|
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: 2229.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 1 MRPIIVLLMAWCLSMGAYAATAPDAKQITQELEQAKAAK-PAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKL 79
Cdd:PRK10929 1 MRLIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKtPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 80 SQTLRAQLNNLRDEPRDVPAGMTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRV 159
Cdd:PRK10929 81 SAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 160 GTQ-NGNTPQAQAQNLGLQAESARLKALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAE 238
Cdd:PRK10929 161 QTLgTPNTPLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 239 RALESTELLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGE 318
Cdd:PRK10929 241 RALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 319 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLHFEDLLNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQRELLNSLLQGGD 398
Cdd:PRK10929 321 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 399 TLILELTKLKVSNSQLEDALKEVNEATHRYLFWTSDVRPMTFSWPIEIVQDLRRLISLDTFSQLGQASVMMLTSKETIFP 478
Cdd:PRK10929 401 TLILELTKLKVANSQLEDALKEVNEATHRYLFWVADVSPISLSYPLEIAQDLRRLLSLDTFSQLGKASVMMLTSKETLLP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 479 LLGALILVGFSIYSRRHFTRFLERSSSRVGKVTQDHFWLTLRTVFWSILVASPLPVLWMTLGYGLREAWPYPLAVAIGDG 558
Cdd:PRK10929 481 LFGALLLVGFSISSRRHYHAFLERSSSRVGKVTQDHFSLTLRTVFWSILVASPLPVLWAALGYGLQNAWPYPLAVAIGDG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 559 VTATVPLLWVVMICATFARPNGLFIAHFGWPRNRVARAMRYYLMSIGLIVPLIMALIMFDNLNDREFSGSLGRLCFMLIC 638
Cdd:PRK10929 561 VTATVPLLWVFMICATFARPNGLFIAHFGWPRERVARAMRYYLLSIGLIVPLIMALITFDNLNDREFSGTLGRLCFILLC 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 639 GALAIVTLSLKRAGIPLYLDKTGSGDNMFNRLLWNLLLSAPLIAMLAAAVGYLATSQALLARLETSVAIWFLLLVVYHVI 718
Cdd:PRK10929 641 GALSLVTLSLKRAGIPLYLDKEGSGDNIINHALWNLLIGAPLVAALASALGYLATAQALLARLETSVAIWFLLLVVYHII 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 719 RRWMLIQRRRLAFDRAKHRRAEILAQRARGEEEPNHVNSTEGTTEADEVELDLDAISTQSLRLVRSILMLIALLSVIFLW 798
Cdd:PRK10929 721 RRWMLIQRRRIAFDRAKQRRAEILAQRARGEEEAHHSSSPEGAIEVEEPVIDLDAISAQSLRLVRSILTLIALLSVIVLW 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 799 SEIHSAFGFLENISLWDVTSTVQGVESLEPITLGAVLIAILVLIITTQLVRNFPALLELALLQHLDLTPGTGYAITTITK 878
Cdd:PRK10929 801 SEIHSAFGFLENISLWDVTSTVQGVESLQPITLGSVLIAILVFIITTQLVRNLPALLELALLQHLDLTPGTGYAITTITK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 879 YLIMLFGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKINTRATT 958
Cdd:PRK10929 881 YLLMLIGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 959 ISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQ 1038
Cdd:PRK10929 961 ISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVLDNPAPEVFLVDLQQGIQ 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 1039 IFELRIYAAEMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLDGRKTGRTLTSAARTRPAGSL 1107
Cdd:PRK10929 1041 IFELRIYAAEMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLGGKQTGRTLTSAGKSRTAGSL 1109
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
4-1076 |
5.66e-157 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 495.97 E-value: 5.66e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 4 IIVLLMAWCLSMGAYAATA----PDAKQITQELEQAKAAKPAQPE---TVESLQSALNALEERKGSLERAQQYQQVIDNF 76
Cdd:PRK11281 13 IAFLFLLLCLSSAFARAASngdlPTEADVQAQLDALNKQKLLEAEdklVQQDLEQTLALLDKIDRQKEETEQLKQQLAQA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 77 PKLSQTLRAQLNNLRDEPRDVP----AGMTSDALNQEILQVSSQLLE--------KSRL-AQQEQ-ERAREIADSLSQLP 142
Cdd:PRK11281 93 PAKLRQAQAELEALKDDNDEETretlSTLSLRQLESRLAQTLDQLQNaqndlaeyNSQLvSLQTQpERAQAALYANSQRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 143 QQqtdARRQLNEverrvGTQNGNTPQAQAQNLgLQAESARLKALVDeLELAQLSANNR-QELSRMRSELAQKQSEQLDAY 221
Cdd:PRK11281 173 QQ---IRNLLKG-----GKVGGKALRPSQRVL-LQAEQALLNAQND-LQRKSLEGNTQlQDLLQKQRDYLTARIQRLEHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 222 LQALRNQLNSQR----QREAERALESTELLAENSDNLpagIVEQFKVNRELSAALNQQAQRMDlVASQQRQATNQTL-QV 296
Cdd:PRK11281 243 LQLLQEAINSKRltlsEKTVQEAQSQDEAARIQANPL---VAQELEINLQLSQRLLKATEKLN-TLTQQNLRVKNWLdRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 297 RQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRV-------QRlhfEDLLNKQPQIRQIRQADGQ 369
Cdd:PRK11281 319 TQSERNIKEQISVLKGSLLLSRILYQQQQALPSADLIEGLADRIADLRLeqfeinqQR---DALFQPDAYIDKLEAGHKS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 370 PLTSEQSRILEAQLRTQREL-------LNSLLQGGDTLILELTKLKVSNSQLEDALKEvneathrYLFWTSDVRPMTFSW 442
Cdd:PRK11281 396 EVTDEVRDALLQLLDERRELldqlnkqLNNQLNLAINLQLNQQQLLSVSDSLQSTLTQ-------QIFWVNSNKPMDLDW 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 443 ----PIEIVQDLRRLISLDTFSQLGQASVmmltskETIFPLLGALILVGFSIYSRRHFTRFLERSSSRVGKVTQDHFWLT 518
Cdd:PRK11281 469 lkafPQALKDQFKSLKITVSFSNLWDGLF------IALLLFLPLLLIAGLIRWRKKWIKARLQKLAADIGTLKRDSQLHT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 519 LRTVFWSILVASPLPVLWMTLGYGLR--------EAWPYPLAVAigdgvtatvpLLWVVMICATFA-RPNGLFIAHFGWP 589
Cdd:PRK11281 543 PKAILITLLLALPVTLIFLAVGLILLtdafnqseLLWSWSLKLA----------LFWLVFATCYRVlRPNGVAERHFGMP 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 590 RNRVARaMRYYLMSIGLIVPLIMALIMFDNLNDREFSGSLGRLCFMLICGALAIVTLSlkragiPLYLDKTGSGDN-MFN 668
Cdd:PRK11281 613 KEQVSH-FRRQIVRLSLALLPLLFWSVVAELSPLGLADDVIGQAVIIIALALIAFLVW------PLCRESWRDKEShTLR 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 669 RLLWNLLLSAPLIAMLAAAVGYLATSQALLARLETSVAIWFLLLVVYHVIRRWMLIQRRRLAFDRAKHRRAeilAQRARG 748
Cdd:PRK11281 686 LVVRTVLTIAPIALIVLVVLGYYYTALRLIGRLIETLYLLIIWNLLYQTVLRGLSVAARRLAYRRALAKRQ---NLVKEG 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 749 EEepnhvnsteGTTEADEVELDLDAISTQSLRLVRsiLMLIALLSVIF--LWSEIHSAFGFLENISLWDVTSTVQGVESL 826
Cdd:PRK11281 763 AE---------GAEPVEEPTLALEQVNQQSLRLTD--LLLFALFFVMFywVWSDLITVFSYLDSITLWHYTTTTAGGAVV 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 827 EPITLGAVLIAILVLIITTQLVRNFPALLELALLQHLDLTPGTGYAITTITKYLIMLFGGLVGFSMIGIEWSKLQWLVAA 906
Cdd:PRK11281 832 ESITLGNLLFALIILVVTYVLVRNLPGLLEVLVLSRLNLRQGTSYAITTLLTYIIIAVGAVTAFSTLGVSWDKLQWLVAA 911
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 907 LGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKINTRATTISDWDRKEIIVPNKAFITEQFINWSLSD 986
Cdd:PRK11281 912 LSVGLGFGLQEIFANFVSGLIILFERPVRIGDTVTIGTFSGTVSKIRIRATTITDFDRKEVIVPNKAFVTERLINWSLSD 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 987 SVTRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQIFELRIYAAEMGHRMPLRHEIHQLILAG 1066
Cdd:PRK11281 992 TVTRVVIKVGVAYGSDLEKVRELLLQAATENPRVMKEPEPQVFFLNFGASTLDHELRLYVRELGDRSPTVDELNRRIDRL 1071
|
1130
....*....|
gi 1513194555 1067 FREHGIDMPF 1076
Cdd:PRK11281 1072 FRENDINIAF 1081
|
|
| MscS_TM |
pfam12794 |
Mechanosensitive ion channel inner membrane domain 1; The small mechanosensitive channel, MscS, ... |
481-813 |
2.67e-119 |
|
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: 370.78 E-value: 2.67e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 481 GALILVGFSI-YSRRHFTRFLERSSSRVGKVTQDHFWLTLRTVFWSILVASPLPVLWMTLGYGLREA-WPYPLAVAIGDG 558
Cdd:pfam12794 1 LLLLLVAGLLlWLRRRLKRRLERLAERVGKVTQDSFLHTLRALLLTLLLALPLPLLLAALGWLLQLSgWATPFSVALGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 559 VTATVPLLWVVMICATFARPNGLFIAHFGWPRNRVARAMRYYLMSIGLIVPLIMALIMFDNLNDREFSGSLGRLCFMLIC 638
Cdd:pfam12794 81 LLALALALLVFEFFRRLLRPDGLAIRHFGWPEERVQRLRRQLRWLIWVLVPLVFVLGLAEALPDSLARDVLGRLAFIILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 639 GALAIVTLSLKRAGIPLYLDKTGSGDN-MFNRLLWNLLLSAPLIAMLAAAVGYLATSQALLARLETSVAIWFLLLVVYHV 717
Cdd:pfam12794 161 LLLAVFLWRLLRPGRGLYASHLGEGPNsRLRRLWWPLLVLAPLALAVLALLGYYYTALQLLGRLIDSLYLLLGWLLVYAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 718 IRRWMLIQRRRLAFDRAKHRRAEILAQRARGEEEPNHVNSTEGtteaDEVELDLDAISTQSLRLVRSILMLIALLSVIFL 797
Cdd:pfam12794 241 ALRWLLVARRRLAYRRAKERRAEALAQRAKEGEEGAEPSESSV----EEPELDLETISAQSLRLLRLLLLLAFLVGLYWI 316
|
330
....*....|....*.
gi 1513194555 798 WSEIHSAFGFLENISL 813
Cdd:pfam12794 317 WSDLLPAFSYLDNITL 332
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis]; |
808-1089 |
2.53e-94 |
|
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442495 [Multi-domain] Cd Length: 281 Bit Score: 302.12 E-value: 2.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 808 LENISLWDVTSTVQGVeslePITLGAVLIAILVLIITTQLVRNFPALLELALLQHLDLTPGTGYAITTITKYLIMLFGGL 887
Cdd:COG3264 1 MEESALLELLFLIGGI----SISLPNLLLALLILVVTYLLARLLSRLLERRLLRRTRLDPGLRYLISKLIRYLIIVLGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 888 VGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKINTRATTISDWDRKEI 967
Cdd:COG3264 77 IALSALGIDLTALAALAGALGVGIGFGLQDIVSNFISGLILLFERPFRVGDWIEIGGTEGTVEEIGLRSTRIRTFDGEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 968 IVPNKAFITEQFINWSLSDSVTRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVDLQQGIQIFELRIYAA 1047
Cdd:COG3264 157 IIPNSELITNPVINWSLSDPRRRVEIPVGVAYGSDLEKVRELLLEAAREHPRVLKDPAPSVLFTEFGDSSVNFELRFWVN 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1513194555 1048 EMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLDGR 1089
Cdd:COG3264 237 DPRDRLRVRSDLNEAIKKAFREEGIEIPFPQRDVHLRNPPGE 278
|
|
| MS_channel |
pfam00924 |
Mechanosensitive ion channel; Two members of this protein family: Swiss:Q57634 and Swiss: ... |
874-1073 |
2.18e-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: 205.14 E-value: 2.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 874 TTITKYLIMLFGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKIN 953
Cdd:pfam00924 1 KKILKYLIIVVGILIVLSYLGVNVSALLAGLGALGLALGFALQDLVSNLVSGIIILFEKPFKIGDWIEIGDIEGTVEDIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 954 TRATTISDWDRKEIIVPNKAFITEQFINWSLSDsVTRVVLTVPAPSDANS---EEVTQILYTAAERCSLVIDNPAPEVFL 1030
Cdd:pfam00924 81 LRTTTIRTFDGRLVTIPNSSILTSNIINYSRSP-TRRVELSIGVAYSSDPdklEKVIEILKEAAYEHPLVLKDPEPPVVF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1513194555 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 ... |
30-251 |
9.36e-55 |
|
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: 190.59 E-value: 9.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 30 QELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRAQLNNLR----DEPRDVPAGMTSDA 105
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQakaeAAPKEILASLSLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 106 LNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRV-GTQNGNTPQAQAQNLGLQAESARLK 184
Cdd:pfam12795 83 LEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLnGPAPPGEPLSEAQRWALQAELAALK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513194555 185 ALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENS 251
Cdd:pfam12795 163 AQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEA 229
|
|
| MscS |
COG0668 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
812-1084 |
8.37e-46 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440432 [Multi-domain] Cd Length: 276 Bit Score: 166.21 E-value: 8.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 812 SLWDVTSTVQGVESLEPITLGAVLIAILVLIIT---TQLVRNFPALLELALLQHLDLTPgtgyAITTITKYLIMLFGGLV 888
Cdd:COG0668 5 QLWSLLGLLLLLGELLLALLPKLLLALLILLIGwllIRLLRRLIRRLLRRARRDRTLLP----LLRNILKILIVIIAILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 889 GFSMIGIEwskLQWLVAALGVG---LGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKINTRATTISDWDRK 965
Cdd:COG0668 81 ILSILGVN---ITSLLAGLGAAglaIGLAAQDLLSNFIAGIFILLERPFRVGDWIEVGGVEGTVEEIGLRSTRLRTLDGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 966 EIIVPNKAFITEQFINWSLSDSVtRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPApEVFLVDLQQGIQIFELRIY 1045
Cdd:COG0668 158 LVTIPNSKILSSPITNYSRGPTR-RVDVTIGVDYDTDIDKARELLKEILEELPRILKDPA-VVGVTELGDSSVNLRVRAW 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 1513194555 1046 AAEmGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLE 1084
Cdd:COG0668 236 TKP-GDYWDVRRDIRERIKAALDEAGIEIPFPTRTVHLA 273
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-326 |
6.06e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 19 AATAPDAKQITQELEQAKAakpaqpetveslQSALNALEERKGSLERAQQYQQVIDNfpkLSQTLRAQLnnlrdeprdvp 98
Cdd:COG1196 209 AEKAERYRELKEELKELEA------------ELLLLKLRELEAELEELEAELEELEA---ELEELEAEL----------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 99 agmtsDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQA 178
Cdd:COG1196 263 -----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 179 ESARLKALVDELELA-QLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALEstELLAENSDNLPAG 257
Cdd:COG1196 338 ELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL--EELEEAEEALLER 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 258 IVEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVAR 326
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
44-424 |
5.31e-11 |
|
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: 67.17 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 44 ETVESLQSALNALEERKGSLERAQQYQQviDNFPKLSQTLRAQLNNLRDEPRDVPAGMTSD--ALNQEILQVSSQL-LEK 120
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTLDDQWKEKRDELNGElsAADAAVAKDRSELeALE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 121 SRLAQQEQERAREIADSLSQLPQQQTDarrqLNEVERRVGTQNGNTPQaqaqnlgLQAESARLKALVDElELAQLSANNR 200
Cdd:pfam12128 329 DQHGAFLDADIETAAADQEQLPSWQSE----LENLEERLKALTGKHQD-------VTAKYNRRRSKIKE-QNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 201 QELSRMRsELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLpAGIVEQFKVNRELSAALNQQAQRMD 280
Cdd:pfam12128 397 DKLAKIR-EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQLENFDERIE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 281 LVASQQRQATNQTLQVRQALNTLR----EQSQWLGSSNLLGEALRAQVARLPEMPKPQQlDTEMAQLRVQRLHFEDLLNK 356
Cdd:pfam12128 475 RAREEQEAANAEVERLQSELRQARkrrdQASEALRQASRRLEERQSALDELELQLFPQA-GTLLHFLRKEAPDWEQSIGK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 357 QPQIRQIRQADGQPLTSEQS---------------RI-------LEAQLRTQRELLNSLLQGGDTLILELTK-LKVSNSQ 413
Cdd:pfam12128 554 VISPELLHRTDLDPEVWDGSvggelnlygvkldlkRIdvpewaaSEEELRERLDKAEEALQSAREKQAAAEEqLVQANGE 633
|
410
....*....|.
gi 1513194555 414 LEDALKEVNEA 424
Cdd:pfam12128 634 LEKASREETFA 644
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-366 |
6.98e-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: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 30 QELEQAKAAKPAQPETVESLQSALNALEerkgslERAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRdvpagmtsdALNQE 109
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 110 ILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDE 189
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 190 LELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSdnlpagiveqfkvnrELS 269
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------------SLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 270 AALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQsqwLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLH 349
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330
....*....|....*..
gi 1513194555 350 FEDLLNKQPQIRQIRQA 366
Cdd:TIGR02168 964 EDDEEEARRRLKRLENK 980
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-306 |
1.20e-10 |
|
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: 64.79 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 104 DALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARL 183
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 184 KALVDELeLAQLSANNRQE-----LSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERAlESTELLAENSDNLPAGI 258
Cdd:COG4942 103 KEELAEL-LRALYRLGRQPplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-ALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1513194555 259 VEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQ 306
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-321 |
1.51e-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: 65.85 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEE-------RKGSLE-RAQQYQQVIDNFPKLSQTLRAQLNNLRDEPR 95
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEkleelrlEVSELEeEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 96 DVPAgmTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTqngntpqaqaqnlg 175
Cdd:TIGR02168 313 NLER--QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-------------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 176 LQAESARLKALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLP 255
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513194555 256 AGIVEQFKVNRELSAA-----------LNQQAQRMDLVASQQRQATNQTLQVRQALNtlrEQSQWLGSSNLLGEALR 321
Cdd:TIGR02168 457 ERLEEALEELREELEEaeqaldaaereLAQLQARLDSLERLQENLEGFSEGVKALLK---NQSGLSGILGVLSELIS 530
|
|
| PRK10334 |
PRK10334 |
small-conductance mechanosensitive channel MscS; |
873-1081 |
1.66e-10 |
|
small-conductance mechanosensitive channel MscS;
Pssm-ID: 182386 [Multi-domain] Cd Length: 286 Bit Score: 63.40 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 873 ITTITKYLIMLFGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKI 952
Cdd:PRK10334 69 LSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 953 NTRATTISDWDRKEIIVPNKAFITEQFINWSlSDSVTRVVLTVPAPSDANSEEVTQILYTAAERCSLVIDNPAPEVFLVD 1032
Cdd:PRK10334 149 QIFSTTMRTADGKIIVIPNGKIIAGNIINFS-REPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNE 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1513194555 1033 LQQGIQIFELRIYaAEMGHRMPLRHEIHQLILAGFREHGIDMPFPpfQM 1081
Cdd:PRK10334 228 LGASSINFVVRVW-SNSGDLQNVYWDVLERIKREFDAAGISFPYP--QM 273
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-389 |
2.94e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 56 LEERKGSLER----AQQYQQVIDNFPKLSQTLRA-QLNNLRDEprdvpagmtSDALNQEILQVSSQLLEKSRLAQQEQER 130
Cdd:COG1196 198 LERQLEPLERqaekAERYRELKEELKELEAELLLlKLRELEAE---------LEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 131 AREIADSLSQLPQQQTDARRQLNEVERRVGTQNGntpQAQAQNLGLQAESARLKALVDEL-ELAQLSANNRQELSRMRSE 209
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQ---DIARLEERRRELEERLEELEEELaELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 210 LAQKQSEQLDAylQALRNQLNSQRQREAERALESTELLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVASQQRQA 289
Cdd:COG1196 346 LEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 290 TNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLHfEDLLNKQPQIRQIRQADGQ 369
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL-EELAEAAARLLLLLEAEAD 502
|
330 340
....*....|....*....|
gi 1513194555 370 PLTSEQSRILEAQLRTQREL 389
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-330 |
2.16e-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: 62.00 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 27 QITQELEQAKAAKPAQPETVESLQSALNALEERKGSLE-RAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDVPAGMTSda 105
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE-- 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 106 LNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKA 185
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 186 LVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRnqlnsQRQREAERAL-ESTELLAENSDNLpagivEQFKV 264
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELE-----SKRSELRRELeELREKLAQLELRL-----EGLEV 936
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 265 NR-ELSAALNQQAQR-MDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLG-EALRAQVARLPEM 330
Cdd:TIGR02168 937 RIdNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAiEEYEELKERYDFL 1005
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-360 |
7.91e-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: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 107 NQEILQVSSQLLE-KSRLAQQEQERArEIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKA 185
Cdd:TIGR02168 676 RREIEELEEKIEElEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 186 LVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQR----------QREAERALESTELLAENSDNLP 255
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealdelraelTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 256 A------GIVEQFKVNRE----LSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSS--NLLGEALRAQ 323
Cdd:TIGR02168 835 AterrleDLEEQIEELSEdiesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElrELESKRSELR 914
|
250 260 270
....*....|....*....|....*....|....*..
gi 1513194555 324 VARLPEMPKPQQLDTEMAQLRVQRLHFEDLLNKQPQI 360
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-240 |
1.02e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 1 MRPIIVLLMAWCLSMGAYAATAPDA----KQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERA-QQYQQVIdn 75
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAeaelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiRALEQEL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 76 fpklsQTLRAQLNNLRDEprdvpagmtSDALNQEILQVSSQLLEKSRLAQQEQERAREI----ADSLSQLPQQQTDARRQ 151
Cdd:COG4942 79 -----AALEAELAELEKE---------IAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 152 LNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDELE-----LAQLSANNRQELSRMRSELAQKQSE--QLDAYLQA 224
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEeeraaLEALKAERQKLLARLEKELAELAAElaELQQEAEE 224
|
250
....*....|....*.
gi 1513194555 225 LRNQLNSQRQREAERA 240
Cdd:COG4942 225 LEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
26-306 |
1.24e-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: 59.58 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 26 KQITQELEQAKAAKPAQPETVESLQSAL----NALEERKgslERAQQYQQV-----------------IDNFPKLSQTLR 84
Cdd:COG3096 371 EEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQ---TRAIQYQQAvqalekaralcglpdltPENAEDYLAAFR 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 85 AQLNNLRDEPRDVPA--GMTSDALNQ-----EIL-------------QVSSQLLEKSR----LAQQEQERAREIADsLSQ 140
Cdd:COG3096 448 AKEQQATEEVLELEQklSVADAARRQfekayELVckiageversqawQTARELLRRYRsqqaLAQRLQQLRAQLAE-LEQ 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 141 LPQQQTDARRQLNEVERRVGTQngntpqaQAQNLGLQAESARLKALVDELElaQLSANNRQELSRMRSELaqkqsEQLDA 220
Cdd:COG3096 527 RLRQQQNAERLLEEFCQRIGQQ-------LDAAEELEELLAELEAQLEELE--EQAAEAVEQRSELRQQL-----EQLRA 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 221 YLQALRNQlnSQRQREAERALEStelLAENSDnlpagivEQFKVNRELSAALNQQAQRM-------DLVASQQRQATNQT 293
Cdd:COG3096 593 RIKELAAR--APAWLAAQDALER---LREQSG-------EALADSQEVTAAMQQLLEREreatverDELAARKQALESQI 660
|
330 340
....*....|....*....|
gi 1513194555 294 LQVRQA-------LNTLREQ 306
Cdd:COG3096 661 ERLSQPggaedprLLALAER 680
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-416 |
1.34e-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: 59.30 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 49 LQSALNALEERKGSLER----AQQYQQvidnfpklsqtLRAQLNNLrdeprdvpagmtsdalnqeilQVSSQLLEKsrla 124
Cdd:TIGR02168 191 LEDILNELERQLKSLERqaekAERYKE-----------LKAELREL---------------------ELALLVLRL---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 125 QQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDELElaqlsanNRQELS 204
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-------QQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 205 RMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTElLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVAS 284
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-LKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 285 QQRQATNQTLQVRQALNTLREQSQWLGSSN---------LLGEALRAQVARLPEmpkpqQLDTEMAQLRVQRLHFEDLLN 355
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQA-----ELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513194555 356 KQPQIRQIRQADGQPLTSEQSRilEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLED 416
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERE--LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
25-239 |
1.82e-08 |
|
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: 58.61 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 25 AKQITQELEQAKAAKPAQPETVESLQSAL----NALEERKGSLERAQ-QYQQVIDNFPKLSQTL---------------- 83
Cdd:pfam07111 375 AKGLQMELSRAQEARRRQQQQTASAEEQLkfvvNAMSSTQIWLETTMtRVEQAVARIPSLSNRLsyavrkvhtikglmar 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 84 RAQLNNLRDE---------PRDVPAGMTSDALNQEILQVSSQLLEKSRLAQQEQERAREiadslsqlpqQQTDARRQLNE 154
Cdd:pfam07111 455 KVALAQLRQEscpppppapPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRARE----------QGEAERQQLSE 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 155 VERRVgTQNGNTPQAQAQNLGLQAESARLkalvDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQ 234
Cdd:pfam07111 525 VAQQL-EQELQRAQESLASVGQQLEVARQ----GQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKR 599
|
....*..
gi 1513194555 235 R--EAER 239
Cdd:pfam07111 600 RlnEARR 606
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-267 |
1.08e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 26 KQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQT---LRAQLNNLRDEPRDVpagmt 102
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaeLEAELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 103 sDALNQEILQVssqlleKSRLAQQEQERaREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESAR 182
Cdd:COG4913 688 -AALEEQLEEL------EAELEELEEEL-DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 183 LKALVDEL--ELAQLSANNRQELSRMRSELAQKQS-----------------EQLDAYLqALRNQLNSQRQREAERALEs 243
Cdd:COG4913 760 GDAVERELreNLEERIDALRARLNRAEEELERAMRafnrewpaetadldadlESLPEYL-ALLDRLEEDGLPEYEERFK- 837
|
250 260
....*....|....*....|....
gi 1513194555 244 tELLAENSDNLPAGIVEQFKVNRE 267
Cdd:COG4913 838 -ELLNENSIEFVADLLSKLRRAIR 860
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
44-416 |
1.39e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 44 ETVESLQSALNALEERKGSLERAQQyQQVIDNFPKLSQtLRAQLNNLRDEprdvpagmtSDALNQEILQVSSQLLEKSRL 123
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALS-EQLRKALFELDK-LQEELEQLREE---------LEQAREELEQLEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 124 AQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGtqngntpQAQAQNLGLQAESARLKALVDELE-----LAQLSAN 198
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE-------ELQEELEELQKERQDLEQQRKQLEaqiaeLQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 199 NRQELSRMRSELAQKQsEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAGIVEQFKVNRELSAAlNQQAQR 278
Cdd:COG4372 148 REEELKELEEQLESLQ-EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE-LLEAKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 279 MDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMA------QLRVQRLHFED 352
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALeeaaleLKLLALLLNLA 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513194555 353 LLNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLED 416
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
25-379 |
1.69e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 25 AKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLEraQQYQQVIDNFPKLSQTLRAQ---------LNNLrdEPR 95
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLE--QDYQAASDHLNLVQTALRQQekieryqadLEEL--EER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 96 DVPAGMTS--------------DALNQEILQVSSQL---------LEKSRLAQQEQERAREIADSLSQLP---------- 142
Cdd:PRK04863 364 LEEQNEVVeeadeqqeenearaEAAEEEVDELKSQLadyqqaldvQQTRAIQYQQAVQALERAKQLCGLPdltadnaedw 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 143 --------QQQTDARRQLnevERRVG-TQNGNTPQAQAQNLglqaesarLKALVDELELAQLSANNRQELSRMRSELAQK 213
Cdd:PRK04863 444 leefqakeQEATEELLSL---EQKLSvAQAAHSQFEQAYQL--------VRKIAGEVSRSEAWDVARELLRRLREQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 214 QS-EQLDAYLQALRNQLNSQRQreAERALESTELLAENSDNLPAgiveqfkvnrELSAALNQQAQRMDLVASQQRQATNQ 292
Cdd:PRK04863 513 EQlQQLRMRLSELEQRLRQQQR--AERLLAEFCKRLGKNLDDED----------ELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 293 TLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEM-----PKPQQLDTEMAQL----RVQRLHFEDLLNKQPQI-RQ 362
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQsgeefEDSQDVTEYMQQLlereRELTVERDELAARKQALdEE 660
|
410
....*....|....*..
gi 1513194555 363 IRQAdGQPLTSEQSRIL 379
Cdd:PRK04863 661 IERL-SQPGGSEDPRLN 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-229 |
2.17e-07 |
|
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: 55.46 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVidnfpklsQTLRAQLNNLRDEPRDVPAGMts 103
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--------PEIQAELSKLEEEVSRIEARL-- 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 104 DALNQEI--LQVSSQLLEKSRlaQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVgtqngntPQAQAQNLGLQAESA 181
Cdd:TIGR02169 815 REIEQKLnrLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-------EELEAALRDLESRLG 885
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1513194555 182 RLKALVDELElAQLSA--NNRQELSRMRsELAQKQSEQLDAYLQALRNQL 229
Cdd:TIGR02169 886 DLKKERDELE-AQLREleRKIEELEAQI-EKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-348 |
2.48e-07 |
|
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: 55.07 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 39 KPAQPETVESLQSALNALeerKGSLERAQQYQQVIDNfpklsqtlraQLNNLRDEPRDVpAGMTSD------ALNQEILQ 112
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL---KRELSSLQSELRRIEN----------RLDELSQELSDA-SRKIGEiekeieQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 113 VSSQLLE-KSRLAQQEQERA---REIADSLSQLPQQQTDA---RRQLNEVERRVGTQngNTPQAQAQNLGLQAESARLKA 185
Cdd:TIGR02169 735 LKERLEElEEDLSSLEQEIEnvkSELKELEARIEELEEDLhklEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 186 LVDELElaqlsannrQELSR--MRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAEnsdnlpagiveqfk 263
Cdd:TIGR02169 813 RLREIE---------QKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------------- 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 264 vNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSS-NLLGEALRAQVARLPEM---------PKP 333
Cdd:TIGR02169 870 -LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEIedpkgedeeIPE 948
|
330
....*....|....*
gi 1513194555 334 QQLDTEMAQLRVQRL 348
Cdd:TIGR02169 949 EELSLEDVQAELQRV 963
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
65-419 |
2.49e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 65 RAQQYQQVID--NFPKLSQTLRAQLNNLRDEPrDVPAGMTSDALNQEILQVSSQLLEKSRLA------QQEQERAREIAD 136
Cdd:PRK10246 369 RAQFSQQTSDreQLRQWQQQLTHAEQKLNALP-AITLTLTADEVAAALAQHAEQRPLRQRLValhgqiVPQQKRLAQLQV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 137 SLSQLPQQQTDARRQLNEVERRVGTQNGNTP------QAQAQNLGLQAESARLKA-----LVDELELAQLSANNRQELSR 205
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMRQRYKEKTQQLAdvkticEQEARIKDLEAQRAQLQAgqpcpLCGSTSHPAVEAYQALEPGV 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 206 MRSELAQ--KQSEQLDAYLQALRNQLN---SQRQR---EAERALESTELLAENSDNLPAGIVEQFKVNRELSAALNQQ-- 275
Cdd:PRK10246 528 NQSRLDAleKEVKKLGEEGAALRGQLDaltKQLQRdesEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQee 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 276 --------AQRMDLvasqQRQATNQTLQVRQAlntlreQSQWLGSSNLLGEALRAQVARLPEMPKP-------------- 333
Cdd:PRK10246 608 herqlrllSQRHEL----QGQIAAHNQQIIQY------QQQIEQRQQQLLTALAGYALTLPQEDEEaswlatrqqeaqsw 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 334 QQLDTEMAQLRVQRLHFEDLLNKQPQiRQIRQADGQPLTSEQSR-------ILEAQLRTQRELlnsllqggdtLILELTK 406
Cdd:PRK10246 678 QQRQNELTALQNRIQQLTPLLETLPQ-SDDLPHSEETVALDNWRqvheqclSLHSQLQTLQQQ----------DVLEAQR 746
|
410
....*....|...
gi 1513194555 407 LKVSNSQLEDALK 419
Cdd:PRK10246 747 LQKAQAQFDTALQ 759
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
51-401 |
2.75e-07 |
|
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: 54.96 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 51 SALNALEERKGSLERAQQYQQVIDNFPKLSQTLRA----QLNNLRDEprdvpagmtSDALNQEILQVSSQLLEKSRLAQQ 126
Cdd:COG3096 747 SVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGRAarekRLEELRAE---------RDELAEQYAKASFDVQKLQRLHQA 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 127 -EQERAREIADSLSQLPQQQ-TDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDELE-LAQLSANNRQEL 203
Cdd:COG3096 818 fSQFVGGHLAVAFAPDPEAElAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANlLADETLADRLEE 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 204 SRMRSELAQ----------KQSEQLDAYLQALRN------QLN------SQRQREAERALESTELLAENSDNLP-AGIVE 260
Cdd:COG3096 898 LREELDAAQeaqafiqqhgKALAQLEPLVAVLQSdpeqfeQLQadylqaKEQQRRLKQQIFALSEVVQRRPHFSyEDAVG 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 261 QFKVNRELSAALNQQAQRMDLVASQQRQAT-------NQTLQVRQALNTLREQSQwlgssNLLGEALRaqvaRLPEMpkP 333
Cdd:COG3096 978 LLGENSDLNEKLRARLEQAEEARREAREQLrqaqaqySQYNQVLASLKSSRDAKQ-----QTLQELEQ----ELEEL--G 1046
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 334 QQLDTEM---AQLRVQRLHFE--------DLLNKQpqiRQIRQADGQPLtSEQSRILEAQLRTQRELLNSLLQGGDTLI 401
Cdd:COG3096 1047 VQADAEAeerARIRRDELHEElsqnrsrrSQLEKQ---LTRCEAEMDSL-QKRLRKAERDYKQEREQVVQAKAGWCAVL 1121
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-366 |
4.94e-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: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 57 EERK---GSLERAQQYQQVIDNFPKLSQTLRAQLNNLRDEprdvpAGMTSDALNQ------EILQVSSQLLEKSRLAQQE 127
Cdd:TIGR00618 163 KEKKellMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLR-----SQLLTLCTPCmpdtyhERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 128 QERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDELELAQLSANNRQELSRMR 207
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 208 SELAQKQSEqLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDlVASQQR 287
Cdd:TIGR00618 318 SKMRSRAKL-LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 288 QATNQ---TLQVRQALNTLREQSQwlgssnllgEALRAQVARLPEMPKPQQLDTEMAQLRVQRlHFEDLLNKQPQIRQIR 364
Cdd:TIGR00618 396 QSLCKeldILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYAELCAAAITC-TAQCEKLEKIHLQESA 465
|
..
gi 1513194555 365 QA 366
Cdd:TIGR00618 466 QS 467
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
31-291 |
8.33e-07 |
|
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: 53.15 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 31 ELEQAKAAKPAQPETVESLQSALNALE--------ERKGSLERAQQYQQVIDNFPKLSQTL---RAQLNNLRDEPRdvpa 99
Cdd:pfam05622 253 ELSQADALLSPSSDPGDNLAAEIMPAEireklirlQHENKMLRLGQEGSYRERLTELQQLLedaNRRKNELETQNR---- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 100 gmtsdALNQEILQVSSQLLEKSRlAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAE 179
Cdd:pfam05622 329 -----LANQRILELQQQVEELQK-ALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKID 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 180 SARLKALVDELELAQLSANNRQELSRMRS---ELAQKQSEQLDAYLQALRNQLNSQRQR--EAERALESTELLAENSDNL 254
Cdd:pfam05622 403 ELQEALRKKDEDMKAMEERYKKYVEKAKSvikTLDPKQNPASPPEIQALKNQLLEKDKKieHLERDFEKSKLQREQEEKL 482
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1513194555 255 PA------GIVEQFKVNRELSAALNQQAQRMdlvASQQRQATN 291
Cdd:pfam05622 483 IVtawynmGMALHRKAIEERLAGLSSPGQSF---LARQRQATN 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-395 |
9.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 30 QELEQAKAAKPAQPETVESLQSALNALEERKGSLERA--------QQYQQVIDNFPKLS--QTLRAQLNNLRDEPrdvpa 99
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAEleelreelEKLEKLLQLLPLYQelEALEAELAELPERL----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 100 gmtsDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQqtdARRQLNEVERRVGTQNGNTPQAQAQNLGLQAE 179
Cdd:COG4717 149 ----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 180 SARLKALVDELELAQLSANNRQELSRMRSELAQ------------------------------------KQSEQLDAYLQ 223
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 224 ALRNQLNSQRQREAERALESTELLAE---NSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTL------ 294
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 295 ----QVRQALNTLREQSQWLGSSNLLGEALRAQ---VARLPEMPKPQQLDTEMAQLRVQRLHFEDLLNK-QPQIRQIRQA 366
Cdd:COG4717 382 edeeELRAALEQAEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEElREELAELEAE 461
|
410 420
....*....|....*....|....*....
gi 1513194555 367 DGQPLTSEQSRILEAQLRTQRELLNSLLQ 395
Cdd:COG4717 462 LEQLEEDGELAELLQELEELKAELRELAE 490
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
21-389 |
1.04e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 21 TAPDAKQI-TQELEQAKAAKPAQPETVESLQSALNALEERkgsLERAQQYQQVIDNFPKLsQTLRAQLNNLRDE----PR 95
Cdd:TIGR00618 216 TYHERKQVlEKELKHLREALQQTQQSHAYLTQKREAQEEQ---LKKQQLLKQLRARIEEL-RAQEAVLEETQERinraRK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 96 DVPAGMTSDAL---NQEILQVSSQLLEKSR-LAQQEQERAREIADSLSQLPQQQTDAR--RQLNEVERRVGTQNGNTPQA 169
Cdd:TIGR00618 292 AAPLAAHIKAVtqiEQQAQRIHTELQSKMRsRAKLLMKRAAHVKQQSSIEEQRRLLQTlhSQEIHIRDAHEVATSIREIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 170 QAQnlglQAESARLKALVDELE-LAQLSANNRQELSRMRSELAQKQSEQ-----LDAYLQALRNQLNSQRQREAERALES 243
Cdd:TIGR00618 372 CQQ----HTLTQHIHTLQQQKTtLTQKLQSLCKELDILQREQATIDTRTsafrdLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 244 TELLAENSDNLPAgIVEQFKVNRELSAALNQ--------------QAQRMDLVASQQRQATNQTLQ-------------- 295
Cdd:TIGR00618 448 TCTAQCEKLEKIH-LQESAQSLKEREQQLQTkeqihlqetrkkavVLARLLELQEEPCPLCGSCIHpnparqdidnpgpl 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 296 ---VRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRVQRLHFEDLLNKQPQIRQIRQADGQPLT 372
Cdd:TIGR00618 527 trrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
410
....*....|....*..
gi 1513194555 373 SEQSRILEAQLRTQREL 389
Cdd:TIGR00618 605 EAEDMLACEQHALLRKL 621
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
17-306 |
3.08e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 17 AYAATAPDAKQITQELEQAKAAKPA-------QPET----VESLQSALNALEERkgsLERAQQYQQVIDNFPKLSQTLRA 85
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGlsalnrlLPRLnllaDETLADRVEEIREQ---LDEAEEAKRFVQQHGNALAQLEP 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 86 QLNNLRDEPRDVpagmtsDALNQEILQvssqlleksrlAQQEQERAREIADSLSQLpqqqtdarrqlneVERRVGTQNGN 165
Cdd:PRK04863 926 IVSVLQSDPEQF------EQLKQDYQQ-----------AQQTQRDAKQQAFALTEV-------------VQRRAHFSYED 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 166 TPQAQAQNLGLQaesARLKALVDELElaqlsannrQELSRMRSELAQKQSeQLDAYLQALrNQLNSQRQREAERALESTE 245
Cdd:PRK04863 976 AAEMLAKNSDLN---EKLRQRLEQAE---------QERTRAREQLRQAQA-QLAQYNQVL-ASLKSSYDAKRQMLQELKQ 1041
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 246 LLAENSDNLPAGIVEQFKVNR-ELSAALNQQAQRMDLV----ASQQRQATNQTLQVRQA---LNTLREQ 306
Cdd:PRK04863 1042 ELQDLGVPADSGAEERARARRdELHARLSANRSRRNQLekqlTFCEAEMDNLTKKLRKLerdYHEMREQ 1110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-408 |
3.37e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 47 ESLQSALNALEERKGSLERAQQY-QQVIDNFPKLS----QTLRAQlnNLRDEPRDVPAGMTS---DALNQEILQVSSQLL 118
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIiDEKRQQLERLRrereKAERYQ--ALLKEKREYEGYELLkekEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 119 EKSRLAQQEQERAREIADSLSQLPQQqtdaRRQLNEVERRVGtqNGNTPQAQAQNLGLQAESARLKALVDELELAQLSAN 198
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQL----LEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 199 NRQ-----ELSRMRSELA---------QKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNlpagIVEQFKV 264
Cdd:TIGR02169 322 ERLakleaEIDKLLAEIEelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY----REKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 265 NRElsaaLNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNL-LGEALRAQVARLPEMPKpqQLDTEMAQL 343
Cdd:TIGR02169 398 KRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAA--DLSKYEQEL 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513194555 344 RVQRLHFEDLLNKQPQI-RQIRQADGQPLTSEQSrilEAQLRTQRELLNSLLQGGDTLILELTKLK 408
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLqRELAEAEAQARASEER---VRGGRAVEEVLKASIQGVHGTVAQLGSVG 534
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
26-369 |
3.70e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 26 KQITQELEQAKAAKPAQPETVESLQSALNALEERKgSLERAQQYQQ--------VIDNFPKLSQTLRAQLNNLRDEPRDv 97
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRR-KLEEAEKARQaemdrqaaIYAEQERMAMERERELERIRQEERK- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 98 pagMTSDALNQEILQVS-SQLLEKSRLA---QQEQERAReiadslsqlpQQQTDARRQ-LNEVERRVGTQNGNTPQAQAQ 172
Cdd:pfam17380 360 ---RELERIRQEEIAMEiSRMRELERLQmerQQKNERVR----------QELEAARKVkILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 173 NlglQAESARlkalvdELELAQLSANNRQELSRMRSELAQKQseqldaylqalrNQLNSQRQREAERALESTELLAENSD 252
Cdd:pfam17380 427 A---EQEEAR------QREVRRLEEERAREMERVRLEEQERQ------------QQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 253 NLPAGIVEQFKVNRELSAalNQQAQrmdLVASQQRQATNQTLQVRQalNTLREQSQwlgsSNLLGEALRAQVarlpEMPK 332
Cdd:pfam17380 486 RKRAEEQRRKILEKELEE--RKQAM---IEEERKRKLLEKEMEERQ--KAIYEEER----RREAEEERRKQQ----EMEE 550
|
330 340 350
....*....|....*....|....*....|....*..
gi 1513194555 333 PQQLDTEMAQLRVQRLHFEDLLNKQPQIRQIRQADGQ 369
Cdd:pfam17380 551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-423 |
3.82e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 17 AYAATAPDAKQITQELEQAKAAKPAQPETVE--SLQSALNALEERKgslERAQQYQQVIDNFPKLSQTLRAQLNNLRDEP 94
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQSLKERE---QQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 95 RDVpAGMTSDaLNQEILQVSSQLLEKSRLAQQEQERAR---EIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQA 171
Cdd:TIGR00618 504 CPL-CGSCIH-PNPARQDIDNPGPLTRRMQRGEQTYAQletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 172 qnlgLQAESARLKALVDEL--ELAQLSANNRQELSRMRSELAQKQsEQLDAYLQALRNQLNSQRQREAERALESTELlae 249
Cdd:TIGR00618 582 ----SKEDIPNLQNITVRLqdLTEKLSEAEDMLACEQHALLRKLQ-PEQDLQDVRLHLQQCSQELALKLTALHALQL--- 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 250 nsdNLPA-GIVEQFKVNRELSAALNQQAQR-MDLVASQQRQATNQTLQVRQALNTLREQSQWLGSS-------------- 313
Cdd:TIGR00618 654 ---TLTQeRVREHALSIRVLPKELLASRQLaLQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdrefneienasssl 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 314 ------------NLLGEALRAQVARL-----------PEMPKPQQLDTEMAQL--------RVQRLHFEDLLNKQPQIRQ 362
Cdd:TIGR00618 731 gsdlaaredalnQSLKELMHQARTVLkarteahfnnnEEVTAALQTGAELSHLaaeiqffnRLREEDTHLLKTLEAEIGQ 810
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513194555 363 IRQADGQPLTSEQSRIL--EAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNE 423
Cdd:TIGR00618 811 EIPSDEDILNLQCETLVqeEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
25-428 |
5.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 25 AKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIdnfpKLSQTLRAQLNNLRDEPrdvpagmtsD 104
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY----QELEALEAELAELPERL---------E 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 105 ALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQqtdARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLK 184
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 185 ALVDELELAQLSANNRQELSRMRSELA---------------QKQSEQLDAYLQAL------------RNQLNSQRQREA 237
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLiaaallallglggslLSLILTIAGVLFLVlgllallflllaREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 238 ERALESTELLAENSdnlPAGIVEQFKVNRELSAA----LNQQAQRMDLVASQQRQATNQtLQVRQALNTLREQSQWLGSS 313
Cdd:COG4717 307 LQALPALEELEEEE---LEELLAALGLPPDLSPEelleLLDRIEELQELLREAEELEEE-LQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 314 NLlgEALRAQVARLPEMpkpQQLDTEMAQLRvqrlhfEDLLNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQRELLNSL 393
Cdd:COG4717 383 DE--EELRAALEQAEEY---QELKEELEELE------EQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430
....*....|....*....|....*....|....*
gi 1513194555 394 LQggdtlilELTKLKVSNSQLEDAlKEVNEATHRY 428
Cdd:COG4717 452 RE-------ELAELEAELEQLEED-GELAELLQEL 478
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-424 |
5.76e-06 |
|
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: 50.56 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 27 QITQELEQAK-------AAKPAQPETVESLQSALNALEERKGSLE--RAQQYQQVIDNFPKLSQTLRA------QLNNLR 91
Cdd:pfam01576 360 ELTEQLEQAKrnkanleKAKQALESENAELQAELRTLQQAKQDSEhkRKKLEGQLQELQARLSESERQraelaeKLSKLQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 92 DEPRDVpAGMTSDA------LNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNE-------VERR 158
Cdd:pfam01576 440 SELESV-SSLLNEAegknikLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEeeeakrnVERQ 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 159 VGTQNGNTP-----------------------QAQAQNLGLQAES------------ARLKALVDELELAQlsANNRQEL 203
Cdd:pfam01576 519 LSTLQAQLSdmkkkleedagtlealeegkkrlQRELEALTQQLEEkaaaydklektkNRLQQELDDLLVDL--DHQRQLV 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 204 SRMrsELAQKQSEQLDAYLQALRNQLNSQRQR-EAE------RALESTELLAENSDNLPagivEQFKVNRELSAALNqqa 276
Cdd:pfam01576 597 SNL--EKKQKKFDQMLAEEKAISARYAEERDRaEAEareketRALSLARALEEALEAKE----ELERTNKQLRAEME--- 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 277 qrmDLVASQQRQATN--------QTLQvrQALNTLREQSQwlgssNLLGEALRAQVARLpempkpqQLDTEMAQLRVQrl 348
Cdd:pfam01576 668 ---DLVSSKDDVGKNvhelerskRALE--QQVEEMKTQLE-----ELEDELQATEDAKL-------RLEVNMQALKAQ-- 728
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513194555 349 HFEDLLNKQPQIRQIRQAdgqplTSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKLKvsnSQLEDALKEVNEA 424
Cdd:pfam01576 729 FERDLQARDEQGEEKRRQ-----LVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELE---AQIDAANKGREEA 796
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
44-306 |
7.54e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 44 ETVESLQSALNALEERKGSL-ERAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDVPAGMTS-----DALNQEILQVSSQ- 116
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELrEEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQElrekrDELNEKVKELKEEr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 117 --LLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVgtqngntpqaQAQNLGLQAEsarlKALVDelelaq 194
Cdd:COG1340 81 deLNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ----------QTEVLSPEEE----KELVE------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 195 lsannrqELSRMRSEL-AQKQSEQLDAYLQALRNQLNSQRqREAERALESTELLAENSDNLPAGIVEQF-------KVNR 266
Cdd:COG1340 141 -------KIKELEKELeKAKKALEKNEKLKELRAELKELR-KEAEEIHKKIKELAEEAQELHEEMIELYkeadelrKEAD 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1513194555 267 ELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQ 306
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-326 |
1.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 124 AQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGL-QAESARLKALVDELE-----LAQLSA 197
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEaelerLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 198 NNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQReaERALESTELLAENSDNLPAGIVEQFKVNR-ELSAALNQQA 276
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEER--ERRRARLEALLAALGLPLPASAEEFAALRaEAAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1513194555 277 QRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGS--SNLLGE--ALRAQVAR 326
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERrkSNIPARllALRDALAE 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
102-305 |
1.03e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 102 TSDALNQEILQVSSQLLEksrlAQQEQERAREIADSLSqLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESA 181
Cdd:COG3206 176 ALEFLEEQLPELRKELEE----AEAALEEFRQKNGLVD-LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 182 RLKALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAY-----LQALRNQLNSQRQREAERALESTELLAENSDNLPA 256
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREA 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1513194555 257 GIVEQFKVNRELSAALNQQAQRMdlvASQQRQATNQTLQVRQALNTLRE 305
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAEL---RRLEREVEVARELYESLLQRLEE 376
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-257 |
1.37e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQ----YQQVI-------DNFPKLSQTLRAQLNNLRD 92
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAeiedLRETIaetererEELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 93 EPRDVPAGMTSDALNQEILqvssqLLEKSRLAQQEQERAREIAdslsqlpQQQTDARRQLNEVERRvgtqngntpQAQAQ 172
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAV-----EARREELEDRDEELRDRLE-------ECRVAAQAHNEEAESL---------REDAD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 173 NLGLQAESARLKA--LVDELELAQLSANNRQE-LSRMRSEL---------AQKQSEQLDAYLQALRNQLNSQRQREAEra 240
Cdd:PRK02224 353 DLEERAEELREEAaeLESELEEAREAVEDRREeIEELEEEIeelrerfgdAPVDLGNAEDFLEELREERDELREREAE-- 430
|
250 260
....*....|....*....|..
gi 1513194555 241 LEST-----ELLAENSDNLPAG 257
Cdd:PRK02224 431 LEATlrtarERVEEAEALLEAG 452
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
30-368 |
1.87e-05 |
|
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: 49.18 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 30 QELEQAKAAKPAQPETVESLQSALNALEERKGSLEraQQYQQVIDNFPKLSQTLRAQ--LNNLRDEprdvpagmtSDALN 107
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELEELSARESDLE--QDYQAASDHLNLVQTALRQQekIERYQED---------LEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 108 qEILQVSSQLLEKSRLAQQE-QERAREIADSLSQLPQQQTDARRQLNEVERRVG-------------TQNGNTP------ 167
Cdd:COG3096 361 -ERLEEQEEVVEEAAEQLAEaEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIqyqqavqalekarALCGLPDltpena 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 168 -------QAQAQN-----LGLQ-----AESAR---------LKALVDELELAQLSANNRQELSRMRSELAQ-KQSEQLDA 220
Cdd:COG3096 440 edylaafRAKEQQateevLELEqklsvADAARrqfekayelVCKIAGEVERSQAWQTARELLRRYRSQQALaQRLQQLRA 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 221 YLQALRNQLnsQRQREAERALESTELLA----ENSDNLPAGIVEQFKVNRELSAALN-QQAQRMDLvaSQQRQATNQT-- 293
Cdd:COG3096 520 QLAELEQRL--RQQQNAERLLEEFCQRIgqqlDAAEELEELLAELEAQLEELEEQAAeAVEQRSEL--RQQLEQLRARik 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 294 ---------LQVRQALNTLREQS-QWLGSSNLLGEALRAQVARLpempkpQQLDTEMAQLRVQRLHFEDllnkqpQIRQI 363
Cdd:COG3096 596 elaarapawLAAQDALERLREQSgEALADSQEVTAAMQQLLERE------REATVERDELAARKQALES------QIERL 663
|
....*
gi 1513194555 364 RQADG 368
Cdd:COG3096 664 SQPGG 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-424 |
2.47e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 119 EKSRLaQQEQERAREIADSLSQLPQqqtDARRQLNEVERRvgtqngntpqAQAQNLGLQAESARLKALVDEL-ELAQLSA 197
Cdd:TIGR02169 689 ELSSL-QSELRRIENRLDELSQELS---DASRKIGEIEKE----------IEQLEQEEEKLKERLEELEEDLsSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 198 NNRQELSRMRSELAQKQSEqldayLQALRNQLNSQRQREAEralestellaensdnlpagivEQFKVNRELSAALNQQAQ 277
Cdd:TIGR02169 755 NVKSELKELEARIEELEED-----LHKLEEALNDLEARLSH---------------------SRIPEIQAELSKLEEEVS 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 278 RMDLVASQQRQATNQTLQVRQalnTLREQSQWLGSSNLLGEALRAQVARLPEmpkpqQLDTEMAQLRvqrlhfEDLLNKQ 357
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKE---YLEKEIQELQEQRIDLKEQIKSIEKEIE-----NLNGKKEELE------EELEELE 874
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513194555 358 PQIRQIRQADGQpLTSEQSRiLEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEA 424
Cdd:TIGR02169 875 AALRDLESRLGD-LKKERDE-LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-425 |
2.69e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 19 AATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQ-QYQQVIDNFPKLSQTLRAQLNNLRDEprdv 97
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAaELAAQLEELEEAEEALLERLERLEEE---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 98 pagmtSDALNQEILQVSSQLLEkSRLAQQE-QERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGL 176
Cdd:COG1196 423 -----LEELEEALAELEEEEEE-EEEALEEaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 177 QAESARLKALVDELELAQLSANNRqELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENsdnlPA 256
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLR-GLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA----KA 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 257 GIVEQFKVN----RELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARL----P 328
Cdd:COG1196 572 GRATFLPLDkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLrevtL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 329 EMPKPQQLDTEMAQLRVQRLHFEDLLNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKLK 408
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
410
....*....|....*..
gi 1513194555 409 VSNSQLEDALKEVNEAT 425
Cdd:COG1196 732 AEREELLEELLEEEELL 748
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
57-213 |
3.41e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 57 EERKGSLERAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDV--PAGMTSDAL---NQEILQVSSQLLEKSRLAQ------ 125
Cdd:PHA02562 206 EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLvmDIEDPSAALnklNTAAAKIKSKIEQFQKVIKmyekgg 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 126 ----------QEQERAREIADSLSQLPQ-----------------QQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQA 178
Cdd:PHA02562 286 vcptctqqisEGPDRITKIKDKLKELQHslekldtaideleeimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKA 365
|
170 180 190
....*....|....*....|....*....|....*..
gi 1513194555 179 ESARLKALV--DELELAQLSaNNRQELSRMRSELAQK 213
Cdd:PHA02562 366 AIEELQAEFvdNAEELAKLQ-DELDKIVKTKSELVKE 401
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
109-429 |
4.12e-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: 48.12 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 109 EILQVSSQLLEKSRLAQQEQE--------RAREIADSLSQLPQQQTDARRQLNEV-ERRVGTQNGNTPQAQAQNlGLQAE 179
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKsteselkkKEKRRDEMLGLAPGRQSIIDLKEKEIpELRNKLQKVNRDIQRLKN-DIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 180 SARLKALVDELELAQLSANNRQELSRMRSEL--AQKQSEQLDAYLQALRNQLNSQRQR-EAERALESTELLAENSDNLPA 256
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELkdVERKIAQQAAKLQGSDLDRTVQQVNqEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 257 GIVEQFKVNRELSAALNQ-QAQRMDL-VASQQRQATNQTLQ--VRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPK 332
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNElKSEKLQIgTNLQRRQQFEEQLVelSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 333 PQQLDTEMAQLRVQRL---------HFEDLLNK--QPQIRQIRQADGQPLT---------SEQSRIlEAQLRTQRELLNS 392
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIkekvknihgYMKDIENKiqDGKDDYLKQKETELNTvnaqleeceKHQEKI-NEDMRLMRQDIDT 1009
|
330 340 350
....*....|....*....|....*....|....*..
gi 1513194555 393 LLQGGDTLILELTKLKVsnsqlEDALKEVNEATHRYL 429
Cdd:TIGR00606 1010 QKIQERWLQDNLTLRKR-----ENELKEVEEELKQHL 1041
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
47-306 |
4.30e-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: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 47 ESLQSALNALEERKGSLERA-----QQYQQ------VIDNFPKLSQTLRAQLNNLRDEPRDVPAgmTSDALNQEILQVSS 115
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNidkikNKLLKlelllsNLKKKIQKNKSLESQISELKKQNNQLKD--NIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 116 QLLEKsrlaqQEQerareiadsLSQLPQQQTDARRQLNEVERRVGTQNG---------NTPQAQAQNLGLQAESARLKAL 186
Cdd:TIGR04523 247 EISNT-----QTQ---------LNQLKDEQNKIKKQLSEKQKELEQNNKkikelekqlNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 187 VDELE---------LAQLSANNR------QELSRMRSELAQKQSEQldaylQALRNQLNSQRQ------REAERALESTE 245
Cdd:TIGR04523 313 KSELKnqekkleeiQNQISQNNKiisqlnEQISQLKKELTNSESEN-----SEKQRELEEKQNeieklkKENQSYKQEIK 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513194555 246 LLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQ 306
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-356 |
4.44e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 135 ADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDELElaqlsannrQELSRMRSELAQKQ 214
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---------QELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 215 SEQldaylQALRNQLNSQRQREAER--------ALESTELLAENSDnlPAGIVEQFKVNRELSAALNQQAQRM----DLV 282
Cdd:COG4942 90 KEI-----AELRAELEAQKEELAELlralyrlgRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELradlAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513194555 283 ASQQRQATNQTLQVRQALNTLREQSQWLgssNLLGEALRAQVARLPEmpKPQQLDTEMAQLRVQRLHFEDLLNK 356
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAAL---EALKAERQKLLARLEK--ELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-245 |
5.02e-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: 47.76 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 27 QITQELEQAKAakpaqpeTVESLQSALNALEER-KGSLERAQQYQQVIDNfpklsqtLRAQLNNLRDEPRDVPAgmTSDA 105
Cdd:TIGR02169 291 RVKEKIGELEA-------EIASLERSIAEKERElEDAEERLAKLEAEIDK-------LLAEIEELEREIEEERK--RRDK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 106 LNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKA 185
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513194555 186 LVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLN--SQRQREAERALESTE 245
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDrvEKELSKLQRELAEAE 496
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
30-536 |
5.35e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.96 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 30 QELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDnfpkLSQTLRAQlnnlrdeprdvpagmtsdalnqe 109
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAE----LEAKRQAE----------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 110 ilqvssqllEKSRLAQQEQERAReiADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQ-----AQAQNLGLQAESARL- 183
Cdd:COG3064 55 ---------EEAREAKAEAEQRA--AELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKeaeaaAAAEKAAAAAEKEKAe 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 184 KALVDELELAQLSANNRQELSRMRS----ELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAGIV 259
Cdd:COG3064 124 EAKRKAEEEAKRKAEEERKAAEAEAaakaEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 260 EQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTE 339
Cdd:COG3064 204 AAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 340 MAQLRVQRLHFEDLLNKQPQIRQIRQADGQPL-TSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDAL 418
Cdd:COG3064 284 ALAGLAAAAAGLVLDDSAALAAELLGAVAAEEaVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGAL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 419 KEVNEATHRYLFWTSDVRPMTFSWPIEIVQDLRRLISLDTFSQLGQASVMMLTSKETIFPLLGALILVGFSIYSRRHFTR 498
Cdd:COG3064 364 GDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVAD 443
|
490 500 510
....*....|....*....|....*....|....*...
gi 1513194555 499 FLERSSSRVGKVTQDHFWLTLRTVFWSILVASPLPVLW 536
Cdd:COG3064 444 LAGGLVGIGKALTGDADALLGILKAVALDGGAVLADLL 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-424 |
7.17e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 193 AQLSANNRQELSRMRSELAQKQSE--QLDAYLQALRNQLNSQRQR--EAERALESTEL-LAENSDNLPAGIVEQFKVNRE 267
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKElaALKKEEKALLKQLAALERRiaALARRIRALEQeLAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 268 LSAalnQQAQRMDLVASQQRQATNQTLQVrqaLNTLREQSQWLGSSNLLGEALRAQVARLpempkpQQLDTEMAQLRVQR 347
Cdd:COG4942 99 LEA---QKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVRRLQYLKYLAPARREQA------EELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513194555 348 lhfEDLLNKQPQIRQIRQAdgqplTSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEA 424
Cdd:COG4942 167 ---AELEAERAELEALLAE-----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-427 |
7.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 118 LEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTqngntpqaqaqnlgLQAESARLKALVDELELAQLSA 197
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--------------LREELEKLEKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 198 NNRQELSRMRSELaqkqsEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAGIVEQFKVNRELSAALNQQAQ 277
Cdd:COG4717 136 ALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 278 RMDLVASQQRQATNQTLQVRQALNTLR-----EQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLHFED 352
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEaaaleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513194555 353 LLNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKlkvSNSQLEDALKEVNEATHR 427
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD---RIEELQELLREAEELEEE 362
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
128-348 |
9.00e-05 |
|
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: 46.87 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 128 QERAREIADSLSQLPQQQTDARRQLNEverrvgtqngntpqaqaqnlglqaESARLKALVDELElaqlsannrqELSRMR 207
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAE------------------------EQYRLVEMARELE----------ELSARE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 208 SELA---QKQSEQLDAYLQALRNQLNSQRQRE-----AERALESTELLAENSDNLpAGIVEQFKVNR-ELSAALNQQAQR 278
Cdd:COG3096 323 SDLEqdyQAASDHLNLVQTALRQQEKIERYQEdleelTERLEEQEEVVEEAAEQL-AEAEARLEAAEeEVDSLKSQLADY 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 279 MDLVASQQRQAtnqtLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRvQRL 348
Cdd:COG3096 402 QQALDVQQTRA----IQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRA--KEQQATEEVLELE-QKL 464
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
119-308 |
1.07e-04 |
|
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: 46.10 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 119 EKSRLAQQEQERAREIADSLSQLPQQQTDA---RRQLNEVERRvgtqngntpqaqaqnlgLQAESARLKALvdELELAQL 195
Cdd:pfam15709 359 EQRRLQQEQLERAEKMREELELEQQRRFEEirlRKQRLEEERQ-----------------RQEEEERKQRL--QLQAAQE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 196 SANNRQ-ELSRMRSELAQKQSEQldaylQALRNQLNSQRQREAERAL-ESTELLAENSDNlpagivEQFKVNRELSAAln 273
Cdd:pfam15709 420 RARQQQeEFRRKLQELQRKKQQE-----EAERAEAEKQRQKELEMQLaEEQKRLMEMAEE------ERLEYQRQKQEA-- 486
|
170 180 190
....*....|....*....|....*....|....*
gi 1513194555 274 qqAQRMDLVASQQRQATNQtlQVRQALNTLREQSQ 308
Cdd:pfam15709 487 --EEKARLEAEERRQKEEE--AARLALEEAMKQAQ 517
|
|
| PRK11465 |
PRK11465 |
putative mechanosensitive channel protein; Provisional |
873-956 |
1.10e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 183147 [Multi-domain] Cd Length: 741 Bit Score: 46.31 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 873 ITTITkylIMLFgglvgFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSITKI 952
Cdd:PRK11465 521 ISTIT---IMIV-----LSEIGVNIAPLLAGAGALGLAISFGSQTLVKDIITGVFIQFENGMNTGDLVTIGPLTGTVERM 592
|
....
gi 1513194555 953 NTRA 956
Cdd:PRK11465 593 SIRS 596
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
31-392 |
1.26e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 31 ELE--QAKAAKPA--QPETVESLQSALNAL-EERKGSLERAQQYQQvidnfpklsqtlraQLNNL--RDE-PRDVPAGMT 102
Cdd:PRK10246 199 ELEklQAQASGVAllTPEQVQSLTASLQVLtDEEKQLLTAQQQQQQ--------------SLNWLtrLDElQQEASRRQQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 103 SDALNQEILQVSSQLLEKSRLAQQEQ------ERAREIADSLSQLPQQQTDARRQLNEV-ERRVGTQNGNTPQAQAqnlg 175
Cdd:PRK10246 265 ALQQALAAEEKAQPQLAALSLAQPARqlrphwERIQEQSAALAHTRQQIEEVNTRLQSTmALRARIRHHAAKQSAE---- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 176 LQAESARLKALVDELELAQLSannRQELSRMRSELAQKQSEQldAYLQALRNQLNSQRQREAEralestelLAENSDNLP 255
Cdd:PRK10246 341 LQAQQQSLNTWLAEHDRFRQW---NNELAGWRAQFSQQTSDR--EQLRQWQQQLTHAEQKLNA--------LPAITLTLT 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 256 AgiveqfkvnRELSAALNQQAQRMDLvasqqrqatnqtlqvRQALNTLREQSQwlgssnllgeALRAQVARLPEmpKPQQ 335
Cdd:PRK10246 408 A---------DEVAAALAQHAEQRPL---------------RQRLVALHGQIV----------PQQKRLAQLQV--AIQN 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 336 LDTEMAQLRVQrlhfedLLNKQPQIRQIRQ--ADGQPLTSEQSRIleAQLRTQRELLNS 392
Cdd:PRK10246 452 VTQEQTQRNAA------LNEMRQRYKEKTQqlADVKTICEQEARI--KDLEAQRAQLQA 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-423 |
1.39e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 24 DAKQITQELEQAKAA-KPAQPE---TVESLQSALNALEERKGSLERAQQyqqVIDNFPKLSQTLRAQLNNLRDEPRDVpa 99
Cdd:TIGR04523 233 NIEKKQQEINEKTTEiSNTQTQlnqLKDEQNKIKKQLSEKQKELEQNNK---KIKELEKQLNQLKSEISDLNNQKEQD-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 100 gmTSDALNQEILQVSSQLLE-KSRLAQQEQeRAREIADSLSQLPQQQTDA-------RRQLNEVERRVGTQNgntpqaqA 171
Cdd:TIGR04523 308 --WNKELKSELKNQEKKLEEiQNQISQNNK-IISQLNEQISQLKKELTNSesensekQRELEEKQNEIEKLK-------K 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 172 QNLGLQAESARLKALVDELELA-----QLSANNRQELSRMRSELAQKQSEQLDayLQALRNQLNSQrQREAERALESTEL 246
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKiqnqeKLNQQKDEQIKKLQQEKELLEKEIER--LKETIIKNNSE-IKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 247 LAENSDNLPAGIVEQFKVN----RELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQwlgSSNLLGEALRA 322
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLsrsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS---SLKEKIEKLES 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 323 QVARLPEmpKPQQLDTEMAQLRvQRLHFEDL----LNKQPQIRQIRQadgqpltsEQSRILEAQLRTQrELLNSLLQGGD 398
Cdd:TIGR04523 532 EKKEKES--KISDLEDELNKDD-FELKKENLekeiDEKNKEIEELKQ--------TQKSLKKKQEEKQ-ELIDQKEKEKK 599
|
410 420
....*....|....*....|....*
gi 1513194555 399 TLILELTKLKVSNSQLEDALKEVNE 423
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-427 |
2.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 27 QITQELEQAKAAkpaqpetVESLQSALNALEERKGSLERAQQYQ--QVIDNFPKLSQTLRAQLNNLRDEPR--------- 95
Cdd:COG4913 299 ELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLERELEERERRRArleallaal 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 96 DVPAGMTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRvgtqNGNTPQAQAQNLG 175
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR----KSNIPARLLALRD 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 176 LQAESARLKAlvDEL----ELAQLSAnnRQELSRMRSELA---QKQS-----EQLDAYLQA-----LRNQLNSQRQREAE 238
Cdd:COG4913 448 ALAEALGLDE--AELpfvgELIEVRP--EEERWRGAIERVlggFALTllvppEHYAAALRWvnrlhLRGRLVYERVRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 239 RALESTELlaensdnLPAGIVE--QFKVNrELSAALNQQ-AQRMDL--VASQQ-----RQATNQTLQVRQAlNTLRE--Q 306
Cdd:COG4913 524 PDPERPRL-------DPDSLAGklDFKPH-PFRAWLEAElGRRFDYvcVDSPEelrrhPRAITRAGQVKGN-GTRHEkdD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 307 SQWLGSSNLLG-------EALRAQVARLPEmpKPQQLDTEMAQLRVQRlhfEDLLNKQPQIRQIRQADGQPLTSEQsriL 379
Cdd:COG4913 595 RRRIRSRYVLGfdnraklAALEAELAELEE--ELAEAEERLEALEAEL---DALQERREALQRLAEYSWDEIDVAS---A 666
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1513194555 380 EAQLRTQRELLNSLLQGGDtlilELTKLKvsnSQLEDALKEVNEATHR 427
Cdd:COG4913 667 EREIAELEAELERLDASSD----DLAALE---EQLEELEAELEELEEE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-428 |
2.52e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 13 LSMGAYAATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRAQLNNLRD 92
Cdd:TIGR00606 207 MELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 93 E---PRDVPAGMTSDALNQEILQVSSQLLEKsrlaqqEQERAReIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQA 169
Cdd:TIGR00606 287 ElelKMEKVFQGTDEQLNDLYHNHQRTVREK------ERELVD-CQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 170 QAQNLG--LQAESARLKALVDELE---LAQLSANNRQELSRMRSELAQKQSEQLDAYLQalrnqlnsQRQREAERALesT 244
Cdd:TIGR00606 360 QEHIRArdSLIQSLATRLELDGFErgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ--------SKERLKQEQA--D 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 245 ELLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVASQQRqatnqTLQVRQAL-NTLREQSQWLGSSN---LLGEAL 320
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR-----ILELDQELrKAERELSKAEKNSLtetLKKEVK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 321 RAQVARLPEMPKPQQLDTEMAQL------RVQRLHF-EDLLNKQPQIRQIRQADGQPLTSE-----QSRILEAQLRTQRE 388
Cdd:TIGR00606 505 SLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQLEDWLHSKSK 584
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1513194555 389 LLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHRY 428
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
16-300 |
2.62e-04 |
|
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: 44.67 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 16 GAYAATAPDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERaQQYQQVIDNfpklsQTLRAQLNNLRDEPR 95
Cdd:pfam19220 76 RRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALER-QLAAETEQN-----RALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 96 dvpagmTSDALNQEILQVSSQLLEKSRLAQQE----QERAREIADSLSQLpqqqtdaRRQLNEVERRVGTQNGNTPQAQA 171
Cdd:pfam19220 150 ------AAEKALQRAEGELATARERLALLEQEnrrlQALSEEQAAELAEL-------TRRLAELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 172 QNLGLQAESARLKALVDElELAQLsannRQELS--RMRSELAQKQSEQLDAYLQALRNQLN--SQRQREAERALESTELL 247
Cdd:pfam19220 217 QLAAEQAERERAEAQLEE-AVEAH----RAERAslRMKLEALTARAAATEQLLAEARNQLRdrDEAIRAAERRLKEASIE 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513194555 248 AENSDNLPAGI-------VEQFK---------------VNRELSA---ALNQQAQRMDLVASQQRQATNQTLQVRQAL 300
Cdd:pfam19220 292 RDTLERRLAGLeadlerrTQQFQemqraraeleeraemLTKALAAkdaALERAEERIASLSDRIAELTKRFEVERAAL 369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
13-243 |
2.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 13 LSMGAYAATA-PDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSL-ERAQQYQQVIDNFPKLSQTLRAQLNNL 90
Cdd:COG3883 5 ALAAPTPAFAdPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELqAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 91 RDEPRDVPA-----GMTSDALNQeILQVSS--QLLEK----SRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRV 159
Cdd:COG3883 85 REELGERARalyrsGGSVSYLDV-LLGSESfsDFLDRlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 160 GTQNGNTPQAQAQNLGLQAESARLKALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAER 239
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
....
gi 1513194555 240 ALES 243
Cdd:COG3883 244 ASAA 247
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
19-322 |
3.22e-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: 44.75 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 19 AATAPDAKQITQELEQAK--AAKPAQPETVESLQSALNALEERKGSLERAQQYQQVIDNFPKLS--------QTLRAQLN 88
Cdd:pfam09731 189 EALAEKLKEVINLAKQSEeeAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVaserivfqQELVSIFP 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 89 NLRDEPRDVPAGMTSDA------LNQEILQVSSQLLEksrlaQQEQERAReIADSLSQLPQQQTDARRQLneverrvgtq 162
Cdd:pfam09731 269 DIIPVLKEDNLLSNDDLnsliahAHREIDQLSKKLAE-----LKKREEKH-IERALEKQKEELDKLAEEL---------- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 163 ngntpqaqaqnlglqaeSARLKALVDElELAQLSANNRQELSRMRSELAQKQSEQLD----AYLQALRNQLNSQRQ---R 235
Cdd:pfam09731 333 -----------------SARLEEVRAA-DEAQLRLEFEREREEIRESYEEKLRTELErqaeAHEEHLKDVLVEQEIelqR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 236 EAERALEstELLAENSDNLPAGIVEQFKVNRELSAALNQQAQrmdlVASQQRQAtnQTLQVR-QALNTLREQSQWLGSSN 314
Cdd:pfam09731 395 EFLQDIK--EKVEEERAGRLLKLNELLANLKGLEKATSSHSE----VEDENRKA--QQLWLAvEALRSTLEDGSADSRPR 466
|
....*...
gi 1513194555 315 LLGEALRA 322
Cdd:pfam09731 467 PLVRELKA 474
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
105-438 |
3.22e-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: 44.78 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 105 ALNQEILQVSSQLL---EKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVgtqNGNTPQAQAQNLGLQAESA 181
Cdd:pfam01576 156 LLEERISEFTSNLAeeeEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKL---EGESTDLQEQIAELQAQIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 182 RLKALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQR----EAERALESTELLA---ENSDNL 254
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaEKQRRDLGEELEAlktELEDTL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 255 PAGIVEQ-FKVNRE-----LSAALNQQAQRMDLVASQQRQATNqtlqvrQALNTLREQSQWL--GSSNL--LGEALRAQV 324
Cdd:pfam01576 313 DTTAAQQeLRSKREqevteLKKALEEETRSHEAQLQEMRQKHT------QALEELTEQLEQAkrNKANLekAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 325 ARLP-EMPKPQQLDTEMAQLRVQrlhfedlLNKQPQIRQIRQADGQPLTSEQSRILeAQLRTQRELLNSLLQGGDTLILE 403
Cdd:pfam01576 387 AELQaELRTLQQAKQDSEHKRKK-------LEGQLQELQARLSESERQRAELAEKL-SKLQSELESVSSLLNEAEGKNIK 458
|
330 340 350
....*....|....*....|....*....|....*.
gi 1513194555 404 LTK-LKVSNSQLEDALKEVNEATHRYLFWTSDVRPM 438
Cdd:pfam01576 459 LSKdVSSLESQLQDTQELLQEETRQKLNLSTRLRQL 494
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
124-304 |
5.39e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 124 AQQEQERARE-----IADSLSQLPQQQTDARRQLNEVERR----VGTQNGNTPQAQAQNLGLQaESArlkalvdELELAQ 194
Cdd:NF041483 726 ADQERERAREqseelLASARKRVEEAQAEAQRLVEEADRRatelVSAAEQTAQQVRDSVAGLQ-EQA-------EEEIAG 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 195 LSANNRQELSRMRSElAQKQSEQL--DAYLQALRNQLNSQR-QREAERALESTELLAENSdnlpagIVEQFKVNRELSAA 271
Cdd:NF041483 798 LRSAAEHAAERTRTE-AQEEADRVrsDAYAERERASEDANRlRREAQEETEAAKALAERT------VSEAIAEAERLRSD 870
|
170 180 190
....*....|....*....|....*....|....*...
gi 1513194555 272 LNQQAQRM-----DLVASQQRQATNQTLQVRQALNTLR 304
Cdd:NF041483 871 ASEYAQRVrteasDTLASAEQDAARTRADAREDANRIR 908
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-356 |
5.64e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 24 DAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAqqyqqvIDNFPKLSQTLRAQLNNLRDEPRDVPAGMTS 103
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD------LGNAEDFLEELREERDELREREAELEATLRT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 104 DalnQEILQVSSQLLEKSRLAQQEQE-RAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAqnlgLQAESAR 182
Cdd:PRK02224 438 A---RERVEEAEALLEAGKCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED----LVEAEDR 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 183 LKALVDELE-LAQLSANNRQELSRMRSELAQ--KQSEQLDAYLQALRNQLNSQRQrEAERALEST----ELLAENSDNLp 255
Cdd:PRK02224 511 IERLEERREdLEELIAERRETIEEKRERAEElrERAAELEAEAEEKREAAAEAEE-EAEEAREEVaelnSKLAELKERI- 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 256 agivEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGS----SNLlgEALRAQVARLPEMp 331
Cdd:PRK02224 589 ----ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefdeARI--EEAREDKERAEEY- 661
|
330 340
....*....|....*....|....*
gi 1513194555 332 kPQQLDTEMAQLRVQRlhfEDLLNK 356
Cdd:PRK02224 662 -LEQVEEKLDELREER---DDLQAE 682
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
28-423 |
6.21e-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: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 28 ITQELEQAKAAKPAQPETVESLQsalNALEERKGS---LERAQQYQQVIDNFPKLSQTLRAQLNNLRDeprdvpagmTSD 104
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIK---ESETGNLGSestLLEKAKEIINIEEALKGFQDPESELEDLAQ---------TSD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 105 ALNQEILQVSSQLLEKSRlaqQEQERAREIADSLSQLPQQQTDARRQLNEVErrvgtqngntpQAQAQNLGLQAESARLK 184
Cdd:COG5185 254 KLEKLVEQNTDLRLEKLG---ENAESSKRLNENANNLIKQFENTKEKIAEYT-----------KSIDIKKATESLEEQLA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 185 ALVDELELAQLSANNRQELSRMRSELAQKQsEQLDAYLQALRNQLNS----QRQREAERALESTEL-LAENSDNLPAGIV 259
Cdd:COG5185 320 AAEAEQELEESKRETETGIQNLTAEIEQGQ-ESLTENLEAIKEEIENivgeVELSKSSEELDSFKDtIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 260 EQFKVNRELSAALNqqaqrmDLVASQQRQATNQTLQVRQALNTLREqsqwlgSSNLLGEALRAQVARLPEMPKPQQLDTE 339
Cdd:COG5185 399 NQRGYAQEILATLE------DTLKAADRQIEELQRQIEQATSSNEE------VSKLLNELISELNKVMREADEESQSRLE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 340 MAQLRVQRLHFEDLLNKQPQIRQIRQadgqpltseQSRILEAQLRTQRELLNSLLQGGDTLILELT-KLKVSNSQLEDAL 418
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIES---------RVSTLKATLEKLRAKLERQLEGVRSKLDQVAeSLKDFMRARGYAH 537
|
....*
gi 1513194555 419 KEVNE 423
Cdd:COG5185 538 ILALE 542
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
17-398 |
6.48e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 17 AYAATAPDAKQ-----ITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQQyqqvidNFPKLSQTLRAQLNNLR 91
Cdd:PRK10246 519 AYQALEPGVNQsrldaLEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQ------ALTQQWQAVCASLNITL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 92 DEPRDVPAGMTS-DALNQEILQVSSQLLEKSRLA-QQEQERAREiadslSQLPQQQTDARRQLNEVERRVGTQNGNTP-- 167
Cdd:PRK10246 593 QPQDDIQPWLDAqEEHERQLRLLSQRHELQGQIAaHNQQIIQYQ-----QQIEQRQQQLLTALAGYALTLPQEDEEASwl 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 168 -----------QAQAQNLGLQAESARLKALVDEL--------ELAQLSANNRQElsrmrselAQKQSEQLDAYLQALRNQ 228
Cdd:PRK10246 668 atrqqeaqswqQRQNELTALQNRIQQLTPLLETLpqsddlphSEETVALDNWRQ--------VHEQCLSLHSQLQTLQQQ 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 229 LNSQRQREAERALESTELLAensdNLPAGIVEQFkvnreLSAALNQQA-QRMDlvasQQRQATNQTLQVRQALNTLREQS 307
Cdd:PRK10246 740 DVLEAQRLQKAQAQFDTALQ----ASVFDDQQAF-----LAALLDEETlTQLE----QLKQNLENQRQQAQTLVTQTAQA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 308 qwlgssnlLGEALRAQVARLPEMPKPQQLDTEMAQLrVQRLhfEDLLNKQPQIRQIRQADGQPLTSEQSRILE-AQLRTQ 386
Cdd:PRK10246 807 --------LAQHQQHRPDGLDLTVTVEQIQQELAQL-AQQL--RENTTRQGEIRQQLKQDADNRQQQQALMQQiAQATQQ 875
|
410
....*....|....*..
gi 1513194555 387 RE---LLNSLL--QGGD 398
Cdd:PRK10246 876 VEdwgYLNSLIgsKEGD 892
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
109-240 |
6.83e-04 |
|
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: 43.79 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 109 EILQVSSQLLEKSRLAQQEQERAREIadslsQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNlgLQAESARLKALVD 188
Cdd:pfam15709 387 EEIRLRKQRLEEERQRQEEEERKQRL-----QLQAAQERARQQQEEFRRKLQELQRKKQQEEAER--AEAEKQRQKELEM 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513194555 189 EL-----ELAQLSANNRQELSRmrselaQKQSEQLDAYLQAlrnqlNSQRQREAERA 240
Cdd:pfam15709 460 QLaeeqkRLMEMAEEERLEYQR------QKQEAEEKARLEA-----EERRQKEEEAA 505
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
56-192 |
7.34e-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: 43.08 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 56 LEERKGSLERAQQYQQVIDNF-PKLS---QTLRAQLNNLRDEPRDVPAGMTS--DALNQEILQVSSQLLEKSRLAQQEQE 129
Cdd:smart00787 153 LEGLKEDYKLLMKELELLNSIkPKLRdrkDALEEELRQLKQLEDELEDCDPTelDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513194555 130 RAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQaqaqnlglqaESARLKALVDELEL 192
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK----------EIEKLKEQLKLLQS 285
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
163-396 |
8.38e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.44 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 163 NGNTPQAQAQnlgLQAESARLK-AL---VDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAE 238
Cdd:pfam13779 481 DGDLSDAERR---LRAAQERLSeALergASDEEIAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQDLQ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 239 RALESTELLAENSDNLPAGiveqfKVNRELSAALNQ-QAQRMdlvASQQRQATNQTLQVRQAL-NTLREQSQwlgssnLL 316
Cdd:pfam13779 558 RMLDRIEELARSGRRAEAQ-----QMLSQLQQMLENlQAGQP---QQQQQQGQSEMQQAMDELgDLLREQQQ------LL 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 317 GEALRaqvarlpEMPKPQQLDTEMAQLRVQRlhfedllNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQ----RELLNS 392
Cdd:pfam13779 624 DETFR-------QLQQQGGQQQGQPGQQGQQ-------GQGQQPGQGGQQPGAQMPPQGGAEALGDLAERqqalRRRLEE 689
|
....
gi 1513194555 393 LLQG 396
Cdd:pfam13779 690 LQDE 693
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
57-390 |
1.03e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 57 EERKGSLERAQQYQQVIDNfpkLSQTLRAQ--LNNLRDEPRDVPAGMTSDALNQEILQVssqllEKSRLAQQEQER-ARE 133
Cdd:pfam10174 60 EQYRVTQEENQHLQLTIQA---LQDELRAQrdLNQLLQQDFTTSPVDGEDKFSTPELTE-----ENFRRLQSEHERqAKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 134 iadsLSQLpqqqtdaRRQLNEVERRVGTQNG--NTPQAQAQNL--GLQAESARLKALVDELELAQLSANNRQELSRMRSE 209
Cdd:pfam10174 132 ----LFLL-------RKTLEEMELRIETQKQtlGARDESIKKLleMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 210 LAQKQSEqldayLQALRNQLNSQRQREAERAleSTELLAENSDNLPAGIVEQFKVNREL---------SAALN-----QQ 275
Cdd:pfam10174 201 LDQKEKE-----NIHLREELHRRNQLQPDPA--KTKALQTVIEMKDTKISSLERNIRDLedevqmlktNGLLHtedreEE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 276 AQRMDLVASQQRQATNQTLQVRQALN-------TLREQSQWLGSSN--------LLGEALRAQVARlpempkPQQLDTEM 340
Cdd:pfam10174 274 IKQMEVYKSHSKFMKNKIDQLKQELSkkesellALQTKLETLTNQNsdckqhieVLKESLTAKEQR------AAILQTEV 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1513194555 341 AQLRVQRLHFEDLLN-KQPQIrqirqadgQPLTSEQSrILEAQLRTQRELL 390
Cdd:pfam10174 348 DALRLRLEEKESFLNkKTKQL--------QDLTEEKS-TLAGEIRDLKDML 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
81-263 |
1.35e-03 |
|
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: 41.45 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 81 QTLRAQLNNLRDEPRDVPAGMtsDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVerrvg 160
Cdd:COG1579 13 QELDSELDRLEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 161 tqnGNTPQAQAqnlgLQAESARLKALVDELELAQLSANNRQE-----LSRMRSELAQKQsEQLDAYLQALRNQLNSQRQR 235
Cdd:COG1579 86 ---RNNKEYEA----LQKEIESLKRRISDLEDEILELMERIEeleeeLAELEAELAELE-AELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|....*...
gi 1513194555 236 EAERALESTELLAEnsdnLPAGIVEQFK 263
Cdd:COG1579 158 LEELEAEREELAAK----IPPELLALYE 181
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
66-313 |
1.38e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 66 AQQYQQVIDNFPKLSQTLRAQLNNLRDEprdvpagmtSDALNQEILQVSSQLLEksrlAQQEQERAR-EIADSLSQLPQQ 144
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---------LEELNEEYNELQAELEA----LQAEIDKLQaEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 145 QTDARRQLNEVERRVGTQN-------GNTPQA---QAQNLGLQAESAR-----LKALVDELELAQLSANN-RQELSRMRS 208
Cdd:COG3883 85 REELGERARALYRSGGSVSyldvllgSESFSDfldRLSALSKIADADAdlleeLKADKAELEAKKAELEAkLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 209 ELAQKQSEqLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAGIVEQFKVNRELSAALNQQAQRMDLVASQQRQ 288
Cdd:COG3883 165 ELEAAKAE-LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|....*
gi 1513194555 289 ATNQTLQVRQALNTLREQSQWLGSS 313
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
47-427 |
1.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 47 ESLQSALNALEERKGSLE-RAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDVPAGMTSDALNQEILQVSSQLLE-KSRLA 124
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEeEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 125 QQEQErarEIADSLSQLPQQQTDARRQLNEVERRVGtqngntpqaqaqnlGLQAESARLKALVDELELAQ---------L 195
Cdd:PRK03918 383 GLTPE---KLEKELEELEKAKEEIEEEISKITARIG--------------ELKKEIKELKKAIEELKKAKgkcpvcgreL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 196 SANNRQEL-SRMRSELA--QKQSEQLDAYLQALRNQLnsqrqREAERALESTELLAENSDnlpagIVEQFKvnrELSAAL 272
Cdd:PRK03918 446 TEEHRKELlEEYTAELKriEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKE-----LAEQLK---ELEEKL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 273 NQqaqrmdLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQL--RVQRLHF 350
Cdd:PRK03918 513 KK------YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--KLDELEEELAELlkELEELGF 584
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513194555 351 EDLLNKQPQIRQIRQADGQPLTSEQS-RILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDALKEVNEATHR 427
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYLELKDAeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
105-326 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 105 ALNQEILQVSSQLLEKSRLAQQ-EQER---AREIADSLSQLPQQQTDARR---QLNEVERRVGTQNGNTP-------QAQ 170
Cdd:pfam01576 837 NLEAELLQLQEDLAASERARRQaQQERdelADEIASGASGKSALQDEKRRleaRIAQLEEELEEEQSNTEllndrlrKST 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 171 AQNLGLQAEsarlkaLVDELELAQLSANNRQELSRmrselaqkQSEQLDAYLQALRNQLNSqRQREAERALESTELLAEN 250
Cdd:pfam01576 917 LQVEQLTTE------LAAERSTSQKSESARQQLER--------QNKELKAKLQEMEGTVKS-KFKSSIAALEAKIAQLEE 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 251 SdnlpagiVEQFKVNRELSAALNQQAQR-----MDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNllGEALRAQVA 325
Cdd:pfam01576 982 Q-------LEQESRERQAANKLVRRTEKklkevLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE--EEASRANAA 1052
|
.
gi 1513194555 326 R 326
Cdd:pfam01576 1053 R 1053
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
24-181 |
1.77e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.28 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 24 DAKQITQELEQAkaakpaqpetVESLQSALNALEERKGSLERAQQYQQvidnfpkLSQTLRAQlNNLRDEP---RDVPAG 100
Cdd:pfam13779 574 EAQQMLSQLQQM----------LENLQAGQPQQQQQQGQSEMQQAMDE-------LGDLLREQ-QQLLDETfrqLQQQGG 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 101 MTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGntpQAQAQNLGlQAES 180
Cdd:pfam13779 636 QQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEELQDELKELGG---KEPGQALG-DAGR 711
|
.
gi 1513194555 181 A 181
Cdd:pfam13779 712 A 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-424 |
1.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 27 QITQELEQAKAAKpaqpETVESLQSALNALEERKGSLE-RAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDVPagmtsda 105
Cdd:PRK03918 218 ELREELEKLEKEV----KELEELKEEIEELEKELESLEgSKRKLEEKIRELEERIEELKKEIEELEEKVKELK------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 106 lnqEILQVSSQLLEKSRLAQQEQERAREIADSLSQLpqqqtdaRRQLNEVERRVGTqngntpqaqaqnlgLQAESARLKA 185
Cdd:PRK03918 287 ---ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-------EEEINGIEERIKE--------------LEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 186 LVDELElaqlsannrqELSRMRSELaqKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAGIVEQFKVN 265
Cdd:PRK03918 343 LKKKLK----------ELEKRLEEL--EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 266 RELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQsqwlgssNLLGEaLRAQVARLPEmpKPQQLDTEMAQLRV 345
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-------ELLEE-YTAELKRIEK--ELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 346 QRLHFEDLLNKQPQIRQIRQadgqplTSEQSRILEAQL---------------RTQRELLNSLlqGGDTLIL--ELTKLK 408
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKE------LAEQLKELEEKLkkynleelekkaeeyEKLKEKLIKL--KGEIKSLkkELEKLE 552
|
410
....*....|....*.
gi 1513194555 409 VSNSQLEDALKEVNEA 424
Cdd:PRK03918 553 ELKKKLAELEKKLDEL 568
|
|
| V_AnPalA_UmRIM20_like |
cd09236 |
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ... |
134-428 |
2.24e-03 |
|
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.
Pssm-ID: 185749 [Multi-domain] Cd Length: 353 Bit Score: 41.57 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 134 IADSLSQLPQQQTDARRQLN------EVERRVGTqngntPQ---AQAQNLGLQAESARLKALVDELelAQLSANNRQELS 204
Cdd:cd09236 23 IIDELEELTNRAHSTLRSLNlpgslqALEKPLGL-----PPsllRHAEEIRQEDGLERIRASLDDV--ARLAASDRAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 205 RMRSELAQKQSEQLDAYLQALRNQLNSQRQREA-----ERALESTELL--AENSDNLpagIVEQFKVNRELSAALN-QQA 276
Cdd:cd09236 96 EAMDILDDEASEDESLRRKFGTDRWTRPDSHEAnpklyTQAAEYEGYLkqAGASDEL---VRRKLDEWEDLIQILTgDER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 277 QRMDLVASQQRQATNQTLQ-----VRQALNTL----REQSQWLGSSNLLGEA--LRAQVARlpEMPKpqqLDTEMAQLRV 345
Cdd:cd09236 173 DLENFVPSSRRPSIPPELErhvraLRVSLEELdrleSRRRRKVERARTKARAddIRPEILR--EAAR---LEREYPATEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 346 QRLHFEDLLNKQPQIRQIRQADGQPLTSEQSRILEaQLRTQRELLnsllqggdtliLELTKLKVSNSQLEDALKEVNEAT 425
Cdd:cd09236 248 APAHFEDLFDKRLAKYDKDLDAVSEEAQEQEEILQ-QIEVANKAF-----------LQSRKGDPATKERERALQSLDLAY 315
|
...
gi 1513194555 426 HRY 428
Cdd:cd09236 316 FKY 318
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
26-135 |
2.63e-03 |
|
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: 40.65 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 26 KQITQELEQAKaakpAQPETVESLQSALNALEERKGSLERAQQYQQVIDNfPKLSQTLRAQLNNLRDEPrdvpagmtsda 105
Cdd:NF038305 111 QQINQQAGQQE----TQLQQQLNQLQAQTSPQQLNQLLKSEQKQGQALAS-GQLPEEQKEQLQQFKSNP----------- 174
|
90 100 110
....*....|....*....|....*....|
gi 1513194555 106 lnQEILQVSSQLLEKSRLAQQEQERAREIA 135
Cdd:NF038305 175 --QALDKFLAQQLTQIRTQAEEAEKQARLE 202
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
92-348 |
3.25e-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: 40.98 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 92 DEPRDVPAGMTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRvgtQNGNTPQAQA 171
Cdd:TIGR02794 24 YHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQAR---QKELEQRAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 172 QNLGLQAESARLKALVDELELAQLSANNRQE--------LSRMRSELAQKQSEQ---LDAYLQALRNQLNSQRQREAErA 240
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEakakaeaeAERKAKEEAAKQAEEeakAKAAAEAKKKAEEAKKKAEAE-A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 241 LESTELLAENSDNLPAGIVEQFKVNRELSA-ALNQQAQRMDLVASQQRQATNQTLQVRQAL-NTLREQSQWLGSSNLLGE 318
Cdd:TIGR02794 180 KAKAEAEAKAKAEEAKAKAEAAKAKAAAEAaAKAEAEAAAAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGS 259
|
250 260 270
....*....|....*....|....*....|
gi 1513194555 319 ALRAQVARLPEMPKPQQLDTEMAQLRVQRL 348
Cdd:TIGR02794 260 EVDKYAAIIQQAIQQNLYDDPSFRGKTCRL 289
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
33-210 |
3.46e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 33 EQAKAAKPAQPEtveslQSALNALEERKGSLERAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDVPAGmtsdalnQEILq 112
Cdd:COG1842 72 EKARLALEKGRE-----DLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK-------KDTL- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 113 vssqlleKSRLAQQE-QERAREIADSLSQlpqqqTDARRQLNEVERRVGTQngntpQAQAQnlgLQAESARLKALVDELE 191
Cdd:COG1842 139 -------KARAKAAKaQEKVNEALSGIDS-----DDATSALERMEEKIEEM-----EARAE---AAAELAAGDSLDDELA 198
|
170
....*....|....*....
gi 1513194555 192 LAQLSANNRQELSRMRSEL 210
Cdd:COG1842 199 ELEADSEVEDELAALKAKM 217
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
53-308 |
3.62e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 53 LNALEERKGSLEraqqyqQVIDNFP----KLSQTLRAQLNNLRD------------EPRDVPAgmTSDALNQEILQVSSQ 116
Cdd:PRK04778 200 LDQLEEELAALE------QIMEEIPellkELQTELPDQLQELKAgyrelveegyhlDHLDIEK--EIQDLKEQIDENLAL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 117 L--LEKSRLAQQEQERAREIaDSLSQLPQQQTDARrqlNEVERRVGTQNGNTPQAQAQNLGLQAESARL----------- 183
Cdd:PRK04778 272 LeeLDLDEAEEKNEEIQERI-DQLYDILEREVKAR---KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVkqsytlnesel 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 184 ---KALVDELE--------LAQLSANNRQELSRMRSELAQ---------KQSEQLDAYLQALRNQLNSQRQR--EAERAL 241
Cdd:PRK04778 348 esvRQLEKQLEslekqydeITERIAEQEIAYSELQEELEEilkqleeieKEQEKLSEMLQGLRKDELEAREKleRYRNKL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513194555 242 ESTELLAENSdNL---PAGIVEQFKV----NRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQ 308
Cdd:PRK04778 428 HEIKRYLEKS-NLpglPEDYLEMFFEvsdeIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENAT 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
27-225 |
4.10e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 27 QITQELEQAKAAKPAQPETVESLQSALNALEERKGSL-ERAQQYQQVIDNFPKLSQTL------RAQLNNLRDEPRDVpa 99
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLaQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEELRSL-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 100 gmtsdalnQEILQVSSQLLE--KSRLAQQEQERAREIAD------SLSQLPQQQTDARRQLNE------VERRVGTQNGN 165
Cdd:pfam07888 243 --------QERLNASERKVEglGEELSSMAAQRDRTQAElhqarlQAAQLTLQLADASLALREgrarwaQERETLQQSAE 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513194555 166 TPQAQAQNLG---LQAESA----RLKALVDELELAQLSANNRQELSRMRSEL---------AQKQSEQLDAYLQAL 225
Cdd:pfam07888 315 ADKDRIEKLSaelQRLEERlqeeRMEREKLEVELGREKDCNRVQLSESRRELqelkaslrvAQKEKEQLQAEKQEL 390
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-395 |
4.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 201 QELSRMRSELAQKQSEQLDAYLQALRNQLnsqrqREAERALEstELLAENSDNLPAgivEQFKVNRELSAALNQQAQRmd 280
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKEL-----EEAEAALE--EFRQKNGLVDLS---EEAKLLLQQLSELESQLAE-- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 281 lVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGE------ALRAQVARL-----PEMPKPQQLDTEMAQLR--VQR 347
Cdd:COG3206 231 -ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlaELEAELAELsarytPNHPDVIALRAQIAALRaqLQQ 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513194555 348 LHFEDLLNKQPQIRQIR---------------QADGQPLTSEQSRILEAQLRTQRELLNSLLQ 395
Cdd:COG3206 310 EAQRILASLEAELEALQareaslqaqlaqleaRLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
98-291 |
5.31e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 98 PAGMTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNL-GL 176
Cdd:pfam06008 44 ILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLsRM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 177 QAESARLKALVDELELAQLSANNRQE-------LSRMRsELAQKQSEQLDAYLQALRNQLN--SQRQREAERALESTELL 247
Cdd:pfam06008 124 LAEAQRMLGEIRSRDFGTQLQNAEAElkaaqdlLSRIQ-TWFQSPQEENKALANALRDSLAeyEAKLSDLRELLREAAAK 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1513194555 248 AENSDNLpagiveqfkvNRELSAALNQQAQRMDLVASQQRQATN 291
Cdd:pfam06008 203 TRDANRL----------NLANQANLREFQRKKEEVSEQKNQLEE 236
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
22-190 |
5.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 22 APDAKQITQELEQAKAAKPAQPETVESLQSALNALEERKGSLERAQ----QYQQV-------IDNFPKLSQTLRAQLNNL 90
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAErllaEFCKRlgknlddEDELEQLQEELEARLESL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 91 RDEPRDVPAGMTsdALNQEILQVSSQLlekSRLAQQEQErAREIADSLSQL----------PQQQTDARRQLNEVERRVg 160
Cdd:PRK04863 571 SESVSEARERRM--ALRQQLEQLQARI---QRLAARAPA-WLAAQDALARLreqsgeefedSQDVTEYMQQLLEREREL- 643
|
170 180 190
....*....|....*....|....*....|....*....
gi 1513194555 161 TQNGNTPQAQAQNLGLQ---------AESARLKALVDEL 190
Cdd:PRK04863 644 TVERDELAARKQALDEEierlsqpggSEDPRLNALAERF 682
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
119-326 |
6.28e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 119 EKSRLAQQEQERAREIadsLSQLPQQQT----------DARRQLNEVERRVGTQNGNTPQAQAQnlglQAESARLKAlvd 188
Cdd:PRK11637 58 AKEKSVRQQQQQRASL---LAQLKKQEEaisqasrklrETQNTLNQLNKQIDELNASIAKLEQQ----QAAQERLLA--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 189 elelAQLSANNRQ----ELSRMRSELAQKQSEQLDAYLqalrNQLNSQRQREAERALESTELLAENSDNLPAGIVEQfkv 264
Cdd:PRK11637 128 ----AQLDAAFRQgehtGLQLILSGEESQRGERILAYF----GYLNQARQETIAELKQTREELAAQKAELEEKQSQQ--- 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513194555 265 nRELSAALNQQAQRMDlVASQQRQATNQTLQvrqalNTLREQSQWLGSSNLLGEALRAQVAR 326
Cdd:PRK11637 197 -KTLLYEQQAQQQKLE-QARNERKKTLTGLE-----SSLQKDQQQLSELRANESRLRDSIAR 251
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
105-235 |
7.35e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.83 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 105 ALNQEILQVSSQLLekSRLAQqeqeRAREiadslsqlpQQQTDARRQLNEVERRVGTqngntpqAQAQNLGLQAESARLK 184
Cdd:COG3524 154 AIAEALLAESEELV--NQLSE----RARE---------DAVRFAEEEVERAEERLRD-------AREALLAFRNRNGILD 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 185 ALVDELELAQLSANNRQELSRMRSELAQKQS---------EQLDAYLQALRNQLNSQRQR 235
Cdd:COG3524 212 PEATAEALLQLIATLEGQLAELEAELAALRSylspnspqvRQLRRRIAALEKQIAAERAR 271
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
18-424 |
7.70e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 40.28 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 18 YAATAPDAKQITQELEQAKAAKPAQPETVESLQSalnALEERKGSLERAQQYQQVIDNFPKLSQTLRAQLNNLRDEPRDV 97
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEA---LIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 98 PAGMTSDALNQEILQVSSQLLEKSRLAQQEQERAREIADSLSQLPQQQTDARRQLNEVERRVGTQNGNTPQAQAQNLGLQ 177
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 178 AESARLKALVDELELAQLSANNRQELSRMRSELAQKQSEQLDAYLQALRNQLNSQRQREAERALESTELLAENSDNLPAG 257
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 258 IVEQFKVNRELSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLD 337
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 338 TEMAQLRVQRLHFEDLLNKQPQIRQIRQADGQPLTSEQSRILEAQLRTQRELLNSLLQGGDTLILELTKLKVSNSQLEDA 417
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
....*..
gi 1513194555 418 LKEVNEA 424
Cdd:COG5278 478 AAAAAAL 484
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
148-306 |
9.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513194555 148 ARRQLNEVERRVGTQNGNTPQAQAQNLGLQAESARLKALVDELElAQLSANNrQELSRMRSELAQKQsEQLDAYLQALRN 227
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ-AELEALQ-AEIDKLQAEIAEAE-AEIEERREELGE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513194555 228 QLNSQRQreAERALESTELLAENSDnlPAGIVEQFKVnreLSAALNQQAQRMDLVASQQRQATNQTLQVRQALNTLREQ 306
Cdd:COG3883 91 RARALYR--SGGSVSYLDVLLGSES--FSDFLDRLSA---LSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
|
| |
