|
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: 2222.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 1 MRLIITFLMAWCLSWGAYAATAPDSKQITQELEQAKAAK-PAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNYPKL 79
Cdd:PRK10929 1 MRLIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKtPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 80 SATLRAQLNNMRDEPRSVSPGMSTDALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRL 159
Cdd:PRK10929 81 SAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 160 GTL-TGNTPLNQAQNFALQSDSARLKALVDELELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAE 238
Cdd:PRK10929 161 QTLgTPNTPLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 239 RALESTELLAENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGE 318
Cdd:PRK10929 241 RALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 319 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPLLRQIHQADGQPLTAEQNRILEAQLRTQRELLNSLLQGGD 398
Cdd:PRK10929 321 ALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 399 TLLLELTKLKVSNGQLEDALKEVNEATHRYLFWTSDVRPMTIAWPLEIAQDLRRLISLDTFSQLGKASVMMLTSKETILP 478
Cdd:PRK10929 401 TLILELTKLKVANSQLEDALKEVNEATHRYLFWVADVSPISLSYPLEIAQDLRRLLSLDTFSQLGKASVMMLTSKETLLP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 479 LFGALILVGCSIYSRRYFTRFLERSAAKVGKVTQDHFWLTLRTLFWSILVASPLPVLWMTLGYGLREAWPYPLAVAIGDG 558
Cdd:PRK10929 481 LFGALLLVGFSISSRRHYHAFLERSSSRVGKVTQDHFSLTLRTVFWSILVASPLPVLWAALGYGLQNAWPYPLAVAIGDG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 559 VTATVPLLWVVMICATFARPNGLFIAHFGWPRERVSRGMRYYLMSIGLIVPLIMALMMFDNLDDREFSGSLGRLCFILIC 638
Cdd:PRK10929 561 VTATVPLLWVFMICATFARPNGLFIAHFGWPRERVARAMRYYLLSIGLIVPLIMALITFDNLNDREFSGTLGRLCFILLC 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 639 GALAVVTLSLKKAGIPLYLNKEGSGDNITNHMLWNMMIGAPLVAILASAVGYLATAQALLARLETSVAIWFLLLVVYHVI 718
Cdd:PRK10929 641 GALSLVTLSLKRAGIPLYLDKEGSGDNIINHALWNLLIGAPLVAALASALGYLATAQALLARLETSVAIWFLLLVVYHII 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 719 RRWMLIQRRRLAFDRAKHRRAEMLAQRARGEEEAHHHSSPEGAIEVDESEVDLDAISAQSLRLVRSILMLIALLSVIVLW 798
Cdd:PRK10929 721 RRWMLIQRRRIAFDRAKQRRAEILAQRARGEEEAHHSSSPEGAIEVEEPVIDLDAISAQSLRLVRSILTLIALLSVIVLW 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 799 SEIHSAFGFLENISLWDVTSTVQGVESLEPITLGAVLIAILVFIITTQLVRNLPALLELAILQHLDLTPGTGYAITTITK 878
Cdd:PRK10929 801 SEIHSAFGFLENISLWDVTSTVQGVESLQPITLGSVLIAILVFIITTQLVRNLPALLELALLQHLDLTPGTGYAITTITK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 879 YLLMLIGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATT 958
Cdd:PRK10929 881 YLLMLIGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 959 ISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVIDNPAPEVFLVDLQQGIQ 1038
Cdd:PRK10929 961 ISDWDRKEIIVPNKAFITEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVLDNPAPEVFLVDLQQGIQ 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131984 1039 IFELRIYAAEMGHRMPLRHEIHQLILAGFHAHGIDMPFPPFQMRLESLNGKQTGRTLTSAGKGRQAGSL 1107
Cdd:PRK10929 1041 IFELRIYAAEMGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLGGKQTGRTLTSAGKSRTAGSL 1109
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1-1076 |
2.69e-163 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 512.53 E-value: 2.69e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 1 MRLIITFLMAWCLSWGAYAATA--PDSKQITQELEQAKAAKPAQPE---VVEALQSALNALEERKGSLERIKQYQQVIDN 75
Cdd:PRK11281 12 FIAFLFLLLCLSSAFARAASNGdlPTEADVQAQLDALNKQKLLEAEdklVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 76 YPKLSATLRAQLNNMRDEPRSVSPgmsTDALNQEILQVSSQLLDKSRQAQQEQErarEIADSLNQLPQQQTDARR----- 150
Cdd:PRK11281 92 APAKLRQAQAELEALKDDNDEETR---ETLSTLSLRQLESRLAQTLDQLQNAQN---DLAEYNSQLVSLQTQPERaqaal 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 151 -----QLNEIERRL-GTLTGNTPLNQAQNFALQSDSARLKALVDeLELAQLSANNR-QELARLRSELAEKESQQLDAYLQ 223
Cdd:PRK11281 166 yansqRLQQIRNLLkGGKVGGKALRPSQRVLLQAEQALLNAQND-LQRKSLEGNTQlQDLLQKQRDYLTARIQRLEHQLQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 224 ALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQ-FKINRELSAALNQQAQRMDlVASQQRQAASQTL-QVRQALN 301
Cdd:PRK11281 245 LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQeLEINLQLSQRLLKATEKLN-TLTQQNLRVKNWLdRLTQSER 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 302 TLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRV-------QRlryEDLLNKQPLLRQIHQADGQPLTAE 374
Cdd:PRK11281 324 NIKEQISVLKGSLLLSRILYQQQQALPSADLIEGLADRIADLRLeqfeinqQR---DALFQPDAYIDKLEAGHKSEVTDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 375 QNRILEAQLRTQRELL---NSLLqggdtllleltklkvsNGQLEDA---------LKEVNEATHRYL----FWTSDVRPM 438
Cdd:PRK11281 401 VRDALLQLLDERRELLdqlNKQL----------------NNQLNLAinlqlnqqqLLSVSDSLQSTLtqqiFWVNSNKPM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 439 TIAW----PLEIAQDLRRLISLDTFSQLGKASVMMLTskeTILPLfgaLILVGCSIYSRRYFTRFLERSAAKVGKVTQDH 514
Cdd:PRK11281 465 DLDWlkafPQALKDQFKSLKITVSFSNLWDGLFIALL---LFLPL---LLIAGLIRWRKKWIKARLQKLAADIGTLKRDS 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 515 FWLTLRTLFWSILVASPLPVLWMTLGYGLR--------EAWPYPLAVAigdgvtatvpLLWVVMICATFA-RPNGLFIAH 585
Cdd:PRK11281 539 QLHTPKAILITLLLALPVTLIFLAVGLILLtdafnqseLLWSWSLKLA----------LFWLVFATCYRVlRPNGVAERH 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 586 FGWPRERVSRGMRYYLMSIGLIVPLIMALMMFDNLDDREFSGSLGrLCFILICGALAVVTLSlkkagiPLYLNKEGSGDN 665
Cdd:PRK11281 609 FGMPKEQVSHFRRQIVRLSLALLPLLFWSVVAELSPLGLADDVIG-QAVIIIALALIAFLVW------PLCRESWRDKES 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 666 itnHMLWNM----MIGAPLVAILASAVGYLATAQALLARLETSVAIWFLLLVVYHVIRRWMLIQRRRLAFDRAKHRRAem 741
Cdd:PRK11281 682 ---HTLRLVvrtvLTIAPIALIVLVVLGYYYTALRLIGRLIETLYLLIIWNLLYQTVLRGLSVAARRLAYRRALAKRQ-- 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 742 lAQRARGEEeahhhsspeGAIEVDESEVDLDAISAQSLRLVRSILMLIALLSVIVLWSEIHSAFGFLENISLWDVTSTVQ 821
Cdd:PRK11281 757 -NLVKEGAE---------GAEPVEEPTLALEQVNQQSLRLTDLLLFALFFVMFYWVWSDLITVFSYLDSITLWHYTTTTA 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 822 GVESLEPITLGAVLIAILVFIITTQLVRNLPALLELAILQHLDLTPGTGYAITTITKYLLMLIGGLVGFSMIGIEWSKLQ 901
Cdd:PRK11281 827 GGAVVESITLGNLLFALIILVVTYVLVRNLPGLLEVLVLSRLNLRQGTSYAITTLLTYIIIAVGAVTAFSTLGVSWDKLQ 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 902 WLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEIIVPNKAFITEQFIN 981
Cdd:PRK11281 907 WLVAALSVGLGFGLQEIFANFVSGLIILFERPVRIGDTVTIGTFSGTVSKIRIRATTITDFDRKEVIVPNKAFVTERLIN 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 982 WSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVIDNPAPEVFLVDLQQGIQIFELRIYAAEMGHRMPLRHEIHQ 1061
Cdd:PRK11281 987 WSLSDTVTRVVIKVGVAYGSDLEKVRELLLQAATENPRVMKEPEPQVFFLNFGASTLDHELRLYVRELGDRSPTVDELNR 1066
|
1130
....*....|....*
gi 16131984 1062 LILAGFHAHGIDMPF 1076
Cdd:PRK11281 1067 RIDRLFRENDINIAF 1081
|
|
| MscS_TM |
pfam12794 |
Mechanosensitive ion channel inner membrane domain 1; The small mechanosensitive channel, MscS, ... |
481-813 |
4.68e-121 |
|
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: 375.40 E-value: 4.68e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 481 GALILVGCSI-YSRRYFTRFLERSAAKVGKVTQDHFWLTLRTLFWSILVASPLPVLWMTLGYGLREA-WPYPLAVAIGDG 558
Cdd:pfam12794 1 LLLLLVAGLLlWLRRRLKRRLERLAERVGKVTQDSFLHTLRALLLTLLLALPLPLLLAALGWLLQLSgWATPFSVALGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 559 VTATVPLLWVVMICATFARPNGLFIAHFGWPRERVSRGMRYYLMSIGLIVPLIMALMMFDNLDDREFSGSLGRLCFILIC 638
Cdd:pfam12794 81 LLALALALLVFEFFRRLLRPDGLAIRHFGWPEERVQRLRRQLRWLIWVLVPLVFVLGLAEALPDSLARDVLGRLAFIILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 639 GALAVVTLSLKKAGIPLYLNKEGSGDN-ITNHMLWNMMIGAPLVAILASAVGYLATAQALLARLETSVAIWFLLLVVYHV 717
Cdd:pfam12794 161 LLLAVFLWRLLRPGRGLYASHLGEGPNsRLRRLWWPLLVLAPLALAVLALLGYYYTALQLLGRLIDSLYLLLGWLLVYAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 718 IRRWMLIQRRRLAFDRAKHRRAEMLAQRARGEEEAHHHSspegAIEVDESEVDLDAISAQSLRLVRSILMLIALLSVIVL 797
Cdd:pfam12794 241 ALRWLLVARRRLAYRRAKERRAEALAQRAKEGEEGAEPS----ESSVEEPELDLETISAQSLRLLRLLLLLAFLVGLYWI 316
|
330
....*....|....*.
gi 16131984 798 WSEIHSAFGFLENISL 813
Cdd:pfam12794 317 WSDLLPAFSYLDNITL 332
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis]; |
808-1089 |
4.50e-100 |
|
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442495 [Multi-domain] Cd Length: 281 Bit Score: 317.53 E-value: 4.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 808 LENISLWDVTSTVQGVeslePITLGAVLIAILVFIITTQLVRNLPALLELAILQHLDLTPGTGYAITTITKYLLMLIGGL 887
Cdd:COG3264 1 MEESALLELLFLIGGI----SISLPNLLLALLILVVTYLLARLLSRLLERRLLRRTRLDPGLRYLISKLIRYLIIVLGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 888 VGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEI 967
Cdd:COG3264 77 IALSALGIDLTALAALAGALGVGIGFGLQDIVSNFISGLILLFERPFRVGDWIEIGGTEGTVEEIGLRSTRIRTFDGEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 968 IVPNKAFITEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVIDNPAPEVFLVDLQQGIQIFELRIYAA 1047
Cdd:COG3264 157 IIPNSELITNPVINWSLSDPRRRVEIPVGVAYGSDLEKVRELLLEAAREHPRVLKDPAPSVLFTEFGDSSVNFELRFWVN 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16131984 1048 EMGHRMPLRHEIHQLILAGFHAHGIDMPFPPFQMRLESLNGK 1089
Cdd:COG3264 237 DPRDRLRVRSDLNEAIKKAFREEGIEIPFPQRDVHLRNPPGE 278
|
|
| MS_channel |
pfam00924 |
Mechanosensitive ion channel; Two members of this protein family: Swiss:Q57634 and Swiss: ... |
874-1073 |
5.23e-62 |
|
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: 209.77 E-value: 5.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 874 TTITKYLLMLIGGLVGFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKIN 953
Cdd:pfam00924 1 KKILKYLIIVVGILIVLSYLGVNVSALLAGLGALGLALGFALQDLVSNLVSGIIILFEKPFKIGDWIEIGDIEGTVEDIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 954 TRATTISDWDRKEIIVPNKAFITEQFINWSLSDsVTRVVLTIPAPADANS---EEVTEILLTAARRCSLVIDNPAPEVFL 1030
Cdd:pfam00924 81 LRTTTIRTFDGRLVTIPNSSILTSNIINYSRSP-TRRVELSIGVAYSSDPdklEKVIEILKEAAYEHPLVLKDPEPPVVF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131984 1031 VDLQQGIQIFELRIYAAE-MGHRMPLRHEIHQLILAGFHAHGID 1073
Cdd:pfam00924 160 GEFGDSSLNFELRVWVKTlPGEYFNVRSELNLRIKKALEENGIE 203
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
30-253 |
3.84e-56 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 194.44 E-value: 3.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMR----DEPRSVSPGMSTDA 105
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQakaeAAPKEILASLSLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 LNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRL-GTLTGNTPLNQAQNFALQSDSARLK 184
Cdd:pfam12795 83 LEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLnGPAPPGEPLSEAQRWALQAELAALK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131984 185 ALVDELELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSAD 253
Cdd:pfam12795 163 AQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAAG 231
|
|
| MscS |
COG0668 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
812-1084 |
3.68e-47 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440432 [Multi-domain] Cd Length: 276 Bit Score: 170.06 E-value: 3.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 812 SLWDVTSTVQGVESLEPITLGAVLIAILVFIITTQLVRNLPALLELAILQHLDLTPGTGYaITTITKYLLMLIGGLVGFS 891
Cdd:COG0668 5 QLWSLLGLLLLLGELLLALLPKLLLALLILLIGWLLIRLLRRLIRRLLRRARRDRTLLPL-LRNILKILIVIIAILLILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 892 MIGIEwskLQWLVAALGVG---LGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEII 968
Cdd:COG0668 84 ILGVN---ITSLLAGLGAAglaIGLAAQDLLSNFIAGIFILLERPFRVGDWIEVGGVEGTVEEIGLRSTRLRTLDGRLVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 969 VPNKAFITEQFINWSLSDSVtRVVLTIPAPADANSEEVTEILLTAARRCSLVIDNPApEVFLVDLQQGIQIFELRIYAAE 1048
Cdd:COG0668 161 IPNSKILSSPITNYSRGPTR-RVDVTIGVDYDTDIDKARELLKEILEELPRILKDPA-VVGVTELGDSSVNLRVRAWTKP 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 16131984 1049 mGHRMPLRHEIHQLILAGFHAHGIDMPFPPFQMRLE 1084
Cdd:COG0668 239 -GDYWDVRRDIRERIKAALDEAGIEIPFPTRTVHLA 273
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-324 |
1.95e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 27 QITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQvidnypKLSATLRAQLNNMRDEprsvspgmsTDAL 106
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE------ERRRELEERLEELEEE---------LAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 107 NQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRlgtltgntpLNQAQNFALQSDSARLKAL 186
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE---------LEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 187 VDELELAQLSANNRQELARLRSELAEKESQqldayLQALRNQLNSQRQLEAERALESTELLAENSAdlpkdivAQFKINR 266
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEEEEEALEEAAEEEAELEEEEEA-------LLELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131984 267 ELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQV 324
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| PRK10334 |
PRK10334 |
small-conductance mechanosensitive channel MscS; |
833-1087 |
4.58e-12 |
|
small-conductance mechanosensitive channel MscS;
Pssm-ID: 182386 [Multi-domain] Cd Length: 286 Bit Score: 68.02 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 833 AVLIAILVFIITTQLVRNlpALLELAILQHLDltpgtgyaiTTITKYLLMLIG-GLVGFSMI------GIEWSKLQWLVA 905
Cdd:PRK10334 33 AALAIIIVGLIIARMISN--AVNRLMISRKID---------ATVADFLSALVRyGIIAFTLIaalgrvGVQTASVIAVLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 906 ALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEIIVPNKAFITEQFINWSlS 985
Cdd:PRK10334 102 AAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFS-R 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 986 DSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVIDNPAPEVFLVDLQQGIQIFELRIYaAEMGHRMPLRHEIHQLILA 1065
Cdd:PRK10334 181 EPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVW-SNSGDLQNVYWDVLERIKR 259
|
250 260
....*....|....*....|..
gi 16131984 1066 GFHAHGIDMPFPPFQMRLESLN 1087
Cdd:PRK10334 260 EFDAAGISFPYPQMDVNFKRVK 281
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-329 |
1.23e-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: 69.32 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 34 QAKAAKPAQpEVVEALQSA-----LNALEERKGSLER----IKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVSpgMSTD 104
Cdd:TIGR02168 208 QAEKAERYK-ELKAELRELelallVLRLEELREELEElqeeLKEAEEELEELTAELQELEEKLEELRLEVSELE--EEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 105 ALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLtgntplnQAQNFALQSDSARLK 184
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL-------EEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 185 ALVDEL-----ELAQLSANNRQELARLRSELAEKESQ--QLDAYLQALRNQLNsqrQLEAERALESTELLAENSADLPKD 257
Cdd:TIGR02168 358 AELEELeaeleELESRLEELEEQLETLRSKVAQLELQiaSLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131984 258 IVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPE 329
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-390 |
1.99e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 DALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARL 183
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 184 KAlvDELELAQLSANNRQELARLRSELAEKEsQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLpKDIVAQFK 263
Cdd:COG1196 322 EE--ELAELEEELEELEEELEELEEELEEAE-EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-EALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 264 INRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQL 343
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16131984 344 RVQRLRYEDLLNKQPLLRQIHQADGQPLTAEQnrILEAQLRTQRELL 390
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEG--VKAALLLAGLRGL 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
30-368 |
7.00e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAKPAQPEVVEALQSALNALEERKGSLEriKQYQQVIDNYPKLSATLRAQ------------LNNMRDEPRSV 97
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLE--QDYQAASDHLNLVQTALRQQekieryqadleeLEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 98 SPGMS---------TDALNQEILQVSSQLLD-------------KSRQAQQEQERAREI-----------ADSLNQLPQQ 144
Cdd:PRK04863 371 VEEADeqqeenearAEAAEEEVDELKSQLADyqqaldvqqtraiQYQQAVQALERAKQLcglpdltadnaEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 145 QTDARRQLNEIERRlgtltgntpLNQAQNFALQSDSAR--LKALVDELELAQLSANNRQELARLRSELAEKES-QQLDAY 221
Cdd:PRK04863 451 EQEATEELLSLEQK---------LSVAQAAHSQFEQAYqlVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 222 LQALRNQLNSQRQleAERALestellaensADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALN 301
Cdd:PRK04863 522 LSELEQRLRQQQR--AERLL----------AEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 302 TLREQSQWLGSSNLLGEALRAQVARLPEM-----PKPQQLDTEMAQ-------LRVQRLRYEDllNKQPLLRQIH---QA 366
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQsgeefEDSQDVTEYMQQllerereLTVERDELAA--RKQALDEEIErlsQP 667
|
..
gi 16131984 367 DG 368
Cdd:PRK04863 668 GG 669
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-347 |
1.12e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAKPAQPEVVEALQSALNALEerkgslERIKQYQQVIDNYPKLSATLRAQLNNMRdeprsvspgMSTDALNQE 109
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEQLRKELEELSRQISALR---------KDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 110 ILQVSsqlldkSRQAQQEQERArEIADSLNQLPQQQTDARRQLNEIERRLGTLtgNTPLNQAQNfALQSDSARLKALVDE 189
Cdd:TIGR02168 742 VEQLE------ERIAQLSKELT-ELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKE-ELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 190 L-ELAQLSANNRQELARLRSELAEKESQqldayLQALRNQL--NSQRQLEAERALESTELLAENSADlpkDIVAQFKINR 266
Cdd:TIGR02168 812 LtLLNEEAANLRERLESLERRIAATERR-----LEDLEEQIeeLSEDIESLAAEIEELEELIEELES---ELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 267 ELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQsqwLGSSNL-----------LGEALRAQVARLPEMPKPQQ 335
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELrleglevridnLQERLSEEYSLTLEEAEALE 960
|
330
....*....|..
gi 16131984 336 LDTEMAQLRVQR 347
Cdd:TIGR02168 961 NKIEDDEEEARR 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-306 |
1.35e-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: 64.40 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 DALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARL 183
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 184 KALVDELeLAQLSANNRQELARL-----RSELAEKESQQLDAYLQALRNQLNSQRQlEAERALESTELLAENSADLPKDI 258
Cdd:COG4942 103 KEELAEL-LRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131984 259 VAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQ 306
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-366 |
4.59e-10 |
|
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: 64.22 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 57 EERK---GSLERIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVspgmsTDALNQ------EILQVSSQLLDKSRQAQQE 127
Cdd:TIGR00618 163 KEKKellMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL-----TLCTPCmpdtyhERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 128 QERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARLKALVDELELAQLSANNRQELARLR 207
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 208 SELAEKEsQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQFKINRELSAALNQQAQRMDlVASQQR 287
Cdd:TIGR00618 318 SKMRSRA-KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 288 QAASQ---TLQVRQALNTLREQSQwlgssnllgEALRAQVARLPEMPKPQQLDTEMAQLRVQRlRYEDLLNKQPLLRQIH 364
Cdd:TIGR00618 396 QSLCKeldILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYAELCAAAITC-TAQCEKLEKIHLQESA 465
|
..
gi 16131984 365 QA 366
Cdd:TIGR00618 466 QS 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-321 |
5.86e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 18 YAATAPDSKQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQvidnypklsatlrAQLNNMRDEPrsv 97
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR-------------ERLANLERQL--- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 98 spgmstDALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGtltgntplnqaqnfALQ 177
Cdd:TIGR02168 319 ------EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE--------------ELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 178 SDSARLKALVDELELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKD 257
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131984 258 IVAQFKINRELSAALNQ--QAQRMDLVASQQRQAASQTLQ---------VRQALNtlrEQSQWLGSSNLLGEALR 321
Cdd:TIGR02168 459 LEEALEELREELEEAEQalDAAERELAQLQARLDSLERLQenlegfsegVKALLK---NQSGLSGILGVLSELIS 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
109-394 |
1.85e-09 |
|
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: 62.01 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 109 EILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNtplnqaqnfaLQSDSARLKALVD 188
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE----------EEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 189 EL-ELAQLSANNRQELARLRSELAEKESQqldayLQALRNQLNSqrqLEAERALESTELLAENSADLPKDIVAQFKINRE 267
Cdd:TIGR02169 745 DLsSLEQEIENVKSELKELEARIEELEED-----LHKLEEALND---LEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 268 LSAALNQQAQRmdlvaSQQRQAASQTLQVRQALNTLREQS--QWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRV 345
Cdd:TIGR02169 817 IEQKLNRLTLE-----KEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEELEEELEELEA--ALRDLESRLGDLKK 889
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16131984 346 QRLRyedlLNKQplLRQIHQADGQ-PLTAEQNRILEAQLRTQRELLNSLL 394
Cdd:TIGR02169 890 ERDE----LEAQ--LRELERKIEElEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-330 |
2.56e-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: 61.61 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 27 QITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLE-RIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVSPGMstDA 105
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI--EE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 LNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARLKA 185
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 186 LVDELELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLnsqRQLEAERAlESTELLAENSADLPKdivAQFKIN 265
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR---SELRRELE-ELREKLAQLELRLEG---LEVRID 939
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131984 266 RELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLG-EALRAQVARLPEM 330
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAiEEYEELKERYDFL 1005
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-216 |
1.72e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 11 WCLSWGAYAATApdskQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNYPKLSATLrAQLNNM 90
Cdd:COG4913 602 YVLGFDNRAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI-AELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 91 RDEprsvspgmsTDALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQ 170
Cdd:COG4913 677 LER---------LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131984 171 AQNFAlqsdsARLKALVDELELAQLSANNRQELARLRSELAEKESQ 216
Cdd:COG4913 748 RALLE-----ERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-424 |
2.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 24 DSKQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQyqqvidnypkLSATLRAQLNNMRDEprsvspgmst 103
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE----------EAEAELAEAEEALLE---------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 daLNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLtgNTPLNQAQNFALQSDSARL 183
Cdd:COG1196 370 --AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL--EEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 184 KALVDELELAQLSANNRQELARLRSELAEKESQ--QLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQ 261
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 262 FKINRELSAALnQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSqwLGSSNLLgEALRAQVARLPEMPKPQQLDTEMA 341
Cdd:COG1196 526 VAVLIGVEAAY-EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK--AGRATFL-PLDKIRARAALAAALARGAIGAAV 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 342 QLRVQRLRYEDLlnkqPLLRQIHQADGQPLTAEQNRILEAQLRTQRELLNSLLQGGDTLLLELTKLKVSNGQLEDALKEV 421
Cdd:COG1196 602 DLVASDLREADA----RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
...
gi 16131984 422 NEA 424
Cdd:COG1196 678 EAE 680
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-356 |
3.45e-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: 57.08 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 114 SSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTgntplnqaqnfalqsdsARLKALVDELELA 193
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----------------RRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 194 QlsannrQELARLRSELAEKEsQQLDAYLQALRNQLNSQRQLEAERALESTeLLAENSADLPKDIVAQFKINRELSAALN 273
Cdd:COG4942 82 E------AELAELEKEIAELR-AELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 274 QQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLgssNLLGEALRAQVARLPEmpKPQQLDTEMAQLRVQRLRYEDL 353
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAAL---EALKAERQKLLARLEK--ELAELAAELAELQQEAEELEAL 228
|
...
gi 16131984 354 LNK 356
Cdd:COG4942 229 IAR 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
41-368 |
8.20e-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: 56.88 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 41 AQPEVVEALQSALNALEERkgslerIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVSPGMstdALNQEILQVSSQLLDK 120
Cdd:COG3096 344 RQQEKIERYQEDLEELTER------LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL---ADYQQALDVQQTRAIQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 121 SRQAQQEQERAREIAD----SLNQLPQQQTDARRQLNEIERRLgtLTGNTPLNQAQNFALQSDSAR--LKALVDELELAQ 194
Cdd:COG3096 415 YQQAVQALEKARALCGlpdlTPENAEDYLAAFRAKEQQATEEV--LELEQKLSVADAARRQFEKAYelVCKIAGEVERSQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 195 LSANNRQELARLRSE--LAEKESQ---QLDAYLQALRNQLNSQRQLEA---------ERALESTELLAENSADLpKDIVA 260
Cdd:COG3096 493 AWQTARELLRRYRSQqaLAQRLQQlraQLAELEQRLRQQQNAERLLEEfcqrigqqlDAAEELEELLAELEAQL-EELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 261 QFkinRELSAALNQQAQRMDLVASQQRQAASQT---LQVRQALNTLREQS-QWLGSSNLLGEALRAQVARLpempkpQQL 336
Cdd:COG3096 572 QA---AEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSgEALADSQEVTAAMQQLLERE------REA 642
|
330 340 350
....*....|....*....|....*....|..
gi 16131984 337 DTEMAQLRVQRLRyedlLNKQplLRQIHQADG 368
Cdd:COG3096 643 TVERDELAARKQA----LESQ--IERLSQPGG 668
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
24-389 |
8.60e-08 |
|
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: 56.77 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 24 DSKQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLE--RIKQYQQVIDNYPklsaTLRAQLNNM--RDEPRSVSP 99
Cdd:pfam12128 295 LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLdaDIETAAADQEQLP----SWQSELENLeeRLKALTGKH 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 100 GMSTDALNQEILQVSSQLLD-----KSRQAQQEQERAREIADSLNQLPQQQTDARRQLN-----------EIERRLG--- 160
Cdd:pfam12128 371 QDVTAKYNRRRSKIKEQNNRdiagiKDKLAKIREARDRQLAVAEDDLQALESELREQLEagklefneeeyRLKSRLGelk 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 161 ------TLTGNTPLNQAQN------------------FALQSDSARLKALVDELELAQLSANNRqeLARLRSELAEKEsQ 216
Cdd:pfam12128 451 lrlnqaTATPELLLQLENFderierareeqeaanaevERLQSELRQARKRRDQASEALRQASRR--LEERQSALDELE-L 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 217 QLDA----YLQALRNQLNSQRQ----LEAERALESTELLAENSADLPKDIVAQFKINREL-------SAALNQQAQRMDL 281
Cdd:pfam12128 528 QLFPqagtLLHFLRKEAPDWEQsigkVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLkridvpeWAASEEELRERLD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 282 VASQQRQAASQTL-QVRQALNTLREQsqwLGSSNL-LGEALRA-QVARLpempKPQQLDTEMAQL--RVQRLRYEDLLNK 356
Cdd:pfam12128 608 KAEEALQSAREKQaAAEEQLVQANGE---LEKASReETFARTAlKNARL----DLRRLFDEKQSEkdKKNKALAERKDSA 680
|
410 420 430
....*....|....*....|....*....|...
gi 16131984 357 QPLLRQIhQADGQPLTAEQNRILEAQLRTQREL 389
Cdd:pfam12128 681 NERLNSL-EAQLKQLDKKHQAWLEEQKEQKREA 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7-292 |
9.89e-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: 55.54 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 7 FLMAWCLSWGAYAATAPDSKQITQELEQAKAAkpaqpevVEALQSALNALEERKGSLER-IKQYQQVIdnypklsATLRA 85
Cdd:COG4942 4 LLLLALLLALAAAAQADAAAEAEAELEQLQQE-------IAELEKELAALKKEEKALLKqLAALERRI-------AALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 86 QLNnmrdeprsvspgmstdALNQEILQVSSQLldksRQAQQEQERAREiadslnQLPQQQTDARRQLNEIErRLGTLTGN 165
Cdd:COG4942 70 RIR----------------ALEQELAALEAEL----AELEKEIAELRA------ELEAQKEELAELLRALY-RLGRQPPL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 166 TPLNQAQNFA-LQSDSARLKALVDEL-ELAQLSANNRQELARLRSELaEKESQQLDAYLQALRNQLNSQRQLEAERAles 243
Cdd:COG4942 123 ALLLSPEDFLdAVRRLQYLKYLAPARrEQAEELRADLAELAALRAEL-EAERAELEALLAELEEERAALEALKAERQ--- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16131984 244 tELLAENSADLPKDivaqfkiNRELSAALNQQAQRMDLVASQQRQAASQ 292
Cdd:COG4942 199 -KLLARLEKELAEL-------AAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
104-420 |
1.06e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 DALNQEILQVSSQL------LDKSRQAQQE-QERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFAL 176
Cdd:COG4372 48 EQLREELEQAREELeqleeeLEQARSELEQlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 177 QSDSARLKALVDELElaQLSANNRQELARLRSELAEKEsQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPK 256
Cdd:COG4372 128 EQQRKQLEAQIAELQ--SEIAEREEELKELEEQLESLQ-EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 257 DIVAQFKINRELSAALnqQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQ-- 334
Cdd:COG4372 205 AEKLIESLPRELAEEL--LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIaa 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 335 -QLDTEMAQLRVQRLRYEDLLNKQPLLRQIHQADGQPLTAEQNRILEAQLRTQRELLNSLLQGGDTLLLELTKLKVSNGQ 413
Cdd:COG4372 283 lELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
....*..
gi 16131984 414 LEDALKE 420
Cdd:COG4372 363 AEAGVAD 369
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
81-382 |
1.21e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 56.35 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 81 ATLRAQLNNMRDEPRSVSPGMSTDALNQEILQ--VSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNeiERR 158
Cdd:PRK10246 390 THAEQKLNALPAITLTLTADEVAAALAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN--EMR 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 159 LGTLTGNTPLNQAQNFA--------LQSDSARLKA-------------LVDELELAQLSANNR------QELARLRSELA 211
Cdd:PRK10246 468 QRYKEKTQQLADVKTICeqearikdLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVNQSrldaleKEVKKLGEEGA 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 212 EKESqQLDAYLQAL-RNQLNSQRQLEAERALesTELLAENSADLPKDIVAQFKINRELSAA------LNQQAQRMDLvas 284
Cdd:PRK10246 548 ALRG-QLDALTKQLqRDESEAQSLRQEEQAL--TQQWQAVCASLNITLQPQDDIQPWLDAQeeherqLRLLSQRHEL--- 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 285 qQRQAASQTLQVRQAlntlreQSQWLGSSNLLGEALRAQVARLPEMPKP--------------QQLDTEMAQLRVQRLRY 350
Cdd:PRK10246 622 -QGQIAAHNQQIIQY------QQQIEQRQQQLLTALAGYALTLPQEDEEaswlatrqqeaqswQQRQNELTALQNRIQQL 694
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131984 351 EDLLNKQPL---------------LRQIH----------QADGQPLTAEQNRILEAQ 382
Cdd:PRK10246 695 TPLLETLPQsddlphseetvaldnWRQVHeqclslhsqlQTLQQQDVLEAQRLQKAQ 751
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
123-424 |
1.53e-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: 55.84 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 123 QAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARLKALVDELE-----LAQLSA 197
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedlssLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 198 NNRQELARLRSELAEKESQqldayLQALRNQLNSqrqLEAERALESTELLAENSADLPKDIVAQFKINRELSAALNQQAQ 277
Cdd:TIGR02169 755 NVKSELKELEARIEELEED-----LHKLEEALND---LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 278 RmdlvaSQQRQAASQTLQVRQALNTLREQS--QWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRVQRLRyedlln 355
Cdd:TIGR02169 827 E-----KEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEELEEELEELEA--ALRDLESRLGDLKKERDE------ 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131984 356 kqpllrqihqadgqpltaeqnriLEAQLRTQRELLNSLLQGGDTLLLELTKLKVSNGQLEDALKEVNEA 424
Cdd:TIGR02169 894 -----------------------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-270 |
4.30e-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: 54.30 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVidnypklsATLRAQLNNMRDEPRSVSpgMSTDA 105
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--------PEIQAELSKLEEEVSRIE--ARLRE 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 LNQEI--LQVSSQLLDKSRqaQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLtgntplnQAQNFALQSDSARL 183
Cdd:TIGR02169 817 IEQKLnrLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-------EAALRDLESRLGDL 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 184 KALVDELElAQLSA-NNRQELARLRSELAEKESQQLDAYLQALRNQLNsqrqlEAERALESTELLAENSADLPkDIVAQF 262
Cdd:TIGR02169 888 KKERDELE-AQLRElERKIEELEAQIEKKRKRLSELKAKLEALEEELS-----EIEDPKGEDEEIPEEELSLE-DVQAEL 960
|
....*....
gi 16131984 263 -KINRELSA 270
Cdd:TIGR02169 961 qRVEEEIRA 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-395 |
5.00e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 152 LNEIERRLGTLTgntplNQAQN----FALQSDSARLKALV-----DELELAQLSANNRQELARLRSELAEKESQQLDAYL 222
Cdd:COG1196 195 LGELERQLEPLE-----RQAEKaeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 223 QALRNQLNSQRQlEAERALESTELLAENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNT 302
Cdd:COG1196 270 EELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 303 LREQSQwlgssnLLGEALRAQVARLPEmpkpqQLDTEMAQLRVQRLRYEDLLNKQPLLRQIHQADGQPLTAEQNRILE-A 381
Cdd:COG1196 349 AEEELE------EAEAELAEAEEALLE-----AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERlE 417
|
250
....*....|....
gi 16131984 382 QLRTQRELLNSLLQ 395
Cdd:COG1196 418 RLEEELEELEEALA 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-395 |
7.88e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAKPAQPEVVEALQSALNALEERKGSLE--------RIKQYQQVIDNYPKLS--ATLRAQLNNMRDEPRSVSP 99
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEaeleelreELEKLEKLLQLLPLYQelEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 100 GMST--------DALNQEILQVSSQLLDKSRQAQQEQERA-REIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQ 170
Cdd:COG4717 154 RLEElreleeelEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 171 AQNFALQsDSARLK-------------ALVDELELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEA 237
Cdd:COG4717 234 NELEAAA-LEERLKearlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 238 ERALESTELLA---------ENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTL-------QVRQALN 301
Cdd:COG4717 313 LEELEEEELEEllaalglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvedeeELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 302 TLREQSQWLGSSNLLGEALRAQ---VARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKqpLLRQIHQADGQPLTAEQNRI 378
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEE--LREELAELEAELEQLEEDGE 470
|
410
....*....|....*..
gi 16131984 379 LeAQLRTQRELLNSLLQ 395
Cdd:COG4717 471 L-AELLQELEELKAELR 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-348 |
1.03e-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: 53.15 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 39 KPAQPEVVEALQSALNALeerKGSLERIKQYQQVIDNypKLSATLRAqlnnMRDEPRSVSPGMST-DALNQEILQVSSQL 117
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL---KRELSSLQSELRRIEN--RLDELSQE----LSDASRKIGEIEKEiEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 118 LDKSRQAQQ-EQERA---REIADSLNQLPQQQTDA---RRQLNEIERRLGtlTGNTPLNQAQNFALQSDSARLKALVDEL 190
Cdd:TIGR02169 740 EELEEDLSSlEQEIEnvkSELKELEARIEELEEDLhklEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 191 ElaqlsannrQELAR--LRSELAEKESQQLDAYLQALRNQLNSQRQL---------EAERALESTEL----LAENSADLP 255
Cdd:TIGR02169 818 E---------QKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlngkkeELEEELEELEAalrdLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 256 KDIvaqfkinRELSAALNQQAQRmdlvasqQRQAASQTLQVRQALNTLREQSQwlgssNLLGE--ALRAQVARLPEMPkP 333
Cdd:TIGR02169 889 KER-------DELEAQLRELERK-------IEELEAQIEKKRKRLSELKAKLE-----ALEEElsEIEDPKGEDEEIP-E 948
|
330
....*....|....*
gi 16131984 334 QQLDTEMAQLRVQRL 348
Cdd:TIGR02169 949 EELSLEDVQAELQRV 963
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
26-369 |
1.13e-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: 52.82 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNypklSATLRAQLNNMRDEPrsvspgmstda 105
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR----QAAIYAEQERMAMER----------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 lNQEILQVssQLLDKSRQAQQ--EQERAREIAdSLNQLPQQQTDaRRQLNEIERRlgtltgntPLNQAQNFALQSDSARL 183
Cdd:pfam17380 347 -ERELERI--RQEERKRELERirQEEIAMEIS-RMRELERLQME-RQQKNERVRQ--------ELEAARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 184 KALVDELELAQLSA---NNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKDIVA 260
Cdd:pfam17380 414 KIQQQKVEMEQIRAeqeEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 261 QFKINRELSAalNQQAQrmdLVASQQRQAASQTLQVRQalNTLREQSQwlgsSNLLGEALRAQVarlpEMPKPQQLDTEM 340
Cdd:pfam17380 494 RKILEKELEE--RKQAM---IEEERKRKLLEKEMEERQ--KAIYEEER----RREAEEERRKQQ----EMEERRRIQEQM 558
|
330 340
....*....|....*....|....*....
gi 16131984 341 AQLRVQRLRYEDLLNKQPLLRQIHQADGQ 369
Cdd:pfam17380 559 RKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
109-296 |
1.75e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 109 EILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPlNQAQNFALQSDSARLKALvd 188
Cdd:COG3206 199 EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAEL-- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 189 ELELAQLSAN---NRQELARLRSELAEKESQ---QLDAYLQALRNQLNSQRQLEAEraLEST-ELLAENSADLPKDIVAQ 261
Cdd:COG3206 276 EAELAELSARytpNHPDVIALRAQIAALRAQlqqEAQRILASLEAELEALQAREAS--LQAQlAQLEARLAELPELEAEL 353
|
170 180 190
....*....|....*....|....*....|....*
gi 16131984 262 FKINRELSAAlnqQAQRMDLVASQQRQAASQTLQV 296
Cdd:COG3206 354 RRLEREVEVA---RELYESLLQRLEEARLAEALTV 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
128-395 |
2.15e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 128 QERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTG-------------------NTPLNQAQN-FALQSDSARLKALV 187
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMAReleelsaresdleqdyqaaSDHLNLVQTaLRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 188 DELE--LAQLS-----ANNRQELARLRSELAEKE----SQQLDAYLQALRNQLNS--------QRQLEAERALESTELLA 248
Cdd:COG3096 357 EELTerLEEQEevveeAAEQLAEAEARLEAAEEEvdslKSQLADYQQALDVQQTRaiqyqqavQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 249 ENSADLPKDIVAQFKinrELSAALNQQAQRMDL--VASQQRQAASQTLQvRQALNTLREQSqWLGSSNLLGEA--LRAQV 324
Cdd:COG3096 437 ENAEDYLAAFRAKEQ---QATEEVLELEQKLSVadAARRQFEKAYELVC-KIAGEVERSQA-WQTARELLRRYrsQQALA 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131984 325 ARLPempkpqQLDTEMAQLRvQRLRYEDllNKQPLLRQIHQADGQPLTAEQNriLEAQLRTQRELLNSLLQ 395
Cdd:COG3096 512 QRLQ------QLRAQLAELE-QRLRQQQ--NAERLLEEFCQRIGQQLDAAEE--LEELLAELEAQLEELEE 571
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-423 |
2.56e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 17 AYAATAPDSKQITQELEQAKAAKPAQPEVVE--ALQSALNALEERKgslERIKQYQQVIDNYPKLSATLRAQLNNMRDEP 94
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQSLKERE---QQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 95 RSVSPgmSTDALNQEILQVSSQLLDKSRQAQQEQERAR---EIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQA 171
Cdd:TIGR00618 504 CPLCG--SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 172 qnfaLQSDSARLKALVDELE-LAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERALESTELlaen 250
Cdd:TIGR00618 582 ----SKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL---- 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 251 saDLPKDIVaqfkinRELSAALNQQAQRMdlvaSQQRQAASQTLQvrqalNTLREQSQWLGSSNLLGEALRAQVARLPEM 330
Cdd:TIGR00618 654 --TLTQERV------REHALSIRVLPKEL----LASRQLALQKMQ-----SEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 331 PKPQQLDTEMAQLRVQRLRYEDLLNKQPLLRQIHQADgqplTAEQNRILEAQLRTQRELLnsLLQGGDTLLLELTKLKVS 410
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR----TVLKARTEAHFNNNEEVTA--ALQTGAELSHLAAEIQFF 790
|
410
....*....|...
gi 16131984 411 NGQLEDALKEVNE 423
Cdd:TIGR00618 791 NRLREEDTHLLKT 803
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-308 |
2.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 118 LDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLgtltgntplnqaqnfalqsdsARLKALVDELELAQLSA 197
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL---------------------EELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 198 NNRQELARLRSELAEKESQ--QLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQFKINRELSAALNQQ 275
Cdd:COG4717 129 PLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190
....*....|....*....|....*....|...
gi 16131984 276 AQRMDLVASQQRQAASQTLQVRQALNTLREQSQ 308
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-428 |
3.41e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 154 EIERRLGTLTGNTPLNQAQNFALQSDSARLKALVDELElaQLSANNRQELARLRSELAEKESQ--QLDAYLQALRNQLNS 231
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELE--EKIAELEKALAELRKELEELEEEleQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 232 QR------QLEAERALESTELLAENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLRE 305
Cdd:TIGR02168 731 LRkdlarlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 306 QSQwlgssnLLGEALRAQVARLPEMPKP--------QQLDTEMAQLRVQRLRYEDLLNKQPLLRQIHQADGQPLTAEQNR 377
Cdd:TIGR02168 811 ELT------LLNEEAANLRERLESLERRiaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16131984 378 ILEA--QLRTQRELLNSLLQGGDTLlleltklkvsNGQLEDALKEVNEATHRY 428
Cdd:TIGR02168 885 LEEAlaLLRSELEELSEELRELESK----------RSELRRELEELREKLAQL 927
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
44-276 |
3.66e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 44 EVVEALQSALNALEERKGSL-ERIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVSPGMST-----DALNQEILQVSSQ- 116
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELrEEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQElrekrDELNEKVKELKEEr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 117 --LLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTltgnTPLNQAQNFALQSDSARLKALVDELElAQ 194
Cdd:COG1340 81 deLNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQT----EVLSPEEEKELVEKIKELEKELEKAK-KA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 195 LSANN-----RQELARLRSELAE---------KESQQLDAYLQALRNQLNSQRQlEAERALESTELLAENSADLPKDIVA 260
Cdd:COG1340 156 LEKNEklkelRAELKELRKEAEEihkkikelaEEAQELHEEMIELYKEADELRK-EADELHKEIVEAQEKADELHEEIIE 234
|
250 260
....*....|....*....|
gi 16131984 261 -QFKINR---ELSAALNQQA 276
Cdd:COG1340 235 lQKELRElrkELKKLRKKQR 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
66-313 |
5.82e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 66 IKQYQQVIDNYPKLSATLRAQLNNMRDEprsvspgmsTDALNQEILQVSSQLldksRQAQQEQERAR-EIADSLNQLPQQ 144
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---------LEELNEEYNELQAEL----EALQAEIDKLQaEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 145 QTDARRQLNEIERRLGTLTGNTPLNQAQNF--------ALQSDSARLKALVDELELAQlsannrQELARLRSELAEKESQ 216
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSESFsdfldrlsALSKIADADADLLEELKADK------AELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 217 qldayLQALRNQLNSQR-QLEAERAlESTELLAENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQ 295
Cdd:COG3883 159 -----LEALKAELEAAKaELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250
....*....|....*...
gi 16131984 296 VRQALNTLREQSQWLGSS 313
Cdd:COG3883 233 AAAAAAAAAAAASAAGAG 250
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
125-392 |
5.87e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 125 QQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLtgNTPLNQAQNFALQSDSARLKALVDELELAQLSANNRQE-- 202
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL--NKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQhg 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 203 ---------LARLRSELAEKESQQLDaYLQAlrnqlnSQRQLEAERALESTELLAENSADLP-KDIVAQFKINRELSAAL 272
Cdd:COG3096 917 kalaqleplVAVLQSDPEQFEQLQAD-YLQA------KEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLGENSDLNEKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 273 NQQAQRMDLVASQQRQAA-------SQTLQVRQALNTLREQSQwlgssNLLGEALRaqvaRLPEMpkPQQLDTEM----- 340
Cdd:COG3096 990 RARLEQAEEARREAREQLrqaqaqySQYNQVLASLKSSRDAKQ-----QTLQELEQ----ELEEL--GVQADAEAeerar 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131984 341 -------AQLRVQRLRYeDLLNKQpllRQIHQADGQPLtAEQNRILEAQLRTQRELLNS 392
Cdd:COG3096 1059 irrdelhEELSQNRSRR-SQLEKQ---LTRCEAEMDSL-QKRLRKAERDYKQEREQVVQ 1112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-200 |
6.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 1 MRLIITFLMAWCLSWGAYAATAPDS----KQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLER--------IKQ 68
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAeaelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriraleqeLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 69 YQQVIDNYPKLSATLRAQLNNMRDE--------------------------PRSVSPGMSTDALNQEILQVSSQLLDKSR 122
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEElaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 123 QAQQEQERAREIADSLNQLPQQQTDARRQL----NEIERRLGTLTGNTPLNQAQNFALQSDSARLKALVDELELAQLSAN 198
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALealkAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 16131984 199 NR 200
Cdd:COG4942 241 ER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-394 |
6.88e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 121 SRQAQQEQERAREIADslnqLPQQQTDARRQLNEIERRLGTLtgntplnQAQNFALQSDSARLKALVDELElaQLSANNR 200
Cdd:TIGR02168 666 AKTNSSILERRREIEE----LEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELS--RQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 201 QELARLrselaEKESQQLD---AYLQALRNQLNSQRQLEAERALESTELLAE---NSADLPKDI---VAQFKINRELSAA 271
Cdd:TIGR02168 733 KDLARL-----EAEVEQLEeriAQLSKELTELEAEIEELEERLEEAEEELAEaeaEIEELEAQIeqlKEELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 272 LNQQAQRmdlvasQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARL-PEMpkpQQLDTEMAQLRVQRLRY 350
Cdd:TIGR02168 808 LRAELTL------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaAEI---EELEELIEELESELEAL 878
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16131984 351 EDLLNKQPLLRQIHQADGQPLTAEQNRILEA--QLRTQRELLNSLL 394
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKrsELRRELEELREKL 924
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-326 |
8.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 122 RQAQQEQERAREIADSLNQLPQQQTD---ARRQLNEIERRLGTLT---GNTPLNQAQNF--ALQSDSARLKALVDELELA 193
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALRlwfAQRRLELLEAEleELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 194 QlsANNRQELARLRSELAEKESQQLDAyLQALRNQLNSQRQLEAERALESTELLAENSADLPKDIvAQFKINR-ELSAAL 272
Cdd:COG4913 318 L--DALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEERERRRARLEALLAALGLPLPASA-EEFAALRaEAAALL 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131984 273 NQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGS--SNLLGE--ALRAQVAR 326
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrkSNIPARllALRDALAE 451
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
26-279 |
1.10e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKAAKpaqpevvEALQSALNALEERKGSLeRIKQYQQvidnypKLSATLRAQLNNMRDEPRSVSPGMSTDA 105
Cdd:TIGR00618 635 QQCSQELALKLTAL-------HALQLTLTQERVREHAL-SIRVLPK------ELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 LNQEILQVSSQLLDKSRQAQQEQERAreiADSLNQLPQQQTDARRQ-LNEIERRLGTLTGNTPLNQAQNFalQSDSARLK 184
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENA---SSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNN--EEVTAALQ 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 185 ALVDELELAQLSANNRQELARLRSELAEKESQ---QLDAYLQALrnqLNSQRQLEAERAlESTELLAENSADLP--KDIV 259
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigqEIPSDEDIL---NLQCETLVQEEE-QFLSRLEEKSATLGeiTHQL 851
|
250 260
....*....|....*....|
gi 16131984 260 AQFKINRELSAALNQQAQRM 279
Cdd:TIGR00618 852 LKYEECSKQLAQLTQEQAKI 871
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-395 |
1.23e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 123 QAQQEQERAREIADSLNQLpQQQTDARRQLNEIERRLgtltgntplnQAQNFALQSDSARLKALVDELELAQLSANNRQE 202
Cdd:TIGR02168 216 KELKAELRELELALLVLRL-EELREELEELQEELKEA----------EEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 203 LAR-----LRSELAEKEsQQLDAYLQALRNQLNSQRQLEAERALestellAENSADLPKDIVAQfkinreLSAALNQQAQ 277
Cdd:TIGR02168 285 ELQkelyaLANEISRLE-QQKQILRERLANLERQLEELEAQLEE------LESKLDELAEELAE------LEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 278 RMDLVASQQRQAASQTLQVRQALNTLREQSqwlgssnllgEALRAQVARLPempkpQQLDTEMAQLRVQRLRYEDLLNKQ 357
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQL----------ETLRSKVAQLE-----LQIASLNNEIERLEARLERLEDRR 416
|
250 260 270
....*....|....*....|....*....|....*...
gi 16131984 358 PLLRQIHQADGQPLTAEQNRILEAQLRTQRELLNSLLQ 395
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
84-352 |
1.29e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 84 RAQLNNMRDEPRSVSPGMSTDALNQEILQVSSQLLDKSRQAQQEQERAREiadSLNQLPQQQTDARRQLNEIERRLgtlt 163
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE---ELEQLEEELEQARSELEQLEEEL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 164 gntplnQAQNFALQSDSARLKALVDELELAQLSANN-RQELARLRSELA--EKESQQLDAYLQALRNQLNSQRQlEAERA 240
Cdd:COG4372 83 ------EELNEQLQAAQAELAQAQEELESLQEEAEElQEELEELQKERQdlEQQRKQLEAQIAELQSEIAEREE-ELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 241 LESTELLAENSADLPKDIvaQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEAL 320
Cdd:COG4372 156 EEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270
....*....|....*....|....*....|..
gi 16131984 321 RAQVARLPEMPKPQQLDTEMAQLRVQRLRYED 352
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
26-287 |
1.41e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKAAKPAQPEVVEALQSALNALEerkgslERIKQYQQVIDNYPKLSATLRAQLNNMRDEprsvspgmsTDA 105
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLE------EELEELNEQLQAAQAELAQAQEELESLQEE---------AEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 LNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTgntplNQAQNFALQSDSARLKA 185
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 186 LVDELELAQLSANNRQELARLRSELAEKESQQ--------LDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKD 257
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEElleakdslEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270
....*....|....*....|....*....|
gi 16131984 258 IVAQFKINRELSAALNQQAQRMDLVASQQR 287
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
124-395 |
1.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 124 AQQEQERAREIADSLNqLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDsarLKALVDELELAQLSANNRQEL 203
Cdd:PRK04863 275 MRHANERRVHLEEALE-LRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD---YQAASDHLNLVQTALRQQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 204 ARLRSELAEKESQqldAYLQALRNQLNSQRQLEAERALEStellAENSADlpkdivaqfkinrELSAALNQQAQRMDLva 283
Cdd:PRK04863 351 ERYQADLEELEER---LEEQNEVVEEADEQQEENEARAEA----AEEEVD-------------ELKSQLADYQQALDV-- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 284 sQQRQAasqtLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEmpKPQQLDTEMAQLRvQRLRYEDLLNKQ-----P 358
Cdd:PRK04863 409 -QQTRA----IQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA--KEQEATEELLSLE-QKLSVAQAAHSQfeqayQ 480
|
250 260 270
....*....|....*....|....*....|....*..
gi 16131984 359 LLRQIHQADGQPLTAEQNRILEAQLRTQRELLNSLLQ 395
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQ 517
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-389 |
2.13e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 27 QITQELEQAK-------AAKPAQPEVVEALQSALNALEERKGSLE--RIKQYQQVIDNYPKLSATLRA------QLNNMR 91
Cdd:pfam01576 360 ELTEQLEQAKrnkanleKAKQALESENAELQAELRTLQQAKQDSEhkRKKLEGQLQELQARLSESERQraelaeKLSKLQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 92 DEPRSVSPGMS-----TDALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNE-------IERRL 159
Cdd:pfam01576 440 SELESVSSLLNeaegkNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEeeeakrnVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 160 GTLtgntplnQAQNFALQSDSARLKALVDELELAQLSAnnRQELARLRSELAEKESQ---------QLDAYLQALRNQLN 230
Cdd:pfam01576 520 STL-------QAQLSDMKKKLEEDAGTLEALEEGKKRL--QRELEALTQQLEEKAAAydklektknRLQQELDDLLVDLD 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 231 SQRQLEAerALESTE-----LLAENsadlpKDIVAQFkinrelsaalnqqAQRMDLVASQQRQAASQTLQVRQALNTLRE 305
Cdd:pfam01576 591 HQRQLVS--NLEKKQkkfdqMLAEE-----KAISARY-------------AEERDRAEAEAREKETRALSLARALEEALE 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 306 QSQWLGSSNllgEALRAQVARL-----------PEMPKPQQ-LDTEMAQLRVQRLRYEDLL------------NKQPLL- 360
Cdd:pfam01576 651 AKEELERTN---KQLRAEMEDLvsskddvgknvHELERSKRaLEQQVEEMKTQLEELEDELqatedaklrlevNMQALKa 727
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16131984 361 ---RQIHQADGQ-----PLTAEQNRILEAQL---RTQREL 389
Cdd:pfam01576 728 qfeRDLQARDEQgeekrRQLVKQVRELEAELedeRKQRAQ 767
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
56-395 |
3.04e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 56 LEERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVspgmstDALNQEILQVSSQLLDKSRQAQQEQERAREIA 135
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATI------DTRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 136 DSLNQLPQQQTDARRQLNEIERRLGTLTgnTPLNQAQNFALQsdSARLKALvdELELAQLSANNRQELARLRSELA---- 211
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKERE--QQLQTKEQIHLQ--ETRKKAV--VLARLLELQEEPCPLCGSCIHPNparq 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 212 ----------------------EKESQQLDAYLQALRNQLNSQRQlEAERALESTELLA----ENSADLPK------DIV 259
Cdd:TIGR00618 519 didnpgpltrrmqrgeqtyaqlETSEEDVYHQLTSERKQRASLKE-QMQEIQQSFSILTqcdnRSKEDIPNlqnitvRLQ 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 260 AQFKINREL--SAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPK----P 333
Cdd:TIGR00618 598 DLTEKLSEAedMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKellaS 677
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131984 334 QQLDTEMAQLRVQRLRY--EDLLNKQPLLRQIHQADGQ--PLTAEQNRILEAQ---LRTQRELLNSLLQ 395
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYwkEMLAQCQTLLRELETHIEEydREFNEIENASSSLgsdLAAREDALNQSLK 746
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
19-293 |
3.05e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 19 AATAPDSKQITQELEQAKAAKPAQPEVVEALQSALNALEER-KGSLERIKQYQQVID----NYPKLSATLRAQLNNMRDE 93
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAElEALQAEIDKLQAEIAeaeaEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 94 PRSVSP-------GMSTDALNQeiLQVSSQLLDKSRQAQQEQERAREiadslnQLPQQQTDARRQLNEIERRLGTLtgnt 166
Cdd:COG3883 99 GGSVSYldvllgsESFSDFLDR--LSALSKIADADADLLEELKADKA------ELEAKKAELEAKLAELEALKAEL---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 167 plnQAQNFALQSDSARLKALVDELELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERALESTEL 246
Cdd:COG3883 167 ---EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16131984 247 LAENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQT 293
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAG 290
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
47-351 |
3.67e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 47 EALQSALN-ALEERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSvspgmSTDALnQEILQVSSQLLDKSRQAQ 125
Cdd:pfam07888 30 ELLQNRLEeCLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES-----RVAEL-KEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 126 QEQERARE-IADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQ--------------AQNFALQSDSARLKA--LVD 188
Cdd:pfam07888 104 KELSASSEeLSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelermkerakkagAQRKEEEAERKQLQAklQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 189 ELELAQLSAnnrqELARLRSELAEKESQ--QLDAYLQALRNQLNSQRQLEAE--------RALESTELLAENSADLPKdi 258
Cdd:pfam07888 184 EEELRSLSK----EFQELRNSLAQRDTQvlQLQDTITTLTQKLTTAHRKEAEnealleelRSLQERLNASERKVEGLG-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 259 vaqfkinRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTLRE-QSQWLGSSNLLGEALRAQVARLpempkpQQLD 337
Cdd:pfam07888 258 -------EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEADKDRI------EKLS 324
|
330
....*....|....*.
gi 16131984 338 TEMAQL--RVQRLRYE 351
Cdd:pfam07888 325 AELQRLeeRLQEERME 340
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-375 |
6.53e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 31 ELEQAKAAkpaqpevVEALQSALNALEERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMRD---EPRSVSPGMSTDALN 107
Cdd:PRK02224 483 ELEDLEEE-------VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAEE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 108 QEilqvssqllDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTplnqaqnfalqsdsARLKALV 187
Cdd:PRK02224 556 KR---------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE--------------DEIERLR 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 188 DELE-LAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLnsQRQLEA-ERALESTELLAENSADLPKDIVAqfkIN 265
Cdd:PRK02224 613 EKREaLAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK--ERAEEYlEQVEEKLDELREERDDLQAEIGA---VE 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 266 RELsaalnqqaqrmdlvasqqrqaasqtlqvrQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKpqQLDTEMAQLRV 345
Cdd:PRK02224 688 NEL-----------------------------EELEELRERREALENRVEALEALYDEAEELESMYG--DLRAELRQRNV 736
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16131984 346 QRLryEDLLNKQ-PLLRQ----------------IHQADGQPLTAEQ 375
Cdd:PRK02224 737 ETL--ERMLNETfDLVYQndayshieldgeyeltVYQKDGEPLEPEQ 781
|
|
| PRK11465 |
PRK11465 |
putative mechanosensitive channel protein; Provisional |
873-956 |
7.60e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 183147 [Multi-domain] Cd Length: 741 Bit Score: 46.70 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 873 ITTITkylLMLIgglvgFSMIGIEWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKI 952
Cdd:PRK11465 521 ISTIT---IMIV-----LSEIGVNIAPLLAGAGALGLAISFGSQTLVKDIITGVFIQFENGMNTGDLVTIGPLTGTVERM 592
|
....
gi 16131984 953 NTRA 956
Cdd:PRK11465 593 SIRS 596
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
105-278 |
7.67e-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: 47.25 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 105 ALNQEILQVSSQLLDKSRQAQQeQERAREIADSLNQLPQQQTDAR----RQLNEIERRLGTLTGNTPLNQAQNFALQSDS 180
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAeeleELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 181 ARLKALVDEL---ELAQLSANNRqeLARLRSELAE--KESQQLDAYLQalrNQLNSQRQLEAERalestELLAENSADLP 255
Cdd:COG3096 588 EQLRARIKELaarAPAWLAAQDA--LERLREQSGEalADSQEVTAAMQ---QLLEREREATVER-----DELAARKQALE 657
|
170 180 190
....*....|....*....|....*....|
gi 16131984 256 KDIvaqfkinRELSAA-------LNQQAQR 278
Cdd:COG3096 658 SQI-------ERLSQPggaedprLLALAER 680
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-425 |
7.98e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNYPKLSATLRAQLnnmrdeprsvspgmstDALNQE 109
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL----------------EELEEA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 110 ILQVSsQLLDKSRQAQQE-QERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGntplnqaqnfALQSDSARLKALVD 188
Cdd:COG1196 430 LAELE-EEEEEEEEALEEaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE----------ELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 189 ELELAQ------LSANNRQELARLRSELAE------KESQQLDAYLQALRNQLNSQRQLEAERALES-TELLAENSADLP 255
Cdd:COG1196 499 AEADYEgflegvKAALLLAGLRGLAGAVAVligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYlKAAKAGRATFLP 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 256 KDIVAQFKINRELSAALnQQAQRMDLVASQQRQAA--------------------------SQTLQVRQALNTLREQSQW 309
Cdd:COG1196 579 LDKIRARAALAAALARG-AIGAAVDLVASDLREADaryyvlgdtllgrtlvaarleaalrrAVTLAGRLREVTLEGEGGS 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 310 LGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPLLRQIHQADGQPLTAEQNRILEAQLRTQREL 389
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
410 420 430
....*....|....*....|....*....|....*.
gi 16131984 390 LNSLLQGGDTLLLELTKLKVSNGQLEDALKEVNEAT 425
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
31-360 |
1.03e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 31 ELEQAKAAKPAQPEVVEALqsaLNALEERKGSLERIKQYQQVIDNYPKLSATLR----AQLNNMRDEPRSVS---PGMST 103
Cdd:pfam09731 206 EEEAAPPLLDAAPETPPKL---PEHLDNVEEKVEKAQSLAKLVDQYKELVASERivfqQELVSIFPDIIPVLkedNLLSN 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 DALN-------QEILQVSSQLLDKSRQAQQEQERAreiadslnqLPQQQTDARRQLNEIERRLgtltgntplnqaqnfal 176
Cdd:pfam09731 283 DDLNsliahahREIDQLSKKLAELKKREEKHIERA---------LEKQKEELDKLAEELSARL----------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 177 qsdsarlkalvdELELAQLSANNRQELARLRSELAEKESQQLDAYL--------QALRNQLNSQRQLEAERALEST-ELL 247
Cdd:pfam09731 337 ------------EEVRAADEAQLRLEFEREREEIRESYEEKLRTELerqaeaheEHLKDVLVEQEIELQREFLQDIkEKV 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 248 AENSADLPKDIVAQFKINRELSAAL---------NQQAQRM-----DLVASQQR-QAASQTLQVRQALNTLREqsqwLGS 312
Cdd:pfam09731 405 EEERAGRLLKLNELLANLKGLEKATsshsevedeNRKAQQLwlaveALRSTLEDgSADSRPRPLVRELKALKE----LAS 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16131984 313 SNllgEALRAQVARLPEMPKPQQLDTEmAQLRVQRLRYEDLLNKQPLL 360
Cdd:pfam09731 481 DD---EVVKAALASLPEEAYQRGVYTE-AALRERFRRVAKEVRKVSLI 524
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
104-267 |
1.45e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 DALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNqaqnfALQSDSARL 183
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE-----ALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 184 KALVDELELAQLSANNRQE-----LARLRSELAEKEsQQLDAYLQALRNQLNSQRQLEAERALESTELlaenSADLPKDI 258
Cdd:COG1579 102 KRRISDLEDEILELMERIEeleeeLAELEAELAELE-AELEEKKAELDEELAELEAELEELEAEREEL----AAKIPPEL 176
|
....*....
gi 16131984 259 VAQFKINRE 267
Cdd:COG1579 177 LALYERIRK 185
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
57-216 |
2.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 57 EERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSV-----SPGMSTDALNQEILQVSSQL--LDK--------- 120
Cdd:PHA02562 206 EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLvmdieDPSAALNKLNTAAAKIKSKIeqFQKvikmyekgg 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 121 -----SRQAQQEQERAREIADSLNQLPQQQT---DARRQLNEIERRLGTLTG-----NTPLNQaQNFALQSDSARLKALV 187
Cdd:PHA02562 286 vcptcTQQISEGPDRITKIKDKLKELQHSLEkldTAIDELEEIMDEFNEQSKkllelKNKIST-NKQSLITLVDKAKKVK 364
|
170 180 190
....*....|....*....|....*....|
gi 16131984 188 DELELAQLS-ANNRQELARLRSELAEKESQ 216
Cdd:PHA02562 365 AAIEELQAEfVDNAEELAKLQDELDKIVKT 394
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-308 |
2.09e-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: 45.55 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAkpaqpeVVEALQSALNALEERKGSLERIKQyqqvidnypklsaTLRAQLNNMRDEPRSVSpgmstdalnqe 109
Cdd:pfam01576 348 QEMRQKHTQ------ALEELTEQLEQAKRNKANLEKAKQ-------------ALESENAELQAELRTLQ----------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 110 ilqvssqlldksrQAQQEQERAREIADS-LNQLPQQQTDARRQLNEIERRLGTLTG-----NTPLNQA--QNFALQSDSA 181
Cdd:pfam01576 398 -------------QAKQDSEHKRKKLEGqLQELQARLSESERQRAELAEKLSKLQSelesvSSLLNEAegKNIKLSKDVS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 182 RLKA-LVDELELAQ--------LSANNRQ---ELARLRSELAEKE--SQQLDAYLQALRNQL-NSQRQLEAEraLESTEL 246
Cdd:pfam01576 465 SLESqLQDTQELLQeetrqklnLSTRLRQledERNSLQEQLEEEEeaKRNVERQLSTLQAQLsDMKKKLEED--AGTLEA 542
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 247 LAENSADLPKDIVAQFKINRELSAA---LNQQAQRM-----DLVASQQRQaasqtlqvRQALNTLrEQSQ 308
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAydkLEKTKNRLqqeldDLLVDLDHQ--------RQLVSNL-EKKQ 603
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
13-273 |
3.66e-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: 44.56 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 13 LSWGAYAATAPDSKQITQ-ELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVidnyPKLSATLRaQLNNMR 91
Cdd:COG5185 312 ESLEEQLAAAEAEQELEEsKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL----SKSSEELD-SFKDTI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 92 DEPRSVSPGMSTDALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIER--RLGTLTGNTPLN 169
Cdd:COG5185 387 ESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKvmREADEESQSRLE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 170 QAQNFALQSDSARLKALVDELELAQlsannrQELARLRSELaEKESQQLDAYLQALRNQLN-SQRQLEAERALESTELLA 248
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIE------SRVSTLKATL-EKLRAKLERQLEGVRSKLDqVAESLKDFMRARGYAHIL 539
|
250 260
....*....|....*....|....*
gi 16131984 249 ENSADLPKDIVAQFKINRELSAALN 273
Cdd:COG5185 540 ALENLIPASELIQASNAKTDGQAAN 564
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
24-159 |
3.76e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.88 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 24 DSKQITQELEQAKAAkpaqpevVEALQSALNALEERKGSLERIKQYQQVIdnypklsATLRAQLNNMRDEPRSVSPGMST 103
Cdd:COG1566 77 DPTDLQAALAQAEAQ-------LAAAEAQLARLEAELGAEAEIAAAEAQL-------AAAQAQLDLAQRELERYQALYKK 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131984 104 DALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRL 159
Cdd:COG1566 143 GAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAAL 198
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
13-254 |
4.08e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 13 LSWGAY-AATAPDSKQITQELE-----------QAKAAKPAQPEVVEALQSALNALEERKGSLE---------------- 64
Cdd:pfam05701 24 VDWKAHrIQTVERRKLVELELEkvqeeipeykkQSEAAEAAKAQVLEELESTKRLIEELKLNLEraqteeaqakqdsela 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 65 --RIKQYQQVIDNypKLSATLRAQLNNMRDepRSVSPGMSTDALNQEILQVSSQLLDKSRQAQQEQERAREIADSlnqlp 142
Cdd:pfam05701 104 klRVEEMEQGIAD--EASVAAKAQLEVAKA--RHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSA----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 143 qqqtdarrqLNEIERRLGTLTgntplnqaqnfalqsdsARLKALVDELELAQlSANNRQELARLRSELA--------EKE 214
Cdd:pfam05701 175 ---------SKEIEKTVEELT-----------------IELIATKESLESAH-AAHLEAEEHRIGAALAreqdklnwEKE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16131984 215 SQQLDAYLQALRNQLNSQRQLEAERAlESTELLAENSADL 254
Cdd:pfam05701 228 LKQAEEELQRLNQQLLSAKDLKSKLE-TASALLLDLKAEL 266
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
26-248 |
4.49e-04 |
|
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: 44.56 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQ---ELEQ----AKAAKpAQPEvvealqSALNALEERKGSLERIKQYQ---QVIDNYPKLSA------TLRAQLNN 89
Cdd:COG3096 451 QQATEevlELEQklsvADAAR-RQFE------KAYELVCKIAGEVERSQAWQtarELLRRYRSQQAlaqrlqQLRAQLAE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 90 M-RDEPRSVSPGMSTDALNQEI-LQVSSQLLDKSRQAQQEQERArEIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTP 167
Cdd:COG3096 524 LeQRLRQQQNAERLLEEFCQRIgQQLDAAEELEELLAELEAQLE-ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 168 lnqaQNFALQSDSARLKALVDElELAqlsanNRQELARLRSELAEKESQ--QLDAYLQALRNQLNSQ-RQLEAERALEST 244
Cdd:COG3096 603 ----AWLAAQDALERLREQSGE-ALA-----DSQEVTAAMQQLLEREREatVERDELAARKQALESQiERLSQPGGAEDP 672
|
....
gi 16131984 245 ELLA 248
Cdd:COG3096 673 RLLA 676
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
26-349 |
5.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQ----YQQVI-------DNYPKLSATLRAQLNNMRDEP 94
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAeiedLRETIaetererEELAEEVRDLRERLEELEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 95 RSVSPGMSTDALNQEILQVSSQLLDK-----------SRQAQQE----------------------QERAREIADSLNQL 141
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDrdeelrdrleeCRVAAQAhneeaeslredaddleeraeelREEAAELESELEEA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 142 PQQQTDARRQLNEIERRLGTLT---GNTP--LNQAQNF--ALQSDSARLKALVDELElAQLS--ANNRQELARLRSE--- 209
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRerfGDAPvdLGNAEDFleELREERDELREREAELE-ATLRtaRERVEEAEALLEAgkc 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 210 ---------------LAEKESQ--QLDAYLQALRNQLNSQRQ--------LEAERALESTELLAENSADLPKDIVAQFKI 264
Cdd:PRK02224 455 pecgqpvegsphvetIEEDRERveELEAELEDLEEEVEEVEErleraedlVEAEDRIERLEERREDLEELIAERRETIEE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 265 NRELSAALNQQAQRMDLVASQQRQAAS-------QTLQV-------RQALNTLREQSQWLGSSNLLGEALRAQVARLPEm 330
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAeaeeeaeEAREEvaelnskLAELKERIESLERIRTLLAAIADAEDEIERLRE- 613
|
410
....*....|....*....
gi 16131984 331 pKPQQLdTEMAQLRVQRLR 349
Cdd:PRK02224 614 -KREAL-AELNDERRERLA 630
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
116-304 |
8.02e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 116 QLLDKSRQ-AQQEQERARE-----IADSLNQLPQQQTDARRQLNEIERRLGTLTGntplnQAQNFALQ-SDS-ARLKALV 187
Cdd:NF041483 717 ETLGSARAeADQERERAREqseelLASARKRVEEAQAEAQRLVEEADRRATELVS-----AAEQTAQQvRDSvAGLQEQA 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 188 DElELAQLSANNRQELARLRSElAEKESQQL--DAYLQALRNQLNSQR-QLEAERALESTELLAENSAdlpKDIVAQfki 264
Cdd:NF041483 792 EE-EIAGLRSAAEHAAERTRTE-AQEEADRVrsDAYAERERASEDANRlRREAQEETEAAKALAERTV---SEAIAE--- 863
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131984 265 NRELSAALNQQAQRM-----DLVASQQRQAASQTLQVRQALNTLR 304
Cdd:NF041483 864 AERLRSDASEYAQRVrteasDTLASAEQDAARTRADAREDANRIR 908
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
123-395 |
8.38e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 123 QAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLgtltgntplnqaQNFALQSDSARLKALVDeLELAQLSANNRQe 202
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAAL------------EEFRQKNGLVDLSEEAK-LLLQQLSELESQ- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 203 LARLRSELAEKESQqldayLQALRNQLNSQRQLEAEralestellaensadlpkdiVAQFKINRELSAALNQQAQRMDLV 282
Cdd:COG3206 228 LAEARAELAEAEAR-----LAALRAQLGSGPDALPE--------------------LLQSPVIQQLRAQLAELEAELAEL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 283 ASQQRQAASQTLQVRQALNTLREQsqwlgssnllgeaLRAQVARLPempkpQQLDTEMAQLRVQRLRYEDLLNKqplLRQ 362
Cdd:COG3206 283 SARYTPNHPDVIALRAQIAALRAQ-------------LQQEAQRIL-----ASLEAELEALQAREASLQAQLAQ---LEA 341
|
250 260 270
....*....|....*....|....*....|...
gi 16131984 363 ihQADGQPLTAEQNRILEAQLRTQRELLNSLLQ 395
Cdd:COG3206 342 --RLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
165-396 |
1.25e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 165 NTPLNQAQNFALQSDSArLKALVDELELAQLSANNRQELARLRSELAEKES--QQLDAYLQALRNQLNSQRQL--EAERA 240
Cdd:PRK11637 12 AVKPRRFAIRPILYASV-LSAGVLLCAFSAHASDNRDQLKSIQQDIAAKEKsvRQQQQQRASLLAQLKKQEEAisQASRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 241 LESTEllaENSADLPKDIVAqfkINRELSAALNQQAQRMDLVASQQ----RQAASQTLQVrqALNTlrEQSQ----WLGS 312
Cdd:PRK11637 91 LRETQ---NTLNQLNKQIDE---LNASIAKLEQQQAAQERLLAAQLdaafRQGEHTGLQL--ILSG--EESQrgerILAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 313 SNLLGEALRAQVARLpempkpQQLDTEMAQlrvQRLRYEDLLNKQPLLRQIHQADGQPLtaEQNRIleAQLRTQRELLNS 392
Cdd:PRK11637 161 FGYLNQARQETIAEL------KQTREELAA---QKAELEEKQSQQKTLLYEQQAQQQKL--EQARN--ERKKTLTGLESS 227
|
....
gi 16131984 393 LLQG 396
Cdd:PRK11637 228 LQKD 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-306 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 144 QQTDARRQLNEIERRLGTLtgntplnQAQNFALQSDSARLKALVDELElAQLSANNrQELARLRSELAEKEsQQLDAYLQ 223
Cdd:COG3883 17 QIQAKQKELSELQAELEAA-------QAELDALQAELEELNEEYNELQ-AELEALQ-AEIDKLQAEIAEAE-AEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 224 ALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQFKINRELSAALNQQAQRMDLVASQQRQAASQTLQVRQALNTL 303
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
...
gi 16131984 304 REQ 306
Cdd:COG3883 167 EAA 169
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
84-225 |
1.32e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.53 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 84 RAQLNNMRDEPRSVSPGMSTDALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTLT 163
Cdd:COG3524 197 REALLAFRNRNGILDPEATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGAS 276
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131984 164 GNTPLNQAqnfalqsdSARLKALVDELELAQL---SANNRQELARlrselAEKESQQLdaYLQAL 225
Cdd:COG3524 277 GGDSLASL--------LAEYERLELEREFAEKaytSALAALEQAR-----IEAARQQR--YLAVI 326
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
112-349 |
1.66e-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: 42.14 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 112 QVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLgtltgntplnQAQNFALQSDSARLKALVDELE 191
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA----------AAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 192 LAQLSAnnRQELARLRSELAEKESQQLD-------------AYLQALRNQLNSQRQLEAErALESTELLAENSADLPKDI 258
Cdd:TIGR02794 121 AEEAKA--KQAAEAKAKAEAEAERKAKEeaakqaeeeakakAAAEAKKKAEEAKKKAEAE-AKAKAEAEAKAKAEEAKAK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 259 VAQFKINRELSA-ALNQQAQRMDLVASQQRQAASQTLQVRQAL-NTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQL 336
Cdd:TIGR02794 198 AEAAKAKAAAEAaAKAEAEAAAAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLY 277
|
250
....*....|...
gi 16131984 337 DTEMAQLRVQRLR 349
Cdd:TIGR02794 278 DDPSFRGKTCRLR 290
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
26-274 |
1.84e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKaakpaqpEVVEALQSALNALEERKGSLErikqyQQVidnypklsATLRAQLNNMRDEPRSVspgmstda 105
Cdd:pfam00261 4 QQIKEELDEAE-------ERLKEAMKKLEEAEKRAEKAE-----AEV--------AALNRRIQLLEEELERT-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 lnQEILQVSSQLLDKSRQAQQEQERAR---------------EIADSLNQLPQQQTDARRQLNEIERRLGTLTGNtpLNQ 170
Cdd:pfam00261 56 --EERLAEALEKLEEAEKAADESERGRkvlenralkdeekmeILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD--LER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 171 AQNFALQSDSaRLKALVDELELAqlsANNRQELarlrsEL-AEKESQQLDAYLQALRNqLNS------QRQLEAERalES 243
Cdd:pfam00261 132 AEERAELAES-KIVELEEELKVV---GNNLKSL-----EAsEEKASEREDKYEEQIRF-LTEklkeaeTRAEFAER--SV 199
|
250 260 270
....*....|....*....|....*....|.
gi 16131984 244 TELLAENSaDLPKDIVAQFKINRELSAALNQ 274
Cdd:pfam00261 200 QKLEKEVD-RLEDELEAEKEKYKAISEELDQ 229
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
102-208 |
2.11e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 42.01 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 102 STDALNQEILQVSSQLLDKSRQAQQE----QERAREIADSLNQLPQQQTDARR-----QLNEIERRLGT------LTGNT 166
Cdd:PRK06975 361 ANDAQTAELRVKTEQAQASVHQLDSQfaqlDGKLADAQSAQQALEQQYQDLSRnrddwMIAEVEQMLSSasqqlqLTGNV 440
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 16131984 167 plnQAQNFALQSDSARLKALVDelelAQLSANNR---QELARLRS 208
Cdd:PRK06975 441 ---QLALIALQNADARLATSDS----PQAVAVRKaiaQDIERLKA 478
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
118-246 |
2.59e-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: 42.08 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 118 LDKSRQAQQEQERAR--------EIADSLNQLPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARLKALVDE 189
Cdd:pfam01576 196 LKKEEKGRQELEKAKrklegestDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131984 190 LElaqlsanNRQELARLRSELAEKESQQLDAYLQALRNQL-------NSQRQLEAERALESTEL 246
Cdd:pfam01576 276 LQ-------EDLESERAARNKAEKQRRDLGEELEALKTELedtldttAAQQELRSKREQEVTEL 332
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
17-398 |
2.67e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 17 AYAATAPDSKQ-----ITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLerIKQYQQVIDNYPKLSATLRAQLNNMR 91
Cdd:PRK10246 519 AYQALEPGVNQsrldaLEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSL--RQEEQALTQQWQAVCASLNITLQPQD 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 92 DeprsVSPGMST-DALNQEILQVSS-QLLDKSRQAQQEQERAREiadslNQLPQQQTDARRQLNEIERRLGTLTGNTPL- 168
Cdd:PRK10246 597 D----IQPWLDAqEEHERQLRLLSQrHELQGQIAAHNQQIIQYQ-----QQIEQRQQQLLTALAGYALTLPQEDEEASWl 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 169 ------------NQAQNFALQSDSARLKALVDEL--------ELAQLSANNRQElarlrselAEKESQQLDAYLQALRNQ 228
Cdd:PRK10246 668 atrqqeaqswqqRQNELTALQNRIQQLTPLLETLpqsddlphSEETVALDNWRQ--------VHEQCLSLHSQLQTLQQQ 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 229 LnsqrQLEAERALESTELLAENSADLPKDIVAQFkinreLSAALNQQA-QRMDlvasQQRQAASQTLQVRQALNTLREQS 307
Cdd:PRK10246 740 D----VLEAQRLQKAQAQFDTALQASVFDDQQAF-----LAALLDEETlTQLE----QLKQNLENQRQQAQTLVTQTAQA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 308 qwlgssnlLGEALRAQVARLPEMPKPQQLDTEMAQLrVQRLRyeDLLNKQPLLRQIHQADGQplTAEQNRILEAQLRTQR 387
Cdd:PRK10246 807 --------LAQHQQHRPDGLDLTVTVEQIQQELAQL-AQQLR--ENTTRQGEIRQQLKQDAD--NRQQQQALMQQIAQAT 873
|
410
....*....|....*....
gi 16131984 388 EL------LNSLL--QGGD 398
Cdd:PRK10246 874 QQvedwgyLNSLIgsKEGD 892
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
141-293 |
2.76e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 141 LPQQQTDARRQLNEIERRLGTLTGNTPLNQAQNFALQSDSARLKALVDELElaqlsaNNRQELARLRSELAEKESqQLDA 220
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAE------AERSRLQALLAELAGAGA-AAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131984 221 YLQALRNQLNSQRQLeAERALESTELLAENSADLPKDIVAqfkinreLSAALNqqaqrmdlvASQQRQAASQT 293
Cdd:PRK09039 117 RAGELAQELDSEKQV-SARALAQVELLNQQIAALRRQLAA-------LEAALD---------ASEKRDRESQA 172
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
106-240 |
2.92e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.92 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 106 LNQEILQVSSQLLDKSRQAQQEQERA-REIADSLNQLPQqqtdarrqlneierrlgtltGNTPLNQAQNFALQSDSARLK 184
Cdd:pfam08614 1 AFLELIDAYNRLLDRTALLEAENAKLqSEPESVLPSTSS--------------------SKLSKASPQSASIQSLEQLLA 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131984 185 ALVDELELAQLS-ANNRQELARLRSELAEKESQqldaylqaLRNQLNSQRQLEAERA 240
Cdd:pfam08614 61 QLREELAELYRSrGELAQRLVDLNEELQELEKK--------LREDERRLAALEAERA 109
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
25-255 |
3.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 25 SKQITQE---LEQ----AKAAKPAQPEVVEALQSAL------NALEERKGSLERIKQYQQVIDNYPKLSA---TLRAQLN 88
Cdd:PRK04863 451 EQEATEEllsLEQklsvAQAAHSQFEQAYQLVRKIAgevsrsEAWDVARELLRRLREQRHLAEQLQQLRMrlsELEQRLR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 89 NMRDEPRsvspgmstdaLNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQ----LPQQQTDARRQLNEIERRLGTLTG 164
Cdd:PRK04863 531 QQQRAER----------LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSEsvseARERRMALRQQLEQLQARIQRLAA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 165 NTPlnqaQNFALQSDSARLKALVDElELAqlsanNRQELARLRSELAEKESQqldayLQALRNQLNSQR-QLEAERales 243
Cdd:PRK04863 601 RAP----AWLAAQDALARLREQSGE-EFE-----DSQDVTEYMQQLLERERE-----LTVERDELAARKqALDEEI---- 661
|
250
....*....|..
gi 16131984 244 TELLAENSADLP 255
Cdd:PRK04863 662 ERLSQPGGSEDP 673
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
30-536 |
3.92e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 30 QELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMRDEPRSVSpgmSTDALNQE 109
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE---LAAEAAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 110 ILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRlgtltgntplnQAQnfalqsDSARLKAlVDE 189
Cdd:COG3064 79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKR-----------KAE------EEAKRKA-EEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 190 LELAQLSANNRQELARLRSELAEKESqqldaylQALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQFKINRELS 269
Cdd:COG3064 141 RKAAEAEAAAKAEAEAARAAAAAAAA-------AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 270 AALNQQAQRMDLVASQQRQAASQTLQVRQALNTLREQSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLR 349
Cdd:COG3064 214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 350 YEDLLNKQPLLRQIHQADGQPL-TAEQNRILEAQLRTQRELLNSLLQGGDTLLLELTKLKVSNGQLEDALKEVNEATHRY 428
Cdd:COG3064 294 GLVLDDSAALAAELLGAVAAEEaVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 429 LFWTSDVRPMTIAWPLEIAQDLRRLISLDTFSQLGKASVMMLTSKETILPLFGALILVGCSIYSRRYFTRFLERSAAKVG 508
Cdd:COG3064 374 ALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGK 453
|
490 500
....*....|....*....|....*...
gi 16131984 509 KVTQDHFWLTLRTLFWSILVASPLPVLW 536
Cdd:COG3064 454 ALTGDADALLGILKAVALDGGAVLADLL 481
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
26-156 |
4.39e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 26 KQITQELEQAKAAKPAQPEVVEALQSALNALEERKGSLERIKQYQQVIDNYPKLSATLRAQLNNMRDEprsvspgmsTDA 105
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE---------ADE 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16131984 106 LNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIE 156
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE 264
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
200-392 |
4.66e-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: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 200 RQELARLRSELaEKESQQLDAYLQALRNQLNSQRQLEAERALESTELLAENSADLPKDIVAQFKInREL---SAALNQQA 276
Cdd:pfam07888 68 REQWERQRREL-ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARI-RELeedIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 277 Q----RMDLVASQQRQAASQtlqvRQALNTLREQSQwlgssnllgEALRAQVARLPEMPKP-QQLDTEMAQLRVQRLRYE 351
Cdd:pfam07888 146 LeretELERMKERAKKAGAQ----RKEEEAERKQLQ---------AKLQQTEEELRSLSKEfQELRNSLAQRDTQVLQLQ 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131984 352 DLLNK-QPLLRQIHQADGQpltaeqNRILEAQLRTQRELLNS 392
Cdd:pfam07888 213 DTITTlTQKLTTAHRKEAE------NEALLEELRSLQERLNA 248
|
|
| BAR |
pfam03114 |
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ... |
204-395 |
4.97e-03 |
|
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.
Pssm-ID: 460810 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 204 ARLRSELAEKESQQLDAYLQALRNQLNSQRQLEaeralESTELLAENSADLPKDivaqFKINRELSAALNQQAQRMDLVA 283
Cdd:pfam03114 35 FDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLE-----QPEELLAESMIEAGKD----LGEDSSFGKALEDYGEALKRLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 284 SQQRQ----AASQTLQ-VRQALNTLRE---QSQWLGSSNLLGEALRAQVARLPEMPKPQQLDTEMA--QLRVQRLRYEDL 353
Cdd:pfam03114 106 QLLEQlddrVETNFLDpLRNLLKEFKEiqkHRKKLERKRLDYDAAKTRVKKAKKKKSSKAKDESQAeeELRKAQAKFEES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131984 354 LNK-QPLLRQIHQADGQPLTAEQNRILEAQLRTQRELLNSLLQ 395
Cdd:pfam03114 186 NEQlKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQ 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-241 |
5.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 104 DALNQEILQVSSQLLDKSRQAQQEQERAREIADSLNQLP------QQQTDARRQLNEIERRLGTLTGnTPLNQAQNFALQ 177
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRaaleqaEEYQELKEELEELEEQLEELLG-ELEELLEALDEE 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131984 178 SDSARLKALVDEL-ELAQLSANNRQELARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERAL 241
Cdd:COG4717 429 ELEEELEELEEELeELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
65-291 |
5.24e-03 |
|
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: 40.83 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 65 RIKQYQQVIDNYPKLSATL---RAQLNNMRDEPRSVspgmstdalNQEILQVSSQLLDKSRqAQQEQERAREIADSLNQL 141
Cdd:pfam05622 295 RLGQEGSYRERLTELQQLLedaNRRKNELETQNRLA---------NQRILELQQQVEELQK-ALQEQGSKAEDSSLLKQK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 142 PQQQTDarrQLNEierrlgtltgntplnqaqnfaLQSDSARLKALVDELELAQLSaNNRQELARLRSELAEKES------ 215
Cdd:pfam05622 365 LEEHLE---KLHE---------------------AQSELQKKKEQIEELEPKQDS-NLAQKIDELQEALRKKDEdmkame 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 216 --------------QQLD--------AYLQALRNQLNSQRQL--EAERALESTELLAEN------SADLPKDIVAQFKIN 265
Cdd:pfam05622 420 erykkyvekaksviKTLDpkqnpaspPEIQALKNQLLEKDKKieHLERDFEKSKLQREQeeklivTAWYNMGMALHRKAI 499
|
250 260
....*....|....*....|....*.
gi 16131984 266 RELSAALNQQAQRMdlvASQQRQAAS 291
Cdd:pfam05622 500 EERLAGLSSPGQSF---LARQRQATN 522
|
|
| H15 |
cd00073 |
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ... |
39-88 |
5.39e-03 |
|
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber
Pssm-ID: 238028 [Multi-domain] Cd Length: 88 Bit Score: 37.22 E-value: 5.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 16131984 39 KPAQPEVVEALQSALNALEERKG-SLERIKQYqqVIDNYPKLSATLRAQLN 88
Cdd:cd00073 1 PPSHPPYSEMVTEAIKALKERKGsSLQAIKKY--IEAKYKVDDENFNKLLK 49
|
|
| H15 |
smart00526 |
Domain in histone families 1 and 5; |
39-89 |
6.33e-03 |
|
Domain in histone families 1 and 5;
Pssm-ID: 197772 [Multi-domain] Cd Length: 66 Bit Score: 36.40 E-value: 6.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16131984 39 KPAQPEVVEALQSALNALEERKG-SLERIKQYqqVIDNYPKLSATLRAQLNN 89
Cdd:smart00526 1 PPSHPPYSEMIVEAISALKERKGsSLQAIKKY--IEANYKVLPNNFRKLLKL 50
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
112-392 |
6.44e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 112 QVSSQLLDKSRQAQQEQERAREIADSLNQLPQQQTDARRQLNEIERRLGTltgNTPLNQAQNFALQSDSARLKAL--VDE 189
Cdd:PRK10246 206 QASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDEL---QQEASRRQQALQQALAAEEKAQpqLAA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 190 LELAQLSANNR------QE----LARLRSELAEKESQQLDAYLQALRNQLNSQRQLEAERAlESTEL---LAEN------ 250
Cdd:PRK10246 283 LSLAQPARQLRphweriQEqsaaLAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQA-QQQSLntwLAEHdrfrqw 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 251 SADLP--KDIVAQFKINRELSAALNQQ------------AQRMDLVASQQRQAASQTLQ---VRQALNTLREQSQwlgss 313
Cdd:PRK10246 362 NNELAgwRAQFSQQTSDREQLRQWQQQlthaeqklnalpAITLTLTADEVAAALAQHAEqrpLRQRLVALHGQIV----- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 314 nllgeALRAQVARLPEmpKPQQLDTEMAQLRVQ----RLRYEDllnkqpllRQIHQADGQPLTAEQNRIleAQLRTQREL 389
Cdd:PRK10246 437 -----PQQKRLAQLQV--AIQNVTQEQTQRNAAlnemRQRYKE--------KTQQLADVKTICEQEARI--KDLEAQRAQ 499
|
...
gi 16131984 390 LNS 392
Cdd:PRK10246 500 LQA 502
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
116-327 |
7.52e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 116 QLLDKSRQaqqeqeraREIADS---LNQLPQQQTDARRQLNEIERRLGTLTgntplNQAQNFALQSDsaRLKALVDELEL 192
Cdd:COG0497 136 SLLDPDAQ--------RELLDAfagLEELLEEYREAYRAWRALKKELEELR-----ADEAERARELD--LLRFQLEELEA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131984 193 AQLSANNRQELARLRSEL--AEKESQQLDAYLQALR-NQLNSQRQL-EAERALEStelLAENSADLpKDIV-----AQFK 263
Cdd:COG0497 201 AALQPGEEEELEEERRRLsnAEKLREALQEALEALSgGEGGALDLLgQALRALER---LAEYDPSL-AELAerlesALIE 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131984 264 INrELSAALNQQAQRMD-----LVASQQRQAASQTLQ---------VRQALNTLREQSQWLGSSNLLGEALRAQVARL 327
Cdd:COG0497 277 LE-EAASELRRYLDSLEfdperLEEVEERLALLRRLArkygvtveeLLAYAEELRAELAELENSDERLEELEAELAEA 353
|
|
| |
