|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1-1107 |
0e+00 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 2235.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 1 MRPIIVLLMAWCLSMGAYAATAPDAKQITQELEQAKAAK-PAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKL 79
Cdd:PRK10929 1 MRLIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKtPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 80 SQTLRSQLNNLRDEPREVPVGLTSDALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRV 159
Cdd:PRK10929 81 SAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 160 GTQ-AGNTPQSQAQNLGLQAESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAE 238
Cdd:PRK10929 161 QTLgTPNTPLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 239 RALESTELLAENSANLPVGIVDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGE 318
Cdd:PRK10929 241 RALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 319 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLHYEDLLNKQPQIRQIRQADGQPLTGEQNRILEAQLRTQRELLNSLLQGGD 398
Cdd:PRK10929 321 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 399 TLILELTKLKVSNSQLEDALKEVNEATHRYLFWTSDVRPMTFSWPIEIVQDLRRLISLDTFSQLGQASVMMITSKETIFP 478
Cdd:PRK10929 401 TLILELTKLKVANSQLEDALKEVNEATHRYLFWVADVSPISLSYPLEIAQDLRRLLSLDTFSQLGKASVMMLTSKETLLP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 479 LLGALILVGFSIYSRRHFTRFLERSSARVGKVTQDHFWLTLRTVFWSILVASPLPVLWMTLGYGLREAWPYPLAVAIGDG 558
Cdd:PRK10929 481 LFGALLLVGFSISSRRHYHAFLERSSSRVGKVTQDHFSLTLRTVFWSILVASPLPVLWAALGYGLQNAWPYPLAVAIGDG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 559 VTATVPLLWVVMICATFARPNGLFVAHFGWPRSRVARGMRYYLMSIGLIVPLIMALIMFDNLNDREFSGSLGRLCFILIC 638
Cdd:PRK10929 561 VTATVPLLWVFMICATFARPNGLFIAHFGWPRERVARAMRYYLLSIGLIVPLIMALITFDNLNDREFSGTLGRLCFILLC 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 639 GALAMVKLSLKRAGIPLYLDKTGSGDNMLNRMLWNLMLSAPLVAILAAAVGYLATAQALLARLETSVAIWFLLLVVYHVI 718
Cdd:PRK10929 641 GALSLVTLSLKRAGIPLYLDKEGSGDNIINHALWNLLIGAPLVAALASALGYLATAQALLARLETSVAIWFLLLVVYHII 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 719 RRGMLIQRRRLAFDRAKHRRAEILAQRARGEEEPNHVNSTEGTTDADDVEIDLDTISTQSLRLVRSLLMLVALLSVIFLW 798
Cdd:PRK10929 721 RRWMLIQRRRIAFDRAKQRRAEILAQRARGEEEAHHSSSPEGAIEVEEPVIDLDAISAQSLRLVRSILTLIALLSVIVLW 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 799 SEIHSAFGFLENISLWDVTSTVQGVESLEPITLGAVLIAILVLIITTQLVRNFPAMLELALLQHLDLTPGTGYAITTITK 878
Cdd:PRK10929 801 SEIHSAFGFLENISLWDVTSTVQGVESLQPITLGSVLIAILVFIITTQLVRNLPALLELALLQHLDLTPGTGYAITTITK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 879 YLIMLFGGLVGFSMIGIEWSKLQWLVAALTVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATT 958
Cdd:PRK10929 881 YLLMLIGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 959 ISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQ 1038
Cdd:PRK10929 961 ISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVLDNPAPEVFLVDLQQGIQ 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047419976 1039 IFELRIYAAEMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLGGTKTSRTLSSAGRKRPAGSL 1107
Cdd:PRK10929 1041 IFELRIYAAEMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLGGKQTGRTLTSAGKSRTAGSL 1109
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
4-1076 |
5.67e-166 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 519.47 E-value: 5.67e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 4 IIVLLMAWCLSMGAYAATA----PDAKQITQELEQAKAAKPAQPE---TVESLQSALNALEERKGSLERAQQYQQVIDNF 76
Cdd:PRK11281 13 IAFLFLLLCLSSAFARAASngdlPTEADVQAQLDALNKQKLLEAEdklVQQDLEQTLALLDKIDRQKEETEQLKQQLAQA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 77 PKLSQTLRSQLNNLRDEPREVpvgLTSDALNQEILQVSSQLLEKSRQAQQEQErarEIADSLSQLPQQQTDARR------ 150
Cdd:PRK11281 93 PAKLRQAQAELEALKDDNDEE---TRETLSTLSLRQLESRLAQTLDQLQNAQN---DLAEYNSQLVSLQTQPERaqaaly 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 151 ----QLNEVERR-VGTQAGNTPQSQAQNLGLQAESARLKALVDeLELAQLSANNR-QELSRMRAELAQKQSQQLDAYLQS 224
Cdd:PRK11281 167 ansqRLQQIRNLlKGGKVGGKALRPSQRVLLQAEQALLNAQND-LQRKSLEGNTQlQDLLQKQRDYLTARIQRLEHQLQL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 225 LRNQLNSQRQREAE---RALESTELLAENSANlPVgIVDQFKVNRELSAALNQQAQRMDlVASQQRQATNQTL-QVRQAL 300
Cdd:PRK11281 246 LQEAINSKRLTLSEktvQEAQSQDEAARIQAN-PL-VAQELEINLQLSQRLLKATEKLN-TLTQQNLRVKNWLdRLTQSE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 301 NTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRV-------QRlhyEDLLNKQPQIRQIRQADGQPLTG 373
Cdd:PRK11281 323 RNIKEQISVLKGSLLLSRILYQQQQALPSADLIEGLADRIADLRLeqfeinqQR---DALFQPDAYIDKLEAGHKSEVTD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 374 EQNRILEAQLRTQREL-------LNSLLQGGDTLILELTKLKVSNSQLEDALKEvneathrYLFWTSDVRPMTFSW---- 442
Cdd:PRK11281 400 EVRDALLQLLDERRELldqlnkqLNNQLNLAINLQLNQQQLLSVSDSLQSTLTQ-------QIFWVNSNKPMDLDWlkaf 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 443 PIEIVQDLRRLISLDTFSQLGQASVmmitskETIFPLLGALILVGFSIYSRRHFTRFLERSSARVGKVTQDHFWLTLRTV 522
Cdd:PRK11281 473 PQALKDQFKSLKITVSFSNLWDGLF------IALLLFLPLLLIAGLIRWRKKWIKARLQKLAADIGTLKRDSQLHTPKAI 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 523 FWSILVASPLPVLWMTLGYGLR--------EAWPYPLAVAigdgvtatvpLLWVVMICATFA-RPNGLFVAHFGWPRSRV 593
Cdd:PRK11281 547 LITLLLALPVTLIFLAVGLILLtdafnqseLLWSWSLKLA----------LFWLVFATCYRVlRPNGVAERHFGMPKEQV 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 594 ARgMRYYLMSIGLIVPLIMALIMFDNLNDREFSGSLGRLCFILICGALAMVKLSlkragiPLYLDKTGSGDNMLNRMLWN 673
Cdd:PRK11281 617 SH-FRRQIVRLSLALLPLLFWSVVAELSPLGLADDVIGQAVIIIALALIAFLVW------PLCRESWRDKESHTLRLVVR 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 674 LMLS-APLVAILAAAVGYLATAQALLARLETSVAIWFLLLVVYHVIRRGMLIQRRRLAFDRAKHRRAEILAQRARGEEEp 752
Cdd:PRK11281 690 TVLTiAPIALIVLVVLGYYYTALRLIGRLIETLYLLIIWNLLYQTVLRGLSVAARRLAYRRALAKRQNLVKEGAEGAEP- 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 753 nhvnsTEGTTdaddveIDLDTISTQSLRLVRsLLMLVALLSVIF-LWSEIHSAFGFLENISLWDVTSTVQGVESLEPITL 831
Cdd:PRK11281 769 -----VEEPT------LALEQVNQQSLRLTD-LLLFALFFVMFYwVWSDLITVFSYLDSITLWHYTTTTAGGAVVESITL 836
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 832 GAVLIAILVLIITTQLVRNFPAMLELALLQHLDLTPGTGYAITTITKYLIMLFGGLVGFSMIGIEWSKLQWLVAALTVGL 911
Cdd:PRK11281 837 GNLLFALIILVVTYVLVRNLPGLLEVLVLSRLNLRQGTSYAITTLLTYIIIAVGAVTAFSTLGVSWDKLQWLVAALSVGL 916
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 912 GFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEIIVPNKAFITEQFINWSLSDSVTRV 991
Cdd:PRK11281 917 GFGLQEIFANFVSGLIILFERPVRIGDTVTIGTFSGTVSKIRIRATTITDFDRKEVIVPNKAFVTERLINWSLSDTVTRV 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 992 VLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQIFELRIYAAEMGHRMPLRHEIHQLILAGFREHG 1071
Cdd:PRK11281 997 VIKVGVAYGSDLEKVRELLLQAATENPRVMKEPEPQVFFLNFGASTLDHELRLYVRELGDRSPTVDELNRRIDRLFREND 1076
|
....*
gi 2047419976 1072 IDMPF 1076
Cdd:PRK11281 1077 INIAF 1081
|
|
| MscS_TM |
pfam12794 |
Mechanosensitive ion channel inner membrane domain 1; The small mechanosensitive channel, MscS, ... |
481-813 |
6.63e-118 |
|
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: 366.92 E-value: 6.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 481 GALILVGFSI-YSRRHFTRFLERSSARVGKVTQDHFWLTLRTVFWSILVASPLPVLWMTLGYGLREA-WPYPLAVAIGDG 558
Cdd:pfam12794 1 LLLLLVAGLLlWLRRRLKRRLERLAERVGKVTQDSFLHTLRALLLTLLLALPLPLLLAALGWLLQLSgWATPFSVALGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 559 VTATVPLLWVVMICATFARPNGLFVAHFGWPRSRVARGMRYYLMSIGLIVPLIMALIMFDNLNDREFSGSLGRLCFILIC 638
Cdd:pfam12794 81 LLALALALLVFEFFRRLLRPDGLAIRHFGWPEERVQRLRRQLRWLIWVLVPLVFVLGLAEALPDSLARDVLGRLAFIILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 639 GALAMVKLSLKRAGIPLYLDKTGSGDN-MLNRMLWNLMLSAPLVAILAAAVGYLATAQALLARLETSVAIWFLLLVVYHV 717
Cdd:pfam12794 161 LLLAVFLWRLLRPGRGLYASHLGEGPNsRLRRLWWPLLVLAPLALAVLALLGYYYTALQLLGRLIDSLYLLLGWLLVYAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 718 IRRGMLIQRRRLAFDRAKHRRAEILAQRARGEEEPNHVNSTEGttdaDDVEIDLDTISTQSLRLVRSLLMLVALLSVIFL 797
Cdd:pfam12794 241 ALRWLLVARRRLAYRRAKERRAEALAQRAKEGEEGAEPSESSV----EEPELDLETISAQSLRLLRLLLLLAFLVGLYWI 316
|
330
....*....|....*.
gi 2047419976 798 WSEIHSAFGFLENISL 813
Cdd:pfam12794 317 WSDLLPAFSYLDNITL 332
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis]; |
808-1089 |
1.25e-97 |
|
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442495 [Multi-domain] Cd Length: 281 Bit Score: 310.98 E-value: 1.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 808 LENISLWDVTSTVQGVeslePITLGAVLIAILVLIITTQLVRNFPAMLELALLQHLDLTPGTGYAITTITKYLIMLFGGL 887
Cdd:COG3264 1 MEESALLELLFLIGGI----SISLPNLLLALLILVVTYLLARLLSRLLERRLLRRTRLDPGLRYLISKLIRYLIIVLGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 888 VGFSMIGIEWSKLQWLVAALTVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEI 967
Cdd:COG3264 77 IALSALGIDLTALAALAGALGVGIGFGLQDIVSNFISGLILLFERPFRVGDWIEIGGTEGTVEEIGLRSTRIRTFDGEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 968 IVPNKAFITEQFINWSLSDSVTRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQIFELRIYAA 1047
Cdd:COG3264 157 IIPNSELITNPVINWSLSDPRRRVEIPVGVAYGSDLEKVRELLLEAAREHPRVLKDPAPSVLFTEFGDSSVNFELRFWVN 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2047419976 1048 EMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLGGT 1089
Cdd:COG3264 237 DPRDRLRVRSDLNEAIKKAFREEGIEIPFPQRDVHLRNPPGE 278
|
|
| MS_channel |
pfam00924 |
Mechanosensitive ion channel; Two members of this protein family: Swiss:Q57634 and Swiss: ... |
874-1073 |
4.11e-60 |
|
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: 204.37 E-value: 4.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 874 TTITKYLIMLFGGLVGFSMIGIEWSKLQWLVAALTVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKIN 953
Cdd:pfam00924 1 KKILKYLIIVVGILIVLSYLGVNVSALLAGLGALGLALGFALQDLVSNLVSGIIILFEKPFKIGDWIEIGDIEGTVEDIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 954 TRATTISDWDRKEIIVPNKAFITEQFINWSLSDsVTRVVLTVPAPSDANS---EEVTQILYTAAERCSLVIDNPAPEVFL 1030
Cdd:pfam00924 81 LRTTTIRTFDGRLVTIPNSSILTSNIINYSRSP-TRRVELSIGVAYSSDPdklEKVIEILKEAAYEHPLVLKDPEPPVVF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2047419976 1031 VDLQQGIQIFELRIYAAE-MGHRMPLRHEIHQLILAGFREHGID 1073
Cdd:pfam00924 160 GEFGDSSLNFELRVWVKTlPGEYFNVRSELNLRIKKALEENGIE 203
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
30-252 |
2.51e-56 |
|
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: 195.21 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRSQLNNLR----DEPREVPVGLTSDA 105
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQakaeAAPKEILASLSLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 106 LNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRV-GTQAGNTPQSQAQNLGLQAESARLK 184
Cdd:pfam12795 83 LEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLnGPAPPGEPLSEAQRWALQAELAALK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047419976 185 ALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSA 252
Cdd:pfam12795 163 AQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAA 230
|
|
| MscS |
COG0668 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
812-1084 |
7.46e-46 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440432 [Multi-domain] Cd Length: 276 Bit Score: 166.59 E-value: 7.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 812 SLWDVTSTVQGVESLEPITLGAVLIAILVLIITTQLVRNFPAMLELALLQHLDLTPGTGYaITTITKYLIMLFGGLVGFS 891
Cdd:COG0668 5 QLWSLLGLLLLLGELLLALLPKLLLALLILLIGWLLIRLLRRLIRRLLRRARRDRTLLPL-LRNILKILIVIIAILLILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 892 MIGIEwskLQWLVAALTVG---LGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEII 968
Cdd:COG0668 84 ILGVN---ITSLLAGLGAAglaIGLAAQDLLSNFIAGIFILLERPFRVGDWIEVGGVEGTVEEIGLRSTRLRTLDGRLVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 969 VPNKAFITEQFINWSLSDSVtRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPApEVFLVDLQQGIQIFELRIYAAE 1048
Cdd:COG0668 161 IPNSKILSSPITNYSRGPTR-RVDVTIGVDYDTDIDKARELLKEILEELPRILKDPA-VVGVTELGDSSVNLRVRAWTKP 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 2047419976 1049 mGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLE 1084
Cdd:COG0668 239 -GDYWDVRRDIRERIKAALDEAGIEIPFPTRTVHLA 273
|
|
| PRK10334 |
PRK10334 |
small-conductance mechanosensitive channel MscS; |
833-1081 |
7.46e-12 |
|
small-conductance mechanosensitive channel MscS;
Pssm-ID: 182386 [Multi-domain] Cd Length: 286 Bit Score: 67.25 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 833 AVLIAILVLIITTQLVRNfpAMLELALLQHLDLTpgTGYAITTITKYLIMLFGGLVGFSMIGIEWSKLQWLVAALTVGLG 912
Cdd:PRK10334 33 AALAIIIVGLIIARMISN--AVNRLMISRKIDAT--VADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 913 FGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEIIVPNKAFITEQFINWSlSDSVTRVV 992
Cdd:PRK10334 109 LALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFS-REPVRRNE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 993 LTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQIFELRIYaAEMGHRMPLRHEIHQLILAGFREHGI 1072
Cdd:PRK10334 188 FIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVW-SNSGDLQNVYWDVLERIKREFDAAGI 266
|
....*....
gi 2047419976 1073 DMPFPpfQM 1081
Cdd:PRK10334 267 SFPYP--QM 273
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-371 |
3.34e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 19 AATAPDAKQITQELEQAKAakpaqpetveslQSALNALEERKGSLERAQQYQQvidnfpKLSQTLRSQLNNLRdeprevp 98
Cdd:COG1196 209 AEKAERYRELKEELKELEA------------ELLLLKLRELEAELEELEAELE------ELEAELEELEAELA------- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 99 vgltsdALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQA 178
Cdd:COG1196 264 ------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 179 ESARLKALVDELELA-QLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERA-LESTELLAENSANLpv 256
Cdd:COG1196 338 ELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLER-- 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 257 gIVDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARlpempkpqQL 336
Cdd:COG1196 416 -LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE--------EL 486
|
330 340 350
....*....|....*....|....*....|....*
gi 2047419976 337 DTEMAQLRVQRLHYEDLLNKQPQIRQIRQADGQPL 371
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-366 |
6.92e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEQAKAAKPAQPETVESLQSALNALEerkgslERAQQYQQVIDNFPKLSQTLRSQLNNLRDEPRevpvgltsdALNQE 109
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 110 ILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARLKALVDE 189
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 190 LELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSanlpvgivdqfkvnrELS 269
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------------SLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 270 AALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQsqwLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLH 349
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330
....*....|....*..
gi 2047419976 350 YEDLLNKQPQIRQIRQA 366
Cdd:TIGR02168 964 EDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-306 |
1.06e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERkgsleraqqyqqvidnfpklSQTLRSQLNNLRDEprevpvgltS 103
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEK--------------------LEELRLEVSELEEE---------I 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARL 183
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 184 KALVDELELAQLSAnnRQELSRMRAELAQKQSQ--QLDAYLQSLRNQLNS---------QRQREAERALESTEL--LAEN 250
Cdd:TIGR02168 364 EAELEELESRLEEL--EEQLETLRSKVAQLELQiaSLNNEIERLEARLERledrrerlqQEIEELLKKLEEAELkeLQAE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2047419976 251 SANLPVGIVDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQ 306
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-330 |
3.41e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 27 QITQELEQAKAAKPAQPETVESLQSALNALEERKGSLE-RAQQYQQVIDNFPKLSQTLRSQLNNLRDEPREVPVGLTSda 105
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE-- 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 106 LNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARLKA 185
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 186 LVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRnqlnsQRQREAERAL-ESTELLAENSANLpvgivDQFKV 264
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELE-----SKRSELRRELeELREKLAQLELRL-----EGLEV 936
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047419976 265 NR-ELSAALNQQAQR-MDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLG-EALRAQVARLPEM 330
Cdd:TIGR02168 937 RIdNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAiEEYEELKERYDFL 1005
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-344 |
1.10e-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: 61.70 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARL 183
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 184 KALVDELeLAQLSANNRQelSRMRAELAQKQSQQLDAYLQSLRnQLNSQRQREAERALESTELLAENSANLPVGIVDQFK 263
Cdd:COG4942 103 KEELAEL-LRALYRLGRQ--PPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 264 VNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSsnlLGEALRAQVARLPEMPKPQQLDTEMAQL 343
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA---LIARLEAEAAAAAERTPAAGFAALKGKL 255
|
.
gi 2047419976 344 R 344
Cdd:COG4942 256 P 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-246 |
7.79e-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: 59.01 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 1 MRPIIVLLMAWCLSMGAYAATAPDA----KQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQqyqqvidnf 76
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAeaelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 77 pklsQTLRSQLNNLRDEPREvpvgltsdaLNQEILQvssqlLEKSRQAQQEQ--ERAREIADSLSQLPQQQTDARRQLNE 154
Cdd:COG4942 72 ----RALEQELAALEAELAE---------LEKEIAE-----LRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDFLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 155 VERRVGTQAGNTPQSQAQNLGLQAESARLKALVDELELAQLS-ANNRQELSRMRAELAQKQSQQlDAYLQSLRNQLNSQR 233
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAElEALLAELEEERAALEALKAER-QKLLARLEKELAELA 212
|
250
....*....|...
gi 2047419976 234 QREAERALESTEL 246
Cdd:COG4942 213 AELAELQQEAEEL 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-321 |
8.39e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 18 YAATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLEraqqyQQVidnfpklsQTLRSQLNNLRDEPREv 97
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-----QQK--------QILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 98 pvgltsdaLNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTqagntpqsqaqnlgLQ 177
Cdd:TIGR02168 321 --------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE--------------LE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 178 AESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTE-LLAENSANLPV 256
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELER 458
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047419976 257 G------IVDQFKVNRE----LSAALNQQAQRMDLVASQQRQATNQTLQVRQALNtlrEQSQWLGSSNLLGEALR 321
Cdd:TIGR02168 459 LeealeeLREELEEAEQaldaAERELAQLQARLDSLERLQENLEGFSEGVKALLK---NQSGLSGILGVLSELIS 530
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
25-368 |
2.34e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 25 AKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLEraQQYQQVIDNFPKLSQTLRSQ---------LNNL----- 90
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLE--QDYQAASDHLNLVQTALRQQekieryqadLEELeerle 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 91 ------------RDEPREvpvglTSDALNQEILQVSSQL---------LEKS----RQAQQEQERAREI----------- 134
Cdd:PRK04863 366 eqnevveeadeqQEENEA-----RAEAAEEEVDELKSQLadyqqaldvQQTRaiqyQQAVQALERAKQLcglpdltadna 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 135 ADSLSQLPQQQTDARRQLNEVERRVG-TQAGNTPQSQAQNLglqaesarLKALVDELELAQLSANNRQELSRMRAELAQK 213
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSvAQAAHSQFEQAYQL--------VRKIAGEVSRSEAWDVARELLRRLREQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 214 QS-QQLDAYLQSLRNQLNSQRQreAERalesteLLAENSANLPVGIVDQfkvnRELSAALNQQAQRMDLVASQQRQATNQ 292
Cdd:PRK04863 513 EQlQQLRMRLSELEQRLRQQQR--AER------LLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 293 TLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEM-----PKPQQLDTEMAQ-------LRVQRLHYEDllNKQP-- 358
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQsgeefEDSQDVTEYMQQllerereLTVERDELAA--RKQAld 658
|
410
....*....|.
gi 2047419976 359 -QIRQIRQADG 368
Cdd:PRK04863 659 eEIERLSQPGG 669
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
44-416 |
3.20e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 44 ETVESLQSALNALEERKGSLERAQQyQQVIDNFPKLSQtLRSQLNNLRDEprevpvgltSDALNQEILQVSSQLLEKSRQ 123
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALS-EQLRKALFELDK-LQEELEQLREE---------LEQAREELEQLEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 124 AQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVgtqagNTPQSQAQNLglQAESARLKALVDELE-----LAQLSAN 198
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA-----EELQEELEEL--QKERQDLEQQRKQLEaqiaeLQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 199 NRQELSRMRAELAQKQsQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSANLPVGIVDQFKVNRELSAAlNQQAQR 278
Cdd:COG4372 148 REEELKELEEQLESLQ-EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE-LLEAKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 279 MDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMA------QLRVQRLHYED 352
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALeeaaleLKLLALLLNLA 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047419976 353 LLNKQPQIRQIRQADGQPLTGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLED 416
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
30-368 |
3.29e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEQAKAAKPAQPETVESLQSALNALEERkgsLERAQQ-----------YQQVIDnfpkLSQTLRSQLNNLRDEPREVP 98
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEAR---LEAAEEevdslksqladYQQALD----VQQTRAIQYQQAVQALEKAR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 99 VGLTSDALNQEilQVSSQLLEKSRQAQQEQERAREIADSLSqlpqQQTDARRQLNEVERRVGTQAGNTPQSQA------- 171
Cdd:COG3096 427 ALCGLPDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKLS----VADAARRQFEKAYELVCKIAGEVERSQAwqtarel 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 172 --QNLGLQAESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAylqslRNQLNSQRQREAERALESTELLAE 249
Cdd:COG3096 501 lrRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----AEELEELLAELEAQLEELEEQAAE 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 250 NSANLpvgivdqfkvnRELSAALNQQAQRMdlvaSQQRQATNQTLQVRQALNTLREQS-QWLGSSNLLGEALRAQVARLp 328
Cdd:COG3096 576 AVEQR-----------SELRQQLEQLRARI----KELAARAPAWLAAQDALERLREQSgEALADSQEVTAAMQQLLERE- 639
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2047419976 329 empkpQQLDTEMAQLRVQRLHYEDllnkqpQIRQIRQADG 368
Cdd:COG3096 640 -----REATVERDELAARKQALES------QIERLSQPGG 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-348 |
4.22e-08 |
|
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: 57.77 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 39 KPAQPETVESLQSALNALeerKGSLERAQQYQQVIDNfpkLSQTLRSQLNNLRDEPREVPVGLtsDALNQEILQVSSQLL 118
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL---KRELSSLQSELRRIEN---RLDELSQELSDASRKIGEIEKEI--EQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 119 EKSRQAQQ-EQERA---REIADSLSQLPQQQTDA---RRQLNEVERRVGTQagNTPQSQAQNLGLQAESARLKALVDELE 191
Cdd:TIGR02169 741 ELEEDLSSlEQEIEnvkSELKELEARIEELEEDLhklEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 192 laqlsannrQELSR--MRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAEnsanlpvgivdqfkvNRELS 269
Cdd:TIGR02169 819 ---------QKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE---------------LEELE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 270 AALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSS-NLLGEALRAQVARLPEM---------PKPQQLDTE 339
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEIedpkgedeeIPEEELSLE 954
|
....*....
gi 2047419976 340 MAQLRVQRL 348
Cdd:TIGR02169 955 DVQAELQRV 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-420 |
8.41e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 107 NQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARLKAL 186
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 187 VDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQR--EAERALESTellaensanlpvgivdqfkv 264
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldELRAELTLL-------------------- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 265 NRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpkpqQLDTEMAQLR 344
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN-----ERASLEEALA 890
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047419976 345 VQRLHYEDLlnkqpqIRQIRQADgqpltgEQNRILEAQLRTQRELLNsllqggdTLILELTKLKVSNSQLEDALKE 420
Cdd:TIGR02168 891 LLRSELEEL------SEELRELE------SKRSELRRELEELREKLA-------QLELRLEGLEVRIDNLQERLSE 947
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
25-239 |
1.15e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.91 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 25 AKQITQELEQAKAAKPAQPETVESLQSAL----NALEERKGSLERAQ-QYQQVIDNFPKLSQTL---------------- 83
Cdd:pfam07111 375 AKGLQMELSRAQEARRRQQQQTASAEEQLkfvvNAMSSTQIWLETTMtRVEQAVARIPSLSNRLsyavrkvhtikglmar 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 84 RSQLNNLRDE---------PREVPVGLTSDALNQEILQVSSQLLEKSRQAQQEQERAREiadslsqlpqQQTDARRQLNE 154
Cdd:pfam07111 455 KVALAQLRQEscpppppapPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRARE----------QGEAERQQLSE 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 155 VERRVGTQAGNTPQSQAqNLGLQAESARLkalvDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQ 234
Cdd:pfam07111 525 VAQQLEQELQRAQESLA-SVGQQLEVARQ----GQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKR 599
|
....*..
gi 2047419976 235 R--EAER 239
Cdd:pfam07111 600 RlnEARR 606
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
21-389 |
2.25e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 21 TAPDAKQI-TQELEQAKAAKPAQPETVESLQSALNALEERkgsLERAQQYQQVIDNFPKLsQTLRSQLNNLRDE----PR 95
Cdd:TIGR00618 216 TYHERKQVlEKELKHLREALQQTQQSHAYLTQKREAQEEQ---LKKQQLLKQLRARIEEL-RAQEAVLEETQERinraRK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 96 EVPVGLTSDAL---NQEILQVSSQLLEKSRQ-AQQEQERAREIADSLSQLPQQQTDAR--RQLNEVERRVGTQAGNTPQS 169
Cdd:TIGR00618 292 AAPLAAHIKAVtqiEQQAQRIHTELQSKMRSrAKLLMKRAAHVKQQSSIEEQRRLLQTlhSQEIHIRDAHEVATSIREIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 170 QAQnlglQAESARLKALVDELE-LAQLSANNRQELSRMRAELAQKQSQQ-----LDAYLQSLRNQLNSQRQREAERALES 243
Cdd:TIGR00618 372 CQQ----HTLTQHIHTLQQQKTtLTQKLQSLCKELDILQREQATIDTRTsafrdLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 244 TELLAENSANLPVgIVDQFKVNRELSAALNQ--------------QAQRMDLVASQQRQATNQTLQ-------------- 295
Cdd:TIGR00618 448 TCTAQCEKLEKIH-LQESAQSLKEREQQLQTkeqihlqetrkkavVLARLLELQEEPCPLCGSCIHpnparqdidnpgpl 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 296 ---VRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRVQRLHYEDLLNKQPQIRQIRQADGQPLT 372
Cdd:TIGR00618 527 trrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
410
....*....|....*..
gi 2047419976 373 GEQNRILEAQLRTQREL 389
Cdd:TIGR00618 605 EAEDMLACEQHALLRKL 621
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-326 |
2.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 122 RQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGL-QAESARLKALVDELE-----LAQL 195
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEaelerLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 196 SANNRQELSRMRAELAQKQSQQLDAyLQSLRNQLNSQRQREAERALESTELLAENSANLPvGIVDQFKVNR-ELSAALNQ 274
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEERERRRARLEALLAALGLPLP-ASAEEFAALRaEAAALLEA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2047419976 275 QAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGS--SNLLGE--ALRAQVAR 326
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrkSNIPARllALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-216 |
2.62e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 26 KQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRS---QLNNLRDEPREVpvglt 102
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEleaELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 103 sDALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRvgtqagntpQSQAQNLGLQaesAR 182
Cdd:COG4913 688 -AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL---------ARLELRALLE---ER 754
|
170 180 190
....*....|....*....|....*....|....
gi 2047419976 183 LKALVDELELAQLSANNRQELSRMRAELAQKQSQ 216
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-427 |
4.37e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQqyqqvidnfpklsQTLRSQLNNLRDEPREVPVGLTSDALNQE 109
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-------------EELREELEKLEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 110 ILQVSSQLleksRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNlgLQAESARLKALVDE 189
Cdd:COG4717 141 LAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE--LEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 190 LELAQlsannrQELSRMRAELAQKQSQQLDAYLQslrNQLNSQRQR-EAERALESTELLAENSANLPVGIVDQFKVNREL 268
Cdd:COG4717 215 LEEAQ------EELEELEEELEQLENELEAAALE---ERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 269 SAALNQQAQRMDLVASQQRQATNQtLQVRQALNTlREQSQWLGSSNLLGEALRAQVARL-PEMPKPQQLDTEMAQLRvQR 347
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQA-LPALEELEE-EELEELLAALGLPPDLSPEELLELlDRIEELQELLREAEELE-EE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 348 LHYEDLLNKQPQIRQIRQADG--------------QPLTGEQNRiLEAQLRTQRELLNSLLQGGDTLILEL------TKL 407
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDeeelraaleqaeeyQELKEELEE-LEEQLEELLGELEELLEALDEEELEEeleeleEEL 441
|
410 420
....*....|....*....|
gi 2047419976 408 KVSNSQLEDALKEVNEATHR 427
Cdd:COG4717 442 EELEEELEELREELAELEAE 461
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-366 |
5.20e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 57 EERK---GSLERAQQYQQVIDNFPKLSQTLRSQLNNLRDEPRevpvGLTSDALNQ-----EILQVSSQLLEKSRQAQQEQ 128
Cdd:TIGR00618 163 KEKKellMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ----LLTLCTPCMpdtyhERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 129 ERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARLKALVDELELAQLsannRQELSRMRA 208
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQI----EQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 209 ELAQKQ---SQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSANLPVGIVDQFKVNRELSAALNQQAQRMDlVASQ 285
Cdd:TIGR00618 315 ELQSKMrsrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 286 QRQATNQ---TLQVRQALNTLREQSQwlgssnllgEALRAQVARLPEMPKPQQLDTEMAQLRVQRlHYEDLLNKQPQIRQ 362
Cdd:TIGR00618 394 KLQSLCKeldILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYAELCAAAITC-TAQCEKLEKIHLQE 463
|
....
gi 2047419976 363 IRQA 366
Cdd:TIGR00618 464 SAQS 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-428 |
6.26e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 49 LQSALNALEERKGSLER----AQQYQQvidnfpklsqtlrsqlnnLRDEPREVPVGLTSDALNQEILQVSSQLLEKSRQA 124
Cdd:TIGR02168 191 LEDILNELERQLKSLERqaekAERYKE------------------LKAELRELELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 125 QQEQERAREIADSLSQLpqqqTDARRQLNEVERRVGTQagntpqsQAQNLGLQAESARLkalvdELELAQLSAnnrqels 204
Cdd:TIGR02168 253 EELEELTAELQELEEKL----EELRLEVSELEEEIEEL-------QKELYALANEISRL-----EQQKQILRE------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 205 rmRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENsanlpVGIVDQFKVNRELSAALNQqaqrmdlvas 284
Cdd:TIGR02168 310 --RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-----ESLEAELEELEAELEELES---------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 285 qqrqatnqtlqvrqALNTLREQSqwlgssnllgEALRAQVARLPempkpQQLDTEMAQLRVQRLHYEDLLNKQPQIRQIR 364
Cdd:TIGR02168 373 --------------RLEELEEQL----------ETLRSKVAQLE-----LQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047419976 365 QADGQPLTGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHRY 428
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
44-306 |
1.12e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 44 ETVESLQSALNALEERKGSL-ERAQQYQQVIDNFPKLSQTLRSQLNNLRDEPREVPVGLTS-----DALNQEILQVSSQ- 116
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELrEEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQElrekrDELNEKVKELKEEr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 117 --LLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVgtqagntpqsQAQNLGLQAEsarlKALVDelELAQ 194
Cdd:COG1340 81 deLNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ----------QTEVLSPEEE----KELVE--KIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 195 LsannRQELSRMRAELAQKQS-QQLDAYLQSLRNQLNSQRQREAERALESTELLAEnsanlpvgIVDQF-------KVNR 266
Cdd:COG1340 145 L----EKELEKAKKALEKNEKlKELRAELKELRKEAEEIHKKIKELAEEAQELHEE--------MIELYkeadelrKEAD 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2047419976 267 ELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQ 306
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
31-291 |
1.22e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.38 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 31 ELEQAKAAKPAQPETVESLQSALNALE--------ERKGSLERAQQYQQVIDNFPKLSQTL---RSQLNNLRDEPREVpv 99
Cdd:pfam05622 253 ELSQADALLSPSSDPGDNLAAEIMPAEireklirlQHENKMLRLGQEGSYRERLTELQQLLedaNRRKNELETQNRLA-- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 100 gltsdalNQEILQVSSQLlEKSRQAQQEQERAreiADSLSQLPQQQTDARRQLNEverrvgtqagntpqsqaqnlgLQAE 179
Cdd:pfam05622 331 -------NQRILELQQQV-EELQKALQEQGSK---AEDSSLLKQKLEEHLEKLHE---------------------AQSE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 180 SARLKALVDELE----------LAQLSANNRQELSRMRA-----------------ELAQKQSQQLDAYLQSLRNQLNSQ 232
Cdd:pfam05622 379 LQKKKEQIEELEpkqdsnlaqkIDELQEALRKKDEDMKAmeerykkyvekaksvikTLDPKQNPASPPEIQALKNQLLEK 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047419976 233 RQR--EAERALESTELLAENSANLPV------GIVDQFKVNRELSAALNQQAQRMdlvASQQRQATN 291
Cdd:pfam05622 459 DKKieHLERDFEKSKLQREQEEKLIVtawynmGMALHRKAIEERLAGLSSPGQSF---LARQRQATN 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-249 |
1.67e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVidnfpklsQTLRSQLNNLRDEPREVPVGLts 103
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--------PEIQAELSKLEEEVSRIEARL-- 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEI--LQVSSQLLEKSRqaQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESA 181
Cdd:TIGR02169 815 REIEQKLnrLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 182 RLKALVDELELAQLSANNRQELSRMRAEL----AQKQSQQLDAYLQSLRN--------------QLNSQRQREAERALES 243
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSElkakLEALEEELSEIEDPKGEdeeipeeelsledvQAELQRVEEEIRALEP 972
|
....*.
gi 2047419976 244 TELLAE 249
Cdd:TIGR02169 973 VNMLAI 978
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
24-424 |
1.80e-06 |
|
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: 52.53 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLE--RAQQYQQVIDNFPklsqTLRSQLNNL--RDEPREVPV 99
Cdd:pfam12128 295 LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLdaDIETAAADQEQLP----SWQSELENLeeRLKALTGKH 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 100 GLTSDALNQEILQVSSQLLE-----KSRQAQQEQERAREIADSLSQLPQQQTDARRQLNeverrvgtqAGNTPQSQAQnL 174
Cdd:pfam12128 371 QDVTAKYNRRRSKIKEQNNRdiagiKDKLAKIREARDRQLAVAEDDLQALESELREQLE---------AGKLEFNEEE-Y 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 175 GLQAESARLKALVD----ELELAQLSANNRQELSRMRAELAQKQSQQLDAY-----LQSLRNQLNSQRQREAERALESTE 245
Cdd:pfam12128 441 RLKSRLGELKLRLNqataTPELLLQLENFDERIERAREEQEAANAEVERLQselrqARKRRDQASEALRQASRRLEERQS 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 246 LLAENSANLpvgivdqFKVNRELSAALNQQAQ----------------RMDLVASQQRQATNQTLQVRQAlnTLREQSQW 309
Cdd:pfam12128 521 ALDELELQL-------FPQAGTLLHFLRKEAPdweqsigkvispellhRTDLDPEVWDGSVGGELNLYGV--KLDLKRID 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 310 LGSSNLLGEALRAQVARLPEM-----PKPQQLDTEMAQLRVQ------------------RLHYEDLLN-KQPQIRQIRQ 365
Cdd:pfam12128 592 VPEWAASEEELRERLDKAEEAlqsarEKQAAAEEQLVQANGElekasreetfartalknaRLDLRRLFDeKQSEKDKKNK 671
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047419976 366 A--DGQPLTGEQNRILEAQLRTQRELLNSLLQGGDTLILELT-----KLKVSNSQLEDALKEVNEA 424
Cdd:pfam12128 672 AlaERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtekqaYWQVVEGALDAQLALLKAA 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-408 |
1.91e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 47 ESLQSALNALEERKGSLERAQQY-QQVIDNFPKLS----QTLRSQlnNLRDEPREVPVGLTS---DALNQEILQVSSQLL 118
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIiDEKRQQLERLRrereKAERYQ--ALLKEKREYEGYELLkekEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 119 EKSRQAQQEQERAREIADSLSQLPQQqtdaRRQLNEVERRVGtqAGNTPQSQAQNLGLQAESARLKALVDELELAQLSAN 198
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQL----LEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 199 NRQ-----ELSRMRAELA---------QKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSanlpvgivdqfKV 264
Cdd:TIGR02169 322 ERLakleaEIDKLLAEIEelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK-----------DY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 265 NRELSAA---LNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNL-LGEALRAQVARLPEMPKpqQLDTEM 340
Cdd:TIGR02169 391 REKLEKLkreINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAA--DLSKYE 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047419976 341 AQLRVQRLHYEDLLNKQPQI-RQIRQADGQPLTGEQNrilEAQLRTQRELLNSLLQGGDTLILELTKLK 408
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLqRELAEAEAQARASEER---VRGGRAVEEVLKASIQGVHGTVAQLGSVG 534
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
30-387 |
2.64e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.68 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEQAKAAKPA---QPETVESLQSALNALEERKGSLE---RAQQYQQvidnfpklsqtlRSQLNNLRDEPREVPVGLTS 103
Cdd:pfam07111 282 QEEELTRKIQPSdslEPEFPKKCRSLLNRWREKVFALMvqlKAQDLEH------------RDSVKQLRGQVAELQEQVTS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEILQVSSQllEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLG----LQAE 179
Cdd:pfam07111 350 QSQEQAILQRALQ--DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETtmtrVEQA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 180 SARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQ---------LDAYLQSLRNQLNSQRQR-EAERALESTELLAE 249
Cdd:pfam07111 428 VARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScpppppappVDADLSLELEQLREERNRlDAELQLSAHLIQQE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 250 NSANLPVGIVDQFKVNrELSAALNQQAQR-----------MDLVASQQRQATNQTLQVRQALNTLREqsqwlgssnLLGE 318
Cdd:pfam07111 508 VGRAREQGEAERQQLS-EVAQQLEQELQRaqeslasvgqqLEVARQGQQESTEEAASLRQELTQQQE---------IYGQ 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047419976 319 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLHYEDLLN-KQPQIRQIRQAD-GQPLT--GEQNRILEAQLRTQR 387
Cdd:pfam07111 578 ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSlRQIQHRATQEKErNQELRrlQDEARKEEGQRLARR 650
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
65-419 |
3.78e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 65 RAQQYQQVID--NFPKLSQTLRSQLNNLRDEPrEVPVGLTSDALNQEILQVSSQ------LLEKSRQAQQEQERAREIAD 136
Cdd:PRK10246 369 RAQFSQQTSDreQLRQWQQQLTHAEQKLNALP-AITLTLTADEVAAALAQHAEQrplrqrLVALHGQIVPQQKRLAQLQV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 137 SLSQLPQQQTDARRQLNEVERRVGTQAGNTP------QSQAQNLGLQAESARLKA-------------LVDELELAQLSA 197
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMRQRYKEKTQQLAdvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGV 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 198 NN--RQELSRMRAELAQKQSQ---QLDAYLQSL-RNQLNSQRQREAERALesTELLAENSANLPVGIVDQFKVNRELSAA 271
Cdd:PRK10246 528 NQsrLDALEKEVKKLGEEGAAlrgQLDALTKQLqRDESEAQSLRQEEQAL--TQQWQAVCASLNITLQPQDDIQPWLDAQ 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 272 ------LNQQAQRMDLvasqQRQATNQTLQVRQAlntlreQSQWLGSSNLLGEALRAQVARLPEMPKP------------ 333
Cdd:PRK10246 606 eeherqLRLLSQRHEL----QGQIAAHNQQIIQY------QQQIEQRQQQLLTALAGYALTLPQEDEEaswlatrqqeaq 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 334 --QQLDTEMAQLRVQRLHYEDLLNKQPQiRQIRQADGQPLTGEQNR-------ILEAQLRTQRELlnsllqggdtLILEL 404
Cdd:PRK10246 676 swQQRQNELTALQNRIQQLTPLLETLPQ-SDDLPHSEETVALDNWRqvheqclSLHSQLQTLQQQ----------DVLEA 744
|
410
....*....|....*
gi 2047419976 405 TKLKVSNSQLEDALK 419
Cdd:PRK10246 745 QRLQKAQAQFDTALQ 759
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
83-286 |
5.83e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 83 LRSQLNNLRDEPREvpvglTSDALNQeiLQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQ 162
Cdd:COG3206 180 LEEQLPELRKELEE-----AEAALEE--FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 163 AGNTPqSQAQNLGLQAESARLKALvdELELAQLSANNR------QELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQRE 236
Cdd:COG3206 253 PDALP-ELLQSPVIQQLRAQLAEL--EAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2047419976 237 AE--RALESTELLAENSANLPVGIVD---QFKVNRELSAALNQQAQRMDLVASQQ 286
Cdd:COG3206 330 ASlqAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEARLAEALT 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-252 |
6.87e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 27 QITQELEQAKAakpaqpeTVESLQSALNALEER-KGSLERAQQYQQVIDNfpklsqtLRSQLNNLRDEPREVPVGLtsDA 105
Cdd:TIGR02169 291 RVKEKIGELEA-------EIASLERSIAEKERElEDAEERLAKLEAEIDK-------LLAEIEELEREIEEERKRR--DK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 106 LNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESARLKA 185
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 186 LVDELELAQLSAnnRQELSRMRAELAQKQsQQLDAYLQSLRNQLNSQRQREAER---ALESTELLAENSA 252
Cdd:TIGR02169 435 KINELEEEKEDK--ALEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELsklQRELAEAEAQARA 501
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-401 |
7.37e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEILQVSSQLLEKSRQAQQ-EQERAREIADSLSQLPQQQ-TDARRQLNEVERRVGTQAGNTPQSQAQNLGLQAESA 181
Cdd:COG3096 795 DELAEQYAKASFDVQKLQRLHQAfSQFVGGHLAVAFAPDPEAElAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 182 RLKALV------DELELAQLSANNRQELSRM---RAELAQ--KQSQQLDAYLQSLRN------QLN------SQRQREAE 238
Cdd:COG3096 875 LLNKLLpqanllADETLADRLEELREELDAAqeaQAFIQQhgKALAQLEPLVAVLQSdpeqfeQLQadylqaKEQQRRLK 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 239 RALESTELLAENSANL----PVGIVDQfkvNRELSAALNQQAQRMDLVASQQRQAT-------NQTLQVRQALNTLREQS 307
Cdd:COG3096 955 QQIFALSEVVQRRPHFsyedAVGLLGE---NSDLNEKLRARLEQAEEARREAREQLrqaqaqySQYNQVLASLKSSRDAK 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 308 QwlgssNLLGEALRaqvaRLPEMpkPQQLDTEM---AQLRVQRLHYE--------DLLNKQpqiRQIRQADGQPLTGEQn 376
Cdd:COG3096 1032 Q-----QTLQELEQ----ELEEL--GVQADAEAeerARIRRDELHEElsqnrsrrSQLEKQ---LTRCEAEMDSLQKRL- 1096
|
330 340
....*....|....*....|....*
gi 2047419976 377 RILEAQLRTQRELLNSLLQGGDTLI 401
Cdd:COG3096 1097 RKAERDYKQEREQVVQAKAGWCAVL 1121
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-427 |
7.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 44 ETVESLQSALNALEERKGSLERAQQYQQvidnfpklsqTLRSQLNNLRDEprevpvgltsdalnQEILQVSSQLLEKSRQ 123
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE----------ELEEELEELEAE--------------LEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 124 AQQEQERAREIADSLSQLPQQQTDARRQLNEVERRvgtqagntpqsQAQNLGLQAESARLKALVDELeLAQLSANNRQEL 203
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELREL-----------EEELEELEAELAELQEELEEL-LEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 204 SRMRAEL--AQKQSQQLDAYLQSLRNQLNSQRQR--EAERALESTELLAENSANLPVGIVdqfkvnreLSAALNQQAQRM 279
Cdd:COG4717 195 QDLAEELeeLQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARLLLLI--------AAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 280 DLVASQQRQATnqTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRV-QRLHYEDLLNKQP 358
Cdd:COG4717 267 SLLSLILTIAG--VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLD 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047419976 359 QIRQIRQADGQpLTGEQNRILEAQLRTQRELLnsLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHR 427
Cdd:COG4717 345 RIEELQELLRE-AEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
15-395 |
1.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 15 MGAYAATAPDAKQITQELEQAKAAKpaqpETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRSQLNNLRDEP 94
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAEL----EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 95 REVpvgltsDALNQEILQVSSQLLEKSRQAQQEQERA-REIADSLSQLPQQQTDARRQLNEVERRVGTQagntpQSQAQN 173
Cdd:COG4717 163 EEL------EELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEEL-----EEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 174 LGLQAESARLKALVDELELAQL-----------------SANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQRE 236
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLiaaallallglggsllsLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 237 AERALESTELLAE------NSANLPVGIVDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTL----------QVRQAL 300
Cdd:COG4717 312 ALEELEEEELEELlaalglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagvedeeELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 301 NTLREQSQWLGSSNLLGEALRAQ---VARLPEMPKPQQLDTEMAQLRVQRLHYEDLLNK-QPQIRQIRQADGQPLTGEQN 376
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEElREELAELEAELEQLEEDGEL 471
|
410
....*....|....*....
gi 2047419976 377 RILEAQLRTQRELLNSLLQ 395
Cdd:COG4717 472 AELLQELEELKAELRELAE 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
123-424 |
1.11e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 123 QAQQEQERAREIADSLSQLPQQQTDARRQLNEV--ERRVGTQAGNTPQSQAQNLG--LQAESARLKALVDEL-ELAQLSA 197
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELsqELSDASRKIGEIEKEIEQLEqeEEKLKERLEELEEDLsSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 198 NNRQELSRMRAELAQKQSQ--QLDAYLQSLRNQLNSQRQREAERALESTE-LLAENSANLpvgivdqfkvnRELSAALNQ 274
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDlhKLEEALNDLEARLSHSRIPEIQAELSKLEeEVSRIEARL-----------REIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 275 QAQRMDLvASQQRQatnqTLQVRQALNTLREQSqwlgssnlLGEALRAQVARLPEmpkpqqLDTEMAQLRVQRLHYEDLL 354
Cdd:TIGR02169 824 LTLEKEY-LEKEIQ----ELQEQRIDLKEQIKS--------IEKEIENLNGKKEE------LEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 355 NKqpqirqirqadgqpLTGEQNRiLEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEA 424
Cdd:TIGR02169 885 GD--------------LKKERDE-LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
17-306 |
1.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 17 AYAATAPDAKQITQELEQAKAAKPA-------QPET----VESLQSALNALEERkgsLERAQQYQQVIDNFPKLSQTLRS 85
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGlsalnrlLPRLnllaDETLADRVEEIREQ---LDEAEEAKRFVQQHGNALAQLEP 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 86 QLNNLRDEPREVpvgltsDALNQEILqvssqlleksrQAQQEQERAREIADSLSQLpqqqtdarrqlneVERRVGTQAGN 165
Cdd:PRK04863 926 IVSVLQSDPEQF------EQLKQDYQ-----------QAQQTQRDAKQQAFALTEV-------------VQRRAHFSYED 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 166 TPQSQAQNLGLQaesARLKALVDELElaqlsannrQELSRMRAELAQKQsQQLDAYLQsLRNQLNSQRQREAERALESTE 245
Cdd:PRK04863 976 AAEMLAKNSDLN---EKLRQRLEQAE---------QERTRAREQLRQAQ-AQLAQYNQ-VLASLKSSYDAKRQMLQELKQ 1041
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047419976 246 LLAENSANLPVGIVDQFKVNR-ELSAALNQQAQRMDLV----ASQQRQATNQTLQVRQA---LNTLREQ 306
Cdd:PRK04863 1042 ELQDLGVPADSGAEERARARRdELHARLSANRSRRNQLekqlTFCEAEMDNLTKKLRKLerdYHEMREQ 1110
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-423 |
1.49e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 17 AYAATAPDAKQITQELEQAKAAKPAQPETVE--SLQSALNALEERKgslERAQQYQQVIDNFPKLSQTLRSQLNNLRDEP 94
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQSLKERE---QQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 95 REV----------------PVGLTS---------DALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDAR 149
Cdd:TIGR00618 504 CPLcgscihpnparqdidnPGPLTRrmqrgeqtyAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 150 RQLNeverrvgtqagntpqsqaqnlGLQAESARLKALVDELELAQlsannRQELSRMRAELAQKQSQQlDAYLQSLRNQL 229
Cdd:TIGR00618 584 EDIP---------------------NLQNITVRLQDLTEKLSEAE-----DMLACEQHALLRKLQPEQ-DLQDVRLHLQQ 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 230 NSQRQREAERALESTELlaensaNLPV-GIVDQFKVNRELSAALNQQAQR-MDLVASQQRQATNQTLQVRQALNTLREQS 307
Cdd:TIGR00618 637 CSQELALKLTALHALQL------TLTQeRVREHALSIRVLPKELLASRQLaLQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 308 QWLGSS--------------------------NLLGEALRAQVARL-----------PEMPKPQQLDTEMAQLRV----- 345
Cdd:TIGR00618 711 THIEEYdrefneienassslgsdlaaredalnQSLKELMHQARTVLkarteahfnnnEEVTAALQTGAELSHLAAeiqff 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 346 QRLHYED---LLNKQPQIRQIRQADGQPLTGEQNRIL--EAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKE 420
Cdd:TIGR00618 791 NRLREEDthlLKTLEAEIGQEIPSDEDILNLQCETLVqeEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
...
gi 2047419976 421 VNE 423
Cdd:TIGR00618 871 IIQ 873
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-428 |
2.06e-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: 48.89 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 13 LSMGAYAATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRSQLNNLRD 92
Cdd:TIGR00606 207 MELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 93 E---PREVPVGLTSDALNQeilqvssqlLEKSRQA---QQEQERAReIADSLSQLPQQQTDARRQLNEVERRVGTQAGNT 166
Cdd:TIGR00606 287 ElelKMEKVFQGTDEQLND---------LYHNHQRtvrEKERELVD-CQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 167 PQSQAQNLG--LQAESARLKALVDELE---LAQLSANNRQELSRMRAELAQKQSQQLDAYLQSlrnqlnsqRQREAERAL 241
Cdd:TIGR00606 357 DRHQEHIRArdSLIQSLATRLELDGFErgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS--------KERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 242 esTELLAENSANLPVGIVDQFKVNRELSAALNQQAQRMDLVASQQRqatnqTLQVRQAL-NTLREQSQWLGSSN---LLG 317
Cdd:TIGR00606 429 --DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR-----ILELDQELrKAERELSKAEKNSLtetLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 318 EALRAQVARLPEMPKPQQLDTEMAQL------RVQRLHY-EDLLNKQPQIRQIRQADGQPLTGE-----QNRILEAQLRT 385
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQLEDWLHS 581
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2047419976 386 QRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHRY 428
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-423 |
2.67e-05 |
|
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: 48.48 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAA-KPAQPE---TVESLQSALNALEERKGSLERAQQyqqVIDNFPKLSQTLRSQLNNLRDEPREvpv 99
Cdd:TIGR04523 233 NIEKKQQEINEKTTEiSNTQTQlnqLKDEQNKIKKQLSEKQKELEQNNK---KIKELEKQLNQLKSEISDLNNQKEQ--- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 100 GLTSDaLNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDA-------RRQLNEVERRVGTQagntpqsQAQ 172
Cdd:TIGR04523 307 DWNKE-LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesensekQRELEEKQNEIEKL-------KKE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 173 NLGLQAESARLKALVDELElaqlsannrQELSRmraelAQKQSQQLDAYLQSLRNQLNsQRQREAERALESTELLAENSA 252
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLE---------SKIQN-----QEKLNQQKDEQIKKLQQEKE-LLEKEIERLKETIIKNNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 253 NLPVGIVDQFKVNRELSAALNQQAQRMDLVaSQQRQATNQTLQVRQA--------LNTLREQSQWLGSSNllgEALRAQV 324
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVL-SRSINKIKQNLEQKQKelkskekeLKKLNEEKKELEEKV---KDLTKKI 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 325 ARLPEmpKPQQLDTEMAQLRVQ-------------RLHYEDL----LNKQPQIRQIRQadgqpltgEQNRILEAQLRTQr 387
Cdd:TIGR04523 520 SSLKE--KIEKLESEKKEKESKisdledelnkddfELKKENLekeiDEKNKEIEELKQ--------TQKSLKKKQEEKQ- 588
|
410 420 430
....*....|....*....|....*....|....*.
gi 2047419976 388 ELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNE 423
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
30-536 |
4.14e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEQAKAAKPAQPETVEslQSALNALEERKGSLERAQQYQQvidnfpklsqtlrsQLNNLRDEPREVPVGLTSDALnQE 109
Cdd:COG3064 16 ERLEQAEAEKRAAAEAEQ--KAKEEAEEERLAELEAKRQAEE--------------EAREAKAEAEQRAAELAAEAA-KK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 110 ILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQ-LNEVERRVGTQAgntpqsqaqnlGLQAESARLKAlvd 188
Cdd:COG3064 79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEkAEEAKRKAEEEA-----------KRKAEEERKAA--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 189 elelaqlsannrQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSANLPVGIVDQFKVNREL 268
Cdd:COG3064 145 ------------EAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 269 SAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRL 348
Cdd:COG3064 213 DAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 349 HYEDLLNKQPQIRQIRQADGQPL-TGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHR 427
Cdd:COG3064 293 AGLVLDDSAALAAELLGAVAAEEaVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 428 YLFWTSDVRPMTFSWPIEIVQDLRRLISLDTFSQLGQASVMMITSKETIFPLLGALILVGFSIYSRRHFTRFLERSSARV 507
Cdd:COG3064 373 GALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIG 452
|
490 500
....*....|....*....|....*....
gi 2047419976 508 GKVTQDHFWLTLRTVFWSILVASPLPVLW 536
Cdd:COG3064 453 KALTGDADALLGILKAVALDGGAVLADLL 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
47-423 |
4.19e-05 |
|
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: 47.71 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 47 ESLQSALNALEERKGSLERA-----QQYQQ------VIDNFPKLSQTLRSQLNNLRDEPREvpvgLTSDA--LNQEILQV 113
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNidkikNKLLKlelllsNLKKKIQKNKSLESQISELKKQNNQ----LKDNIekKQQEINEK 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 114 SSQLLEKsrqaqQEQerareiadsLSQLPQQQTDARRQLNEVERRVGTQAG---------NTPQSQAQNLGLQAESARLK 184
Cdd:TIGR04523 245 TTEISNT-----QTQ---------LNQLKDEQNKIKKQLSEKQKELEQNNKkikelekqlNQLKSEISDLNNQKEQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 185 ALVDELE---------LAQLSANNrQELSRMRAELAQ--KQSQQLDAYLQSLRNQLNsQRQREAERALESTELLAENSAN 253
Cdd:TIGR04523 311 ELKSELKnqekkleeiQNQISQNN-KIISQLNEQISQlkKELTNSESENSEKQRELE-EKQNEIEKLKKENQSYKQEIKN 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 254 LPVGIVDqfkvnrelsaaLNQQAQRMDLVaSQQRQATNQTLQvrQALNTLREQSQWLGSSNllgEALRAQVARLPEmpkp 333
Cdd:TIGR04523 389 LESQIND-----------LESKIQNQEKL-NQQKDEQIKKLQ--QEKELLEKEIERLKETI---IKNNSEIKDLTN---- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 334 qqldtemaQLRVQRLHYEDLLNKQPQIRQIRQAdgqpLTGEQNRILEAQLRTQRELlnsllqggDTLILELTKLKVSNSQ 413
Cdd:TIGR04523 448 --------QDSVKELIIKNLDNTRESLETQLKV----LSRSINKIKQNLEQKQKEL--------KSKEKELKKLNEEKKE 507
|
410
....*....|
gi 2047419976 414 LEDALKEVNE 423
Cdd:TIGR04523 508 LEEKVKDLTK 517
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
25-252 |
4.75e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 25 AKQITQELEQAKAAKpaqpETVESLQSALNALE-ERK------------GSLERAQQYQQVIDnfpkLSQTLRSQLNNLR 91
Cdd:pfam15709 321 SKALLEKREQEKASR----DRLRAERAEMRRLEvERKrreqeeqrrlqqEQLERAEKMREELE----LEQQRRFEEIRLR 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 92 DEPREvpvgltsdalnQEILQVSSQLLEKSRQAQQEQERAReiadslsqlpQQQTDARRQLNEVERRvgtqagnTPQSQA 171
Cdd:pfam15709 393 KQRLE-----------EERQRQEEEERKQRLQLQAAQERAR----------QQQEEFRRKLQELQRK-------KQQEEA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 172 QNlgLQAESARLKALVDEL-----ELAQLSANNRQELSRMRAELAQKQSQQLDaylqslrnqlnSQRQREAERA---LES 243
Cdd:pfam15709 445 ER--AEAEKQRQKELEMQLaeeqkRLMEMAEEERLEYQRQKQEAEEKARLEAE-----------ERRQKEEEAArlaLEE 511
|
....*....
gi 2047419976 244 TELLAENSA 252
Cdd:pfam15709 512 AMKQAQEQA 520
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
116-304 |
6.28e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 116 QLLEKSRQ-AQQEQERARE-----IADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSqAQNL-----GLQaESArlk 184
Cdd:NF041483 717 ETLGSARAeADQERERAREqseelLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQT-AQQVrdsvaGLQ-EQA--- 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 185 alvdELELAQLSANNRQELSRMRAElAQKQSQQL--DAYLQSLRNQLNSQR-QREAERALESTELLAENSANlpvgivDQ 261
Cdd:NF041483 792 ----EEEIAGLRSAAEHAAERTRTE-AQEEADRVrsDAYAERERASEDANRlRREAQEETEAAKALAERTVS------EA 860
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2047419976 262 FKVNRELSAALNQQAQRM-----DLVASQQRQATNQTLQVRQALNTLR 304
Cdd:NF041483 861 IAEAERLRSDASEYAQRVrteasDTLASAEQDAARTRADAREDANRIR 908
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-427 |
7.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 27 QITQELEQAKAAkpaqpetVESLQSALNALEERKGSLERAQQYQ--QVIDNFPKLSQTLRSQLNNLRDEPR--------- 95
Cdd:COG4913 299 ELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLERELEERERRRArleallaal 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 96 EVPVGLTSDALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRvgtqAGNTPQSQAQNLG 175
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR----KSNIPARLLALRD 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 176 LQAESARLKAlvDEL----ELAQLSAnnRQELSRMRAELA-----------QKQSQQLDAYLQS--LRNQLNSQRQREAE 238
Cdd:COG4913 448 ALAEALGLDE--AELpfvgELIEVRP--EEERWRGAIERVlggfaltllvpPEHYAAALRWVNRlhLRGRLVYERVRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 239 RALESTELLaENSAnlpVGIVDqFKVNrELSAALNQQ-AQRMDL--VASQQ-----RQATNQTLQVRQAlNTLRE--QSQ 308
Cdd:COG4913 524 PDPERPRLD-PDSL---AGKLD-FKPH-PFRAWLEAElGRRFDYvcVDSPEelrrhPRAITRAGQVKGN-GTRHEkdDRR 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 309 WLGSSNLLG-------EALRAQVARLPE-----MPKPQQLDTEMAQLRVQRLHYEDLLNKQPQIRQIRQAdgqpltgeqn 376
Cdd:COG4913 597 RIRSRYVLGfdnraklAALEAELAELEEelaeaEERLEALEAELDALQERREALQRLAEYSWDEIDVASA---------- 666
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2047419976 377 rilEAQLRTQRELLNSLLQGGDtlilELTKLKvsnSQLEDALKEVNEATHR 427
Cdd:COG4913 667 ---EREIAELEAELERLDASSD----DLAALE---EQLEELEAELEELEEE 707
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-249 |
9.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 32 LEQAKAAKpAQPETVESLQSALNALEERKGSLERAQQYQQVIdnfpklsQTLRSQLNNLRDEprevpvgltSDALNQEIL 111
Cdd:COG4913 224 FEAADALV-EHFDDLERAHEALEDAREQIELLEPIRELAERY-------AAARERLAELEYL---------RAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 112 QVSSQLLEK-SRQAQQEQERAREiadSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQS-QAQNLGLQAE-------SAR 182
Cdd:COG4913 287 QRRLELLEAeLEELRAELARLEA---ELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLEREleererrRAR 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047419976 183 LKALVDELELAqlSANNRQELSRMRAELAQkQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAE 249
Cdd:COG4913 364 LEALLAALGLP--LPASAEEFAALRAEAAA-LLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
56-192 |
1.17e-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: 45.39 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 56 LEERKGSLERAQQYQQVIDNF-PKLS---QTLRSQLNNLRDEPREVPVGLTS--DALNQEILQVSSQLLEKSRQAQQEQE 129
Cdd:smart00787 153 LEGLKEDYKLLMKELELLNSIkPKLRdrkDALEEELRQLKQLEDELEDCDPTelDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047419976 130 RAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQsqaqnlglqaESARLKALVDELEL 192
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK----------EIEKLKEQLKLLQS 285
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
19-322 |
1.23e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 19 AATAPDAKQITQELEQAK--AAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLS--------QTLRSQLN 88
Cdd:pfam09731 189 EALAEKLKEVINLAKQSEeeAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVaserivfqQELVSIFP 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 89 NLRDEPREVPVGLTSDA------LNQEILQVSSQLLEKSRQAQQEQERAreiadslsqLPQQQTDARRQLNEVERRVgtq 162
Cdd:pfam09731 269 DIIPVLKEDNLLSNDDLnsliahAHREIDQLSKKLAELKKREEKHIERA---------LEKQKEELDKLAEELSARL--- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 163 agntpqsqaqnlglqaesarlkalvdELELAQLSANNRQELSRMRAELAQKQSQQLDAYL--------QSLRNQLNSQRQ 234
Cdd:pfam09731 337 --------------------------EEVRAADEAQLRLEFEREREEIRESYEEKLRTELerqaeaheEHLKDVLVEQEI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 235 ---REAERALEstELLAENSANLpvgivdQFKVNrELSAALNQqaqrMDLVASQQRQATNQTLQVRQ------ALNTLRE 305
Cdd:pfam09731 391 elqREFLQDIK--EKVEEERAGR------LLKLN-ELLANLKG----LEKATSSHSEVEDENRKAQQlwlaveALRSTLE 457
|
330
....*....|....*..
gi 2047419976 306 QSQWLGSSNLLGEALRA 322
Cdd:pfam09731 458 DGSADSRPRPLVRELKA 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-425 |
1.44e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 19 AATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQ-QYQQVIDNFPKLSQTLRSQLNNLRDEprev 97
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAaELAAQLEELEEAEEALLERLERLEEE---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 98 pvgltSDALNQEILQVSSQLLEkSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQ 177
Cdd:COG1196 423 -----LEELEEALAELEEEEEE-EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 178 AESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSAN---- 253
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratf 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 254 LPVGIVDQfkvnRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARL----PE 329
Cdd:COG1196 577 LPLDKIRA----RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLrevtLE 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 330 MPKPQQLDTEMAQLRVQRLHYEDLLNKQPQIRQIRQADGQPLTGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKV 409
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
410
....*....|....*.
gi 2047419976 410 SNSQLEDALKEVNEAT 425
Cdd:COG1196 733 EREELLEELLEEEELL 748
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
81-254 |
1.51e-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: 44.53 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 81 QTLRSQLNNLRDEPREVPvgltsdalnQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVG 160
Cdd:COG1579 13 QELDSELDRLEHRLKELP---------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 161 tQAGNTPQSQAqnlgLQAESARLKALVDELELAQLSANNRQE-----LSRMRAELAQKQsQQLDAYLQSLRNQLNSQRQR 235
Cdd:COG1579 84 -NVRNNKEYEA----LQKEIESLKRRISDLEDEILELMERIEeleeeLAELEAELAELE-AELEEKKAELDEELAELEAE 157
|
170
....*....|....*....
gi 2047419976 236 EAERALESTELLAENSANL 254
Cdd:COG1579 158 LEELEAEREELAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-424 |
2.60e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 193 AQLSANNRQELSRMRAELAQKQS--QQLDAYLQSLRNQLNSQRQR--EAERALESTEL-LAENSANLPVGIVDQFKVNRE 267
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKelAALKKEEKALLKQLAALERRiaALARRIRALEQeLAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 268 LSAalnQQAQRMDLVASQQRQATNQTLQVrqaLNTLREQSQWLGSSNLLGEALRAQVARLpempkpQQLDTEMAQLRVQR 347
Cdd:COG4942 99 LEA---QKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVRRLQYLKYLAPARREQA------EELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047419976 348 lhyEDLLNKQPQIRQIRQAdgqplTGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEA 424
Cdd:COG4942 167 ---AELEAERAELEALLAE-----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-356 |
2.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAqqyqqvIDNFPKLSQTLRSQLNNLRDEPREVPVGLTS 103
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD------LGNAEDFLEELREERDELREREAELEATLRT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DalnQEILQVSSQLLEKSR-----QAQQEQERAREIADS---LSQLPQQQTDARRQLNEVERRVgTQAgntpqSQAQNLG 175
Cdd:PRK02224 438 A---RERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDrerVEELEAELEDLEEEVEEVEERL-ERA-----EDLVEAE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 176 LQAES--ARLKALVDELELAQLSANNRQElsrmRAELAQKQSQQLDAYLQSLRNQLNSQRQrEAERALESTELLAENSAN 253
Cdd:PRK02224 509 DRIERleERREDLEELIAERRETIEEKRE----RAEELRERAAELEAEAEEKREAAAEAEE-EAEEAREEVAELNSKLAE 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 254 LPVGIvDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGS----SNLlgEALRAQVARLPE 329
Cdd:PRK02224 584 LKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefdeARI--EEAREDKERAEE 660
|
330 340
....*....|....*....|....*..
gi 2047419976 330 MpkPQQLDTEMAQLRVQRlhyEDLLNK 356
Cdd:PRK02224 661 Y--LEQVEEKLDELREER---DDLQAE 682
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-242 |
3.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQ----YQQVI-------DNFPKLSQTLRSQLNNLRD 92
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAeiedLRETIaetererEELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 93 EPREV--PVGLTS----------DALNQEILQVSSQLLEKSRQAQQ---EQERAREIADslsQLPQQQTDARRQLNEVER 157
Cdd:PRK02224 294 ERDDLlaEAGLDDadaeavearrEELEDRDEELRDRLEECRVAAQAhneEAESLREDAD---DLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 158 RVGT--QAGNTPQSQAQNLGLQAESARLK---ALVDELELAQLSANNRQELSRMRAELAqkqsqQLDAYLQSLRNqlnsq 232
Cdd:PRK02224 371 ELEEarEAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDFLEELREERDELREREA-----ELEATLRTARE----- 440
|
250
....*....|
gi 2047419976 233 RQREAERALE 242
Cdd:PRK02224 441 RVEEAEALLE 450
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
31-299 |
3.83e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 31 ELE--QAKAAKPA--QPETVESLQSALNAL-EERKGSLERAQQYQQvidnfpklsqtlrsQLNNLRDEprevpvgltsDA 105
Cdd:PRK10246 199 ELEklQAQASGVAllTPEQVQSLTASLQVLtDEEKQLLTAQQQQQQ--------------SLNWLTRL----------DE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 106 LNQEiLQVSSQLLEKSRQAQ---QEQERAREIADSLSQL------PQQQTDA----RRQLNEV--------ERRVGTQAG 164
Cdd:PRK10246 255 LQQE-ASRRQQALQQALAAEekaQPQLAALSLAQPARQLrphwerIQEQSAAlahtRQQIEEVntrlqstmALRARIRHH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 165 NTPQSQAqnlgLQAESARLKALVDELELAQLSannRQELSRMRAELAQKQSQQldAYLQSLRNQLNSQRQREAERALEST 244
Cdd:PRK10246 334 AAKQSAE----LQAQQQSLNTWLAEHDRFRQW---NNELAGWRAQFSQQTSDR--EQLRQWQQQLTHAEQKLNALPAITL 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2047419976 245 ELLAENSANLPVGIVDQFKVNRELSAALNQQAQRMDLVAsqQRQATNQTLQVRQA 299
Cdd:PRK10246 405 TLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLA--QLQVAIQNVTQEQT 457
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
104-313 |
3.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQ--------------S 169
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYldvllgsesfsdflD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 170 QAQNLGLQAESAR-----LKALVDELELAQLSANN-RQELSRMRAELAQKQsQQLDAYLQSLRNQLNSQRQREAERALES 243
Cdd:COG3883 120 RLSALSKIADADAdlleeLKADKAELEAKKAELEAkLAELEALKAELEAAK-AELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 244 TELLAENSANLPVGIVDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSS 313
Cdd:COG3883 199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
28-423 |
6.82e-04 |
|
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: 43.79 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 28 ITQELEQAKAAKPAQPETVESLQsalNALEERKGS---LERAQQYQQVIDNFPKLSQTLRSQLNNLRDeprevpvglTSD 104
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIK---ESETGNLGSestLLEKAKEIINIEEALKGFQDPESELEDLAQ---------TSD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 105 ALNQEILQVSSQLLEKSRQaqqEQERAREIADSLSQLPQQQTDARRQLNEVErrvgtqagntpQSQAQNLGLQAESARLK 184
Cdd:COG5185 254 KLEKLVEQNTDLRLEKLGE---NAESSKRLNENANNLIKQFENTKEKIAEYT-----------KSIDIKKATESLEEQLA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 185 ALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYlQSLRNQLNS----QRQREAERALESTEL-LAENSANLPVGIV 259
Cdd:COG5185 320 AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL-EAIKEEIENivgeVELSKSSEELDSFKDtIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 260 DQFKVNRELSAALNqqaqrmDLVASQQRQATNQTLQVRQALNTLREqsqwlgSSNLLGEALRAQVARLPEMPKPQQLDTE 339
Cdd:COG5185 399 NQRGYAQEILATLE------DTLKAADRQIEELQRQIEQATSSNEE------VSKLLNELISELNKVMREADEESQSRLE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 340 MAQLRVQRLHYEDLLNKQPQIRQIRQadgqpltgeQNRILEAQLRTQRELLNSLLQGGDTLILELT-KLKVSNSQLEDAL 418
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIES---------RVSTLKATLEKLRAKLERQLEGVRSKLDQVAeSLKDFMRARGYAH 537
|
....*
gi 2047419976 419 KEVNE 423
Cdd:COG5185 538 ILALE 542
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
26-135 |
7.54e-04 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 42.19 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 26 KQITQELEQAKaakpAQPETVESLQSALNALEERKGSLERAQQYQQVIDNfPKLSQTLRSQLNNLRDEPrevpvgltsda 105
Cdd:NF038305 111 QQINQQAGQQE----TQLQQQLNQLQAQTSPQQLNQLLKSEQKQGQALAS-GQLPEEQKEQLQQFKSNP----------- 174
|
90 100 110
....*....|....*....|....*....|
gi 2047419976 106 lnQEILQVSSQLLEKSRQAQQEQERAREIA 135
Cdd:NF038305 175 --QALDKFLAQQLTQIRTQAEEAEKQARLE 202
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-424 |
8.61e-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: 43.63 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 27 QITQELEQAK-------AAKPAQPETVESLQSALNALEERKGSLE--RAQQYQQVIDNFPKLSQTLRS------QLNNLR 91
Cdd:pfam01576 360 ELTEQLEQAKrnkanleKAKQALESENAELQAELRTLQQAKQDSEhkRKKLEGQLQELQARLSESERQraelaeKLSKLQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 92 DEPREVpVGLTSDA------LNQEILQVSSQL-----------------------LEKSRQAQQEQ-----ERAREIADS 137
Cdd:pfam01576 440 SELESV-SSLLNEAegknikLSKDVSSLESQLqdtqellqeetrqklnlstrlrqLEDERNSLQEQleeeeEAKRNVERQ 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 138 LSQLPQQQTDARRQLNEVERRV--GTQAGNTPQSQAQNLGLQAES------------ARLKALVDELELAQlsANNRQEL 203
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEDAGTLeaLEEGKKRLQRELEALTQQLEEkaaaydklektkNRLQQELDDLLVDL--DHQRQLV 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 204 SRMraELAQKQSQQLDAYLQSLRNQLNSQRQR-EAE------RALESTELLAENsanlpVGIVDQF-KVNRELSAALNqq 275
Cdd:pfam01576 597 SNL--EKKQKKFDQMLAEEKAISARYAEERDRaEAEareketRALSLARALEEA-----LEAKEELeRTNKQLRAEME-- 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 276 aqrmDLVASQQRQATN--------QTLQvrQALNTLREQSQwlgssNLLGEALRAQVARLpempkpqQLDTEMAQLRVQr 347
Cdd:pfam01576 668 ----DLVSSKDDVGKNvhelerskRALE--QQVEEMKTQLE-----ELEDELQATEDAKL-------RLEVNMQALKAQ- 728
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047419976 348 lHYEDLLNKQPQIRQIRQAdgqplTGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKvsnSQLEDALKEVNEA 424
Cdd:pfam01576 729 -FERDLQARDEQGEEKRRQ-----LVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELE---AQIDAANKGREEA 796
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-243 |
9.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEE----RKGSL-ERAQQYQQVIDNFPKLSQTLRSQ-----LNNLrde 93
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieeRREELgERARALYRSGGSVSYLDVLLGSEsfsdfLDRL--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 94 prevpvgltsDALNQeILQVSSQLLEKSRQAQQEQERAR-EIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQ 172
Cdd:COG3883 122 ----------SALSK-IADADADLLEELKADKAELEAKKaELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047419976 173 NLGLQAESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALES 243
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS 261
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
16-246 |
1.00e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 16 GAYAATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERaQQYQQVIDNfpklsQTLRSQLNNLRDEPR 95
Cdd:pfam19220 76 RRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALER-QLAAETEQN-----RALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 96 EVPVGLTsdALNQEILQVSSQ--LLEKSRQAQQE--QERAREIAD---SLSQLPQQQTDARRQLNEVErrvgtqagntpq 168
Cdd:pfam19220 150 AAEKALQ--RAEGELATARERlaLLEQENRRLQAlsEEQAAELAEltrRLAELETQLDATRARLRALE------------ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 169 sqAQNLGLQAESARLKALVDElELAQLsannRQELS--RMRAELAQKQSQQLDAYLQSLRNQLN--SQRQREAERALEST 244
Cdd:pfam19220 216 --GQLAAEQAERERAEAQLEE-AVEAH----RAERAslRMKLEALTARAAATEQLLAEARNQLRdrDEAIRAAERRLKEA 288
|
..
gi 2047419976 245 EL 246
Cdd:pfam19220 289 SI 290
|
|
| PRK11465 |
PRK11465 |
putative mechanosensitive channel protein; Provisional |
873-956 |
1.29e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 183147 [Multi-domain] Cd Length: 741 Bit Score: 42.84 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 873 ITTITkylIMLFgglvgFSMIGIEWSKLQWLVAALTVGLGFGLQEIFANFVSGLIILFEKPIRIGDTVTIRDLTGSVTKI 952
Cdd:PRK11465 521 ISTIT---IMIV-----LSEIGVNIAPLLAGAGALGLAISFGSQTLVKDIITGVFIQFENGMNTGDLVTIGPLTGTVERM 592
|
....
gi 2047419976 953 NTRA 956
Cdd:PRK11465 593 SIRS 596
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-427 |
1.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 27 QITQELEQAKAAKpaqpETVESLQSALNALEERKGSL--------ERAQQYQQVIDNFPKLSQTLRSQ------------ 86
Cdd:PRK03918 218 ELREELEKLEKEV----KELEELKEEIEELEKELESLegskrkleEKIRELEERIEELKKEIEELEEKvkelkelkekae 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 87 --------LNNLRDEPREVPVGLTS-DALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLP---QQQTDARRQLNE 154
Cdd:PRK03918 294 eyiklsefYEEYLDELREIEKRLSRlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 155 VERRVGTQAGNTPQSQAQNL----------------------GLQAESARLKALVDELELAQ---------LSANNRQEL 203
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELeelekakeeieeeiskitarigELKKEIKELKKAIEELKKAKgkcpvcgreLTEEHRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 204 -SRMRAELA--QKQSQQLDAYLQSLRNQLnsqRQREAERALEStELLAENSanlpvgIVDQFKvnrELSAALNQqaqrmd 280
Cdd:PRK03918 454 lEEYTAELKriEKELKEIEEKERKLRKEL---RELEKVLKKES-ELIKLKE------LAEQLK---ELEEKLKK------ 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 281 LVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQL--RVQRLHYEDLLNKQP 358
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--KLDELEEELAELlkELEELGFESVEELEE 592
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047419976 359 QIRQIRqadgqPLTGEQNRI------LEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHR 427
Cdd:PRK03918 593 RLKELE-----PFYNEYLELkdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-438 |
1.94e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 30 QELEqakaakpaqpETVESLQSALNALEERKGSL--ERAQQYQQVIDNFPKLSQ-------------TLRSQLNNLRDEp 94
Cdd:pfam01576 71 QELE----------EILHELESRLEEEEERSQQLqnEKKKMQQHIQDLEEQLDEeeaarqklqlekvTTEAKIKKLEED- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 95 revpVGLTSDA---LNQEILQVSSQLLEKSRQAQQEQERAReiadSLSQLPQQQ----TD----------ARRQLNEVER 157
Cdd:pfam01576 140 ----ILLLEDQnskLSKERKLLEERISEFTSNLAEEEEKAK----SLSKLKNKHeamiSDleerlkkeekGRQELEKAKR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 158 RVgtqAGNTPQSQAQNLGLQAESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQ--- 234
Cdd:pfam01576 212 KL---EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarn 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 235 ------REAERALES--TELlaENSanLPVGIVDQ-FKVNRE-----LSAALNQQAQRMDLVASQQRQATNqtlqvrQAL 300
Cdd:pfam01576 289 kaekqrRDLGEELEAlkTEL--EDT--LDTTAAQQeLRSKREqevteLKKALEEETRSHEAQLQEMRQKHT------QAL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 301 NTLREQsqwlgssnlLGEALRAQVArlpeMPKPQQ-LDTEMAQLRVQ-RL---------HYEDLLNKQPQIRQIRQADGQ 369
Cdd:pfam01576 359 EELTEQ---------LEQAKRNKAN----LEKAKQaLESENAELQAElRTlqqakqdseHKRKKLEGQLQELQARLSESE 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 370 PLTGEQNRILeAQLRTQRELLNSLLQGGDTLILELTK-LKVSNSQLEDALKEVNEATHRYLFWTSDVRPM 438
Cdd:pfam01576 426 RQRAELAEKL-SKLQSELESVSSLLNEAEGKNIKLSKdVSSLESQLQDTQELLQEETRQKLNLSTRLRQL 494
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
24-181 |
2.01e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.28 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAkaakpaqpetVESLQSALNALEERKGSLERAQQYQQvidnfpkLSQTLRSQlNNLRDEP---REVPVG 100
Cdd:pfam13779 574 EAQQMLSQLQQM----------LENLQAGQPQQQQQQGQSEMQQAMDE-------LGDLLREQ-QQLLDETfrqLQQQGG 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 101 LTSDALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPqsqAQNLGlQAES 180
Cdd:pfam13779 636 QQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEELQDELKELGGKEP---GQALG-DAGR 711
|
.
gi 2047419976 181 A 181
Cdd:pfam13779 712 A 712
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
33-210 |
2.45e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 33 EQAKAAKPAQPEtveslQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRSQLNNLRDEPREvpvgltsdaLNQEILQ 112
Cdd:COG1842 72 EKARLALEKGRE-----DLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEE---------LKAKKDT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 113 VSSQLleksrQAQQEQERAREIADSLSQlpqqqTDARRQLNEVERRVGTQagntpQSQAQnlgLQAESARLKALVDELEL 192
Cdd:COG1842 138 LKARA-----KAAKAQEKVNEALSGIDS-----DDATSALERMEEKIEEM-----EARAE---AAAELAAGDSLDDELAE 199
|
170
....*....|....*...
gi 2047419976 193 AQLSANNRQELSRMRAEL 210
Cdd:COG1842 200 LEADSEVEDELAALKAKM 217
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
26-246 |
3.47e-03 |
|
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: 41.57 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 26 KQITQELEQAKAAKPAQPETVESLQSALNALEERKGSL-ERAQQYQQVIDNFPKLSQTLRSQLNNLRDEPREV-PVGLTS 103
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIgTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDsPLETFL 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 104 DALNQEILQVSSQLLEKSRQAQQEQERAREIADSL----------------SQLPQQQTDARR---QLNEVERR------ 158
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkdDYLKQKETELNTvnaQLEECEKHqekine 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 159 -VGTQAGNTPQSQAQNLGLQAESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQ----LNSQR 233
Cdd:TIGR00606 999 dMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNhvlaLGRQK 1078
|
250
....*....|...
gi 2047419976 234 QREAERALESTEL 246
Cdd:TIGR00606 1079 GYEKEIKHFKKEL 1091
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
26-156 |
5.06e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 26 KQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRSQLNNLRDEprevpvgltSDA 105
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE---------ADE 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2047419976 106 LNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVE 156
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE 264
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
128-348 |
5.29e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 128 QERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNtpqsqaqnlgLQAESARLKALVDELELAqlsannRQELSRMR 207
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARE----------LEELSARESDLEQDYQAA------SDHLNLVQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 208 AelAQKQSQQLDAYLQSLrNQLNSQRQREAERALESTELLAENSANLPVG--IVDQFKVNrelsAALNQQAQRMdlvasQ 285
Cdd:COG3096 341 T--ALRQQEKIERYQEDL-EELTERLEEQEEVVEEAAEQLAEAEARLEAAeeEVDSLKSQ----LADYQQALDV-----Q 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047419976 286 QRQAtnqtLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRvQRL 348
Cdd:COG3096 409 QTRA----IQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRA--KEQQATEEVLELE-QKL 464
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
18-424 |
5.47e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 40.66 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 18 YAATAPDAKQITQELEQAKAAKPAQPETVESLQSalnALEERKGSLERAQQYQQVIDNFPKLSQTLRSQLNNLRDEPREV 97
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEA---LIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 98 PVGLTSDALNQEILQVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAQNLGLQ 177
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 178 AESARLKALVDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENSANLPVG 257
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 258 IVDQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLD 337
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 338 TEMAQLRVQRLHYEDLLNKQPQIRQIRQADGQPLTGEQNRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDA 417
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
....*..
gi 2047419976 418 LKEVNEA 424
Cdd:COG5278 478 AAAAAAL 484
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
177-396 |
6.71e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.74 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 177 QAESARLKAL---VDELELAQLSANNRQELSRMRAELAQKQSQQLDAYLQSLRNQLNSQRQREAERALESTELLAENsan 253
Cdd:pfam13779 493 AAQERLSEALergASDEEIAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELARS--- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 254 lpvGIVDQfkvNRELSAALNQ-----QAQRMdlvASQQRQATNQTLQVRQAL-NTLREQSQwlgssnLLGEALRaqvarl 327
Cdd:pfam13779 570 ---GRRAE---AQQMLSQLQQmlenlQAGQP---QQQQQQGQSEMQQAMDELgDLLREQQQ------LLDETFR------ 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047419976 328 pEMPKPQQLDTEMAQLRVQRlhyedllNKQPQIRQIRQADGQPLTGEQNRILEAQL-RTQREL---LNSLLQG 396
Cdd:pfam13779 629 -QLQQQGGQQQGQPGQQGQQ-------GQGQQPGQGGQQPGAQMPPQGGAEALGDLaERQQALrrrLEELQDE 693
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
105-235 |
6.79e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 105 ALNQEILQVSSQLLEK-SRQAQQEQ-ERAREiadSLSQLPQQQTDARRQLNEVerrvgtqagntpQSQAQNLGLQAESAR 182
Cdd:COG3524 154 AIAEALLAESEELVNQlSERAREDAvRFAEE---EVERAEERLRDAREALLAF------------RNRNGILDPEATAEA 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047419976 183 LKALVDELElaqlsannrQELSRMRAELAQKQS---------QQLDAYLQSLRNQLNSQRQR 235
Cdd:COG3524 219 LLQLIATLE---------GQLAELEAELAALRSylspnspqvRQLRRRIAALEKQIAAERAR 271
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
32-365 |
6.89e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 32 LEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDnfpKLSQ--TLRSQLNnlrdeprevpvgltsdALNQE 109
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLR---LLSQrhELQGQIA----------------AHNQQ 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 110 ILQVSSQLleksrQAQQEQERAREIADSLSqLPQQQTDARrQLNEVErrvgTQAGNTPQSQAQNLGLQAESARLKALVDE 189
Cdd:PRK10246 632 IIQYQQQI-----EQRQQQLLTALAGYALT-LPQEDEEAS-WLATRQ----QEAQSWQQRQNELTALQNRIQQLTPLLET 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 190 L--------ELAQLSANNRQElsrmraelAQKQSQQLDAYLQSLRNQLnsqrQREAERALESTELLAENSANLPVGIVDQ 261
Cdd:PRK10246 701 LpqsddlphSEETVALDNWRQ--------VHEQCLSLHSQLQTLQQQD----VLEAQRLQKAQAQFDTALQASVFDDQQA 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 262 FkvnreLSAALNQQA-QRMDlvasQQRQATNQTLQVRQALNTLREQSqwlgssnlLGEALRAQVARLPEMPKPQQLDTEM 340
Cdd:PRK10246 769 F-----LAALLDEETlTQLE----QLKQNLENQRQQAQTLVTQTAQA--------LAQHQQHRPDGLDLTVTVEQIQQEL 831
|
330 340
....*....|....*....|....*.
gi 2047419976 341 AQLrVQRLhyEDLLNKQPQIR-QIRQ 365
Cdd:PRK10246 832 AQL-AQQL--RENTTRQGEIRqQLKQ 854
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
22-225 |
7.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 22 APDAKQITQELEQAKAAKPAQPETVESLQSALNALEERkgsLERAQQYQQVIDNFpklSQTLRSQLNNlrdeprevpvgl 101
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQR---LRQQQRAERLLAEF---CKRLGKNLDD------------ 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 102 tSDALNQEilqvssqlleksrQAQQEQERArEIADSLSQLPQQQTDARRQLNEVERRVGTQAGNTPQSQAqnlgLQAESA 181
Cdd:PRK04863 553 -EDELEQL-------------QEELEARLE-SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA----AQDALA 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2047419976 182 RLKALVDE--------LELAQLSANNRQELSRMRAELAQKQsQQLDAYLQSL 225
Cdd:PRK04863 614 RLREQSGEefedsqdvTEYMQQLLERERELTVERDELAARK-QALDEEIERL 664
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
112-245 |
8.09e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 39.83 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 112 QVSSQLLEKSRQAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVgtqagntpqsQAQNLGLQAESARLKALVDELE 191
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA----------AAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2047419976 192 LAQLSANNRQELSRmRAELAQKQSQQLDAylqslrnqlnsQRQREAERALESTE 245
Cdd:TIGR02794 121 AEEAKAKQAAEAKA-KAEAEAERKAKEEA-----------AKQAEEEAKAKAAA 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
24-158 |
8.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQyqqvidnfpklsqtLRSQLNNLRDEPREVPVGLTS 103
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE--------------LEEQLEELLGELEELLEALDE 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047419976 104 DALNQEILQVSSQLLEKSRQAQQEQERAREI---------ADSLSQLPQQQTDARRQLNEVERR 158
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELeaeleqleeDGELAELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-395 |
9.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 201 QELSRMRAELAQKQSQQLDAYLQSLRNQLnsqrqREAERALEstELLAENsanlpvGIVDQFKVNRELSAALNQQAQRMD 280
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKEL-----EEAEAALE--EFRQKN------GLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047419976 281 LVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGE------ALRAQVARL-----PEMPKPQQLDTEMAQLRVQRLH 349
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlaELEAELAELsarytPNHPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047419976 350 ------------YEDLLNKQPQIRQI-----RQADGQPLTGEQNRILEAQLRTQRELLNSLLQ 395
Cdd:COG3206 310 eaqrilasleaeLEALQAREASLQAQlaqleARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| |
