPKLGIPAMDVVSYDPRFRN- 611
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQeMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKi 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 612 ---------AVAYALGDTLIVNDM--DEAREVGIGKVRMVTLGGELlersgaitgghykprGKLGVNVDEIRKRVEALEG 680
Cdd:TIGR00606 555 ksrhsdeltSLLGYFPNKKQLEDWlhSKSKEINQTRDRLAKLNKEL---------------ASLEQNKNHINNELESKEE 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 681 RKEALEAQV------NALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAE--------DRSLKEEIEENErLIS 746
Cdd:TIGR00606 620 QLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcQRVFQTEAELQE-FIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 747 ELEKRIEESKGEMAKLRGRIERLEKKREKI---------KKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLD 817
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrqsIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIM 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 818 SrineellprKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEEL--KTAEENVKDELKELREGREQIRVEIAELR 895
Cdd:TIGR00606 779 P---------EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 896 KEKDELTSKLQELRIEANTLKVRLAQVETTLQ------EKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEeiRSLE 969
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrrqqfeEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ--EKEE 927
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 57159276 970 PVNMKAIEDfEVVERRYLELSSKREQVLAEKESIEEFIQE 1009
Cdd:TIGR00606 928 LISSKETSN-KKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
260-513 |
1.45e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.16 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 260 SLEDRLKEIAKEIVA-KEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIEnaqkeiEESQARL-RKSKEELK 337
Cdd:NF033838 51 SGNESQKEHAKEVEShLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLK------EKSEAELtSKTKKELD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 338 HVSEEIEKskgaikrwgkrrEQLLVQIKERETVRnelviKLGEIDKRfSEAREEFDKVVAELEEAKKAlymkESEISKFE 417
Cdd:NF033838 125 AAFEQFKK------------DTLEPGKKVAEATK-----KVEEAEKK-AKDQKEEDRRNYPTNTYKTL----ELEIAESD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 418 EEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEgkisKVESRHRKAEKELEEKT--RELQKVESELAKARE 495
Cdd:NF033838 183 VEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLE----KIKTDREKAEEEAKRRAdaKLKEAVEKNVATSEQ 258
|
250
....*....|....*...
gi 57159276 496 ELIKAEAQREVRGNRAVE 513
Cdd:NF033838 259 DKPKRRAKRGVLGEPATP 276
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
667-934 |
1.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 667 NVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLIS 746
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 747 ELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEAR--ELNSKIREVEAEISKLKEELSRVEskLESLDSRINEEL 824
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALS--EAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 825 LPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSK 904
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270
....*....|....*....|....*....|
gi 57159276 905 LQELRIEANTLKVRLAQVETTLQEKRAELK 934
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLA 299
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
665-1005 |
1.53e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.00 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 665 GVNVDEIRKRVEAlegRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDV--QVIQKeldsylaedrsLKEEI--EE 740
Cdd:PLN03229 410 GVPVDPERKVNMK---KREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELAlnEMIEK-----------LKKEIdlEY 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 741 NERLIS-ELEKRIEESKGEMAKL--------RGRIERLEKKREKIKKALENPEARE-LNSKIrEVEAEISKLKEeLSRVE 810
Cdd:PLN03229 476 TEAVIAmGLQERLENLREEFSKAnsqdqlmhPVLMEKIEKLKDEFNKRLSRAPNYLsLKYKL-DMLNEFSRAKA-LSEKK 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 811 SKLESLDSRINEELlPRKADLEEEIEglvnKINALNAYIEENKnaitelekeleelKTAEENVKDELKE-LREGREQIRV 889
Cdd:PLN03229 554 SKAEKLKAEINKKF-KEVMDRPEIKE----KMEALKAEVASSG-------------ASSGDELDDDLKEkVEKMKKEIEL 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 890 EIAELRKEKDeltskLQELRIEANTLKVRLAQVETTLQEKRAELKH----------FDPALVRSIKEIPLEVEK------ 953
Cdd:PLN03229 616 ELAGVLKSMG-----LEVIGVTKKNKDTAEQTPPPNLQEKIESLNEeinkkierviRSSDLKSKIELLKLEVAKasktpd 690
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 57159276 954 --LRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAEKESIEE 1005
Cdd:PLN03229 691 vtEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKN 744
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-91 |
1.57e-04 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 44.51 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 5 IEKIEMKGFKSYGnkKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIfagSKGEPPAkYAEVA 84
Cdd:cd03277 3 IVRIKLENFVTYD--ETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFV---KRGCDEG-TIEIE 76
|
....*..
gi 57159276 85 MYFNNED 91
Cdd:cd03277 77 LYGNPGN 83
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1069-1146 |
1.75e-04 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 43.58 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1069 KRIEAMSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVI--THrDVMMA--QADR 1144
Cdd:cd03214 93 RPFNELSGGERQRVLLARALAQE----PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVmvLH-DLNLAarYADR 167
|
..
gi 57159276 1145 II 1146
Cdd:cd03214 168 VI 169
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1069-1153 |
1.88e-04 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 44.65 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1069 KRIEAMSGGEK--AIIALAFVfaiQRykpAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVI--THrDVMMA--QA 1142
Cdd:COG1120 133 RPVDELSGGERqrVLIARALA---QE---PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVmvLH-DLNLAarYA 205
|
90
....*....|.
gi 57159276 1143 DRIIGvsMRNG 1153
Cdd:COG1120 206 DRLVL--LKDG 214
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
652-908 |
1.89e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 652 AITGGHYKPRgKLGVNVDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAED 731
Cdd:pfam06008 6 SLTGALPAPY-KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 732 RSLKEEIEENERLISELEKRIEESKGEMAKLRGRieRLEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVES 811
Cdd:pfam06008 85 KELAEAIKNLIDNIKEINEKVATLGENDFALPSS--DLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 812 KLESLdsriNEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEI 891
Cdd:pfam06008 163 WFQSP----QEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
250
....*....|....*..
gi 57159276 892 AELRKEKDELTSKLQEL 908
Cdd:pfam06008 239 KTARDSLDAANLLLQEI 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
241-457 |
2.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 241 EKFIEE-GGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLeeksgdGILEITRKISEVKSKIEVAKRNIENAQ 319
Cdd:COG3206 159 EAYLEQnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKN------GLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 320 KEIEESQARLRKSKEELKHVSEEIEKSKGAikrwgkrreQLLVQIKERetvRNELVIKLGEIDKRFSEAREEFDKVVAEL 399
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQS---------PVIQQLRAQ---LAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 400 EEAKKALYMKESEI-SKFEEEISRAKARITQFNARRNLLKEKIAEAkASLEAKRSELSQ 457
Cdd:COG3206 301 AALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAEL-PELEAELRRLER 358
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
4-308 |
2.20e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 44.90 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 4 YIEKIEMKGFKSYgnKKVVVPLARGFTAIVGANGSGKSNIGDAVLFVLGGLSAKAMRASRISDLIFAGSKGEPPAKYaev 83
Cdd:pfam13175 2 KIKSIIIKNFRCL--KDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNI--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 84 aMYFNNEDRGFPIDEDEVVIKRRVYPDGRStywLNGKRATRSEIIDLLSAAMISPEGYNLVLQGDITKFIKmspierrLI 163
Cdd:pfam13175 77 -FENISFSIDIEIDVEFLLILFGYLEIKKK---YLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKK-------YL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 164 IDEISGIAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLekF 243
Cdd:pfam13175 146 KQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHENVLENLQIKKLL--I 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57159276 244 IEEGGSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKsgdgILEITRKISEVKSKI 308
Cdd:pfam13175 224 SADRNASDEDSEKINSLLGALKQRIFEEALQEELELTEKLKETQNK----LKEIDKTLAEELKNI 284
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
876-1017 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 876 ELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPAL--VRSIKEIplevEK 953
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEY----EA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 954 LRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAE----KESIEEFIQEIEGQKRQV 1017
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEEL 161
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
695-855 |
2.32e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.44 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 695 EVKGLENELFELRMKKselskdvQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKgemaKLRGRIERLEKKRE 774
Cdd:pfam05911 682 ENKRLKEEFEQLKSEK-------ENLEVELASCTENLESTKSQLQESEQLIAELRSELASLK----ESNSLAETQLKCMA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 775 KIKKALEnpearelnSKIREVEAEISKLKEELSRVESKLESlDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKN 854
Cdd:pfam05911 751 ESYEDLE--------TRLTELEAELNELRQKFEALEVELEE-EKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKK 821
|
.
gi 57159276 855 A 855
Cdd:pfam05911 822 L 822
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1059-1146 |
2.35e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.34 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1059 IEAKPAGKDV---KRIEAMSGGEKAIIALAFvfAIqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHR 1135
Cdd:PRK13657 454 IERKPDGYDTvvgERGRQLSGGERQRLAIAR--AL--LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHR 529
|
90
....*....|.
gi 57159276 1136 DVMMAQADRII 1146
Cdd:PRK13657 530 LSTVRNADRIL 540
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-505 |
2.38e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 263 DRLKEIAKEIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEE 342
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 343 IEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISR 422
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 423 AKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEA 502
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
...
gi 57159276 503 QRE 505
Cdd:COG4372 242 LEL 244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
668-989 |
2.65e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEaleaQVNALKVEVKGLENELFE---------LRMKKSE-LSKDVQVIQKEldsylaeDRSLKEE 737
Cdd:pfam05557 230 VEDLKRKLEREEKYRE----EAATLELEKEKLEQELQSwvklaqdtgLNLRSPEdLSRRIEQLQQR-------EIVLKEE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 738 IEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKalenpEARELNSKIREVEAEISKLKEelsrvesKLESLD 817
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA-----LVRRLQRRVLLLTKERDGYRA-------ILESYD 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 818 SRIN-EELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQ--IRVEIAEL 894
Cdd:pfam05557 367 KELTmSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPsySKEEVDSL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 895 RKEKDELTSKLQELRIEANTLKVRLAQVET--TLQEKRAELKHF--DPALV--RSIKEiplEVEKLRQDIEKMEEEIRSL 968
Cdd:pfam05557 447 RRKLETLELERQRLREQKNELEMELERRCLqgDYDPKKTKVLHLsmNPAAEayQQRKN---QLEKLQAEIERLKRLLKKL 523
|
330 340
....*....|....*....|....*
gi 57159276 969 EPVNMKA----IEDFEVVERRYLEL 989
Cdd:pfam05557 524 EDDLEQVlrlpETTSTMNFKEVLDL 548
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
769-969 |
2.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 769 LEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESklesldsriNEELLPRKADLEEEIEGLVNKINALNAY 848
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE---------YAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 849 IEENKNAItelekeleelktaeenvkdELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQE 928
Cdd:COG4717 118 LEKLEKLL-------------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 57159276 929 KRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLE 969
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
700-1017 |
2.90e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 700 ENELFELRMKKSELSKDVQVIQKELdsylaedrslKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKI--K 777
Cdd:pfam05483 207 ENARLEMHFKLKEDHEKIQHLEEEY----------KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLeeK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 778 KALENPEARELNSKIREVEAEISKLKEELSRVESKLESL--DSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNA 855
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALeeDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 856 ITElekeleelkTAEENVKDELKELREGREQIRVEIAELRKEkdelTSKLQELRIEANTLKVRLAQVETTLQEKRAELKH 935
Cdd:pfam05483 357 TTC---------SLEELLRTEQQRLEKNEDQLKIITMELQKK----SSELEEMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 936 FDpalvrsikeiplEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVverrylelsskreQVLAEKESIEEFIQEIEGQKR 1015
Cdd:pfam05483 424 KK------------QFEKIAEELKGKEQELIFLLQAREKEIHDLEI-------------QLTAIKTSEEHYLKEVEDLKT 478
|
..
gi 57159276 1016 QV 1017
Cdd:pfam05483 479 EL 480
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
683-854 |
2.96e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 43.58 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 683 EALEAQVNALKvevkgleNELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKL 762
Cdd:pfam17078 6 ESLHDQIDALT-------KTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 763 RGRIERLEKKREKIKKALENPEARE--LNSKIREVEA------------------EISKLKEELSRVESKLESLDSRINE 822
Cdd:pfam17078 79 KNSYEELTESNKQLKKRLENSSASEttLEAELERLQIqydalvdsqneykdhyqqEINTLQESLEDLKLENEKQLENYQQ 158
|
170 180 190
....*....|....*....|....*....|..
gi 57159276 823 ELLPRKADLEEEIEGLVNKINALNAyIEENKN 854
Cdd:pfam17078 159 RISSNDKDIDTKLDSYNNKFKNLDN-IYVNKN 189
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
251-573 |
3.09e-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: 45.21 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 251 EEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEEKSgdgileitRKISEVKSKIEVAKRNIENAQKEIEESQARLR 330
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS--------REETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 331 KS-KEELKHVSEEIEKSKGAIKRWGKRREQLLVQIKE------------RETVRNELVIKLG----EIDKRFSEAREEFD 393
Cdd:pfam12128 671 KAlAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkreartekqayWQVVEGALDAQLAllkaAIAARRSGAKAELK 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 394 KVVAELEEAKKALYMKESEISKFEEEISRAKARITQ------------------FNARRNLLKEKIAEAKASLEAKRSEL 455
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERiavrrqevlryfdwyqetWLQRRPRLATQLSNIERAISELQQQL 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 456 ----SQVEGKISKVES-RH--RKAEKELEEKTRELQKVESELAKAREELIKAEAQREV-RGNRAVEFLKSQRiEGLYGTL 527
Cdd:pfam12128 831 arliADTKLRRAKLEMeRKasEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIgERLAQLEDLKLKR-DYLSESV 909
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 57159276 528 GELISVPKSEYALAVEVALGGNYDNVVVEDDRVAEKAIKLLKEKKL 573
Cdd:pfam12128 910 KKYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKL 955
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
669-912 |
3.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 669 DEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISEL 748
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 749 EKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELLPRK 828
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 829 ADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQEL 908
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
....
gi 57159276 909 RIEA 912
Cdd:COG4372 309 LIGA 312
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-505 |
3.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 260 SLEDRLKEIAKEIVakeKELAE--IERQLEeksgdgileitRKISEVKSKIEVAKRNIENAQKEIEESQARLR--KSKEE 335
Cdd:COG3206 141 SYTSPDPELAAAVA---NALAEayLEQNLE-----------LRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 336 LKHVSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREefDKVVAELEEAKKALYMKESEIS- 414
Cdd:COG3206 207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSa 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 415 KFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAR 494
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364
|
250
....*....|.
gi 57159276 495 EELIKAEAQRE 505
Cdd:COG3206 365 ELYESLLQRLE 375
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
188-503 |
3.42e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 188 EENLARVDLLIREVKAQLDKLEKERNDALRylDLKEKLEKARVTLLLAEIKRLEKfieeggsreeeiEGQIKSLEDRLKE 267
Cdd:pfam10174 442 EEALSEKERIIERLKEQREREDRERLEELE--SLKKENKDLKEKVSALQPELTEK------------ESSLIDLKEHASS 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 268 IAKEIVAKEKELAEIERQLEEKSGDGIleitrKISEVKSKIEvakrNIENAQKEIEESQARLRKSKEELKHVSEEIEKSK 347
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQKKEECS-----KLENQLKKAH----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQ 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 348 GAIKRwgkrreqLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKAlyMKESEISKFEEeisrakARI 427
Cdd:pfam10174 579 AEVER-------LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQE--MKKKGAQLLEE------ARR 643
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 428 TQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESrhrkaekELEEKTRELQKVESELAKAREELIKAEAQ 503
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQ-------SLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1069-1154 |
3.91e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 43.11 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1069 KRIEAMSGGEK---AII-ALA----FVFAiqrykpapfyllDEIDAHLDDANVKRVADLIKEASQNSQ--FIVITHRDVM 1138
Cdd:COG1136 140 HRPSQLSGGQQqrvAIArALVnrpkLILA------------DEPTGNLDSKTGEEVLELLRELNRELGttIVMVTHDPEL 207
|
90
....*....|....*.
gi 57159276 1139 MAQADRIIgvSMRNGV 1154
Cdd:COG1136 208 AARADRVI--RLRDGR 221
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
265-497 |
3.92e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 265 LKEIAKEIVAK--EKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEEL-KHVSE 341
Cdd:PRK05771 14 LKSYKDEVLEAlhELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELiKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 342 EIEKSKGAIKRWGKRREQLLVQIKERETVRNELvIKLGEIDKRFSEAREE--FDKVVAELEEAKKALYMKESEISkFEEE 419
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVE-NVEY 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57159276 420 ISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSqVEGKISKVesrHRKAEKELEEKTRELQKVESELAKAREEL 497
Cdd:PRK05771 172 ISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELE-EEGTPSEL---IREIKEELEEIEKERESLLEELKELAKKY 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1074-1153 |
3.95e-04 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 42.84 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1074 MSGGEKAIIALAfvfaiqR--YKPAPFYLLDEI----DAHLDDANVKRVadLIKEASQNSQFIVITHRDVMMAQADRIIg 1147
Cdd:cd03250 128 LSGGQKQRISLA------RavYSDADIYLLDDPlsavDAHVGRHIFENC--ILGLLLNNKTRILVTHQLQLLPHADQIV- 198
|
....*.
gi 57159276 1148 vSMRNG 1153
Cdd:cd03250 199 -VLDNG 203
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
200-342 |
4.65e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 200 EVKAQLDKLEKER-------------NDALRYLDLKEKLEKarvtlllaEIKRLEKFIEEGGSREEEIEGQIKSLEDRLK 266
Cdd:PRK11281 40 DVQAQLDALNKQKlleaedklvqqdlEQTLALLDKIDRQKE--------ETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57159276 267 EIAKEIVAKEkELAEIERQLEEKSGDgiLEITRK-ISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEE 342
Cdd:PRK11281 112 EETRETLSTL-SLRQLESRLAQTLDQ--LQNAQNdLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1074-1146 |
5.15e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.17 E-value: 5.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57159276 1074 MSGGEKAIIALAFVFAiqryKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQ--FIVITHrDVMMAQ--ADRII 1146
Cdd:cd03237 116 LSGGELQRVAIAACLS----KDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEktAFVVEH-DIIMIDylADRLI 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
423-499 |
5.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57159276 423 AKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIK 499
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
748-969 |
5.58e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 748 LEKRIEESKGEMAKLRGRIERLEKKREKIKKALENpEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELLPR 827
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKR-DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 828 kADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDE-------LKELREGREQIRVEIAELRKEKDE 900
Cdd:pfam07888 111 -EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERakkagaqRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 901 LTSKLQELRieaNTLKVRLAQVEtTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLE 969
Cdd:pfam07888 190 LSKEFQELR---NSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVE 254
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
711-806 |
6.54e-04 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.94 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 711 SELSKD-VQVIQKELDSYLAEDRSLKEEIE---ENERLISELEKRIEESKGEM-AKLRGRIerlEKKREKIKKALENPEA 785
Cdd:PRK00290 498 SGLSDEeIERMVKDAEANAEEDKKRKELVEarnQADSLIYQTEKTLKELGDKVpADEKEKI---EAAIKELKEALKGEDK 574
|
90 100
....*....|....*....|.
gi 57159276 786 RELNSKIREVEAEISKLKEEL 806
Cdd:PRK00290 575 EAIKAKTEELTQASQKLGEAM 595
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-337 |
6.85e-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: 42.60 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 188 EENLARVDLLIREVKAQLDKLEKERNdalrylDLKEKLEKARvtlllAEIKRLEKFIEEGGSREEeiegqIKSLEDRLKE 267
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIK------RLELEIEEVE-----ARIKKYEEQLGNVRNNKE-----YEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 268 IAKEIVAKEKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELK 337
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEE-LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-302 |
8.24e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 29 FTAIVGANGSGKSNIGDAVLFVlgglsaKAMRASRISDLIFAGSKGEPPakyaevaMYFNNEDRGFPIDEDEVVIKRRVY 108
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFL------ADFDALVIGLTDERSRNGGIG-------GIPSLLNGIDPKEPIEFEISEFLE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 109 PDGRSTYWLNGKRATRSEIIdllsaamispegynlvlqgditkFIKMSPIERRLIIDEISGIAEYDAKKEKALKELKQTE 188
Cdd:pfam13304 68 DGVRYRYGLDLEREDVEEKL-----------------------SSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 189 ENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLlaeikRLEKFIEEGGSREEEIEGQIKSLEDRLKEI 268
Cdd:pfam13304 125 EERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVL-----DLAADLALFPDLKELLQRLVRGLKLADLNL 199
|
250 260 270
....*....|....*....|....*....|....
gi 57159276 269 AKEIVAKEKELAEIERQLEEKSGDGILEITRKIS 302
Cdd:pfam13304 200 SDLGEGIEKSLLVDDRLRERGLILLENGGGGELP 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1074-1146 |
8.31e-04 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 42.22 E-value: 8.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 1074 MSGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:cd03251 139 LSGGQRQRIAIARAL----LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIV 207
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
1071-1189 |
8.43e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.11 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1071 IEAMSGGEKAIIALAFVFAIQRYKPApFYLLDEIDAHLDDANVKRVADLIKEASQ--NSQFIVITH-RDVMMAQA----- 1142
Cdd:COG1106 200 LSEESDGTKRLLALAGALLDALAKGG-VLLIDEIEASLHPSLLRKLLKLFLDLANknNAQLIFTTHsTELLDAFLellrr 278
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 57159276 1143 DRIIGVS-MRNGVSKVVSLSLEKarkileeIRKKDEAEHREMFGRLEA 1189
Cdd:COG1106 279 DQIWFVEkDKDGASELYSLEDFK-------VRKDENLEKGYLQGRYGA 319
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
250-510 |
8.72e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.78 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 250 REEEIEGqiksLEDRLKEIAKEIVAKEKELAEIERQLE------EKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIE 323
Cdd:pfam15818 90 KEKEIEG----LKETLKALQVSKYSLQKKVSEMEQKLQlhllakEDHHKQLNEIEKYYATITGQFGLVKENHGKLEQNVQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 324 ES--------------QARLRKSKEELKHVSEEIEKSKgAIKRWGKRREQLLVQIKERetvrnelviKLGEIDKRFSEAR 389
Cdd:pfam15818 166 EAiqlnkrlsalnkkqESEICSLKKELKKVTSDLIKSK-VTCQYKMGEENINLTIKEQ---------KFQELQERLNMEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 390 EEFDKVVAE---LEEAKKALYMKESEISKFEEEISRAKARItqfNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVE 466
Cdd:pfam15818 236 ELNKKINEEithIQEEKQDIIISFQHMQQLLQQQTQANTEM---EAELKALKENNQTLERDNELQREKVKENEEKFLNLQ 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 57159276 467 SRHRKA----EKELEEKTRELQKVESELAKAREELIKAEAQREVRGNR 510
Cdd:pfam15818 313 NEHEKAlgtwKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQ 360
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
697-822 |
9.08e-04 |
|
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: 42.70 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 697 KGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEEskgEMAKLRGRIERLEKKREKI 776
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPT---ELDRAKEKLKKLLQEIMIK 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 57159276 777 KKALEnpearELNSKIREVEAEISKLKEELSRVESKLESLDSRINE 822
Cdd:smart00787 224 VKKLE-----ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
285-581 |
9.30e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 285 QLEEKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQI 364
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 365 KERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEA 444
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 445 KASLEAKRSELS-----QVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQR 519
Cdd:COG4372 163 QEELAALEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 520 IEGLYGTLGELISVPKSEYALAVEVALGGNYDNVVVEDDRVAEKAIKLLKEKKLGRLTFLPL 581
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
671-1037 |
9.36e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 671 IRKRVEALEGRKEALEAQ-VNALKVEVKGL------ENELFELRMKKSELskdVQVIQKELDSYL--AED-------RSL 734
Cdd:pfam06160 8 IYKEIDELEERKNELMNLpVQEELSKVKKLnltgetQEKFEEWRKKWDDI---VTKSLPDIEELLfeAEElndkyrfKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 735 KEEIEENERLISELEKRIEESKGEMAKL-------RGRIERLEKKREKIKKALEN------PEARELNSKIREVEAEIS- 800
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELleseeknREEVEELKDKYRELRKTLLAnrfsygPAIDELEKQLAEIEEEFSq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 801 ------------------KLKEELSRVESKLE---SLDSRINEELLPRKADLEEEIEGLVNK------------INALNA 847
Cdd:pfam06160 165 feeltesgdylearevleKLEEETDALEELMEdipPLYEELKTELPDQLEELKEGYREMEEEgyalehlnvdkeIQQLEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 848 YIEENKNAItelekELEELKTAEENVKDELKELREGREQIRVEI---AELRKEKDELTSKLQELRIEANTLKVRLAQVet 924
Cdd:pfam06160 245 QLEENLALL-----ENLELDEAEEALEEIEERIDQLYDLLEKEVdakKYVEKNLPEIEDYLEHAEEQNKELKEELERV-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 925 tlqEKRAELKHFDPALVRSIKEIPLEVEK-LRQDIEKMEE------EIRSLEPVNMKAIEDFEVVERRYLE-LSSKREQV 996
Cdd:pfam06160 318 ---QQSYTLNENELERVRGLEKQLEELEKrYDEIVERLEEkevaysELQEELEEILEQLEEIEEEQEEFKEsLQSLRKDE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 57159276 997 LAEKESIEEFIQEIEGQKRQVFLQTLNAIAKNFSELFAKLS 1037
Cdd:pfam06160 395 LEAREKLDEFKLELREIKRLVEKSNLPGLPESYLDYFFDVS 435
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
736-911 |
9.46e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 42.06 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 736 EEIEENERLISELEKRIEESKGEmakLRGRIERLEKKREKIKKALEnpEARELNSKIREVEAEISKLKEELSRVESKLES 815
Cdd:pfam14988 29 QECEEIERRRQELASRYTQQTAE---LQTQLLQKEKEQASLKKELQ--ALRPFAKLKESQEREIQDLEEEKEKVRAETAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 816 LDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELR 895
Cdd:pfam14988 104 KDREAHLQFLKEKALLEKQLQELRILELGERATRELKRKAQALKLAAKQALSEFCRSIKRENRQLQKELLQLIQETQALE 183
|
170
....*....|....*.
gi 57159276 896 KEKDELTSKLQELRIE 911
Cdd:pfam14988 184 AIKSKLENRKQRLKEE 199
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
681-960 |
1.13e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 681 RKEALEAQVNALKVEVKGLENELFELrmkkSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMA 760
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEM----TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 761 KLRGRIERLE--------------KKREKIKKALENPEAR--ELNSKIREVEAEISKLKEELSRVESKLESLDSRIN--- 821
Cdd:pfam05483 447 AREKEIHDLEiqltaiktseehylKEVEDLKTELEKEKLKniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIInck 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 822 ---EELLPRKADLEEEIEGLVNKINALNAYI--------------EENKNAITELEKELEELKTAEENVKDELKELREGR 884
Cdd:pfam05483 527 kqeERMLKQIENLEEKEMNLRDELESVREEFiqkgdevkckldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 885 EQirvEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEK 960
Cdd:pfam05483 607 NK---NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
363-485 |
1.15e-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: 42.31 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 363 QIKERETVRNELVIKLGEIDKRFSEAREEFDKVVAELEEAKKALYMK-ESEISKFEEEISRAKARITQFNARRNLLKEKI 441
Cdd:smart00787 162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRaKEKLKKLLQEIMIKVKKLEELEEELQELESKI 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 57159276 442 AEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQK 485
Cdd:smart00787 242 EDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQS 285
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
742-974 |
1.16e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 742 ERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENpearELNSKiREVEAEISKLK-----EELSRV--ESKLE 814
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED----ELNLR-TSAENDLVGLRkdldeATLARVdlEAKIE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 815 SLdsriNEELLPRKADLEEEIEGLVNKINA--------------LNAYIEENKNaiTELEKELEELKTAEENVKDELKEL 880
Cdd:pfam00038 128 SL----KEELAFLKKNHEEEVRELQAQVSDtqvnvemdaarkldLTSALAEIRA--QYEEIAAKNREEAEEWYQSKLEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 881 REGRE-------QIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELKhfdpalvRSIKEIPLEVEK 953
Cdd:pfam00038 202 QQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQ-------ELISELEAELQE 274
|
250 260
....*....|....*....|.
gi 57159276 954 LRQDIEKMEEEIRSLEPVNMK 974
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLA 295
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1074-1146 |
1.19e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 1074 MSGGEKAIIALAFvFAIQRYKPApFYLLDEIDAHLDDANVKRVADLIKE-ASQNSQFIVITHRDVMMAQADRII 1146
Cdd:cd03238 88 LSGGELQRVKLAS-ELFSEPPGT-LFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWII 159
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
195-288 |
1.21e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 40.27 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 195 DLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKfieeggsREEEIEGQIKSLEDRLKEIAKEIVA 274
Cdd:pfam17675 8 DLLLEELDKQLEDAEKERDAYISFLKKLEKETPEELEELEKELEKLEK-------EEEELLQELEELEKEREELDAELEA 80
|
90
....*....|....
gi 57159276 275 KEKELAEIERQLEE 288
Cdd:pfam17675 81 LEEELEALDEEEEE 94
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
724-1134 |
1.27e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 724 LDSYlAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKAleNPEARElnskirevEAEISKLK 803
Cdd:COG0497 147 LDAF-AGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAA--ALQPGE--------EEELEEER 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 804 EELSRVESKLESLdSRINEELLPRKADLEEEIEGLVNKINALNAYIEEnknaitelekeleelktaeenvkdeLKELREG 883
Cdd:COG0497 216 RRLSNAEKLREAL-QEALEALSGGEGGALDLLGQALRALERLAEYDPS-------------------------LAELAER 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 884 REQIRVEIAELRkekDELTSKLQELRIEANtlkvRLAQVEttlqEKRAELKhfdpALVR----SIKEIPLEVEKLRQDIE 959
Cdd:COG0497 270 LESALIELEEAA---SELRRYLDSLEFDPE----RLEEVE----ERLALLR----RLARkygvTVEELLAYAEELRAELA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 960 KM---EEEIRSLEpvnmkaiEDFEVVERRYLE----LSSKReqvlaeKESIEEFIQEIEGQkrqvfLQTLNaiaknfsel 1032
Cdd:COG0497 335 ELensDERLEELE-------AELAEAEAELLEaaekLSAAR------KKAAKKLEKAVTAE-----LADLG--------- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1033 faklSPGGEAKLILENPEDPFSGGLE-IE----------AKPAGKdvkrieAMSGGEKAIIALAF--VFAiqRYKPAPFY 1099
Cdd:COG0497 388 ----MPNARFEVEVTPLEEPGPNGADqVEflfsanpgepPKPLAK------VASGGELSRIMLALkvVLA--DKDAVPTL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 57159276 1100 LLDEIDAhlddaNV-----KRVADLIKEASQNSQFIVITH 1134
Cdd:COG0497 456 IFDEVDT-----GVggrvaEAVGEKLARLARNHQVLCVTH 490
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
672-1001 |
1.28e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 672 RKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKR 751
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 752 IE-------ESKGEMAKLRGRIERLEK-----------------KREKIKKALENPEARELNSKIREVEA---EISKLKE 804
Cdd:pfam10174 403 IEnlqeqlrDKDKQLAGLKERVKSLQTdssntdtalttleealsEKERIIERLKEQREREDRERLEELESlkkENKDLKE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 805 ELSRVESKLESLDSRINeELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVK------DELK 878
Cdd:pfam10174 483 KVSALQPELTEKESSLI-DLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIR 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 879 ELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVettlqEKRAELKHFDPAL-VRSIKEIPLEVEK--LR 955
Cdd:pfam10174 562 LLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL-----ESLTLRQMKEQNKkVANIKHGQQEMKKkgAQ 636
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 57159276 956 QDIEKMEEEIRSLEPVNMKAIEDF-EVVERRYLELS------SKREQVLAEKE 1001
Cdd:pfam10174 637 LLEEARRREDNLADNSQQLQLEELmGALEKTRQELDatkarlSSTQQSLAEKD 689
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
234-521 |
1.38e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 234 LAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKeIVAKEKELAEIERQLEEKSGDGILEITRKISEVKSKIEVAKR 313
Cdd:COG5185 211 ETGNLGSESTLLEKAKEIINIEEALKGFQDPESELED-LAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 314 NIENAQKEIEESQARLRKSKEelkhvseeIEKSKGAIKRWGKRREqLLVQIKERETVRNELViklGEIDKRFSEAREEFD 393
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKA--------TESLEEQLAAAEAEQE-LEESKRETETGIQNLT---AEIEQGQESLTENLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 394 KVVAELEEAKKalymkeseiskfEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQvegkisKVESRHRKAE 473
Cdd:COG5185 358 AIKEEIENIVG------------EVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILA------TLEDTLKAAD 419
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 57159276 474 KELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFLKSQRIE 521
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEE 467
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
186-407 |
1.46e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.53 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDL-----LIREVKAQLDKL----EKE---RNDALRYLD-LKEKLEKARVTL--LLAEIKRLEK---FIEEG 247
Cdd:pfam06160 248 ENLALLENLELdeaeeALEEIEERIDQLydllEKEvdaKKYVEKNLPeIEDYLEHAEEQNkeLKEELERVQQsytLNENE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 248 GSREEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLEeksgdgilEITRKISEvkskievakrnIENAQKEIEESQA 327
Cdd:pfam06160 328 LERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELE--------EILEQLEE-----------IEEEQEEFKESLQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 328 RLRKSKEELKHVSEEIEKSKGAIKRWGKRR------EQLLVQIKERETvrnelviKLGEIDKRFSEAREEFDKVVAELEE 401
Cdd:pfam06160 389 SLRKDELEAREKLDEFKLELREIKRLVEKSnlpglpESYLDYFFDVSD-------EIEDLADELNEVPLNMDEVNRLLDE 461
|
....*.
gi 57159276 402 AKKALY 407
Cdd:pfam06160 462 AQDDVD 467
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
733-834 |
1.49e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 733 SLKEEIEENERLISELEKRIEE--------SKGEMAKLRGRIERLEKKREKIKKALEnpEARELNSKIREVEAEISKLKE 804
Cdd:COG0542 408 SKPEELDELERRLEQLEIEKEAlkkeqdeaSFERLAELRDELAELEEELEALKARWE--AEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|
gi 57159276 805 ELSRVESKLESLDSRINEELLPRKADLEEE 834
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREEVTEE 515
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1069-1134 |
1.57e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 1069 KRIEAMSGGEKAIIALAFVFAiqryKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITH 1134
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALL----RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
658-829 |
1.60e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 658 YKPRGKLGVNVDEIRKRVEALEGRkeaLEAQVNALKVEvKGLENELFELRmKKSELSKDVQVIQKELDSYLAEDRSLKEE 737
Cdd:COG1340 101 LAELNKAGGSIDKLRKEIERLEWR---QQTEVLSPEEE-KELVEKIKELE-KELEKAKKALEKNEKLKELRAELKELRKE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 738 IEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALEN--PEARELNSKIREVEAEISKLKEELSRVESKLES 815
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEaqEKADELHEEIIELQKELRELRKELKKLRKKQRA 255
|
170
....*....|....
gi 57159276 816 LDSRINEELLPRKA 829
Cdd:COG1340 256 LKREKEKEELEEKA 269
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-391 |
1.63e-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: 42.06 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 170 IAEYDAKKEKALKELKQTEENLARVDLLIREVKAQLDKLEKERNDAlryldlkekleKARVTLLLAEIKRLEKFIEEggs 249
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-----------EAELAELEKEIAELRAELEA--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 250 REEEIEGQIKSLEDRLKEIAKEIVAKEKELAEIERQLE--EKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQA 327
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 328 RLRKSKEELkhvSEEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREE 391
Cdd:COG4942 182 ELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
733-968 |
1.64e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 733 SLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKrekIKKALENPEARELNSKIREVEAEI-SKLKEELSRVES 811
Cdd:pfam05667 325 TEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESS---IKQVEEELEELKEQNEELEKQYKVkKKTLDLLPDAEE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 812 KLESLDSRInEELLPRKADLEEEIEG----LVNKINALNAYIEENKNAItelekeleelktaeENVKDELKELREgreQI 887
Cdd:pfam05667 402 NIAKLQALV-DASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDES--------------QRKLEEIKELRE---KI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 888 RVEIAELRKeKDELTSKLQELRIEANTLKVRLAQVETTLQekraelkhfdpaLVRSIKEIPLEVEKLRQDIEKMEEEIRS 967
Cdd:pfam05667 464 KEVAEEAKQ-KEELYKQLVAEYERLPKDVSRSAYTRRILE------------IVKNIKKQKEEITKILSDTKSLQKEINS 530
|
.
gi 57159276 968 L 968
Cdd:pfam05667 531 L 531
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-87 |
1.76e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.10 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1 MMPyiEKIEMKGFKSYGNKKVV--VPL-ARGFTAIVGANGSGKSNIGDAVLFVLGGlsaKAMRASRISDLIFAGSKGEpp 77
Cdd:cd03279 1 MKP--LKLELKNFGPFREEQVIdfTGLdNNGLFLICGPTGAGKSTILDAITYALYG---KTPRYGRQENLRSVFAPGE-- 73
|
90
....*....|
gi 57159276 78 aKYAEVAMYF 87
Cdd:cd03279 74 -DTAEVSFTF 82
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
670-794 |
1.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 670 EIRKRVEALEGRKEALE--AQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISE 747
Cdd:COG1340 148 ELEKAKKALEKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 57159276 748 LEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKIRE 794
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
795-926 |
1.99e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 795 VEAEISKLKEELSRVESKLESLDSRINEellPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELeelktaeENVK 874
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI-------ERLE 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 57159276 875 DELKELR-EGREQIRV--EIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTL 926
Cdd:COG2433 448 RELSEARsEERREIRKdrEISRLDREIERLERELEEERERIEELKRKLERLKELW 502
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
710-933 |
2.02e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 710 KSELSKDVQVIQKELDSYLAEDRSLKE-------EIEENERLISELEKRIEESKGEMAKLRGRIERLE----KKRE---- 774
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEkvsalqpELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEiaveQKKEecsk 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 775 ---KIKKALENPEAR----ELNSKIREVEAEISKLKEELSRVESKLESLdSRINEELLPRKADLEEEIEGLvnKINALNA 847
Cdd:pfam10174 536 lenQLKKAHNAEEAVrtnpEINDRIRLLEQEVARYKEESGKAQAEVERL-LGILREVENEKNDKDKKIAEL--ESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 848 YIEENKNAITELEKEleelktaEENVKDELKELREGREQIRVEIAELRKEK-DELTSKLQELRIEANTLKVRLAQVETTL 926
Cdd:pfam10174 613 MKEQNKKVANIKHGQ-------QEMKKKGAQLLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLSSTQQSL 685
|
....*..
gi 57159276 927 QEKRAEL 933
Cdd:pfam10174 686 AEKDGHL 692
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
721-906 |
2.02e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 721 QKELDSYLaedRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKrekIKKALENPEARELNSKireveAEIS 800
Cdd:pfam05010 3 QKDMDAAL---EKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKT---IAQMIEEKQKQKELEH-----AEIQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 801 KLKEELSRVESKLESLDSRINEeLLPRKADLEEEIEGLVNKINALNAYIEENKNAITElekeleelktaEENVKDELKEL 880
Cdd:pfam05010 72 KVLEEKDQALADLNSVEKSFSD-LFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKK-----------EEQRYQALKAH 139
|
170 180
....*....|....*....|....*..
gi 57159276 881 REGR-EQIRVEIAELRKEKDELTSKLQ 906
Cdd:pfam05010 140 AEEKlDQANEEIAQVRSKAKAETAALQ 166
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
716-900 |
2.03e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.89 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 716 DVQVIQKELDSYLAEDRSLKEEIEE----NERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALEnpEARELNSK 791
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEERVEAlnelGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLE--EALDLQQF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 792 IREVEAEISKLKEELSRVESKLESLDSRINEELLPRKADLEEEIEGLVNKINALNAYIEEnknaiteleKELEELKTAEE 871
Cdd:cd00176 112 FRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEE---------LLEEGHPDADE 182
|
170 180
....*....|....*....|....*....
gi 57159276 872 NVKDELKELREGREQIRVEIAELRKEKDE 900
Cdd:cd00176 183 EIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1056-1135 |
2.03e-03 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 42.35 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1056 GLE--IEAKPAGKDVKRIE---AMSGGEKAIIALAFVFAiqryKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFI 1130
Cdd:TIGR02868 449 GLAdwLRALPDGLDTVLGEggaRLSGGERQRLALARALL----ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
....*
gi 57159276 1131 VITHR 1135
Cdd:TIGR02868 525 LITHH 529
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
694-905 |
2.23e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 694 VEVKGLENELFElRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESK------GEMAKLR---- 763
Cdd:PRK05771 66 LPKLNPLREEKK-KVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLgfky 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 764 -----GRIErlEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEelLPRKADLEEEIEGL 838
Cdd:PRK05771 145 vsvfvGTVP--EDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLE--LEEEGTPSELIREI 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 839 VNKINALNAYIEEnknaitelekeleelktaeenVKDELKELREGREQIRVEIAEL---RKEKDELTSKL 905
Cdd:PRK05771 221 KEELEEIEKERES---------------------LLEELKELAKKYLEELLALYEYleiELERAEALSKF 269
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
357-499 |
2.24e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.67 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 357 REQLLVQIKERETVRNELVIKLgeidkrfsEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNL 436
Cdd:pfam10186 25 RVDLARLLSEKDSLKKKVEEAL--------EGKEEGEQLEDNIGNKKLKLRLLKSEVAISNERLNEIKDKLDQLRREIAE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 437 LKEKIAEAKASLEAKRSELSQVEGKISKVESRH-RKAEKELEEKTRELQKVESELAKAREELIK 499
Cdd:pfam10186 97 KKKKIEKLRSSLKQRRSDLESASYQLEERRASQlAKLQNSIKRIKQKWTALHSKTAESRSFLCR 160
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
205-517 |
2.25e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 205 LDKLEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLEDRLKEIAKEIvAKEKELAEIER 284
Cdd:COG5185 238 FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSI-DIKKATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 285 QLeeKSGDGILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKH---VSEEIEKSKGAIKRWGKRREQLL 361
Cdd:COG5185 317 QL--AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGeveLSKSSEELDSFKDTIESTKESLD 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 362 VQIKERETVRNELVIKL----GEIDKRFSEAREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARR--N 435
Cdd:COG5185 395 EIPQNQRGYAQEILATLedtlKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEinR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 436 LLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVRGNRAVEFL 515
Cdd:COG5185 475 SVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
..
gi 57159276 516 KS 517
Cdd:COG5185 555 NA 556
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
27-51 |
2.27e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 2.27e-03
10 20
....*....|....*....|....*
gi 57159276 27 RGFTAIVGANGSGKSNIGDAVLFVL 51
Cdd:pfam13555 22 RGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1075-1146 |
2.30e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.10 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1075 SGGEKAIIALAFVFaiqRYKPApFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:COG4178 487 SLGEQQRLAFARLL---LHKPD-WLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
670-957 |
2.34e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 670 EIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERliselE 749
Cdd:pfam15905 77 ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGT-----Q 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 750 KRIEESKGEMAKLRGRIErlEKKREKIKKAlenpeaRELNSKIREVEAEISKLKEELSRVESKLESLDSRINEEllprKA 829
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLE--AKMKEVMAKQ------EGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE----KS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 830 DLEEeieglvnkinaLNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELR 909
Cdd:pfam15905 220 ETEK-----------LLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 57159276 910 IEANTLKVRLAQVETTLQEKRAELKHfdpaLVRSIKEiplEVEKLRQD 957
Cdd:pfam15905 289 SEKEELLREYEEKEQTLNAELEELKE----KLTLEEQ---EHQKLQQK 329
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1075-1146 |
2.37e-03 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 40.37 E-value: 2.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1075 SGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:cd03247 100 SGGERQRLALARIL----LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKIL 167
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1074-1146 |
2.59e-03 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 1074 MSGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:cd03253 138 LSGGEKQRVAIARAI----LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKII 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1075-1153 |
2.64e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 41.75 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1075 SGGEKAIIALAfvfaiqR--YKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRIigVSMRN 1152
Cdd:PRK11174 487 SVGQAQRLALA------RalLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI--WVMQD 558
|
.
gi 57159276 1153 G 1153
Cdd:PRK11174 559 G 559
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
668-802 |
2.68e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALegRKEA-LEAqvnalKVEVKGLENEL-FELRMKKSELSK-DVQVIQKEldsylaedRSLKEEIEENERL 744
Cdd:PRK12704 44 LEEAKKEAEAI--KKEAlLEA-----KEEIHKLRNEFeKELRERRNELQKlEKRLLQKE--------ENLDRKLELLEKR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 745 ISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALEN------PEARE--LNSKIREVEAEISKL 802
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEAKEilLEKVEEEARHEAAVL 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
713-1158 |
2.72e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 713 LSKD-VQVIQKELDSYLAEDRSLKEEIEENERLISELEKRieeSKGEMAKLRGRIERLEKKREKIKKALENPEAR--ELN 789
Cdd:PHA02562 171 LNKDkIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKK---NGENIARKQNKYDELVEEAKTIKAEIEELTDEllNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 790 SKIREVEAEISKLKEELSRVESKLESLDsriNEELLPRKADL----EEEIEGLVNKINAlnayIEENKNAITELEkelee 865
Cdd:PHA02562 248 MDIEDPSAALNKLNTAAAKIKSKIEQFQ---KVIKMYEKGGVcptcTQQISEGPDRITK----IKDKLKELQHSL----- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 866 lktaeenvkDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAElkhfdpalVRSIK 945
Cdd:PHA02562 316 ---------EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE--------FVDNA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 946 EiplEVEKLRQDIEK---------MEEEIRS-----LEPVNMKAiedfeVVERRYLELSSKReqvlaekesIEEFIQEIE 1011
Cdd:PHA02562 379 E---ELAKLQDELDKivktkselvKEKYHRGivtdlLKDSGIKA-----SIIKKYIPYFNKQ---------INHYLQIME 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1012 GQkrqvFLQTLNAiakNFSELFaklspggeaklilenpedpfsggleieaKPAGKDVKRIEAMSGGEKAIIALAFVFA-- 1089
Cdd:PHA02562 442 AD----YNFTLDE---EFNETI----------------------------KSRGREDFSYASFSQGEKARIDLALLFTwr 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57159276 1090 -IQRYKPA---PFYLLDEI-DAHLDDANVKRVADLIkEASQNSQFIVITHRDVMMAQADRIIGVSMRNGVSKVV 1158
Cdd:PHA02562 487 dVASKVSGvdtNLLILDEVfDGALDAEGTKALLSIL-DSLKDTNVFVISHKDHDPQKFDRHLKMEKVGRFSVMV 559
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
695-854 |
2.84e-03 |
|
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: 41.97 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 695 EVKGLENELFELRMKKSELSKDVQVIQKELDSYLAeDRSLKEEIEENERLISElekrIEESKGEMAKLRGRIERLEKKRE 774
Cdd:pfam05911 638 KVTLSENKVAQVDNGCSEIDNLSSDPEIPSDGPLV-SGSNDLKTEENKRLKEE----FEQLKSEKENLEVELASCTENLE 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 775 KIKKALEnpearELNSKIREVEAEISKLKEELSRVESKLESLdSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKN 854
Cdd:pfam05911 713 STKSQLQ-----ESEQLIAELRSELASLKESNSLAETQLKCM-AESYEDLETRLTELEAELNELRQKFEALEVELEEEKN 786
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1000-1146 |
3.02e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.89 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1000 KESIEEFIQEIE-GQKRQVFLQTLNAIAKNFSELFAKLSpggeakLILENPEDPFSG---------GLEIEAKP------ 1063
Cdd:PRK13648 48 KSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLRKHIG------IVFQNPDNQFVGsivkydvafGLENHAVPydemhr 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1064 ----AGKDVKRIE-------AMSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKE--ASQNSQFI 1130
Cdd:PRK13648 122 rvseALKQVDMLEradyepnALSGGQKQRVAIAGVLALN----PSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITII 197
|
170
....*....|....*.
gi 57159276 1131 VITHRDVMMAQADRII 1146
Cdd:PRK13648 198 SITHDLSEAMEADHVI 213
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
388-523 |
3.52e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 388 AREEFDKVVAELEEAKKALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQV--------- 458
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseerreir 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 459 -EGKISKVESRHRKAEKELEEKTRELQKVESELAKAReELIKAEAQREVRGNRAVEFLKSQRIEGL 523
Cdd:COG2433 463 kDREISRLDREIERLERELEEERERIEELKRKLERLK-ELWKLEHSGELVPVKVVEKFTKEAIRRL 527
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
187-506 |
3.53e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 187 TEENLARVDLLIREVKAQLDKLEKERNDALRYLDLKEKLEKARVtlllAEIKRLEKFIEeggSREEEIEgQIKSLEDRLK 266
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN----AEITKLRSRVD---LKLQELQ-HLKNEGDHLR 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 267 EIAKEIVAKEKELAEIERQLE--EKSGDGILEITRKISEVKSKIEVAKRNIEnaqKEIEESQARLRKSK----------E 334
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEilRQQIENMTQLVGQHGRTAGAMQVEKAQLE---KEINDRRLELQEFKilkdkkdakiR 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 335 ELKHVSEEIEKSKGAIKRWGKRREQLLVQIK-ERETVRNELviklgeidkrfSEAREEFDKVVAELEEAKKALYMKESEI 413
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKqERDQLLNEV-----------KTSRNELNSLSEDYEVLKRNFRNKSEEM 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 414 ----SKFEEEISRAKARITQfnaRRNLLKE---------KIAEA-KASLEAKRSELSQVEGKISKVESRHRKAEKELEEK 479
Cdd:pfam15921 691 etttNKLKMQLKSAQSELEQ---TRNTLKSmegsdghamKVAMGmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFL 767
|
330 340
....*....|....*....|....*..
gi 57159276 480 TRELQKVESELAKAREELIKAEAQREV 506
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKMAGELEV 794
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
668-763 |
3.69e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEALEAQVNALKVE-VKGLENELFELRMKKSELSKDVQViQKELdsyLAEDRSLKEEIEENERLIS 746
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEA-EKEL---IEEIQELKEELEQRYGKIP 488
|
90
....*....|....*..
gi 57159276 747 ELEKRIEESKGEMAKLR 763
Cdd:COG0542 489 ELEKELAELEEELAELA 505
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1075-1146 |
3.74e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 41.30 E-value: 3.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57159276 1075 SGGEKAIIALAFVFaiqrYKPAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRDVMMAQADRII 1146
Cdd:COG1132 478 SGGQRQRIAIARAL----LKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRIL 545
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
670-1032 |
3.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 670 EIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELE 749
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 750 KRIEESKGEMAKLRGRIERLEKKREKIKKALEnpearELNSKIREVEAEISKLKEELSRVESKLESLDSRINEellprka 829
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELE-----ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 830 dLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELR 909
Cdd:COG4372 155 -LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 910 IEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIEDFEVVERRYLEL 989
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 57159276 990 SSKREQVLAEKESIEEFIQEIEGQKRQVFLQTLNAIAKNFSEL 1032
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVL 356
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
682-928 |
4.06e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 682 KEALEAQVNALKvevkglenelfelrmKKSELSKDVQVIQKELDSYLAedrsLKEEIEENERLISELEKRIEESKGEMAK 761
Cdd:PRK11281 38 EADVQAQLDALN---------------KQKLLEAEDKLVQQDLEQTLA----LLDKIDRQKEETEQLKQQLAQAPAKLRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 762 LRGRIERLEKKR-EKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSR-----------------INEE 823
Cdd:PRK11281 99 AQAELEALKDDNdEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaqaalyansqrlqqIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 824 LLPRKADLEEEIEGLVNKINA----LNAYIEENKnaitelekeleelktaeenvkdelKELrEGREQIrveIAELRKEKD 899
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAeqalLNAQNDLQR------------------------KSL-EGNTQL---QDLLQKQRD 230
|
250 260 270
....*....|....*....|....*....|....
gi 57159276 900 ELTSKLQELRIEANTLKV-----RLAQVETTLQE 928
Cdd:PRK11281 231 YLTARIQRLEHQLQLLQEainskRLTLSEKTVQE 264
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
711-824 |
4.13e-03 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 41.25 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 711 SELSKD-VQVIQKELDSYLAEDRSLKEEIE---ENERLISELEKRIEESKGEMAKlrGRIERLEKKREKIKKALEN---P 783
Cdd:CHL00094 500 STLPKDeVERMVKEAEKNAAEDKEKREKIDlknQAESLCYQAEKQLKELKDKISE--EKKEKIENLIKKLRQALQNdnyE 577
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 57159276 784 EARELNSKIREVEAEISKLKEELSRVESKLESLDSRINEEL 824
Cdd:CHL00094 578 SIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDDVIDTDF 618
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
732-969 |
4.24e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 732 RSLKEEIEENERLISELEkrIEESKGEMAKLRGRIERL----EKKREKIKKALENpeARELNSKIREVEAEISKLKEELS 807
Cdd:PRK04778 259 QDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLydilEREVKARKYVEKN--SDTLPDFLEHAKEQNKELKEEID 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 808 RVeskleSLDSRINEELLPRKADLEEEIEGLVNKINALNAYIEENKNAITELEKELeelktaeENVKDELKELREGREQI 887
Cdd:PRK04778 335 RV-----KQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEEL-------EEILKQLEEIEKEQEKL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 888 RVEIAELRKEKDELTSKLQELRIEANTLKVRL---------AQVETTLQEKRAELKHfdpaLVRSIKEIPLEVEKLRQDI 958
Cdd:PRK04778 403 SEMLQGLRKDELEAREKLERYRNKLHEIKRYLeksnlpglpEDYLEMFFEVSDEIEA----LAEELEEKPINMEAVNRLL 478
|
250
....*....|.
gi 57159276 959 EKMEEEIRSLE 969
Cdd:PRK04778 479 EEATEDVETLE 489
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
869-934 |
4.38e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 40.38 E-value: 4.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 869 AEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVETTLQEKRAELK 934
Cdd:pfam14932 68 DVEALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLE 133
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
197-288 |
4.64e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.82 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 197 LIRE----VKAQLDK-LEKERNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKsledRLKEIAKE 271
Cdd:PRK05431 6 LIREnpeaVKEALAKrGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIA----EVKELKEE 81
|
90
....*....|....*..
gi 57159276 272 IVAKEKELAEIERQLEE 288
Cdd:PRK05431 82 IKALEAELDELEAELEE 98
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1072-1175 |
4.67e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 39.82 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1072 EAMSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKE-ASQNSQFIVITHRDVMMA--QADRIigV 1148
Cdd:cd03217 103 EGFSGGEKKRNEILQLLLLE----PDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDyiKPDRV--H 176
|
90 100
....*....|....*....|....*..
gi 57159276 1149 SMRNGvsKVVslsLEKARKILEEIRKK 1175
Cdd:cd03217 177 VLYDG--RIV---KSGDKELALEIEKK 198
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
257-505 |
4.84e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 257 QIKSLEDRLKEIAKEIVAKEKELAEIErqlEEKSGDgileiTRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEEL 336
Cdd:pfam10174 346 EVDALRLRLEEKESFLNKKTKQLQDLT---EEKSTL-----AGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 337 KHVSEEIEkskgAIKRWGKRREQLLVQIKERETVRNELVIKLGE-IDKRFSEAREEFDKVVAELEEAKKALYMKESEISK 415
Cdd:pfam10174 418 AGLKERVK----SLQTDSSNTDTALTTLEEALSEKERIIERLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 416 FEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRhRKAEKELEEKTRELQKVESELAKARE 495
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQEVARYKE 572
|
250
....*....|
gi 57159276 496 ELIKAEAQRE 505
Cdd:pfam10174 573 ESGKAQAEVE 582
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
186-329 |
4.85e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.17 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKErndalryldlkekLEKARVTlLLAEIKRLEkfiEEGGSREEEIEGQ---IKSLE 262
Cdd:pfam05667 398 DAEENIAKLQALVDASAQRLVELAGQ-------------WEKHRVP-LIEEYRALK---EAKSNKEDESQRKleeIKELR 460
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57159276 263 DRLKEIAKEIVAKEKELAEIERQLEEKSGDGI-LEITRKISEVKSKIEVAKRNIE-------NAQKEIEESQARL 329
Cdd:pfam05667 461 EKIKEVAEEAKQKEELYKQLVAEYERLPKDVSrSAYTRRILEIVKNIKKQKEEITkilsdtkSLQKEINSLTGKL 535
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
671-1037 |
4.86e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 671 IRKRVEALEGRKEALEAQ-VNALKVEVKGLE-----NELFELRMKKSELSKDVQVIQKELDSYLAED-------RSLKEE 737
Cdd:PRK04778 27 NYKRIDELEERKQELENLpVNDELEKVKKLNltgqsEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEElndkfrfRKAKHE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 738 IEENERLISELEKRIEESKGEMAKL-------RGRIERLEKKREKIKKALeNPEARELNSKIREVEAEISKLKEELSRVE 810
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELleseeknREEVEQLKDLYRELRKSL-LANRFSFGPALDELEKQLENLEEEFSQFV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 811 sklesldsRINEELLPRKAdlEEEIEGLVNKINALNAYIEENKNAITelekeleelkTAEENVKDELKELREGREQ---- 886
Cdd:PRK04778 186 --------ELTESGDYVEA--REILDQLEEELAALEQIMEEIPELLK----------ELQTELPDQLQELKAGYRElvee 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 887 --------IRVEIAELRKEKDELTSKLQELRIEAntLKVRLAQVETTLQ------EKRAELKHF----DPALVRSIKEIP 948
Cdd:PRK04778 246 gyhldhldIEKEIQDLKEQIDENLALLEELDLDE--AEEKNEEIQERIDqlydilEREVKARKYveknSDTLPDFLEHAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 949 LEVEKLRQDIE-----------------KMEEEIRSLEPVNMKAIEDFEVVERRYLELSSKREQVLAE------------ 999
Cdd:PRK04778 324 EQNKELKEEIDrvkqsytlneselesvrQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQleeiekeqekls 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 57159276 1000 -------------KESIEEFIQEIEGQKRQVFLQTLNAIAKNFSELFAKLS 1037
Cdd:PRK04778 404 emlqglrkdeleaREKLERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVS 454
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1073-1145 |
4.91e-03 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 39.86 E-value: 4.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57159276 1073 AMSGGEKAIIALAFVFAIQrykPApFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVITHRdvmMAQADRI 1145
Cdd:cd03260 141 GLSGGQQQRLCLARALANE---PE-VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHN---MQQAARV 206
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
197-1023 |
5.00e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 197 LIREVKAQLD-------KLEKERNDAL-RYLDLKEklEKARVTLLLAEIKRLEKFIEEggsREEEIEGQIKsledrLKEI 268
Cdd:TIGR01612 559 LIHEIKKELEeenedsiHLEKEIKDLFdKYLEIDD--EIIYINKLKLELKEKIKNISD---KNEYIKKAID-----LKKI 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 269 AKEIVAKEKELAEIE-RQLEE--KSGDGILeitrkiSEVKSKI-EVAKRNIENAQKE----IEESQARLRKSKEELKHVS 340
Cdd:TIGR01612 629 IENNNAYIDELAKISpYQVPEhlKNKDKIY------STIKSELsKIYEDDIDALYNElssiVKENAIDNTEDKAKLDDLK 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 341 EEIEKSKGAIKRwgKRREQLLVQIKERETVRNELVIKLGEIDKR-FSEAREEFDKVVAELEEAKKALYMKESEISKFEEE 419
Cdd:TIGR01612 703 SKIDKEYDKIQN--METATVELHLSNIENKKNELLDIIVEIKKHiHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDE 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 420 ISRAKARIT----QFNARRNLLKEKIAEAKASLEAKRS---ELSQVEGKISKVESRHRKAEKELEEKTREL--------Q 484
Cdd:TIGR01612 781 LNKYKSKISeiknHYNDQINIDNIKDEDAKQNYDKSKEyikTISIKEDEIFKIINEMKFMKDDFLNKVDKFinfennckE 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 485 KVESELAKARE--ELIKAEAQREVRGNRAVEFLKSQRIeglygtLGELISVPKSEYALAVEVALGGNYDNVVVEDDRVAE 562
Cdd:TIGR01612 861 KIDSEHEQFAEltNKIKAEISDDKLNDYEKKFNDSKSL------INEINKSIEEEYQNINTLKKVDEYIKICENTKESIE 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 563 KAIKllKEKKLGRLTFLPLNKIKPRSMREKpklgipamdvvSYDPRFRNavayalgdTLI--VNDMDEA-REVGIGKVRm 639
Cdd:TIGR01612 935 KFHN--KQNILKEILNKNIDTIKESNLIEK-----------SYKDKFDN--------TLIdkINELDKAfKDASLNDYE- 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 640 vTLGGELLERSGAITGGHYKPRGK-LGVNVDEIRKRVEALEGRKEALEAQVNALKVEV--------KGLENELFE-LRMK 709
Cdd:TIGR01612 993 -AKNNELIKYFNDLKANLGKNKENmLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIhtsiyniiDEIEKEIGKnIELL 1071
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 710 KSELSKDVQV-------IQKELDSYLAED--------------------RSLKEEIEENERLISELEKRIEESKGEMakl 762
Cdd:TIGR01612 1072 NKEILEEAEInitnfneIKEKLKHYNFDDfgkeenikyadeinkikddiKNLDQKIDHHIKALEEIKKKSENYIDEI--- 1148
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 763 RGRIERLEKKREkikKALENPEARELNSKI----------REVEAEISKLKEELSRVESKLESLDSRINEELLPRKA--- 829
Cdd:TIGR01612 1149 KAQINDLEDVAD---KAISNDDPEEIEKKIenivtkidkkKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNlgk 1225
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 830 ----DLEEEIEGLVNKINALNAYIEENKNaITELEKELEELKTAEENVKDELKELREGREQIRvEIAELRKEKDELTSKL 905
Cdd:TIGR01612 1226 lfleKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK-DHHIISKKHDENISDI 1303
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 906 QELR---IEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIP-----LEVEKLRQDIEKMEEEIRSLEPVN----- 972
Cdd:TIGR01612 1304 REKSlkiIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYTKEIEENNknikd 1383
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 973 --------MKAIEDFEVVErrylELSSKREQVLAEKEsIEEFIQEIEGQKRQVFLQTLN 1023
Cdd:TIGR01612 1384 eldkseklIKKIKDDINLE----ECKSKIESTLDDKD-IDECIKKIKELKNHILSEESN 1437
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1064-1146 |
5.03e-03 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 39.78 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1064 AGKDVKRIEAMSGGEKAIIALAFVFAIQRykpaPFYLLDEIDAHLDDANVKRVADLIKEASQNSQFIVI--THR-DVMMA 1140
Cdd:cd03298 119 AGLEKRLPGELSGGERQRVALARVLVRDK----PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLmvTHQpEDAKR 194
|
....*.
gi 57159276 1141 QADRII 1146
Cdd:cd03298 195 LAQRVV 200
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
707-928 |
5.04e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.98 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 707 RMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKRE-KIKKALENPEA 785
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEaAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 786 RELNSKIREVEAEISKLKEELSRVESKLESLDSRINEellprkadLEEEIEGLVNKINALNAYIEENKNAITELEKELEE 865
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPER--------AQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRW 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57159276 866 LKTAEENV-KDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLK-----VRLAQVETTLQE 928
Cdd:pfam12795 153 ALQAELAAlKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQellneKRLQEAEQAVAQ 221
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
198-307 |
5.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 198 IREVKAQLDKLEKERNDALRyldLKEKLEKARVTLLLAEIKRLEKFIEEGGSR---EEEIEGQIKSLEDRLKEIAKEIVA 274
Cdd:COG0542 413 LDELERRLEQLEIEKEALKK---EQDEASFERLAELRDELAELEEELEALKARweaEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110
....*....|....*....|....*....|....
gi 57159276 275 KEKELAEIERQLEEKSGDGILEITRK-ISEVKSK 307
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEVTEEdIAEVVSR 523
|
|
| DUF5082 |
pfam16888 |
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized. |
745-849 |
5.45e-03 |
|
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized.
Pssm-ID: 407125 [Multi-domain] Cd Length: 122 Bit Score: 38.05 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 745 ISELEKRIEESKGEMAKLRGRIERLEKKREKI----------KKALENPEA--RELNSKIREVEAEI-SKLKEELSRVES 811
Cdd:pfam16888 5 ISRLQAQIAQLRSEIAALEEKIERLKEAKTKLdaekeslhdkKTKLQGPLNssESWNGSNENNYDGIrSNLETSYQNYVD 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 57159276 812 KLESLDSRINEELlprkADLEEEIEGLVNKINALNAYI 849
Cdd:pfam16888 85 ELDELIDAIEEEI----TRLENQINEAQGVIDTLQSQL 118
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
874-1010 |
5.54e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 874 KDELKELREGREQIRVEIAELRKEKDELTSKLQELRIEANTLKVRLAQVE---TTLQEKRAELKHfdpaLVRSIKEIPLE 950
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEkdkQSLKNLKARLKV----LEKELKDLKWE 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57159276 951 VEKLRQDIEKMEEEIRSLEPVNMKAIED-FEVVERRYLELSSKREQVLAEKESIEEFIQEI 1010
Cdd:pfam13851 108 HEVLEQRFEKVERERDELYDKFEAAIQDvQQKTGLKNLLLEKKLQALGETLEKKEAQLNEV 168
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
732-844 |
6.01e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 732 RSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEA-----RELNSKIREVEAEISKLKEEl 806
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKdkqslKNLKARLKVLEKELKDLKWE- 107
|
90 100 110
....*....|....*....|....*....|....*...
gi 57159276 807 srvesklesldsriNEELLPRKADLEEEIEGLVNKINA 844
Cdd:pfam13851 108 --------------HEVLEQRFEKVERERDELYDKFEA 131
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
723-842 |
6.24e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 723 ELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEmaklrgRIERLEKKREKIKKALENpeARELNSKIREVEAEISKL 802
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQ------QQEEAESSREQLQELEEQ--LATERSARREAEAELERL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 57159276 803 KEELSRVESKLesldSRINEELLPRKADLEEEIEGLVNKI 842
Cdd:pfam09787 120 QEELRYLEEEL----RRSKATLQSRIKDREAEIEKLRNQL 155
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
441-532 |
6.52e-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: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 441 IAEAKASLEAKRSELSQVEGKISKVESRHRKAEKELEEKTRELQKVESELAKAREELIKAEAQREVrgnraveflKSQRI 520
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------AEAEI 81
|
90
....*....|..
gi 57159276 521 EGLYGTLGELIS 532
Cdd:COG3883 82 EERREELGERAR 93
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1069-1153 |
6.59e-03 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 39.40 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1069 KRIEAMSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKEASQNSQ--FIVITHRDVMMAQADRII 1146
Cdd:cd03255 136 HYPSELSGGQQQRVAIARALAND----PKIILADEPTGNLDSETGKEVMELLRELNKEAGttIVVVTHDPELAEYADRII 211
|
....*..
gi 57159276 1147 gvSMRNG 1153
Cdd:cd03255 212 --ELRDG 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1074-1168 |
6.90e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.69 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 1074 MSGGEKAIIALAFVFAIQrykpAPFYLLDEIDAHLDDANVKRVADLIKEASQNS--QFIVITHRDVMMAQADRII----G 1147
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMR----PECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIvmdsG 220
|
90 100
....*....|....*....|.
gi 57159276 1148 VSMRNGVSKVVSLSLEKARKI 1168
Cdd:PRK13633 221 KVVMEGTPKEIFKEVEMMKKI 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
668-978 |
7.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 668 VDEIRKRVEALEGRKEALEAQVNALKVEVKGLENELFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISE 747
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 748 LEKRIEESKGEMAKLRGRIERLEKKREKIKKALENPEARELNSKIREVEAEISKLKEELSRVESKLESLDSRIneellpR 827
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE------K 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 828 KADLEEEIEGLVNKINALNAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAELRKEKDELTSKLQE 907
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57159276 908 LRIEANTLKVRLAQVETTLQEKRAELKHFDPALVRSIKEIPLEVEKLRQDIEKMEEEIRSLEPVNMKAIED 978
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
250-503 |
7.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 250 REEEIEGQIKSLEDRLKEiAKEIVAKEKE-LAEIERQLEEkSGDGILEITRKISEVKSKIEVA-KRNIE--NAQKEIEES 325
Cdd:PRK04863 349 KIERYQADLEELEERLEE-QNEVVEEADEqQEENEARAEA-AEEEVDELKSQLADYQQALDVQqTRAIQyqQAVQALERA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 326 QARLRKSKEELKHVSEEIEKSKGAIKRWGKRREQLLVQ------IKERETVRNELVIKL-GEIDKrfSEAREEFDKVVAE 398
Cdd:PRK04863 427 KQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvaqaAHSQFEQAYQLVRKIaGEVSR--SEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 399 LEEAK------KALYMKESEISKFEEEISRAKARITQFNAR--RNLLKEKIAEAKAS-LEAKRSELSQVEGKISKVESRH 469
Cdd:PRK04863 505 LREQRhlaeqlQQLRMRLSELEQRLRQQQRAERLLAEFCKRlgKNLDDEDELEQLQEeLEARLESLSESVSEARERRMAL 584
|
250 260 270
....*....|....*....|....*....|....
gi 57159276 470 RKAEKELEEKTRELQKVESELAKAREELIKAEAQ 503
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALARLREQ 618
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
718-897 |
8.11e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.43 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 718 QVIQKELDSYLaeDRSLKEEIEENERLISELEKRIEESK---GEMAKLRGRIERLEKKREKIKKALENPEA------REL 788
Cdd:pfam13166 267 AERKAALEAHF--DDEFTEFQNRLQKLIEKVESAISSLLaqlPAVSDLASLLSAFELDVEDIESEAEVLNSqldglrRAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 789 NSKIREV--EAEISKLKEELSRVESKLESLDSRI---NEellpRKADLEEEIEGLVNKINAlnAYIEENKNAITELEKEL 863
Cdd:pfam13166 345 EAKRKDPfkSIELDSVDAKIESINDLVASINELIakhNE----ITDNFEEEKNKAKKKLRL--HLVEEFKSEIDEYKDKY 418
|
170 180 190
....*....|....*....|....*....|....
gi 57159276 864 EELKTAEENVKDELKELREGREQIRVEIAELRKE 897
Cdd:pfam13166 419 AGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQ 452
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
325-507 |
8.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 325 SQARLRKSKEELKHVSEEIEKSKGAIKRwgkrreQLLVQIKEretvrnelviklgEIDKRFSEAREEFDKVVAELEEAKK 404
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKK------EALLEAKE-------------EIHKLRNEFEKELRERRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 405 ALYMKESEISKFEEEISRAKARITQFNARRNLLKEKIAEAKASLEAKRSELSQVEGKISKVESRHRKAE--KELEEKTRE 482
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIllEKVEEEARH 169
|
170 180
....*....|....*....|....*
gi 57159276 483 LQkveSELAKAREELIKAEAQREVR 507
Cdd:PRK12704 170 EA---AVLIKEIEEEAKEEADKKAK 191
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
703-842 |
8.83e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 703 LFELRMKKSELSKDVQVIQKELDSYLAEDRSLKEEIEENERLISELEKRI--EESKGEMAKLRGRIERLEKKREKIKKAL 780
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRerEELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57159276 781 ENPEARE--LNSKIREVEAEISKLKEELSRVESKLEsldSRINEELLPR-KADLEEEIEGLVNKI 842
Cdd:PRK12705 105 NQLEEREkaLSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLlDAELEEEKAQRVKKI 166
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
690-1014 |
9.09e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 690 NALKVEVKGLENELFELRMkkSELSKDvqvIQKELDSYLAEDRSLKEEIEENERLISELEKRIEESKGEMAKLRGRIERL 769
Cdd:PTZ00440 936 NNLNKEKEKIEKQLSDTKI--NNLKMQ---IEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNIL 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 770 EKKREKIKKALENPEA----RELNSKIREVEAEISKLKEELSRVESKLESLDSRINEELLpRKADLEEEIEGLVNKINAL 845
Cdd:PTZ00440 1011 NKKIDDLIKKQHDDIIelidKLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKY-KNPKIKEEIKLLEEKVEAL 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 846 NAYIEENKNAITELEKELEELKTAEENVKDELKELREGREQIRVEIAE-LRKEKDELTSKLQELRIEANTLKVRlaqvet 924
Cdd:PTZ00440 1090 LKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKqMEKTLKELENMNLEDITLNEVNEIE------ 1163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 925 tLQEKRAELKHfdpaLVRSIKEiplEVEKLRQDIEKMEEEIRSLEPVnMKAIEDFEVVERRYLELSSKREQVLAEKESIE 1004
Cdd:PTZ00440 1164 -IEYERILIDH----IVEQINN---EAKKSKTIMEEIESYKKDIDQV-KKNMSKERNDHLTTFEYNAYYDKATASYENIE 1234
|
330
....*....|
gi 57159276 1005 EFIQEIEGQK 1014
Cdd:PTZ00440 1235 ELTTEAKGLK 1244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
186-396 |
9.11e-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: 40.39 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 186 QTEENLARVDLLIREVKAQLDKLEKE---RNDALRYLDLKEKLEKARVTLLLAEIKRLEKFIEEGGSREEEIEGQIKSLE 262
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKElksKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 263 DRLKEIAKEIVAK--EKELAEIERQLEEKSGDgILEITRKISEVKSKIEVAKRNIENAQKEIEESQARLRKSKEELKHVS 340
Cdd:TIGR04523 545 DELNKDDFELKKEnlEKEIDEKNKEIEELKQT-QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 57159276 341 EEIEKSKGAIKRWGKRREQLLVQIKERETVRNELVIKLGEIDKRFSEAREEFDKVV 396
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDII 679
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
735-969 |
9.51e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 735 KEEIEENERLISELEKRIEESKGEMAKLRGRI--------------ERLEKKREKIKKALEN-PEArelnskirevEAEI 799
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIkqveeeleelkeqnEELEKQYKVKKKTLDLlPDA----------EENI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 800 SKLKEELSRVESKLESLDSRINEEllpRKADLEEeieglvnkinalnayIEENKNAITELEKELeelktaeENVKDELKE 879
Cdd:pfam05667 404 AKLQALVDASAQRLVELAGQWEKH---RVPLIEE---------------YRALKEAKSNKEDES-------QRKLEEIKE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57159276 880 LregREQIRVEIAELRKeKDELTSKLQelrieantlkvrlAQVETTLQEK-RaelkhfdPALVRSIKEIPLEVEKLRQDI 958
Cdd:pfam05667 459 L---REKIKEVAEEAKQ-KEELYKQLV-------------AEYERLPKDVsR-------SAYTRRILEIVKNIKKQKEEI 514
|
250
....*....|.
gi 57159276 959 EKMEEEIRSLE 969
Cdd:pfam05667 515 TKILSDTKSLQ 525
|
|
| |
