|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
7-1120 |
0e+00 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 1854.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 7 YKRSRHFVFSAFIAFVFVLLCQNTAFARASSNGDLPTKADLQAQLDSLNKQKDLSAQDKLVQQDLTDTLATLDKIDRIKE 86
Cdd:PRK11281 1 YKRSRHFVFRAFIAFLFLLLCLSSAFARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 87 ETVQLRQKVAEAPEKMRQATAALTALSDvDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPE 166
Cdd:PRK11281 81 ETEQLKQQLAQAPAKLRQAQAELEALKD-DNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 167 RVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARL 246
Cdd:PRK11281 160 RAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 247 EHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPLVKQELEINQQLSQRLITATENGNQLMQQNIKVKNWLERAL 326
Cdd:PRK11281 240 EHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 327 QSERNIKEQIAVLKGSLLLSRILYQQQQTLPSADELENMTNRIADLRLEQFEVNQQRDALFQSDAFVNKLEEGHTNEVNS 406
Cdd:PRK11281 320 QSERNIKEQISVLKGSLLLSRILYQQQQALPSADLIEGLADRIADLRLEQFEINQQRDALFQPDAYIDKLEAGHKSEVTD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 407 EVHDALLQVVDMRRELLDQLNKQLGNQLMMAINLQINQQQLMSVSKNLKSILTQQIFWVNSNRPMDWDWIKAFPQSLKDE 486
Cdd:PRK11281 400 EVRDALLQLLDERRELLDQLNKQLNNQLNLAINLQLNQQQLLSVSDSLQSTLTQQIFWVNSNKPMDLDWLKAFPQALKDQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 487 FKSMKITVNWEKAWPAVFIAFLAGLPLLLIAGLIHWRLGWLKAYQQKLASAVGSLRNDSQLNTPKAILIDLIRALPVCLI 566
Cdd:PRK11281 480 FKSLKITVSFSNLWDGLFIALLLFLPLLLIAGLIRWRKKWIKARLQKLAADIGTLKRDSQLHTPKAILITLLLALPVTLI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 567 ILAVGLILLTMQLNISELLWSFSKKLAIFWLVFGLCWKVLEKNGVAVRHFGMPEQQTSHWRRQIVRISLALLPIHFWSVV 646
Cdd:PRK11281 560 FLAVGLILLTDAFNQSELLWSWSLKLALFWLVFATCYRVLRPNGVAERHFGMPKEQVSHFRRQIVRLSLALLPLLFWSVV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 647 AELSPLHLMDDVLGQAMIFFNLLLIAFLVWPMCRESWRDKESHTMRLVTITVLSIIPIALMVLTATGYFYTTLRLSGRWI 726
Cdd:PRK11281 640 AELSPLGLADDVIGQAVIIIALALIAFLVWPLCRESWRDKESHTLRLVVRTVLTIAPIALIVLVVLGYYYTALRLIGRLI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 727 ETVYLVIIWNLLYQTVLRGLSVAARRIAWRRALARRQNLVKEGAEGAEPPEEPTIALEQVNQQTLRITMLLMFALFGVMF 806
Cdd:PRK11281 720 ETLYLLIIWNLLYQTVLRGLSVAARRLAYRRALAKRQNLVKEGAEGAEPVEEPTLALEQVNQQSLRLTDLLLFALFFVMF 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 807 WAIWSDLITVFSYLDSITLWHYNGTEAGAAVVKNVTMGSLLFAIIASMVAWALIRNLPGLLEVLVLSRLNMRQGASYAIT 886
Cdd:PRK11281 800 YWVWSDLITVFSYLDSITLWHYTTTTAGGAVVESITLGNLLFALIILVVTYVLVRNLPGLLEVLVLSRLNLRQGTSYAIT 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 887 TILNYIIIAVGAMTVFGSLGVSWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRI 966
Cdd:PRK11281 880 TLLTYIIIAVGAVTAFSTLGVSWDKLQWLVAALSVGLGFGLQEIFANFVSGLIILFERPVRIGDTVTIGTFSGTVSKIRI 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 967 RATTITDFDRKEVIIPNKAFVTERLINWSLTDTTTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVMHEPMPEVFFTAFG 1046
Cdd:PRK11281 960 RATTITDFDRKEVIVPNKAFVTERLINWSLSDTVTRVVIKVGVAYGSDLEKVRELLLQAATENPRVMKEPEPQVFFLNFG 1039
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446099871 1047 ASTLDHELRLYVRELRDRSRTVDELNRTIDQLCRENDINIAFNQLEVHLHNEKGDEVTEVKRDYKGDDPTPAVG 1120
Cdd:PRK11281 1040 ASTLDHELRLYVRELGDRSPTVDELNRRIDRLFRENDINIAFNQLDVFLKNQKGDEVVEVKRDLKGDDPTPAVG 1113
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
18-1101 |
1.19e-114 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 382.48 E-value: 1.19e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 18 FIAFVFVLLCQNTAFARAssngdLPTKADLQAQLDSLNKQKDlsAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAE 97
Cdd:PRK10929 4 IITFLMAWLLSWGAYAAT-----APDEKQITQELEQAKAAKT--PAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 98 APEKMRQATAALTALSDvdndeETRKILSTLSLRQLETRVAQALDDL----------QNAQNDLASYNSQLVSLQTQper 167
Cdd:PRK10929 77 FPKLSAELRQQLNNERD-----EPRSVPPNMSTDALEQEILQVSSQLleksrqaqqeQDRAREISDSLSQLPQQQTE--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 168 vqnamynASQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNAEIDQ-QRKSLEGN-----TVLQDTLQKQRdyvta 241
Cdd:PRK10929 149 -------ARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDElELAQLSANnrqelARLRSELAKKR----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 242 nSARLEHQLQLLQEAVNSKRltltEKTAQEAVSPDEAARIQANPLVK---QELEINQQLSQRLITATENGNQLMQQNIKV 318
Cdd:PRK10929 217 -SQQLDAYLQALRNQLNSQR----QREAERALESTELLAEQSGDLPKsivAQFKINRELSQALNQQAQRMDLIASQQRQA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 319 KNWLERALQSERNIKEQIAVLKGSLLLSRILYQQQQTLPSADELENMTNRIADLRLEQFEVNQQRDALFQSDAFVNKLEE 398
Cdd:PRK10929 292 ASQTLQVRQALNTLREQSQWLGVSNALGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 399 GHTNEVNsEVHDALLQVvdmRRELLDQLNKQLGNQLMMAINLQINQQQLMSVSKNLKSILTQQIFWVNSNRPMDWDWIKA 478
Cdd:PRK10929 372 PLTAEQN-RILDAQLRT---QRELLNSLLSGGDTLILELTKLKVANSQLEDALKEVNEATHRYLFWVADVSPISLSYPLE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 479 FPQSLK-----DEF----KSMKITVNWEKAWPAVFIAFLagLPLLLIAGLIHWRlgwlkAYQQKLASAVGSLRNDSQLNT 549
Cdd:PRK10929 448 IAQDLRrllslDTFsqlgKASVMMLTSKETLLPLFGALL--LVGFSISSRRHYH-----AFLERSSSRVGKVTQDHFSLT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 550 PKAILIDLIRALPVCLIILAVGLILLTMqlnisellWSFSKKLAI----------FWlVFGLCWKVLEKNGVAVRHFGMP 619
Cdd:PRK10929 521 LRTVFWSILVASPLPVLWAALGYGLQNA--------WPYPLAVAIgdgvtatvplLW-VFMICATFARPNGLFIAHFGWP 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 620 EQQTSHWRR-------QIVRISLALLPIHFWSVvAELSPlhlmddVLGQamIFFNLLLIAF-LVWPMCRES----WRDKE 687
Cdd:PRK10929 592 RERVARAMRyyllsigLIVPLIMALITFDNLND-REFSG------TLGR--LCFILLCGALsLVTLSLKRAgiplYLDKE 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 688 SHTMRLVTIT---VLSIIPIALMVLTATGYFYTTLRLSGRwIETVylVIIWNLL---YQTVLRGLSVAARRIAWRRALAR 761
Cdd:PRK10929 663 GSGDNIINHAlwnLLIGAPLVAALASALGYLATAQALLAR-LETS--VAIWFLLlvvYHIIRRWMLIQRRRIAFDRAKQR 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 762 RQNLVKEGAEGAEPP------------EEPTIALEQVNQQTLRI--TMLLMFALFGVMFwaIWSDLITVFSYLDSITLWH 827
Cdd:PRK10929 740 RAEILAQRARGEEEAhhssspegaievEEPVIDLDAISAQSLRLvrSILTLIALLSVIV--LWSEIHSAFGFLENISLWD 817
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 828 YNGTEAGAAVVKNVTMGSLLFAIIASMVAWALIRNLPGLLEVLVLSRLNMRQGASYAITTILNYIIIAVGAMTVFGSLGV 907
Cdd:PRK10929 818 VTSTVQGVESLQPITLGSVLIAILVFIITTQLVRNLPALLELALLQHLDLTPGTGYAITTITKYLLMLIGGLVGFSMIGI 897
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 908 SWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRIRATTITDFDRKEVIIPNKAFV 987
Cdd:PRK10929 898 EWSKLQWLVAALGVGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEIIVPNKAFI 977
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 988 TERLINWSLTDTTTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVMHEPMPEVFFTAFGASTLDHELRLYVRELRDRSRT 1067
Cdd:PRK10929 978 TEQFINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVLDNPAPEVFLVDLQQGIQIFELRIYAAEMGHRMPL 1057
|
1130 1140 1150
....*....|....*....|....*....|....
gi 446099871 1068 VDELNRTIDQLCRENDINIAFNQLEVHLHNEKGD 1101
Cdd:PRK10929 1058 RHEIHQLILAGFREHGIDMPFPPFQMRLESLGGK 1091
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis]; |
840-1100 |
6.30e-109 |
|
Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442495 [Multi-domain] Cd Length: 281 Bit Score: 341.41 E-value: 6.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 840 NVTMGSLLFAIIASMVAWALIRNLPGLLEVLVLSRLNMRQGASYAITTILNYIIIAVGAMTVFGSLGVSWDKLQWLAAAL 919
Cdd:COG3264 17 SISLPNLLLALLILVVTYLLARLLSRLLERRLLRRTRLDPGLRYLISKLIRYLIIVLGLLIALSALGIDLTALAALAGAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 920 SVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRIRATTITDFDRKEVIIPNKAFVTERLINWSLTDT 999
Cdd:COG3264 97 GVGIGFGLQDIVSNFISGLILLFERPFRVGDWIEIGGTEGTVEEIGLRSTRIRTFDGEEVIIPNSELITNPVINWSLSDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 1000 TTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVMHEPMPEVFFTAFGASTLDHELRLYVRELRDRSRTVDELNRTIDQLC 1079
Cdd:COG3264 177 RRRVEIPVGVAYGSDLEKVRELLLEAAREHPRVLKDPAPSVLFTEFGDSSVNFELRFWVNDPRDRLRVRSDLNEAIKKAF 256
|
250 260
....*....|....*....|.
gi 446099871 1080 RENDINIAFNQLEVHLHNEKG 1100
Cdd:COG3264 257 REEGIEIPFPQRDVHLRNPPG 277
|
|
| MscS_TM |
pfam12794 |
Mechanosensitive ion channel inner membrane domain 1; The small mechanosensitive channel, MscS, ... |
511-825 |
3.36e-94 |
|
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: 303.75 E-value: 3.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 511 LPLLLIAGLIHWRLGWLKAYQQKLASAVGSLRNDSQLNTPKAILIDLIRALPVCLIILAVGLILLTM--QLNISELLWSF 588
Cdd:pfam12794 1 LLLLLVAGLLLWLRRRLKRRLERLAERVGKVTQDSFLHTLRALLLTLLLALPLPLLLAALGWLLQLSgwATPFSVALGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 589 SKKLAIFWLVFGLCWKVLEKNGVAVRHFGMPEQQTSHWRRQIVRISLALLPIHFWSVVAELSPLHLMDDVLGQAMIFFNL 668
Cdd:pfam12794 81 LLALALALLVFEFFRRLLRPDGLAIRHFGWPEERVQRLRRQLRWLIWVLVPLVFVLGLAEALPDSLARDVLGRLAFIILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 669 LLIAFLVWPMCRESWRDKESHT-------MRLVTITVLSIIPIALMVLTATGYFYTTLRLSGRWIETVYLVIIWNLLYQT 741
Cdd:pfam12794 161 LLLAVFLWRLLRPGRGLYASHLgegpnsrLRRLWWPLLVLAPLALAVLALLGYYYTALQLLGRLIDSLYLLLGWLLVYAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 742 VLRGLSVA----ARRIAWRRALARRQNLVKEGAEGAEP----PEEPTIALEQVNQQTLRITMLLMFALFGVMFWAIWSDL 813
Cdd:pfam12794 241 ALRWLLVArrrlAYRRAKERRAEALAQRAKEGEEGAEPsessVEEPELDLETISAQSLRLLRLLLLLAFLVGLYWIWSDL 320
|
330
....*....|..
gi 446099871 814 ITVFSYLDSITL 825
Cdd:pfam12794 321 LPAFSYLDNITL 332
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
50-289 |
9.71e-68 |
|
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: 227.57 E-value: 9.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 50 QLDSLNKQKDLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDvDNDEETRKILSTLS 129
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 130 LRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQA 209
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 210 LLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKtAQEAVSPDEAARIQANPLVKQ 289
Cdd:pfam12795 160 ALKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQ-AVAQTEQLAEEAAGDHPLVQQ 238
|
|
| MS_channel |
pfam00924 |
Mechanosensitive ion channel; Two members of this protein family: Swiss:Q57634 and Swiss: ... |
886-1085 |
8.30e-67 |
|
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: 223.25 E-value: 8.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 886 TTILNYIIIAVGAMTVFGSLGVSWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIR 965
Cdd:pfam00924 1 KKILKYLIIVVGILIVLSYLGVNVSALLAGLGALGLALGFALQDLVSNLVSGIIILFEKPFKIGDWIEIGDIEGTVEDIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 966 IRATTITDFDRKEVIIPNKAFVTERLINWSLTDtTTRLVIRLGVAYGSD---LEKVRKVLLKAATEHPRVMHEPMPEVFF 1042
Cdd:pfam00924 81 LRTTTIRTFDGRLVTIPNSSILTSNIINYSRSP-TRRVELSIGVAYSSDpdkLEKVIEILKEAAYEHPLVLKDPEPPVVF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446099871 1043 TAFGASTLDHELRLYVREL-RDRSRTVDELNRTIDQLCRENDIN 1085
Cdd:pfam00924 160 GEFGDSSLNFELRVWVKTLpGEYFNVRSELNLRIKKALEENGIE 203
|
|
| MscS |
COG0668 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
842-1099 |
5.92e-53 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440432 [Multi-domain] Cd Length: 276 Bit Score: 187.01 E-value: 5.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 842 TMGSLLFAIIASMVAWALIRNLPGLLEVLVLSRLNMRQGASYaITTILNYIIIAVGAMTVFGSLGVSwdkLQWLAAALSV 921
Cdd:COG0668 23 LLPKLLLALLILLIGWLLIRLLRRLIRRLLRRARRDRTLLPL-LRNILKILIVIIAILLILSILGVN---ITSLLAGLGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 922 G---LGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRIRATTITDFDRKEVIIPNKAFVTERLINWSlTD 998
Cdd:COG0668 99 AglaIGLAAQDLLSNFIAGIFILLERPFRVGDWIEVGGVEGTVEEIGLRSTRLRTLDGRLVTIPNSKILSSPITNYS-RG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 999 TTTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVmHEPMPEVFFTAFGASTLDHELRLYVRElRDRSRTVDELNRTIDQL 1078
Cdd:COG0668 178 PTRRVDVTIGVDYDTDIDKARELLKEILEELPRI-LKDPAVVGVTELGDSSVNLRVRAWTKP-GDYWDVRRDIRERIKAA 255
|
250 260
....*....|....*....|.
gi 446099871 1079 CRENDINIAFNQLEVHLHNEK 1099
Cdd:COG0668 256 LDEAGIEIPFPTRTVHLAEEA 276
|
|
| PRK10334 |
PRK10334 |
small-conductance mechanosensitive channel MscS; |
885-1102 |
1.43e-18 |
|
small-conductance mechanosensitive channel MscS;
Pssm-ID: 182386 [Multi-domain] Cd Length: 286 Bit Score: 87.28 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 885 ITTILNYIIIAVGAMTVFGSLGVSWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKI 964
Cdd:PRK10334 69 LSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 965 RIRATTITDFDRKEVIIPNKAFVTERLINWSlTDTTTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVMHEPMPEVFFTA 1044
Cdd:PRK10334 149 QIFSTTMRTADGKIIVIPNGKIIAGNIINFS-REPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNE 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446099871 1045 FGASTLDHELRLYVRELRDRSRTVDELNRtIDQLCRENDINIAFNQLEVHLHNEKGDE 1102
Cdd:PRK10334 228 LGASSINFVVRVWSNSGDLQNVYWDVLER-IKREFDAAGISFPYPQMDVNFKRVKEDK 284
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-398 |
2.01e-12 |
|
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: 72.01 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 68 QQDLTDTLATLDKIDRIKEET---VQLRQKVAEAPEKMRQATAALtalsdvdndEETRKILSTLSLRQLETRVAQALDDL 144
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELerqLKSLERQAEKAERYKELKAEL---------RELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 145 QNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTdVGETALRPSQKvlMQAQQALLNAEIDQQRKSLEg 224
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-ANEISRLEQQK--QILRERLANLERQLEELEAQ- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 225 ntvlQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTA--QEAVSPDEAARIQANPLVKQELEINQQLSQRLI 302
Cdd:TIGR02168 325 ----LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 303 TATENGNQLMQQNIKVKNWLERALQSERNIKE-QIAVLKGSL-LLSRILYQQQQTLPSADE-LENMTNRIADLRLEQFEV 379
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELeELEEELEELQEELERLEEaLEELREELEEAEQALDAA 480
|
330
....*....|....*....
gi 446099871 380 NQQRDALFQSDAFVNKLEE 398
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQE 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-306 |
5.35e-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: 62.86 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 74 TLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLAS 153
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 154 YNSQLVSLQTQPERVQNAMYNASQQlQQIRSRLDGTDVGETALRpsqKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQ 233
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRR---LQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446099871 234 KQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANplvKQELeinQQLSQRLITATE 306
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE---AEEL---EALIARLEAEAA 237
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
76-407 |
7.69e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.23 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 76 ATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALtalsdvdndEETRKILSTLS--LRQLETRVAQALDDLQNAQNDLAS 153
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEEL---------EQARSELEQLEeeLEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 154 YNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDvGETALRPSQKVLMQAQQALLNAEIDQQRKSLEG--NTVLQDT 231
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ-SEIAEREEELKELEEQLESLQEELAALEQELQAlsEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 232 LQKQRD---------YVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPLVKQELEINQQLSQRLI 302
Cdd:COG4372 185 LDELLKeanrnaekeEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 303 TATENGNQLMQQNIKVKNWLERALQSERNIKEQIAVLKGSLLLSRILYQQQQTLPSADELENMTNRIADLRLEQFEVNQQ 382
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*
gi 446099871 383 RDALFQSDAFVNKLEEGHTNEVNSE 407
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
46-343 |
1.22e-08 |
|
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: 59.42 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 46 DLQAQLDSLNKQKD--------LSAQDKLVQQDLTDTLATLD-----------KIDRIKEETVQLRQKVAEAPEKMRQAT 106
Cdd:pfam01576 781 ELEAQIDAANKGREeavkqlkkLQAQMKDLQRELEEARASRDeilaqskesekKLKNLEAELLQLQEDLAASERARRQAQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 107 AALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQN---AMYNASQQLQQIR 183
Cdd:pfam01576 861 QERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTelaAERSTSQKSESAR 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 184 SRLDgtdvgetalRPSQKVLMQAQqallnaEIDQQRKSlegntvlqdtlqKQRDYVTANSARLEhQL--QLLQEA----V 257
Cdd:pfam01576 941 QQLE---------RQNKELKAKLQ------EMEGTVKS------------KFKSSIAALEAKIA-QLeeQLEQESrerqA 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 258 NSKRLTLTEKTAQEAVSPDEAARIQANPLVKQELEIN---QQLSQRLITATENGNQLMQQNIKVKNWLERALQSERNIKE 334
Cdd:pfam01576 993 ANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNsrmKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNR 1072
|
....*....
gi 446099871 335 QIAVLKGSL 343
Cdd:pfam01576 1073 EVSTLKSKL 1081
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
20-285 |
1.36e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 20 AFVFVLLCQNTAFARASSNGDLPTKADLQAQLDSLNKQkdLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAEAP 99
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAE--LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 100 EKMRQATAAL-TALSDVDNDEETRKILSTL----SLRQLETRVaQALDDLQNAQNDLasynsqLVSLQTQPERVQNAMYN 174
Cdd:COG3883 79 AEIEERREELgERARALYRSGGSVSYLDVLlgseSFSDFLDRL-SALSKIADADADL------LEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 175 ASQQLQQIRSrldgtdvgetalrpsQKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQ 254
Cdd:COG3883 152 LEAKLAELEA---------------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
250 260 270
....*....|....*....|....*....|.
gi 446099871 255 EAVNSKRLTLTEKTAQEAVSPDEAARIQANP 285
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
78-189 |
3.04e-08 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 52.97 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 78 LDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDlqnaqnDLASYNSQ 157
Cdd:COG1382 13 LAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEE------KKETLELR 86
|
90 100 110
....*....|....*....|....*....|..
gi 446099871 158 LVSLQTQPERVQNAMYNASQQLQQIRSRLDGT 189
Cdd:COG1382 87 LKTLEKQEERLQKQLEELQEKLQEALSGAGGG 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-266 |
6.08e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLNKQ-KDLSAQDKLVQQDLTDTLATLD----KIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDE 119
Cdd:TIGR02168 687 EELEEKIAELEKAlAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 120 ETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRpS 199
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-E 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 200 QKVLMQAQQALLNAEIDQQRKS-------LEGNTVLQDTLQKQR-----DYVTANSA---------RLEHQLQLLQEAVN 258
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELieeleseLEALLNERASLEEALallrsELEELSEElreleskrsELRRELEELREKLA 925
|
....*...
gi 446099871 259 SKRLTLTE 266
Cdd:TIGR02168 926 QLELRLEG 933
|
|
| PRK11465 |
PRK11465 |
putative mechanosensitive channel protein; Provisional |
823-1028 |
8.55e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 183147 [Multi-domain] Cd Length: 741 Bit Score: 56.33 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 823 ITLWHYNGTEAGAAVVKNVTMGSLLFAIiaSMVAWALirnLPGLLEVLVLSRLNMRQGASYAITTILNY-------IIIA 895
Cdd:PRK11465 449 FDFWNWLQNGAGEKTVDILIRIALILFF--SAVGWTV---LASLIENRLASDIHGRPLPSARTRTLLTLfrnalavIIST 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 896 VGAMTVFGSLGVSWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRIRATTITDFD 975
Cdd:PRK11465 524 ITIMIVLSEIGVNIAPLLAGAGALGLAISFGSQTLVKDIITGVFIQFENGMNTGDLVTIGPLTGTVERMSIRSVGVRQDT 603
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 976 RKEVIIPnkafvterlinWSLTDTTTRLVIRLG-------VAYGSDLEKVRKVLLKAATE 1028
Cdd:PRK11465 604 GAYHIIP-----------WSSITTFANFVRGIGsvvanydVDRHEDADKANQALKDAVAE 652
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
80-452 |
1.08e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 80 KIDRIKEETVQLRQKVAEAPEKM-RQATAALTALSDVDND-EETRKILSTLS--LRQLETRVAQALDDLQNAQNDLASYN 155
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALsEQLRKALFELDKLQEElEQLREELEQAReeLEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 156 SQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVLmQAQQALLNAEIDQQRKSLEgntvlqdTLQKQ 235
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-EAQIAELQSEIAEREEELK-------ELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 236 RDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPLVKQELEINQQLSQRLITATENgnqlmqqn 315
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 316 ikvknwLERALQSERNIKEQIAVLKGSLLLSRILYQQQQTLPSADELENMTNRIADLRLEQFEVNQQRDALFQSDAFVNK 395
Cdd:COG4372 231 ------LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446099871 396 LEEGHTNEVNSEVHDALLQVVDMRRELLDQLNKQLGNQLMMAINLQINQQQLMSVSK 452
Cdd:COG4372 305 AALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSK 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-447 |
1.92e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 44 KADLQAQLDSLNKQKDlSAQDKL-----VQQDLTDTLATLDK-IDRIKEETVQLRQKVAEAPEKMRQATAALTALSD--- 114
Cdd:TIGR02168 339 LAELEEKLEELKEELE-SLEAELeeleaELEELESRLEELEEqLETLRSKVAQLELQIASLNNEIERLEARLERLEDrre 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 115 --VDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVG 192
Cdd:TIGR02168 418 rlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 193 ETALRpsqkvlmQAQQALlnAEIDQQRKSLEGNT-VLQDTLQKQRDYVTANSARLEHQLQLL--------QEAVNSKRLT 263
Cdd:TIGR02168 498 QENLE-------GFSEGV--KALLKNQSGLSGILgVLSELISVDEGYEAAIEAALGGRLQAVvvenlnaaKKAIAFLKQN 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 264 LTEKTAQEAVSPDEAARIQANPL-VKQELEINQQLSQRLITATENGNQLMQ---QNIKVKNWLERALQSERNIKEQ--IA 337
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIQGNDReILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNALELAKKLRPGyrIV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 338 VLKGSLLLSRILYQQQQTLPSADELENmTNRIADLRLeqfEVNQQRDALFQSDAFVNKLEEGHTNevnsevhdaLLQVVD 417
Cdd:TIGR02168 649 TLDGDLVRPGGVITGGSAKTNSSILER-RREIEELEE---KIEELEEKIAELEKALAELRKELEE---------LEEELE 715
|
410 420 430
....*....|....*....|....*....|
gi 446099871 418 MRRELLDQLNKQLGNQLMMAINLQINQQQL 447
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQL 745
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-401 |
3.73e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 86 EETVQLRQKVAEAPEKMRQATAALTAL----SDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSL 161
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLtlrsQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 162 QTQPERvqnamynaSQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNA-------EIDQQRKslEGNTVLQDTLQK 234
Cdd:TIGR00618 253 EEQLKK--------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAahikavtQIEQQAQ--RIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 235 ------QRDYVTANSARLEHQLQLLQeavnskrlTLTEKTAQEAVSPDEAARIQANplVKQELEINQ---QLSQRLITAT 305
Cdd:TIGR00618 323 rakllmKRAAHVKQQSSIEEQRRLLQ--------TLHSQEIHIRDAHEVATSIREI--SCQQHTLTQhihTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 306 ENGNQLMQQNIKVKNWLERA---LQSERNIKEQIAVLKGSLLLSRiLYQQQQTLPSADELENMTNRIADLRLEQFEVNQQ 382
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIdtrTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
330
....*....|....*....
gi 446099871 383 RDALFQSDAFVNKLEEGHT 401
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKA 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-343 |
4.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 79 DKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILS--TLSLRQLETRVA---QALDDLQNAQNDLAS 153
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAeleAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 154 YNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNAEIDQQRKSLEGNTV---LQD 230
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVereLRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 231 TLQKQRDYVTANSARLEHQLQLLQEAVNSKrltLTEKTAQEAVSPDEA-------ARIQANPLVKQELEINQQLsqrlit 303
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLpeylallDRLEEDGLPEYEERFKELL------ 840
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446099871 304 atengNQLMQQNIK-VKNWLERAlqsERNIKEQIAVLKGSL 343
Cdd:COG4913 841 -----NENSIEFVAdLLSKLRRA---IREIKERIDPLNDSL 873
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-498 |
4.21e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLNKQK-DLSAQDKLVQQDLTDTLATLDKID---RIKEETVQLRQKVAEapeKMRQATAALTALSDVDNDEE 120
Cdd:TIGR04523 155 EKLNNKYNDLKKQKeELENELNLLEKEKLNIQKNIDKIKnklLKLELLLSNLKKKIQ---KNKSLESQISELKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 121 TRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLdgtdvgetalrpsQ 200
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI-------------S 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 201 KVLMQAQQAL---LNAEIDQQRKSLEgntvlqdTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDE 277
Cdd:TIGR04523 299 DLNNQKEQDWnkeLKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 278 AARI----QANPLVKQELEINQQLSQRLITATENGNQLMQQNIKVknwleraLQSERNIKE-QIAVLKgslllsrilyqq 352
Cdd:TIGR04523 372 IEKLkkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-------LQQEKELLEkEIERLK------------ 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 353 QQTLPSADELENMTNRIADLRLEQFEVNQQRDALFQsdafvnKLEEgHTNEVNSEVHDallqvvdmrrelLDQLNKQLGN 432
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET------QLKV-LSRSINKIKQN------------LEQKQKELKS 493
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446099871 433 QLMMAINLQINQQQLMSVSKNLK---SILTQQIFWVNSNRPMDWDWIKafpqSLKDEFKSMKITVNWEK 498
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTkkiSSLKEKIEKLESEKKEKESKIS----DLEDELNKDDFELKKEN 558
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-429 |
5.88e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLNKQ-KDLSAQDKLVQQDLtDTLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRK 123
Cdd:COG4717 91 AELQEELEELEEElEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 124 ilstLSLRQLETRVAQALDDLQNA-QNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKV 202
Cdd:COG4717 170 ----AELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 203 LMQAQQALLNAEI---DQQRKSLEGNT-------------VLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLT--L 264
Cdd:COG4717 246 KEARLLLLIAAALlalLGLGGSLLSLIltiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEelL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 265 TEKTAQEAVSPDEA--ARIQANPLVKQELEINQQLSQRLITATENGNQLMQQNIKVKN------WLERAlQSERNIKEQI 336
Cdd:COG4717 326 AALGLPPDLSPEELleLLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDeeelraALEQA-EEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 337 AVLKGSLLLSRILYQQQQTLPSADELEnmtNRIADLRLEQFEVNQQRDALFQSDAfvnKLEEGHTNEVNSEVHDALLQVV 416
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEELE---EELEELEEELEELEEELEELREELA---ELEAELEQLEEDGELAELLQEL 478
|
410
....*....|...
gi 446099871 417 DMRRELLDQLNKQ 429
Cdd:COG4717 479 EELKAELRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
94-433 |
7.29e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 94 KVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASY--------NSQLVSLQTQP 165
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLteklseaeDMLACEQHALL 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 166 ERVQNAM--YNASQQLQQIRSRLDgtdVGETALRPSQKVLMQAQQALLNAEIDQQRK-SLEGNTVLQDTLQKQRDYVTAN 242
Cdd:TIGR00618 619 RKLQPEQdlQDVRLHLQQCSQELA---LKLTALHALQLTLTQERVREHALSIRVLPKeLLASRQLALQKMQSEKEQLTYW 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 243 SARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPLVKQEL----------------EINQQLSQRLITATE 306
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkelmhqartvlkartEAHFNNNEEVTAALQ 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 307 NGNQLMQ--QNIKVKNWLERALQS-----ERNIKEQIAVLKGSLLLSRILYQQ--QQTLPSADELENMTNRIADLRLEQF 377
Cdd:TIGR00618 776 TGAELSHlaAEIQFFNRLREEDTHllktlEAEIGQEIPSDEDILNLQCETLVQeeEQFLSRLEEKSATLGEITHQLLKYE 855
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446099871 378 EVNQQRDALFQSDAFVNKLEE---GHTNEVNSEVHDALLQVVdmrRELLDQLNKQLGNQ 433
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDklnGINQIKIQFDGDALIKFL---HEITLYANVRLANQ 911
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-431 |
1.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 205 QAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQE-----AVNSKRLTLTEKTAQEAVSPDEAA 279
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrelEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 280 RIQANPLVKQELEINQQLSQRLITATENGNQLMQQNIKVKNWLERALQSERNIKEQIAVLKgslllSRILYQQQQTLPSA 359
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-----AQLEELEEAEEALL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446099871 360 DELENMTNRIADLRLEQFEVNQQRDALFQSDAFVNKLEEGHTNEVNS--EVHDALLQVVDMRRELLDQLNKQLG 431
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAllELLAELLEEAALLEAALAELLEELA 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
45-429 |
1.52e-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: 49.40 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLNKQkdLSAQDKlvqqDLTDTLAtldkidRIKEETVQlrqkVAEAPEKMRQATAALTAL-SDVDND----- 118
Cdd:pfam01576 225 AELQAQIAELRAQ--LAKKEE----ELQAALA------RLEEETAQ----KNNALKKIRELEAQISELqEDLESEraarn 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 119 --EETRKILSTlSLRQLETRVAQALDDlQNAQNDLASYNSQLVSL---------QTQPERVQNAMYNASQQLQQIRSRLD 187
Cdd:pfam01576 289 kaEKQRRDLGE-ELEALKTELEDTLDT-TAAQQELRSKREQEVTElkkaleeetRSHEAQLQEMRQKHTQALEELTEQLE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 188 GTDVGETALRPSQKVL------MQAQQALLNA---EIDQQRKSLEGNtvLQDTLQKQRDYVTANSARLE--HQLQLLQEA 256
Cdd:pfam01576 367 QAKRNKANLEKAKQALesenaeLQAELRTLQQakqDSEHKRKKLEGQ--LQELQARLSESERQRAELAEklSKLQSELES 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 257 VNSkrlTLTEKTAQEAVSPDEAARIQANPLVKQEL---EINQQL--SQRLITATENGNQLMQQnikvknwLERALQSERN 331
Cdd:pfam01576 445 VSS---LLNEAEGKNIKLSKDVSSLESQLQDTQELlqeETRQKLnlSTRLRQLEDERNSLQEQ-------LEEEEEAKRN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 332 IKEQIAVLKGSLLLSRilYQQQQTLPSADELENMTNRIadlrleQFEVNQQRDALFQSDAFVNKLEEGHtNEVNSEVHDA 411
Cdd:pfam01576 515 VERQLSTLQAQLSDMK--KKLEEDAGTLEALEEGKKRL------QRELEALTQQLEEKAAAYDKLEKTK-NRLQQELDDL 585
|
410
....*....|....*...
gi 446099871 412 LLQvVDMRRELLDQLNKQ 429
Cdd:pfam01576 586 LVD-LDHQRQLVSNLEKK 602
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-258 |
1.67e-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: 49.28 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 44 KADLQAQLDSLNKQKDLSAQDKLVQQDLTDTLAtlDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALsdvdnDEEtrk 123
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRLEEL-----EEQ--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 124 ilstlsLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQ-----TQPERVQNAMYNASQQLQQIRSRLDGTD-------- 190
Cdd:TIGR02168 381 ------LETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerLQQEIEELLKKLEEAELKELQAELEELEeeleelqe 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446099871 191 ---VGETALRPSQKVLMQAQQALLNAEIDQQRKSLEgNTVLQDTLQKQRDY------VTANSARLEHQLQLLQEAVN 258
Cdd:TIGR02168 455 eleRLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFsegvkaLLKNQSGLSGILGVLSELIS 530
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-292 |
2.83e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLNKQKDLSAQDKlvqQDLTDTLA----TLDKIDRIKEETVQLRQKVAEA-------PEKMRQATAALTALS 113
Cdd:PRK02224 216 AELDEEIERYEEQREQARETR---DEADEVLEeheeRREELETLEAEIEDLRETIAETerereelAEEVRDLRERLEELE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 114 DVDND-----EETRKILSTLSLRQ--LETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRL 186
Cdd:PRK02224 293 EERDDllaeaGLDDADAEAVEARReeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 187 DGTdvgETALRPSqkvlmQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLqllqeavnsKRLTLTE 266
Cdd:PRK02224 373 EEA---REAVEDR-----REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE---------AELEATL 435
|
250 260
....*....|....*....|....*....
gi 446099871 267 KTAQEAVspDEAARIQAN---PLVKQELE 292
Cdd:PRK02224 436 RTARERV--EEAEALLEAgkcPECGQPVE 462
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
40-296 |
3.57e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 40 DLPTKADLQaqldslNKQKDLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAEAPEKMRQataaltalsdvDNDE 119
Cdd:pfam15709 318 EDPSKALLE------KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE-----------ELEL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 120 ETRKILSTLSLRQletrvaQALDDLQNAQNDlaSYNSQLVSLQTQPERvqnamynASQQLQQIRSRLdgtdvgetalrps 199
Cdd:pfam15709 381 EQQRRFEEIRLRK------QRLEEERQRQEE--EERKQRLQLQAAQER-------ARQQQEEFRRKL------------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 200 QKVLMQAQQ-ALLNAEIDQQR-KSLEgntvLQDTLQKQRDYVTANSARLEHQLQlLQEAVNSKRLTLTEKTAQEavspDE 277
Cdd:pfam15709 433 QELQRKKQQeEAERAEAEKQRqKELE----MQLAEEQKRLMEMAEEERLEYQRQ-KQEAEEKARLEAEERRQKE----EE 503
|
250
....*....|....*....
gi 446099871 278 AARIQANPLVKQELEINQQ 296
Cdd:pfam15709 504 AARLALEEAMKQAQEQARQ 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-434 |
3.64e-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: 48.13 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 119 EETRKIL------STLSLRQLET--RVAQALDDLQNAQNDLASYNSQLVSLQTQPERVqnamynasQQLQQIRSRLDgtd 190
Cdd:TIGR02168 155 EERRAIFeeaagiSKYKERRKETerKLERTRENLDRLEDILNELERQLKSLERQAEKA--------ERYKELKAELR--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 191 vgetalrpsqkvlmQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKrltltEKTAQ 270
Cdd:TIGR02168 224 --------------ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-----EEEIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 271 EAVSPDEAARIQANPLVKQELEINQQLSQRLITATENGNQLMQqnikVKNWLERALQSERNIKEQIAVLKGSLLLsrily 350
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----LESKLDELAEELAELEEKLEELKEELES----- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 351 QQQQTLPSADELENMTNRIADLRlEQFEvnQQRDALFQsdafVNKLEEGHTNEVnsEVHDALLQVVDMRRELLDQLNKQL 430
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELE-EQLE--TLRSKVAQ----LELQIASLNNEI--ERLEARLERLEDRRERLQQEIEEL 426
|
....
gi 446099871 431 GNQL 434
Cdd:TIGR02168 427 LKKL 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
205-454 |
5.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 205 QAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVspdeaariqan 284
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 285 pLVKQELEINQQLSQRLITAtengnQLMQQNIKVKNWL--ERALQSERNIKeqiavlkgslLLSRILYQQQQtlpsadel 362
Cdd:COG4942 95 -LRAELEAQKEELAELLRAL-----YRLGRQPPLALLLspEDFLDAVRRLQ----------YLKYLAPARRE-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 363 enmtnRIADLRLEQFEVNQQRDALFQSDAFVNKLEEGHTNEvnsevHDALLQVVDMRRELLDQLNKQLGNQLMMAINLQI 442
Cdd:COG4942 151 -----QAEELRADLAELAALRAELEAERAELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|..
gi 446099871 443 NQQQLMSVSKNL 454
Cdd:COG4942 221 EAEELEALIARL 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
132-401 |
1.30e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 132 QLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLdgtdvgetalrpsqkvlmqaqQALL 211
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL---------------------RRLF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 212 NAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTaQEAVSPDEAARIQANPLVKQEL 291
Cdd:pfam12128 660 DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK-QAYWQVVEGALDAQLALLKAAI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 292 EINQQLSQRLITA--TENGNQLMQQNIKVKNWLERALQSERNIK--EQIAVLKGSLLLSRILYQQQ-------------Q 354
Cdd:pfam12128 739 AARRSGAKAELKAleTWYKRDLASLGVDPDVIAKLKREIRTLERkiERIAVRRQEVLRYFDWYQETwlqrrprlatqlsN 818
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446099871 355 TLPSADELE-NMTNRIADLRLEQFEVNQQRDAlfqSDAFVNKLEEGHT 401
Cdd:pfam12128 819 IERAISELQqQLARLIADTKLRRAKLEMERKA---SEKQQVRLSENLR 863
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
81-256 |
1.44e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 81 IDRIKEETVQLRQKVAEAPEKMRQATAaltALSDVDNDEETRKILSTLSlrQLETRVAQALDDLQNAQNDLASYNSQLVS 160
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLS--ELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 161 -LQTQPERVQNAMYNA-SQQLQQIRSRLDGTDVGETALRPSQKVLmQAQQALLNAEIDQQ-RKSLEGNTVLQDTLQKQRD 237
Cdd:COG3206 252 gPDALPELLQSPVIQQlRAQLAELEAELAELSARYTPNHPDVIAL-RAQIAALRAQLQQEaQRILASLEAELEALQAREA 330
|
170
....*....|....*....
gi 446099871 238 YVTANSARLEHQLQLLQEA 256
Cdd:COG3206 331 SLQAQLAQLEARLAELPEL 349
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
85-376 |
1.53e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.90 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 85 KEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLvslqtq 164
Cdd:pfam07111 330 RDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQL------ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 165 pERVQNAMYNASQQLQQIRSRLDgtdvgETALR-PS---------QKV-----LMQAQQALLNAEIDQQRKSLEGNTVLQ 229
Cdd:pfam07111 404 -KFVVNAMSSTQIWLETTMTRVE-----QAVARiPSlsnrlsyavRKVhtikgLMARKVALAQLRQESCPPPPPAPPVDA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 230 DtLQKQRDYVTANSARLEHQLQLlqeavnSKRLTLTEktAQEAVSPDEAARIQANplvkqelEINQQLSQRLITATENGN 309
Cdd:pfam07111 478 D-LSLELEQLREERNRLDAELQL------SAHLIQQE--VGRAREQGEAERQQLS-------EVAQQLEQELQRAQESLA 541
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446099871 310 QLMQQnikvknwLERALQSERNIKEQIAVLKGSLLLSRILYQQ--QQTLPSA-----DELENMTNRIADLRLEQ 376
Cdd:pfam07111 542 SVGQQ-------LEVARQGQQESTEEAASLRQELTQQQEIYGQalQEKVAEVetrlrEQLSDTKRRLNEARREQ 608
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-256 |
1.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 47 LQAQLDSLNKQKDlSAQDKLV----QQDLTD----TLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDND 118
Cdd:COG3206 180 LEEQLPELRKELE-EAEAALEefrqKNGLVDlseeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 119 eetrkILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMynaSQQLQQIRSRLDgtdvgetalrp 198
Cdd:COG3206 259 -----LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLE----------- 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446099871 199 SQKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQK-QRDYvTANSARLEHQLQLLQEA 256
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREV-EVARELYESLLQRLEEA 377
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
129-223 |
2.35e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.72 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 129 SLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGT-----DVGETALRPSQKVL 203
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaqnnlATAQAALANAEARL 334
|
90 100
....*....|....*....|..
gi 446099871 204 MQAQQAL--LNAEIDQQRKSLE 223
Cdd:TIGR04320 335 AKAKEALanLNADLAKKQAALD 356
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
44-224 |
2.85e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 44 KADLQAQLDSLnkQKDLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTAlsdvDNDEETRK 123
Cdd:pfam00038 119 RVDLEAKIESL--KEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAA----KNREEAEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 124 ILSTlSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQN-------------AMYNAsqQLQQIRSRLDGTd 190
Cdd:pfam00038 193 WYQS-KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKqkaslerqlaeteERYEL--QLADYQELISEL- 268
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446099871 191 vgETALRpSQKVLMQAQ----QALLN------AEIDQQRKSLEG 224
Cdd:pfam00038 269 --EAELQ-ETRQEMARQlreyQELLNvklaldIEIATYRKLLEG 309
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-340 |
3.51e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 124 ILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVL 203
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 204 mQAQQALLNAEIDQQRKSLEGntvLQDTLQK--QRDYVT-----ANSARLEHQLQLLQeAVNSKRLTLTEKTAQeavspd 276
Cdd:COG4942 89 -EKEIAELRAELEAQKEELAE---LLRALYRlgRQPPLAlllspEDFLDAVRRLQYLK-YLAPARREQAEELRA------ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446099871 277 EAARIQAnplVKQELEINQQLSQRLITATENGNQLMQQNIKVKNWLERALQSERN-IKEQIAVLK 340
Cdd:COG4942 158 DLAELAA---LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAeLAAELAELQ 219
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
13-272 |
4.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 13 FVFSAFIAFVFVLLCQNTAFARASSngDLPTKADLQAQLDSLNKQKDLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLR 92
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEA--EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 93 QKVAEAP-EKMRQATAALTALSDVDNDEETRKILSTLS-LRQLETRVAQALDDLQNAQNDLASYnsqlvSLQTQPERVQN 170
Cdd:COG4717 358 ELEEELQlEELEQEIAALLAEAGVEDEEELRAALEQAEeYQELKEELEELEEQLEELLGELEEL-----LEALDEEELEE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 171 AMYNASQQLQQIRSRLDgtdvgetalrpsqkvlmQAQQALlnAEIDQQRKSLEGNTVLQDTLQKQrdyvtansARLEHQL 250
Cdd:COG4717 433 ELEELEEELEELEEELE-----------------ELREEL--AELEAELEQLEEDGELAELLQEL--------EELKAEL 485
|
250 260
....*....|....*....|....
gi 446099871 251 QLLQEAVNSKRLTLT--EKTAQEA 272
Cdd:COG4717 486 RELAEEWAALKLALEllEEAREEY 509
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2-337 |
4.75e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 2 TMFQYYKRSRHFVFSAFIAFVF---VLLCQNTAFArassngdlptkADLQAQLDSLnkQKDLSAQDKLVQQdltdtlatl 78
Cdd:PRK11637 8 TMTRAVKPRRFAIRPILYASVLsagVLLCAFSAHA-----------SDNRDQLKSI--QQDIAAKEKSVRQ--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 79 dkidrikeetvQLRQKvaeapekmrqataalTALSDvdndeetrkilstlSLRQLETRVAQALDDLQNAQNDLASYNSQL 158
Cdd:PRK11637 66 -----------QQQQR---------------ASLLA--------------QLKKQEEAISQASRKLRETQNTLNQLNKQI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 159 VSLQTQPERVQnamynaSQQLQQIRS---RLDgtdvgeTALRPSQKvlmQAQQALLNAEIDQQRKSLEG-----NTVLQD 230
Cdd:PRK11637 106 DELNASIAKLE------QQQAAQERLlaaQLD------AAFRQGEH---TGLQLILSGEESQRGERILAyfgylNQARQE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 231 T---LQKQRDYVTAnsarlehQLQLLQEAVNSKRLTLTEKTAQeavspdeaariqanplvKQELEINQQLSQRLITATEN 307
Cdd:PRK11637 171 TiaeLKQTREELAA-------QKAELEEKQSQQKTLLYEQQAQ-----------------QQKLEQARNERKKTLTGLES 226
|
330 340 350
....*....|....*....|....*....|
gi 446099871 308 GNQLMQQNikvknwLERALQSERNIKEQIA 337
Cdd:PRK11637 227 SLQKDQQQ------LSELRANESRLRDSIA 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
134-337 |
4.85e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 134 ETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTdvgetalrpsqkvlmQAQQALLNA 213
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---------------QAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 214 EIDQQRKSLE---------GNTV-----------LQDTLQKQ--RDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQE 271
Cdd:COG3883 80 EIEERREELGeraralyrsGGSVsyldvllgsesFSDFLDRLsaLSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446099871 272 AVSPDEAARIQANplVKQELEINQQLSQRLITATENGNQLMQQNIKVKNWLERALQSERNIKEQIA 337
Cdd:COG3883 160 EALKAELEAAKAE--LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
130-284 |
5.18e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.69 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 130 LRQLETRVAQALDDLQNAQNDLASY--NSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDgtdVGETALRPS--QKVLMQ 205
Cdd:COG3524 179 VRFAEEEVERAEERLRDAREALLAFrnRNGILDPEATAEALLQLIATLEGQLAELEAELA---ALRSYLSPNspQVRQLR 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446099871 206 AQQALLNAEIDQQRKSLegntvlqdTLQKQRDYVTANSARLEhQLQLlqeavnskRLTLTEKTAQEAVSPDEAARIQAN 284
Cdd:COG3524 256 RRIAALEKQIAAERARL--------TGASGGDSLASLLAEYE-RLEL--------EREFAEKAYTSALAALEQARIEAA 317
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
45-392 |
8.64e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLnkQKDLSAQDKLVQQDLTDTLatlDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEEtrki 124
Cdd:COG5185 246 EDLAQTSDKL--EKLVEQNTDLRLEKLGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE---- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 125 lstlslrqletrVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMynaSQQLQQIRSRLDGTdVGETALRPSQKVLM 204
Cdd:COG5185 317 ------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESL---TENLEAIKEEIENI-VGEVELSKSSEELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 205 QAQQALLNA--EIDQQRKSLEGNTvlQDTLQKQRDYVTANsarlEHQLQLLQEAVNSKrltlTEKTAQEAVSPDEAARIq 282
Cdd:COG5185 381 SFKDTIESTkeSLDEIPQNQRGYA--QEILATLEDTLKAA----DRQIEELQRQIEQA----TSSNEEVSKLLNELISE- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 283 anpLVKQELEINQQLSQRLITATENGNQLMQQNIKVKNW-LERALQSERNIKEQIAVLKGSllLSRILYQQQQTLPSADE 361
Cdd:COG5185 450 ---LNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEeLTQIESRVSTLKATLEKLRAK--LERQLEGVRSKLDQVAE 524
|
330 340 350
....*....|....*....|....*....|.
gi 446099871 362 LENMTNRIADLRLEQFEVNQQRDALFQSDAF 392
Cdd:COG5185 525 SLKDFMRARGYAHILALENLIPASELIQASN 555
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
41-314 |
1.08e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 41 LPTKADLQAQLDSLNKQ-KDLSAQDKLVQQDLTDTLATLD-KIDRIKEETVQLRQKVAEAPEKMRQATAaLTALSDVDNd 118
Cdd:PRK10246 615 LSQRHELQGQIAAHNQQiIQYQQQIEQRQQQLLTALAGYAlTLPQEDEEASWLATRQQEAQSWQQRQNE-LTALQNRIQ- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 119 eETRKILSTLSlrQLETRVAQA----LDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLqqirsrldgtdvgET 194
Cdd:PRK10246 693 -QLTPLLETLP--QSDDLPHSEetvaLDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF-------------DT 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 195 ALRPSqkvLMQAQQALLNAEIDQQ-RKSLEGntvLQDTLQKQRDYVTANSARLEHQLQL-LQEAVNSKRLTLTEKTAQEA 272
Cdd:PRK10246 757 ALQAS---VFDDQQAFLAALLDEEtLTQLEQ---LKQNLENQRQQAQTLVTQTAQALAQhQQHRPDGLDLTVTVEQIQQE 830
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446099871 273 VSpDEAARIQANplVKQELEINQQLSQRlitaTENGNQ---LMQQ 314
Cdd:PRK10246 831 LA-QLAQQLREN--TTRQGEIRQQLKQD----ADNRQQqqaLMQQ 868
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
46-245 |
1.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 46 DLQAQLDSLNKQKDLSAQDKLVQQDLTDTLATLDKIDRI----KEETVQLRQKVAEAPEKMRQATAALTALSDVDND--- 118
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRrah 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 119 ---EETRKILSTLS---------LRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRL 186
Cdd:PRK04863 971 fsyEDAAEMLAKNSdlneklrqrLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 187 D---------GTDVGETALRP--SQKVLMQAQQALLNAEIDQQRKSLegnTVLQDTLQKQRDYVTANSAR 245
Cdd:PRK04863 1051 DsgaeeraraRRDELHARLSAnrSRRNQLEKQLTFCEAEMDNLTKKL---RKLERDYHEMREQVVNAKAG 1117
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
44-186 |
2.93e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 44 KADLQAQLDSLNKQkdLSAQDKLVQQdLTDTLATL-DKID--RIKEETVQLRQKVAEAPEKMRQATAALTALSDVDndee 120
Cdd:COG1842 93 KAELEAQAEALEAQ--LAQLEEQVEK-LKEALRQLeSKLEelKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATS---- 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446099871 121 trkilstlSLRQLETRV------AQALDDLqNAQNDLAsynSQLVSLQTQPErvqnamynASQQLQQIRSRL 186
Cdd:COG1842 166 --------ALERMEEKIeemearAEAAAEL-AAGDSLD---DELAELEADSE--------VEDELAALKAKM 217
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
60-343 |
5.05e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 60 LSAQDKLVQQDLTDTLATLDKIDRIKEETvQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQ 139
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQ-QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 140 ALDDLQNAQndlaSYNSQLVSLQTQPERVQNAMYNASQQ---LQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNAEID 216
Cdd:TIGR00606 876 IGTNLQRRQ----QFEEQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 217 QQ---RKSLEgnTVLQDTLQKQRDYVTANSARLEHQL-------QLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPL 286
Cdd:TIGR00606 952 NIhgyMKDIE--NKIQDGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE 1029
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446099871 287 VKQ-ELEINQ---QLSQRLITATENGNQLMQQNIK-VKNWLERALQSERNIKEQIAVLKGSL 343
Cdd:TIGR00606 1030 LKEvEEELKQhlkEMGQMQVLQMKQEHQKLEENIDlIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-259 |
5.32e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 45 ADLQAQLDSLNKQKDlSAQDKLVQQDltDTLATLD-KIDRIKEETVQLRQKVAEAPEKMRQ-----ATAALTALSDVDND 118
Cdd:TIGR02168 757 TELEAEIEELEERLE-EAEEELAEAE--AEIEELEaQIEQLKEELKALREALDELRAELTLlneeaANLRERLESLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 119 EETRKILSTLS--LRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVG---- 192
Cdd:TIGR02168 834 AATERRLEDLEeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrsel 913
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446099871 193 ETALRPSQKVLMQAQQAL--LNAEIDQQRKSL--EGNTVLQDTLQKQRDyVTANSARLEHQLQLLQEAVNS 259
Cdd:TIGR02168 914 RRELEELREKLAQLELRLegLEVRIDNLQERLseEYSLTLEEAEALENK-IEDDEEEARRRLKRLENKIKE 983
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
56-306 |
7.77e-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: 40.26 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 56 KQKDLSA-QDKLVQQDLTDTLATLDKIDRIKE--ETVQ-LRQKVAEAP---EKMRQATAALTALSdvdNDEETRKILSTL 128
Cdd:pfam07888 102 KYKELSAsSEELSEEKDALLAQRAAHEARIREleEDIKtLTQRVLEREtelERMKERAKKAGAQR---KEEEAERKQLQA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 129 SLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQ----------QLQQIRSRLDGTDVGETALRP 198
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleELRSLQERLNASERKVEGLGE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 199 -----------SQKVLMQA--QQALLNAEIDQQRKSL-EGN-------TVLQDTLQKQRDYVTANSARLEHQLQLLQEA- 256
Cdd:pfam07888 259 elssmaaqrdrTQAELHQArlQAAQLTLQLADASLALrEGRarwaqerETLQQSAEADKDRIEKLSAELQRLEERLQEEr 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446099871 257 --------------------VNSKRLTLTEKTAQEAVSPDEAARIQANplvKQEL-EINQQLSQRLITATE 306
Cdd:pfam07888 339 mereklevelgrekdcnrvqLSESRRELQELKASLRVAQKEKEQLQAE---KQELlEYIRQLEQRLETVAD 406
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
32-316 |
8.40e-03 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 40.05 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 32 FARASSNGDLPTKADLQAQLDSLNKQKDLSAQ------DKLVQQDLtdtLATLDKIDRIKEETVQLRQKVAEApekmrqa 105
Cdd:TIGR01844 83 GGSTWNAVRAAEAAALAARETLRATAQDLILRtaeaymEVLRAQEI---LALAEANLAALKEQLDLARARFDV------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 106 taALTALSDVdndeetrkilstlslRQLETRVAQALDDLQNAQNDLASYNSQLVSL----QTQPERVQNAMYNASQQLQQ 181
Cdd:TIGR01844 153 --GLGTRTDV---------------LQAEARYASARAQLIQAQNNLDDAKAQLRRLvgqpELAPLAVPSFPAELPEPLDQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 182 IRsrldgtdvgETALRPSQKVLmqAQQALLNA---EIDQQRK------SLEGNTVLQDTLQKQR--DYVTANSARL---- 246
Cdd:TIGR01844 216 LL---------EIAEASNPLLL--AAQAAVDAaryQVEQARAghlptlSLTASTGNSDTSSGGSgnSDSDTYSVGLnvsi 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 247 ---------------EHQLQLLQEAVNSKRLTLTEKTaQEAVSPDEAARIQanplvKQELEINQQLSQRLITATENGNQL 311
Cdd:TIGR01844 285 plyqggatsaqvrqaAHQLNQSRSTLESQKRTVRQQV-RNAWSNLNAAAAS-----VQAYEQQVASAQKALDAYRQEYQV 358
|
....*
gi 446099871 312 MQQNI 316
Cdd:TIGR01844 359 GTRTL 363
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
80-344 |
9.46e-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: 39.88 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 80 KIDRIKEETVQLRQKVAEAPEKMRQATAALTALSdvdndeETRKILstlsLRQLETRVAQalddLQNAQNDLASYNSQLV 159
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELS------EEKDAL----LAQRAAHEAR----IRELEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 160 SLQTQPERVQNAMYNASQQLQQIrsrldgtdvgETALRPSQKVLMQAQQAL--LNAEIDQQRKSLEGN-----------T 226
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEE----------EAERKQLQAKLQQTEEELrsLSKEFQELRNSLAQRdtqvlqlqdtiT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 227 VLQDTLQKQRDYVTANSARLEhQLQLLQEavnskRLTLTEKTAqeavspdEAARIQANPLVKQELEINQQLSQRLITATE 306
Cdd:pfam07888 217 TLTQKLTTAHRKEAENEALLE-ELRSLQE-----RLNASERKV-------EGLGEELSSMAAQRDRTQAELHQARLQAAQ 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446099871 307 NGNQLMQQNIKVK----NWL-ERA--LQSERNIKEQIAVLKGSLL 344
Cdd:pfam07888 284 LTLQLADASLALRegraRWAqEREtlQQSAEADKDRIEKLSAELQ 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
54-300 |
9.92e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 54 LNKQKDLSAQDKLVQQDLTDTLATL-DKIDRIKEETVQLRQKVAEAPEKMRQATAALTALS----DVDNDEETRKILSTL 128
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEFqAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiagEVSRSEAWDVARELL 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 129 slRQLETRVAQA--LDDLQNAQNDLA-SYNSQ--LVSLQTQPERVQNAMYNASQQLQQIRSRL-----DGTDVGETALrp 198
Cdd:PRK04863 503 --RRLREQRHLAeqLQQLRMRLSELEqRLRQQqrAERLLAEFCKRLGKNLDDEDELEQLQEELearleSLSESVSEAR-- 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446099871 199 SQKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYV---TANSARLEHQLQLLQEavnskrltlTEKTAQEAVSp 275
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSgeeFEDSQDVTEYMQQLLE---------RERELTVERD- 648
|
250 260
....*....|....*....|....*
gi 446099871 276 DEAARIQAnplVKQELEinqQLSQR 300
Cdd:PRK04863 649 ELAARKQA---LDEEIE---RLSQP 667
|
|
| |
