|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
27-1081 |
0e+00 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 741.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 27 IEALLKEIPEGDKPELQKLRDSYNQALQLVREGERYQQQTDRLRQFMDDYPNALKKLEQEKAALKGTSTESIPLLDGPDL 106
Cdd:PRK10929 28 ITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 107 EQALVDAqarrlelrrqreelantfNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQ------FTEEQGRQQ---NANRI 177
Cdd:PRK10929 108 EQEILQV------------------SSQLLEKSRQAQQEQDRAREISDSLSQLPQQQtearrqLNEIERRLQtlgTPNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 178 LAMVREQSLQR-------RIQMLELEQLSSGNRDTLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAIAESERL 250
Cdd:PRK10929 170 LAQAQLTALQAesaalkaLVDELELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 251 LDEVQTDSPLLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLEWLEVSRGFGENLRNRLSEL 330
Cdd:PRK10929 250 AEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGEALRAQVARL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 331 PTPYPLPQLEARIVQSRVDKYSYQE------DLDDIANNSYRNrlLTLEQglseeqLLLLDELLTTRARLLERLQAATDT 404
Cdd:PRK10929 330 PEMPKPQQLDTEMAQLRVQRLRYEDllnkqpQLRQIRQADGQP--LTAEQ------NRILDAQLRTQRELLNSLLSGGDT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 405 QIHEQTRLKVAYSRQNGQLEEIRALTEERLFWLPDLRPVGSGFPAALRETLEWLTLGATWTALPKALQQQGGASLTL-YG 483
Cdd:PRK10929 402 LILELTKLKVANSQLEDALKEVNEATHRYLFWVADVSPISLSYPLEIAQDLRRLLSLDTFSQLGKASVMMLTSKETLlPL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 484 ISTLVVLYLWLLSRRSLRDYLTRISPRIGNVTQDKYGYT----FNTLLLSLLTALPLPALLSLLSHAIDSPLASPIVVSL 559
Cdd:PRK10929 482 FGALLLVGFSISSRRHYHAFLERSSSRVGKVTQDHFSLTlrtvFWSILVASPLPVLWAALGYGLQNAWPYPLAVAIGDGV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 560 SAALrelmlPV-FILLLVGNLTLPKGLLVMHFNLPAEQVRRVWRQFRTLMLSLLPMLLLLYTSREF--REFSlyDTLGRL 636
Cdd:PRK10929 562 TATV-----PLlWVFMICATFARPNGLFIAHFGWPRERVARAMRYYLLSIGLIVPLIMALITFDNLndREFS--GTLGRL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 637 AFVYTCVLMSLFSWRLYRQDMPLLVSspRQEH-LTLANHLLWGLLITAPLLALAAAIMGYLFTAHTLLRQLEISVLAGLG 715
Cdd:PRK10929 635 CFILLCGALSLVTLSLKRAGIPLYLD--KEGSgDNIINHALWNLLIGAPLVAALASALGYLATAQALLARLETSVAIWFL 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 716 FVMAYFSVRRWMLLQRRRLAFERAKARRAEILAQRKEKErDEPQETPPSPEAEAAAVAEVDLDAISAQSLGLLRSVLMLG 795
Cdd:PRK10929 713 LLVVYHIIRRWMLIQRRRIAFDRAKQRRAEILAQRARGE-EEAHHSSSPEGAIEVEEPVIDLDAISAQSLRLVRSILTLI 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 796 YILTLMLLWSEINTAFSFLDSIEVWHVSSSLAGEDTLVPISLKDLVIAVFLVVLTLVTARNLPGLMELSVLQHLDLSPGT 875
Cdd:PRK10929 792 ALLSVIVLWSEIHSAFGFLENISLWDVTSTVQGVESLQPITLGSVLIAILVFIITTQLVRNLPALLELALLQHLDLTPGT 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 876 GFAITTISKYLVLVFGAFATFAMLGIDWSKLQWLVAALSVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTI 955
Cdd:PRK10929 872 GYAITTITKYLLMLIGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSV 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 956 SKIKTRATTIVDWDRREIIVPNKAFITEQFVNWSLSDAITRVKLYVRVRLDADVELVQGLLQEAIDECSLILDNPVPEAF 1035
Cdd:PRK10929 952 TKINTRATTISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVLDNPAPEVF 1031
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 372984579 1036 LVELTDSALVYEVRVYVNDMGHRMPMTHELHNLLLERLRRHDIRIP 1081
Cdd:PRK10929 1032 LVDLQQGIQIFELRIYAAEMGHRMPLRHEIHQLILAGFREHGIDMP 1077
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
23-1096 |
1.53e-143 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 460.15 E-value: 1.53e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 23 SVADIEALLKEIPEGDKPELQK--LRDSYNQALQLVREGERYQQQTDRLRQFMDDYPNALKKLEQEKAALKGTSTESIPL 100
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEAEDklVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 101 ----LDGPDLEQALVDAQARRLelrrqreelantfNLQE-LS--NS---GLHNQLDELrqqlrqtqqnldQLQFTEEQGR 170
Cdd:PRK11281 117 tlstLSLRQLESRLAQTLDQLQ-------------NAQNdLAeyNSqlvSLQTQPERA------------QAALYANSQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 171 QQNANRILAMVREQSLQRR---IQMLELEQ------------LSSGN---RDTLNKlRLEILQSRLTDLDQYIDALQNRQ 232
Cdd:PRK11281 172 LQQIRNLLKGGKVGGKALRpsqRVLLQAEQallnaqndlqrkSLEGNtqlQDLLQK-QRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 233 NELRRATTEAAIAESERLLDEVQ-TDSPLLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLE 311
Cdd:PRK11281 251 NSKRLTLSEKTVQEAQSQDEAARiQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 312 WLEVSRGFGENLRNRLSELPTPYPLPQLEARIVQSRVDKYSYQEDLDDIAN-NSYRNRLLTLEQGLSEEQLLLL-DELLT 389
Cdd:PRK11281 331 VLKGSLLLSRILYQQQQALPSADLIEGLADRIADLRLEQFEINQQRDALFQpDAYIDKLEAGHKSEVTDEVRDAlLQLLD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 390 TRARLLERLQAATDTQIHEQTRLKVaySRQngQL----EEIRALTEERLFWLPDLRPVG----SGFPAALRETLEWLTLG 461
Cdd:PRK11281 411 ERRELLDQLNKQLNNQLNLAINLQL--NQQ--QLlsvsDSLQSTLTQQIFWVNSNKPMDldwlKAFPQALKDQFKSLKIT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 462 ATWTALPKALQQqggasLTLYGISTLVVLYLWLLSRRSLRDYLTRISPRIGNVTQDKYGYTfntlllslltalplpalls 541
Cdd:PRK11281 487 VSFSNLWDGLFI-----ALLLFLPLLLIAGLIRWRKKWIKARLQKLAADIGTLKRDSQLHT------------------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 542 llshaidsPLASPIVVSLSaalrelmLPV-FILLLVGNLTL--------------------------------PKGLLVM 588
Cdd:PRK11281 543 --------PKAILITLLLA-------LPVtLIFLAVGLILLtdafnqsellwswslklalfwlvfatcyrvlrPNGVAER 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 589 HFNLPAEQVRRVWRQFRTLMLSLLPMLLLLYTSrEFREFSL-YDTLGRLAFVYTCVLMSLFSWrlyrqdmPLLVSSPRQE 667
Cdd:PRK11281 608 HFGMPKEQVSHFRRQIVRLSLALLPLLFWSVVA-ELSPLGLaDDVIGQAVIIIALALIAFLVW-------PLCRESWRDK 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 668 HLTLANHLLWGLLITAPLLALAAAIMGYLFTAHTLLRQLEISVLAGLGFVMAYFSVRRWMLLQRRRLAFERAKARRAeil 747
Cdd:PRK11281 680 ESHTLRLVVRTVLTIAPIALIVLVVLGYYYTALRLIGRLIETLYLLIIWNLLYQTVLRGLSVAARRLAYRRALAKRQ--- 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 748 AQRKEK-ERDEPQETPPspeaeaaavaeVDLDAISAQSLGLLRSVLMLGYILTLMLLWSEINTAFSFLDSIEVWHVSSSL 826
Cdd:PRK11281 757 NLVKEGaEGAEPVEEPT-----------LALEQVNQQSLRLTDLLLFALFFVMFYWVWSDLITVFSYLDSITLWHYTTTT 825
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 827 AGEDTLVPISLKDLVIAVFLVVLTLVTARNLPGLMELSVLQHLDLSPGTGFAITTISKYLVLVFGAFATFAMLGIDWSKL 906
Cdd:PRK11281 826 AGGAVVESITLGNLLFALIILVVTYVLVRNLPGLLEVLVLSRLNLRQGTSYAITTLLTYIIIAVGAVTAFSTLGVSWDKL 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 907 QWLVAALSVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTISKIKTRATTIVDWDRREIIVPNKAFITEQFV 986
Cdd:PRK11281 906 QWLVAALSVGLGFGLQEIFANFVSGLIILFERPVRIGDTVTIGTFSGTVSKIRIRATTITDFDRKEVIVPNKAFVTERLI 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 987 NWSLSDAITRVKLYVRVRLDADVELVQGLLQEAIDECSLILDNPVPEAFLVELTDSALVYEVRVYVNDMGHRMPMTHELH 1066
Cdd:PRK11281 986 NWSLSDTVTRVVIKVGVAYGSDLEKVRELLLQAATENPRVMKEPEPQVFFLNFGASTLDHELRLYVRELGDRSPTVDELN 1065
|
1130 1140 1150
....*....|....*....|....*....|
gi 372984579 1067 NLLLERLRRHDIRIPHQQVDIRLvgeHNAA 1096
Cdd:PRK11281 1066 RRIDRLFRENDINIAFNQLDVFL---KNQK 1092
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis]; |
833-1096 |
8.67e-100 |
|
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442495 [Multi-domain] Cd Length: 281 Bit Score: 316.76 E-value: 8.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 833 VPISLKDLVIAVFLVVLTLVTARNLPGLMELSVLQHLDLSPGTGFAITTISKYLVLVFGAFATFAMLGIDWSKLQWLVAA 912
Cdd:COG3264 16 ISISLPNLLLALLILVVTYLLARLLSRLLERRLLRRTRLDPGLRYLISKLIRYLIIVLGLLIALSALGIDLTALAALAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 913 LSVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTISKIKTRATTIVDWDRREIIVPNKAFITEQFVNWSLSD 992
Cdd:COG3264 96 LGVGIGFGLQDIVSNFISGLILLFERPFRVGDWIEIGGTEGTVEEIGLRSTRIRTFDGEEVIIPNSELITNPVINWSLSD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 993 AITRVKLYVRVRLDADVELVQGLLQEAIDECSLILDNPVPEAFLVELTDSALVYEVRVYVNDMGHRMPMTHELHNLLLER 1072
Cdd:COG3264 176 PRRRVEIPVGVAYGSDLEKVRELLLEAAREHPRVLKDPAPSVLFTEFGDSSVNFELRFWVNDPRDRLRVRSDLNEAIKKA 255
|
250 260
....*....|....*....|....
gi 372984579 1073 LRRHDIRIPHQQVDIRLVGEHNAA 1096
Cdd:COG3264 256 FREEGIEIPFPQRDVHLRNPPGEV 279
|
|
| MscS_TM |
pfam12794 |
Mechanosensitive ion channel inner membrane domain 1; The small mechanosensitive channel, MscS, ... |
486-818 |
2.68e-69 |
|
Mechanosensitive ion channel inner membrane domain 1; 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 domain is one of the inner membrane domains.
Pssm-ID: 432789 [Multi-domain] Cd Length: 332 Bit Score: 235.19 E-value: 2.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 486 TLVVLYLWLL-SRRSLRDYLTRISPRIGNVTQDKYGYTFNTLLLSLLTALPLPALLSLLSHAI-DSPLASPIVVSLSAAL 563
Cdd:pfam12794 2 LLLLVAGLLLwLRRRLKRRLERLAERVGKVTQDSFLHTLRALLLTLLLALPLPLLLAALGWLLqLSGWATPFSVALGAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 564 RELMLPVFILLLVGNLTLPKGLLVMHFNLPAEQVRRVWRQFRTLMLSLLPMLLLLYTSREFREFSLYDTLGRLAFVYTCV 643
Cdd:pfam12794 82 LALALALLVFEFFRRLLRPDGLAIRHFGWPEERVQRLRRQLRWLIWVLVPLVFVLGLAEALPDSLARDVLGRLAFIILML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 644 LMSLFSWRLYRQDMPLLVSSPRQEHLTLANHLLWGLLITAPLLALAAAIMGYLFTAHTLLRQLEISVLAGLGFVMAYFSV 723
Cdd:pfam12794 162 LLAVFLWRLLRPGRGLYASHLGEGPNSRLRRLWWPLLVLAPLALAVLALLGYYYTALQLLGRLIDSLYLLLGWLLVYALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 724 RRWMLLQRRRLAFERAKARRAEILAQRKEKERDEPQETPPSPeaeaaAVAEVDLDAISAQSLGLLRSVLMLGYILTLMLL 803
Cdd:pfam12794 242 LRWLLVARRRLAYRRAKERRAEALAQRAKEGEEGAEPSESSV-----EEPELDLETISAQSLRLLRLLLLLAFLVGLYWI 316
|
330
....*....|....*
gi 372984579 804 WSEINTAFSFLDSIE 818
Cdd:pfam12794 317 WSDLLPAFSYLDNIT 331
|
|
| MS_channel |
pfam00924 |
Mechanosensitive ion channel; Two members of this protein family: Swiss:Q57634 and Swiss: ... |
880-1079 |
2.57e-57 |
|
Mechanosensitive ion channel; Two members of this protein family: Swiss:Q57634 and Swiss:Q58543 of M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.
Pssm-ID: 459999 [Multi-domain] Cd Length: 203 Bit Score: 196.67 E-value: 2.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 880 TTISKYLVLVFGAFATFAMLGIDWSKLQWLVAALSVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTISKIK 959
Cdd:pfam00924 1 KKILKYLIIVVGILIVLSYLGVNVSALLAGLGALGLALGFALQDLVSNLVSGIIILFEKPFKIGDWIEIGDIEGTVEDIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 960 TRATTIVDWDRREIIVPNKAFITEQFVNWSLSDAiTRVKLYVRVRLDADV---ELVQGLLQEAIDECSLILDNPVPEAFL 1036
Cdd:pfam00924 81 LRTTTIRTFDGRLVTIPNSSILTSNIINYSRSPT-RRVELSIGVAYSSDPdklEKVIEILKEAAYEHPLVLKDPEPPVVF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 372984579 1037 VELTDSALVYEVRVYVN-DMGHRMPMTHELHNLLLERLRRHDIR 1079
Cdd:pfam00924 160 GEFGDSSLNFELRVWVKtLPGEYFNVRSELNLRIKKALEENGIE 203
|
|
| MscS |
COG0668 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
818-1092 |
3.49e-49 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440432 [Multi-domain] Cd Length: 276 Bit Score: 175.84 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 818 EVWHVSSSLAGEDTLVPISLKDLVIAVFLVVLTLVTARNLPGLMELSVLQHLDLSPGTGFaITTISKYLVLVFGAFATFA 897
Cdd:COG0668 5 QLWSLLGLLLLLGELLLALLPKLLLALLILLIGWLLIRLLRRLIRRLLRRARRDRTLLPL-LRNILKILIVIIAILLILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 898 MLGIDwskLQWLVAALSVG---LGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTISKIKTRATTIVDWDRREII 974
Cdd:COG0668 84 ILGVN---ITSLLAGLGAAglaIGLAAQDLLSNFIAGIFILLERPFRVGDWIEVGGVEGTVEEIGLRSTRLRTLDGRLVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 975 VPNKAFITEQFVNWSLSDAItRVKLYVRVRLDADVELVQGLLQEAIDECSLILDNPvPEAFLVELTDSALVYEVRVYVND 1054
Cdd:COG0668 161 IPNSKILSSPITNYSRGPTR-RVDVTIGVDYDTDIDKARELLKEILEELPRILKDP-AVVGVTELGDSSVNLRVRAWTKP 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 372984579 1055 mGHRMPMTHELHNLLLERLRRHDIRIPHQQVDIRLVGE 1092
Cdd:COG0668 239 -GDYWDVRRDIRERIKAALDEAGIEIPFPTRTVHLAEE 275
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
35-263 |
3.45e-36 |
|
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: 137.05 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 35 PEGDKPELQKLRDSYNQALQLVREGERYQQQTDRLRQFMDDYPNALKKLEQEKAALKGTST----ESIPLLDGPDLEQAL 110
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEaapkEILASLSLEELEQRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 111 VDAQARRLELRRQREELANTFNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQFTEEQGRQqnANRILAMVREQSLQRRI 190
Cdd:pfam12795 88 LQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSE--AQRWALQAELAALKAQI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372984579 191 QMLELEQLSSGNRDTLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAIAESERLLDEVQTDSPLLAR 263
Cdd:pfam12795 166 DMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| PRK10334 |
PRK10334 |
small-conductance mechanosensitive channel MscS; |
839-1096 |
1.79e-17 |
|
small-conductance mechanosensitive channel MscS;
Pssm-ID: 182386 [Multi-domain] Cd Length: 286 Bit Score: 84.20 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 839 DLVIAVFLVVLTLVTARNLPG-LMELSVLQHLDLSPGTgfAITTISKYLVLVFGAFATFAMLGIDWSKLQWLVAALSVGL 917
Cdd:PRK10334 30 NIVAALAIIIVGLIIARMISNaVNRLMISRKIDATVAD--FLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 918 GFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTISKIKTRATTIVDWDRREIIVPNKAFITEQFVNWSlSDAITRV 997
Cdd:PRK10334 108 GLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFS-REPVRRN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 998 KLYVRVRLDADVELVQGLLQEAIDECSLILDNPVPEAFLVELTDSALVYEVRVYVNdmghrmpmTHELHNL---LLERLR 1074
Cdd:PRK10334 187 EFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSN--------SGDLQNVywdVLERIK 258
|
250 260
....*....|....*....|....*.
gi 372984579 1075 R----HDIRIPHQQVDIRLVGEHNAA 1096
Cdd:PRK10334 259 RefdaAGISFPYPQMDVNFKRVKEDK 284
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
41-329 |
1.01e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 41 ELQKLRDSYNQALQLVregerYQQQTDRLRQFMDDYPNALKKLeQEKAALKGTSTESIPlldgPDLEqaLVDAQARRLel 120
Cdd:pfam15921 246 QLEALKSESQNKIELL-----LQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQ----SQLE--IIQEQARNQ-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 121 rrqreelaNTFNLQELSN-----SGLHNQLDELRQQLRQTQQNLD-QL---------------QFTEEQGRQQNA-NRIL 178
Cdd:pfam15921 312 --------NSMYMRQLSDlestvSQLRSELREAKRMYEDKIEELEkQLvlanseltearterdQFSQESGNLDDQlQKLL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 179 AmvreqSLQRRIQMLELEQLSSG---NRDTLNKLRLEILQSRLTD-------LDQYIDALQNR-QNELRRATteAAIAES 247
Cdd:pfam15921 384 A-----DLHKREKELSLEKEQNKrlwDRDTGNSITIDHLRRELDDrnmevqrLEALLKAMKSEcQGQMERQM--AAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 248 ERLLDEVQTDSPLL--AREQERN--QQLSA---TLVERSRTIE----SLQLENQAVESAVSELTTLKNNLKEQLEWLEVS 316
Cdd:pfam15921 457 NESLEKVSSLTAQLesTKEMLRKvvEELTAkkmTLESSERTVSdltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
330
....*....|...
gi 372984579 317 RGFGENLRNRLSE 329
Cdd:pfam15921 537 KNEGDHLRNVQTE 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-432 |
1.26e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 129 NTFNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQFTEEQGRQQ----NANRILAMVREQSLQRRIQMLELEQLSSGNRD 204
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 205 TLNKLRLEILQSRL-------TDLDQYIDALQNRQNELRRATTEAAiAESERLLDEVQTDSPLLAREQERNQQLSATLVE 277
Cdd:TIGR02168 764 EELEERLEEAEEELaeaeaeiEELEAQIEQLKEELKALREALDELR-AELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 278 RSRTIESLQLENQAVESAVSELTTLKNNLKEQLEWLEVSRGFGENLRNRLSELptpypLPQLEARI--VQSRVDKYSYQE 355
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE-----LEELSEELreLESKRSELRREL 917
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372984579 356 DLDDIANNSYRNRLLTLEQglseeqlllldelltTRARLLERL--QAATDTQIHEQTRLKVAYSRQNGQlEEIRALTEE 432
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEV---------------RIDNLQERLseEYSLTLEEAEALENKIEDDEEEAR-RRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-330 |
1.92e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 48 SYNQALQLVREGERYQQQTDRLRQFMDDYPNALKKLEQEKAALKGTSTEsiplldgpdLEQALVDAQARRLELRRQREEL 127
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE---------LEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 128 ANT-----FNLQELSNSG---------LHNQLDELRQQLRQTQQNLDQLQ---------FTEEQGRQQNANRILAMVREQ 184
Cdd:TIGR02168 301 EQQkqilrERLANLERQLeeleaqleeLESKLDELAEELAELEEKLEELKeelesleaeLEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 185 --SLQRRIQMLELEQLSSGNRDTLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAIAESERLLDEVQTDSP--- 259
Cdd:TIGR02168 381 leTLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErle 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372984579 260 -LLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLEWLEVSRGfgenLRNRLSEL 330
Cdd:TIGR02168 461 eALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG----ILGVLSEL 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
143-316 |
2.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 143 NQLDELRQQLRQTQQNLDQLQFTEEQGRQQNANRILAMVREQSLQRRIQMLELEQLSSGNRDTLNKLR--LEILQSRLTD 220
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 221 LDQYIDALQNRQNELRRAttEAAIAESERLLDEVQTDSPLLAREQ-----ERNQQLSATLVERSRTIESLQLENQAVESA 295
Cdd:COG4717 151 LEERLEELRELEEELEEL--EAELAELQEELEELLEQLSLATEEElqdlaEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|...
gi 372984579 296 VSELTT--LKNNLKEQLEWLEVS 316
Cdd:COG4717 229 LEQLENelEAAALEERLKEARLL 251
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
166-433 |
2.49e-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: 48.56 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 166 EEQGRQQNANRILAMVREQSLQRRIQMLELEQLS-SGNRDTLNKLRLEiLQSRLTDLDQYIDALQNRQNELRRATTeaAI 244
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRlEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVELEELKK--IL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 245 AESERLLDEVQTDSPLLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLEwlevsrgfGENLR 324
Cdd:pfam05483 415 AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE--------KEKLK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 325 NrlSELPTPYPLPQLEAR-IVQSRVDKY----SYQEDLddIANNSYRNRLL----TLEQglseeqlllldelltTRARLL 395
Cdd:pfam05483 487 N--IELTAHCDKLLLENKeLTQEASDMTlelkKHQEDI--INCKKQEERMLkqieNLEE---------------KEMNLR 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 372984579 396 ERLQAATD--TQIHEQTRLKVAYSRQNGQLEEIRALTEER 433
Cdd:pfam05483 548 DELESVREefIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
208-293 |
4.11e-05 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 45.77 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 208 KLRLEILQSRLTDLDQYIDALQNRQNELR---------RATTEAAIAESERLLDEVQTDSPLLAREQERNQQLSATLVER 278
Cdd:TIGR04211 65 RERLPELQQELAELQEELAELQEQLAELRqenqelkqqLSTLEAELEELQKELERIKQISANAIELDEENRELREELAEL 144
|
90
....*....|....*
gi 372984579 279 SRTIESLQLENQAVE 293
Cdd:TIGR04211 145 KQENEALEAENERLQ 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-432 |
4.59e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 158 NLDQLQF-TEEQGRQQN--------ANRILAMVRE-QSLQRRIQMLELEQLssgnRDTLNKLRLEI--LQSRLTDLDQYI 225
Cdd:TIGR02168 187 NLDRLEDiLNELERQLKslerqaekAERYKELKAElRELELALLVLRLEEL----REELEELQEELkeAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 226 DALQNRQNELRRATTEAAiAESERLLDEVQTDSPLLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNN 305
Cdd:TIGR02168 263 QELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 306 LKEQLEWLEVSRgfgENLRNRLSELPTpyPLPQLEARIVQSRVDKYSYQEDLDDIAN--NSYRNRLLTLEQGLSEEQLLL 383
Cdd:TIGR02168 342 LEEKLEELKEEL---ESLEAELEELEA--ELEELESRLEELEEQLETLRSKVAQLELqiASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 372984579 384 LDELLTTRARL-------LERLQAATDTQIHEQTRLKVAYSRQNGQLEEIRALTEE 432
Cdd:TIGR02168 417 ERLQQEIEELLkkleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-350 |
5.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 187 QRRIQML--ELEQLssgnrdtlnKLRLEILQSRLTDLDQYIDALQNRQNELRR-----------ATTEAAIAESERLLDE 253
Cdd:COG4913 609 RAKLAALeaELAEL---------EEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 254 VQTDSPLLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLEwlevsrgfgenlrnRLSELPTP 333
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--------------AAEDLARL 745
|
170
....*....|....*..
gi 372984579 334 YPLPQLEARIVQSRVDK 350
Cdd:COG4913 746 ELRALLEERFAAALGDA 762
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
42-495 |
6.97e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 42 LQKLRDSYNQALQLVREGERYQQQTDRLRQFMDDYPNALKKLEQEKAALKGTSTESIPLLDGPDLEQALVDAQARRLELR 121
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 122 RQREELANTFNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQFTEEQGRQQNANRILAMVREQSLQRRIQMLELEQLSSG 201
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 202 NRDTLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAIAESERLLDEVQTDSPLLAREQERNQQLSATLVERSRT 281
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 282 IESLQLENQAVESAVSELTTLKNNLKEQLEWLEVSRGFGENLRNRLSELPTPYPLPQLEARIVQSRVDKYSYQEDLDDIA 361
Cdd:COG4995 247 AAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 362 NNSYRNRLLTLEQGLSEEQLLLLDELLTTRARLLERLQAATDTQIHEQTRLKVAYSRQNGQLEEIRALTEERLFWLPDLR 441
Cdd:COG4995 327 LAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 372984579 442 PVGsgfpAALRETLEWLTLGATWTALPKALQQQGGASLTLYGISTLVVLYLWLL 495
Cdd:COG4995 407 QLL----RLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLI 456
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
182-310 |
9.95e-05 |
|
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: 45.78 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 182 REQSLQRRIQMLElEQLSSGNRD-TLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAiaeserlldevQTDSPL 260
Cdd:smart00787 138 RMKLLEGLKEGLD-ENLEGLKEDyKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELE-----------DCDPTE 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 372984579 261 LAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQL 310
Cdd:smart00787 206 LDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-330 |
1.30e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 210 RLEILQSRLTDLDQYIDALQNRQNELRRatteaAIAESERLLDEVQTDSPLLAREQERNQQLSATLVER----SRTIESL 285
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQ-----ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDlsslEQEIENV 756
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 372984579 286 QLENQAVESAVSELTTLKNNLKEQLEWLE--VSRGFGENLRNRLSEL 330
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKL 803
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-457 |
1.82e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 153 RQTQQNLDQLQFTEEQGRQQNANRILAMVREQ--SLQRRIQMLELEqlssgnrdtLNKLRLEI--LQSRLTDLDQYIDAL 228
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEEleELTAELQELEEK---------LEELRLEVseLEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 229 QNRQNEL--RRATTEAAIAESERLLDEVQTDsplLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNL 306
Cdd:TIGR02168 294 ANEISRLeqQKQILRERLANLERQLEELEAQ---LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 307 KEQLEWLEVSRgfgENLRNRLSELPTpyPLPQLEARIVQSRVDKysyqEDLDDIANNSYRNRLLTLEQGLSEEQLLLLDE 386
Cdd:TIGR02168 371 ESRLEELEEQL---ETLRSKVAQLEL--QIASLNNEIERLEARL----ERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372984579 387 LLTTRARL------LERLQAATDTQIHEQTRLKVAYSRQNGQLEEIRAlteeRLFWLPDLRPVGSGFPAALRETLEW 457
Cdd:TIGR02168 442 LEELEEELeelqeeLERLEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSEGVKALLKN 514
|
|
| PRK11465 |
PRK11465 |
putative mechanosensitive channel protein; Provisional |
879-1087 |
3.83e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 183147 [Multi-domain] Cd Length: 741 Bit Score: 44.77 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 879 ITTISKYLVLvfgafatfAMLGIDWSKLQWLVAALSVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGTISKI 958
Cdd:PRK11465 521 ISTITIMIVL--------SEIGVNIAPLLAGAGALGLAISFGSQTLVKDIITGVFIQFENGMNTGDLVTIGPLTGTVERM 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 959 KTRATTIVDWDRREIIVPnkafiteqfvnWSlsdAITRVKLYVR----------VRLDADVELVQGLLQEAIDEC----- 1023
Cdd:PRK11465 593 SIRSVGVRQDTGAYHIIP-----------WS---SITTFANFVRgigsvvanydVDRHEDADKANQALKDAVAELmenee 658
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372984579 1024 --SLILDNPVpEAFLVELTDSAlvYEVRVYVNDmghrMPMTHELHNLLLERL-RRH----DIRIPHQQVDI 1087
Cdd:PRK11465 659 irGLIIGEPN-FAGIVGLTNTA--FTLRVSFTT----LPLKQWTVRFALDSQvKKHfdlaGVRAPVQTYQV 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-330 |
9.02e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 141 LHNQLDELRQQLRQTQQNLDQLQFTEEQGRQQnanRILAMVREQSLQRRIQMLELEQLSSGNRDTLNKLRLEILQSRLTD 220
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQD---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 221 LDQYIDALQNRQNELRRATTEAAIAESE----------RLLDEVQTDSPLLAREQERNQQLSATLVERSRTIESLQLENQ 290
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEaeeeleelaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 372984579 291 AVESAVSELTTLKNNLKEQLEWLEVSRGFGENLRNRLSEL 330
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
27-311 |
1.05e-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: 43.09 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 27 IEALLKEIpEGDKPELQKLRDSYNQALQLVREGERYQQQTDrlrqfmddypNALKKLEQEKAALKgtstESIPlldgpDL 106
Cdd:TIGR04523 372 IEKLKKEN-QSYKQEIKNLESQINDLESKIQNQEKLNQQKD----------EQIKKLQQEKELLE----KEIE-----RL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 107 EQALVDAQARRLELRRQREELANTFNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQ------------FTEEqgRQQNA 174
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQkelkskekelkkLNEE--KKELE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 175 NRILAMVREQS-LQRRIQMLELE------QLSSGNRDTLNK---LRLEILQSRLTDLDQYIDALQNRQNELRRATTEAai 244
Cdd:TIGR04523 510 EKVKDLTKKISsLKEKIEKLESEkkekesKISDLEDELNKDdfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK-- 587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372984579 245 aesERLLDEVQTDSPLLAREQERNQQLSATLverSRTIESLQLENQAVESAVSELTTLKNNLKEQLE 311
Cdd:TIGR04523 588 ---QELIDQKEKEKKDLIKEIEEKEKKISSL---EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-311 |
1.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 134 QELSNSglHNQLDELRQQLRQTQQNLDQLQFTEEQGRQQNANRILAmvreQSLQRRIQMLE--LEQLSSGNRDtlnklrL 211
Cdd:COG4913 620 AELEEE--LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----ASAEREIAELEaeLERLDASSDD------L 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 212 EILQSRLTDLDQYIDALQNRQNEL--RRATTEAAIAESERLLDEVQTDspLLAREQERNQQLSATLVERSRTIESLQLEN 289
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELkgEIGRLEKELEQAEEELDELQDR--LEAAEDLARLELRALLEERFAAALGDAVER 765
|
170 180
....*....|....*....|....*
gi 372984579 290 Q---AVESAVSELTTLKNNLKEQLE 311
Cdd:COG4913 766 ElreNLEERIDALRARLNRAEEELE 790
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-434 |
2.45e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 156 QQNLDQLQ-FTEEQGRQ--------QNANRILAMVRE------QSLQRRIQMLELEQLSSGNRDTLNKLRLEILQSRLTD 220
Cdd:COG1196 185 EENLERLEdILGELERQleplerqaEKAERYRELKEElkeleaELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 221 LDQYIDALQNRQNELRRAtTEAAIAESERLLDEVQTDSPLLAREQERNQQLSATLVERSRTIESLQLENQAVESAVSELT 300
Cdd:COG1196 265 LEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 301 TLKNNLKEQLEWLEVSRGFGENLRNRLSElptpyplpQLEARIVQSRVDKYSYQEDLDDIANnsYRNRLLTLEQgLSEEQ 380
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEA--------ELAEAEEELEELAEELLEALRAAAE--LAAQLEELEE-AEEAL 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 372984579 381 LLLLDELLTTRARLLERLQAATDTQIHEQTRLKVAYSRQNGQLEEIRALTEERL 434
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-311 |
2.65e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 106 LEQALVDAQARRLELRRQREELANTFNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQ--FTEEQGRQQNANRILAMVRE 183
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEaeLAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 184 QSLQRRIQMLELEQlssgnRDTLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAIAESERLLDEVQTDSpLLAR 263
Cdd:COG1196 380 ELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE-EEAE 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 372984579 264 EQERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLE 311
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-314 |
3.39e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 105 DLEQALVDAQARRLELRRQREELANTFNLQELSNSGLHNQLDELRQQLRQTQQNLDQLQFTEEQGRQQNANrilamvREQ 184
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA------QKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 185 SLQRRIQMLELEQLSSGNRDTLNKLRLEILQSRLTDLDQYIDALQNRQNELRRATTEAAiAESERLLDEVQTDSPLLARE 264
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-ALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 372984579 265 QERNQQLSATLVERSRTIESLQLENQAVESAVSELTTLKNNLKEQLEWLE 314
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-311 |
4.47e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 28 EALLKEIPEGDKPELQKLRDSYNQALQLVREGERYQQQTDRLRQFMDDypnaLKKLEQEKAALKGTSTESIPLLDGPDLE 107
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE----LTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 108 QALVDAQArrlelrrqreelaNTFNLQELSNSglhNQLDELRQqlrqtqqnldqlQFTEEQGRQQNANRILAMVREQSLQ 187
Cdd:TIGR02168 784 IEELEAQI-------------EQLKEELKALR---EALDELRA------------ELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372984579 188 RRIQMLELEQLSSGNRDTLNKLRLEILQSRlTDLDQYIDALQNRQNElrRATTEAAIAESERLLDEVQTDspllAREQER 267
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELE-ELIEELESELEALLNE--RASLEEALALLRSELEELSEE----LRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 372984579 268 nqqlsatlvERSRTIESLQLENQAVESAVSELTTLKNNLKEQLE 311
Cdd:TIGR02168 909 ---------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| |
