|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-1167 |
4.06e-159 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 505.28 E-value: 4.06e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 82 TFDNSDKKqsplGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463 80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLL 241
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGK 561
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 562 KLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPeLQKAMEFVFGTTFVCDNMDNAKKVAF 641
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTEL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 642 DKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEM 721
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 722 KTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCA 801
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 802 KTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEV 881
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 882 ITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNN 961
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 962 PKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDF 1041
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1042 GSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 110347420 1122 SHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-1144 |
2.23e-127 |
|
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: 420.62 E-value: 2.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNG---QAGITKASV 79
Cdd:TIGR02168 2 LKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 80 SITFDNSDKkqsPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPP 159
Cdd:TIGR02168 80 ELVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQF 239
Cdd:TIGR02168 156 ERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 240 LLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI--------------------LRSL 299
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqkqilrerLANL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 300 EDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQH 379
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 380 FNAVSAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEvkkmdsgyrKDQEALEAVKRLKE 459
Cdd:TIGR02168 395 IASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------ELQEELERLEEALE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 460 KLEAEMKKlnyeenKEESLLEKRRQLSRDIGRLKETyEALLARFPNLRFAYKDPEKN-WNRNCVKGLVASLISVkDTSAT 538
Cdd:TIGR02168 465 ELREELEE------AEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNqSGLSGILGVLSELISV-DEGYE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 539 TALELVAGERLYNVVVDTEVTGKK---LLERGELKRRyTIIPLNKISARCIAPETLRVAQNlvGPDNVHVALSLVEYKPE 615
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPK 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 616 LQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENEL 695
Cdd:TIGR02168 614 LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 696 RALEEELAGLKntaekyrqlKQQWEMKTEEADLLQTKLQQS-SYHKQQEELDALKKTIEESEETLKNT-KEIQRKAEEKY 773
Cdd:TIGR02168 694 AELEKALAELR---------KELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLEERIAQLsKELTELEAEIE 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 774 EVLENKMKNAE--AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYE 851
Cdd:TIGR02168 765 ELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 852 SQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV 931
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 932 SKMLKDYDWINAER-HLFGQPNSAY-----------DFKTNNPKEAGQRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYN 999
Cdd:TIGR02168 925 AQLELRLEGLEVRIdNLQERLSEEYsltleeaealeNKIEDDEEEARRRLKRLENKIKELG-PVNLAAIEEYEELKERYD 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1000 DLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTW 1078
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaGIEIFAQPPGKK 1083
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 1079 KENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1144
Cdd:TIGR02168 1084 NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1168 |
1.58e-121 |
|
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: 404.06 E-value: 1.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK-NGQAGITKASVS 80
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNgKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 81 ITFDNSDKKqsplgfeVHDEITVTRQVVIGGRNK---YLINGVNANNTRVQDLFCSVGLNVNNPHFlIMQGRITKVLNMK 157
Cdd:TIGR02169 80 VTFKNDDGK-------FPDELEVVRRLKVTDDGKysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 318 DLKKKNL-------ACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSN 390
Cdd:TIGR02169 311 AEKERELedaeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 391 EDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMK 466
Cdd:TIGR02169 391 REKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewkLEQLAADLSKYEQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 467 KLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKdpEKNWNRNCVKGLVASLISVKDTSATtALELVAG 546
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE--VLKASIQGVHGTVAQLGSVGERYAT-AIEVAAG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 547 ERLYNVVVDTEVTGKKLLERgeLKR----RYTIIPLNKISARCIAPETLRVaqnlvgPDNVHVALSLVEYKPELQKAMEF 622
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIEL--LKRrkagRATFLPLNKMRDERRDLSILSE------DGVIGFAVDLVEFDPKYEPAFKY 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 623 VFGTTFVCDNMDNAKkvafdkRIM--TRTVTLGGDVFDPHGTLSGGARSQAASILTKFQ---ELKDVQDELRIKENELRA 697
Cdd:TIGR02169 619 VFGDTLVVEDIEAAR------RLMgkYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaELQRLRERLEGLKRELSS 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 698 LEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLE 777
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 778 ---NKMKNAEAERERELKDAQKKldcaktKADASSKKMKEKQQEVEAITLELE-ELKREHTSyKQQLEavnEAIKSYESQ 853
Cdd:TIGR02169 772 edlHKLEEALNDLEARLSHSRIP------EIQAELSKLEEEVSRIEARLREIEqKLNRLTLE-KEYLE---KEIQELQEQ 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 854 IEvmaaEVAKNKESVNKAQEEVTKQKEVItaqDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSK 933
Cdd:TIGR02169 842 RI----DLKEQIKSIEKEIENLNGKKEEL---EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 934 MLKDYDWINAERHLFGQPNSAYDFKTNNPKE---AGQRLQKLQEMKEKLGRN------VNMRAMNVLTEAEERYNDLMKK 1004
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEiralepVNMLAIQEYEEVLKRLDELKEK 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1005 KRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGanamlappEGQTVLD--------GLEFKVALGN 1076
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGG--------TGELILEnpddpfagGLELSAKPKG 1066
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1077 TWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA-NV 1155
Cdd:TIGR02169 1067 KPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYAdRA 1146
|
1210
....*....|...
gi 110347420 1156 LFKTKFVDGVSTV 1168
Cdd:TIGR02169 1147 IGVTMRRNGESQV 1159
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-172 |
3.32e-103 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 326.18 E-value: 3.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 81 ITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:cd03273 81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
|
170
....*....|..
gi 110347420 161 ILSMIEEAAGTR 172
Cdd:cd03273 161 KESLTELSGGQR 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1157 |
6.16e-88 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 306.86 E-value: 6.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNGQAG---ITKA 77
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 78 SVSITFDNSDKKqSPLGFevhDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMK 157
Cdd:COG1196 79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:COG1196 154 PEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGE-LERQLEPLERQAEKAERYRELKEELKELEAELLLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 318 DLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgAEAT 397
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-ELLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN----YEEN 473
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 474 KEESLLEKRRQLSRDIGRLKETYEALL---ARFPNLRFAYKDPEKNWNRNCVKGLVASLISVkDTSATTALELVAGERLY 550
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 551 NVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTF 628
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 629 VCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASiltkfqelkdvqdELRIKENELRALEEELAglknt 708
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------ALLEAEAELEELAERLA----- 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 709 aekyrqlkqqwemkteeadllqtklqqssyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERE 788
Cdd:COG1196 690 -------------------------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 789 RELKDAQKKLDcaktkadasskkmkEKQQEVEAITLELEELKRehtsykqqleavneaiksyesqievmaaevaknkesv 868
Cdd:COG1196 739 EELLEEEELLE--------------EEALEELPEPPDLEELER------------------------------------- 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 869 nkaqeevtkqkevitaqdtvikakyaevakhkeqnndsqlkikeldhniskhkreaedgaakvskmlkdydwinaerhlf 948
Cdd:COG1196 --------------------------------------------------------------------------------
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 949 gqpnsaydfktnnpkeagqRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQ 1028
Cdd:COG1196 768 -------------------ELERLEREIEALG-PVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1029 ALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPA 1107
Cdd:COG1196 828 RFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPS 907
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 110347420 1108 PIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:COG1196 908 PFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1074-1168 |
2.18e-63 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 216.01 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1074 LGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA 1153
Cdd:cd03273 156 MGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNA 235
|
90
....*....|....*
gi 110347420 1154 NVLFKTKFVDGVSTV 1168
Cdd:cd03273 236 NVLFRTRFVDGTSTV 250
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
522-639 |
2.16e-33 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 125.04 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 522 VKGLVASLISVKDtSATTALELVAGERLYNVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARCIAPETLRvAQNLVG 599
Cdd:smart00968 3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 110347420 600 PDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKV 639
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1085-1167 |
5.01e-31 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 120.49 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTKFVD 1163
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 110347420 1164 GVST 1167
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-164 |
7.86e-29 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 116.21 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVYKNGQAGITKASVSIT 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPSVMSAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 83 FDNSDKKqsplgFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEIL 162
Cdd:cd03272 80 FDNSDNR-----FPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQ 154
|
..
gi 110347420 163 SM 164
Cdd:cd03272 155 EM 156
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-86 |
4.15e-26 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 106.24 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQdLVYKNGQAGITKASVSIT 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLF-LAGGGVKAGINSASVEIT 78
|
....
gi 110347420 83 FDNS 86
Cdd:cd03239 79 FDKS 82
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-89 |
4.57e-25 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 103.70 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK--NGQAGITKASVS 80
Cdd:cd03278 1 LKKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAgsETRKPANFAEVT 79
|
....*....
gi 110347420 81 ITFDNSDKK 89
Cdd:cd03278 80 LTFDNSDGR 88
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1081-1157 |
1.75e-23 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 99.46 E-value: 1.75e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:cd03278 110 RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
522-640 |
4.01e-23 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 95.41 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 522 VKGLVASLISVKDTsATTALELVAGERLYNVVVDTEVTGKKLLErgELKR----RYTIIPLNKISARCIAPETLRVAqnl 597
Cdd:pfam06470 4 VLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIE--FLKKnklgRATFLPLDRLKPRPRRPGADLKG--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110347420 598 vgpdNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVA 640
Cdd:pfam06470 78 ----GAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-159 |
2.62e-21 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 94.56 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVY--KNGQAGITKASVS 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYraRVGKPDSNSAYVT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 81 ITFDNSDKkqsplgfevhdEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 159
Cdd:cd03275 79 AVYEDDDG-----------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPP 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1082-1167 |
5.96e-19 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 85.10 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1082 LTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154
|
....*...
gi 110347420 1161 FV-DGVST 1167
Cdd:cd03227 155 KViTGVYK 162
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1081-1168 |
4.61e-18 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 85.00 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*...
gi 110347420 1161 FVDGVSTV 1168
Cdd:cd03272 235 FRNKVSTI 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-961 |
4.36e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 165 IEEAagTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaed 244
Cdd:PTZ00121 1214 AEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---------------- 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 245 tKVRSAEELKEMQDKviKLQEELSENDKKIKAlnheiEELEKRKDKEtggilRSLEDALAEAQRVNTKSQSAfdlKKKnl 324
Cdd:PTZ00121 1276 -EARKADELKKAEEK--KKADEAKKAEEKKKA-----DEAKKKAEEA-----KKADEAKKKAEEAKKKADAA---KKK-- 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 325 aCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHAlQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmma 404
Cdd:PTZ00121 1338 -AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-------- 1407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 405 ckNDISKAQTEAKQAQmklkhaqqELKNKQAEVKKMDSGYRKDQE---ALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:PTZ00121 1408 --DELKKAAAAKKKAD--------EAKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvkdtsattALELVAGErlynvvvdtEVTGK 561
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK------------------------ADEAKKAE---------EAKKA 1524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 562 KLLERGELKRRytiiplnkisarciaPETLRVAQNLVGPDNVHVAlslveykPELQKAMEfvfgttfvCDNMDNAKKVAF 641
Cdd:PTZ00121 1525 DEAKKAEEAKK---------------ADEAKKAEEKKKADELKKA-------EELKKAEE--------KKKAEEAKKAEE 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 642 DKRIMTRTVTLGGDV----FDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQ 717
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 718 QWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAE----AERERELK- 792
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKa 1732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 793 -DAQKKLDCAKTKADASSKKMKEK----------QQEVEAITLELEELKREHTSYK--QQLEAVNEAIKSYESQIEVMAA 859
Cdd:PTZ00121 1733 eEAKKEAEEDKKKAEEAKKDEEEKkkiahlkkeeEKKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIE 1812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 860 EVAKNKESVNKAQE-EVTKQKEVITAQDTVIKaKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV--SKMLK 936
Cdd:PTZ00121 1813 GGKEGNLVINDSKEmEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIE 1891
|
810 820
....*....|....*....|....*
gi 110347420 937 DYDWINAERHLfgqPNSAYDFKTNN 961
Cdd:PTZ00121 1892 KIDKDDIEREI---PNNNMAGKNND 1913
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1085-1156 |
3.27e-16 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 79.54 E-value: 3.27e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347420 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFT-HSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03275 156 LSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADAL 228
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-156 |
7.32e-16 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 77.72 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGIsNLSQVRASNLQDLVYK-NGQAGITKASVSI 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLIHNsAGHPNLDSCSVEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347420 82 TFDnsdkkqsplgfEVHDEitvtrqvviggrnkylingvnanntrvqDLFCSVGLNVNNPHFLIMQGRITKVLNM 156
Cdd:cd03274 82 HFQ-----------EIIDK----------------------------PLLKSKGIDLDHNRFLILQGEVEQIAQM 117
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1078-1156 |
2.60e-15 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 76.18 E-value: 2.60e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 1078 WKeNLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03274 122 WK-NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-83 |
2.97e-14 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 71.62 E-value: 2.97e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 5 SIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRasnlqdlvYKNGQAGITKASVSITF 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-203 |
4.15e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 69.65 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSqvRASNLQDLVYKngqaGITKASVSI 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINV----GSEEASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 82 TFDNSDKkqsplgfevhdEITVTRQvviggrnkylingvnanntrvqdlfcsvglnvnnphflimQGRITKVLNMKPPEI 161
Cdd:COG0419 74 EFEHGGK-----------RYRIERR----------------------------------------QGEFAEFLEAKPSER 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110347420 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTI--LEEEI 203
Cdd:COG0419 103 KEALKRLLGLEIYEELKERLKELEEALESALEELAELqkLKQEI 146
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-913 |
1.83e-12 |
|
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: 71.92 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYaQRTEVNGFDPL--FNAITGLNGSGKSNILDSICFLLgisnLSQVRASNlQDLVYKNGQAGITKAS 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL----YGKLPRRS-EVIRSLNSLYAAPSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 79 VSITFDNSDKKQSplgFEVHDEITVTR---------QVVI---GGRNKYLINGVNANNTRVQDLfcsvgLNVNNPHF--- 143
Cdd:TIGR00618 75 AFAELEFSLGTKI---YRVHRTLRCTRshrkteqpeQLYLeqkKGRGRILAAKKSETEEVIHDL-----LKLDYKTFtrv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 144 -LIMQGRITKVLNMKPPEILSMIEEAAGTRMYE---------YKKIAAQKTIEKKEAKL------------KEIKTILEE 201
Cdd:TIGR00618 147 vLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTqlalmefakKKSLHGKAELLTLRSQLltlctpcmpdtyHERKQVLEK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 202 EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHeI 281
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ-I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 282 EELEKRKDKETGGILRSLEDALAEAQRVnTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEvKKITDGLHA 361
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 362 LQEASNKDAEALAAAQQHFNAVS--AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK 439
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 440 MDSGYRKDQEALEAVKRLKEKlEAEMKKLnyEENKEESLLEKRRQLSrdiGRLKETYEAllarfpnlrfaykdpeknwnr 519
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ-ETRKKAV--VLARLLELQEEPCPLC---GSCIHPNPA--------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 520 ncvkgLVASLISVKDTSATTALE------LVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISA-RCIAPETLR 592
Cdd:TIGR00618 517 -----RQDIDNPGPLTRRMQRGEqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRsKEDIPNLQN 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 593 VAQNLvgpdnvhvalslveyKPELQKamefvfgttfvcdNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAA 672
Cdd:TIGR00618 592 ITVRL---------------QDLTEK-------------LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 673 SILTKFQELKDVQDE------LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQ---TKLQQSS--YHKQ 741
Cdd:TIGR00618 644 KLTALHALQLTLTQErvrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLReleTHIEEYDreFNEI 723
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 742 QEELDALKKTIEESEETLKNT-KEIQRKAEEKYEVLENKMKNAEaerERELKDAQKKLDCAKTKADasskkMKEKQQEVE 820
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSlKELMHQARTVLKARTEAHFNNN---EEVTAALQTGAELSHLAAE-----IQFFNRLRE 795
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 821 AITLELEELKREHTSYkqqleavneaIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQdtviKAKYAEVAKHK 900
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQE----------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ----LLKYEECSKQL 861
|
970
....*....|...
gi 110347420 901 EQNNDSQLKIKEL 913
Cdd:TIGR00618 862 AQLTQEQAKIIQL 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-947 |
2.30e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 198 ILEE-EITPTIQKLKEERSSYLEYQKVM----REIEHLSRLYIAYQFLLAEDTKVRSAEELKEM------QDKVIKLQEE 266
Cdd:COG4913 217 MLEEpDTFEAADALVEHFDDLERAHEALedarEQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 267 LSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAEA--QRVNtksqsafDLKKknlaceESKRKEleknmvedsKT 344
Cdd:COG4913 297 LEELRAELARLEAELERLEARLD-ALREELDELEAQIRGNggDRLE-------QLER------EIERLE---------RE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 345 LAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmmackndiskAQTEAKQAQMKLK 424
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---------------ALAEAEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 425 HAQQELKNKQAEVKKMDSGYRKDQEALeavkrlkekleaemkklnyeenkeesllekRRQLSRDIGrLKETyeallarfp 504
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLAL------------------------------RDALAEALG-LDEA--------- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 505 NLRFaykdpeknwnrncvkglVASLISVKDTSA--TTALELVAGERLYNVVVDTEVTGK--KLLERGELKRRytiIPLNK 580
Cdd:COG4913 459 ELPF-----------------VGELIEVRPEEErwRGAIERVLGGFALTLLVPPEHYAAalRWVNRLHLRGR---LVYER 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 581 ISARCIAPETLRVAQN-LVGpdnvhvalsLVEYKP-ELQKAMEFVFGTTFV---CDNMDNAKKVafdkrimTRTVTLGGD 655
Cdd:COG4913 519 VRTGLPDPERPRLDPDsLAG---------KLDFKPhPFRAWLEAELGRRFDyvcVDSPEELRRH-------PRAITRAGQ 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 656 VFDPHGTLSGGARSQAAS-----------ILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEmktE 724
Cdd:COG4913 583 VKGNGTRHEKDDRRRIRSryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW---D 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 725 EADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERelkdAQKKLDCAKTK 804
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 805 ADASSKKmkekqqEVEAITLELEELKREHtsykQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ-KEVIT 883
Cdd:COG4913 736 LEAAEDL------ARLELRALLEERFAAA----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETA 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 884 AQDTVIKA--KYAEV---------AKHKEQ-----NNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWiNAERHL 947
Cdd:COG4913 806 DLDADLESlpEYLALldrleedglPEYEERfkellNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPF-GPGRYL 884
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1046-1144 |
1.02e-11 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 64.19 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1046 STLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKEN---LTELSGGQRSLVALSLILsmlLFKPaPIYILDEVDAALDLS 1122
Cdd:cd00267 39 STLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRigyVPQLSGGQRQRVALARAL---LLNP-DLLLLDEPTSGLDPA 114
|
90 100
....*....|....*....|...
gi 110347420 1123 HTQNIGQMLRTHF-THSQFIVVS 1144
Cdd:cd00267 115 SRERLLELLRELAeEGRTVIIVT 137
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-912 |
4.10e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 668 RSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDA 747
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL-----EERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 748 LKKTIEESEETLKNTKEIQRKAEE---------KYEVLENKMKNAEAERERELKDAQKKLdcaktkadassKKMKEKQQE 818
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEyiklsefyeEYLDELREIEKRLSRLEEEINGIEERI-----------KELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 819 VEAITLELEELKREHTSYKQQLEAVNEAiKSYESQIEVMAAEVA-KNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVA 897
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|....*
gi 110347420 898 KHKEQNNDSQLKIKE 912
Cdd:PRK03918 419 KEIKELKKAIEELKK 433
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-126 |
6.42e-11 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 65.56 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 2 HIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVSI 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELE-FSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELI-RFGADG---FRVRA 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 110347420 82 TFDNSDKKqsplgFEVhdEITVTRqvviGGRNKYLINGVNANNTR 126
Cdd:COG1195 72 EVERDGRE-----VRL--GLGLSR----GGKKRVRINGKPVRRLS 105
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-196 |
6.72e-11 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 62.90 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 6 IILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:pfam13476 1 LTIENFRSF-RDQTID-FSKGLTLITGPNGSGKTTILDAIKLALYgkTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 84 DNSDKKQSplgFEVHDEITVTRQVVIGGRNKYL-INGVNANNTRVQDLFCSvgLNVNNPHFLIM-QGRITKVLNMKPPEI 161
Cdd:pfam13476 79 ENNDGRYT---YAIERSRELSKKKGKTKKKEILeILEIDELQQFISELLKS--DKIILPLLVFLgQEREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|....*
gi 110347420 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIK 196
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-509 |
8.05e-11 |
|
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: 65.17 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 257 QDKVIKLQEELSENDKKIKALNHEIEELEKRKdKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLAceeskrkELEK 336
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-KALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 337 NMVEDSKTLAAKEKEVKKItdgLHALQEASNKDAEALaaaqqhfnavsagLSSNEDGAEATLAGQMMACKNDISKAQTEA 416
Cdd:COG4942 91 EIAELRAELEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 417 -KQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEM-KKLNYEENKEESLLEKRRQLSRDIGRLKE 494
Cdd:COG4942 155 lRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|....*
gi 110347420 495 TYEALLARFPNLRFA 509
Cdd:COG4942 235 EAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
242-937 |
8.22e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 242 AEDtkVRSAEELKEMQDkVIKLQEELSENDKKIKALNHEIEELEKRKdketggILRSLEDAL-AEAQRVNTKSQSAFDLK 320
Cdd:PTZ00121 1124 AED--ARKAEEARKAED-ARKAEEARKAEDAKRVEIARKAEDARKAE------EARKAEDAKkAEAARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 321 KknlaCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAvsaGLSSNEDGAEATLAG 400
Cdd:PTZ00121 1195 K----AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE---EIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 401 QMMACKNDISKAQTEAKQAQMKLKHAQ----------QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE-------A 463
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaeekkkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaaeA 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 464 EMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvKDTSATTALEL 543
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK-----------------AEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 544 VAGERLYNVVVDTEVTGKKLLERGELKRRytiiplnkisarciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAmefv 623
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKKK--------------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---- 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 624 fgttfvcdnmDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELA 703
Cdd:PTZ00121 1473 ----------DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 704 GLKNTAEKYR---QLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIqrKAEEKYEVLENKM 780
Cdd:PTZ00121 1543 EEKKKADELKkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 781 KNAEAERERELKdaqKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMA-- 858
Cdd:PTZ00121 1621 KAEELKKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKke 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 859 AEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNND--SQLKIKELDHNISKHKREAEDGAAKVSKMLK 936
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
.
gi 110347420 937 D 937
Cdd:PTZ00121 1778 E 1778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1030 |
1.29e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 667 ARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKtEEADLLQTKLQQssyhkqQEELD 746
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK-KKADEAKKKAEE------KKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 747 ALKKTIEESeetlKNTKEIQRKAEEKYEVLENKMKnaeAERERELKDAQKKLDCAKtKADASSKKMKEKQQEVEAITLEL 826
Cdd:PTZ00121 1435 EAKKKAEEA----KKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 827 EELKREHTSYKQQLEAVNEAIKSYEsqiEVMAAEVAKNKESVNKAqEEVTKQKEVITAQDTvikaKYAEVAKHKEQNNDS 906
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAE---EAKKADEAKKAEEKKKA-DELKKAEELKKAEEK----KKAEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 907 QLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmR 986
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---------KIKAEELKKAEEEKKKVEQLKKKEAEEKK-K 1648
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 110347420 987 AMNVLTEAEERYNDLMKKKRIVENDKSKI--LTTIEDLDQKKNQAL 1030
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
23-130 |
3.21e-10 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 62.22 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 23 FDPLFNAITGLNGSGKSNILDSICFLLGIsnlsqvRASNlqDLVykngQAGITKASVSITFDNSDK-----KQSPLGFEV 97
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGG------RASA--DLI----RSGAEKAVVEGVFDISDEeeakaLLLELGIED 86
|
90 100 110
....*....|....*....|....*....|...
gi 110347420 98 HDEITVTRQVVIGGRNKYLINGVNANNTRVQDL 130
Cdd:cd03241 87 DDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-499 |
3.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYAQrTEVnGFDPLFNAITGLNGSGKSNILDSiCF--LLGISNLSQVrasnLQDLVYKngqaGITKAS 78
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADL-RLEDGVTVIHGVNGSGKSSLLEA-CFfaLYGSKALDDT----LDDVITI----GAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 79 VSITFdnsdkkqSPLGFEVH---------DEITVTRQVVIGGRNkyLINGVNANNTRVQDLfcsvgLNVNNPHFL----I 145
Cdd:PRK02224 70 IELWF-------EHAGGEYHierrvrlsgDRATTAKCVLETPEG--TIDGARDVREEVTEL-----LRMDAEAFVncayV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 146 MQGRITKVLNMKPPEILSMIEEAAGT-RMYEYKKIAA--------------------QKTIEKKEAK------------L 192
Cdd:PRK02224 136 RQGEVNKLINATPSDRQDMIDDLLQLgKLEEYRERASdarlgvervlsdqrgsldqlKAQIEEKEEKdlherlngleseL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 193 KEIKTILE--EEITPTIQKLKEERSSYLE-YQKVMREIEHLSRLYIAYQFLLAEDTKVRS--AEELKEMQDKVIKLQEEL 267
Cdd:PRK02224 216 AELDEEIEryEEQREQARETRDEADEVLEeHEERREELETLEAEIEDLRETIAETEREREelAEEVRDLRERLEELEEER 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 268 SE-------NDKKIKALNHEIEELEKRKDketgGILRSLEDALAEAQRVNTKSQS----AFDLKKKNLACEEsKRKELEK 336
Cdd:PRK02224 296 DDllaeaglDDADAEAVEARREELEDRDE----ELRDRLEECRVAAQAHNEEAESlredADDLEERAEELRE-EAAELES 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 337 NMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHfnavSAGLSSNEDGA---EATLAGQMMACKNDISKAq 413
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF----LEELREERDELrerEAELEATLRTARERVEEA- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 414 tEAKQAQMKLKHAQQELKnkqaevkkmDSGyrkDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLS---RDIG 490
Cdd:PRK02224 446 -EALLEAGKCPECGQPVE---------GSP---HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIE 512
|
....*....
gi 110347420 491 RLKETYEAL 499
Cdd:PRK02224 513 RLEERREDL 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-882 |
7.78e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 7.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGqagiTKASVS 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVE-FDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGG----SGTEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 81 ITFDNSDKKqsplgfevhdeITVTRQVVIGgrNKYLINGVNANNTRVQDLFCS------VGLNVNNPHFLIMQGRITKVL 154
Cdd:PRK03918 75 LKFEKNGRK-----------YRIVRSFNRG--ESYLKYLDGSEVLEEGDSSVRewverlIPYHVFLNAIYIRQGEIDAIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 155 nmkppeilsmieEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEitptIQKLKEERSSYLEYQKVMREiehlsrly 234
Cdd:PRK03918 142 ------------ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKE-------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 235 iayqfllAEDTKVRSAEELKEMQDKVIKLQEEL---SENDKKIKALNHEIEELEKRKDKETGGiLRSLEDALAEAQrvnt 311
Cdd:PRK03918 198 -------KEKELEEVLREINEISSELPELREELeklEKEVKELEELKEEIEELEKELESLEGS-KRKLEEKIRELE---- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 312 ksqsafdlkkKNLACEESKRKELEKNmVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNE 391
Cdd:PRK03918 266 ----------ERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 392 DgaeatlagqMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDsGYRKDQEALEAVKRLKEKLEAEMKKLNYE 471
Cdd:PRK03918 335 E---------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 472 EnKEESLLEKRRQLSRDIGRLKETYEALlarfpnlrfaykdpeKNWNRNCvkglvaslisvkdtsattalelvagerlyn 551
Cdd:PRK03918 405 E-EISKITARIGELKKEIKELKKAIEEL---------------KKAKGKC------------------------------ 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 552 vvvdtEVTGKKLLE--RGELKRRYTiIPLNKISA---------RCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAM 620
Cdd:PRK03918 439 -----PVCGRELTEehRKELLEEYT-AELKRIEKelkeieekeRKLRKELRELEKVLKKESELIKLKELAEQLKELEEKL 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 621 EFVfgttfvcdNMDNAKKVAFDKRIMTRtvtlggdvfdphgtLSGGARSQAASILTKFQELKDVQDELRIKENELRALEE 700
Cdd:PRK03918 513 KKY--------NLEELEKKAEEYEKLKE--------------KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 701 ELAGLkntaekyrqLKQQWEMKTEEADLLQTKLQQ-SSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENK 779
Cdd:PRK03918 571 ELAEL---------LKELEELGFESVEELEERLKElEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 780 MKnaeaERERELKDAQKKLDcaktkadasskkmkekQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAA 859
Cdd:PRK03918 642 LE----ELRKELEELEKKYS----------------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
890 900
....*....|....*....|....*....
gi 110347420 860 EVAKNK------ESVNKAQEEVTKQKEVI 882
Cdd:PRK03918 702 ELEEREkakkelEKLEKALERVEELREKV 730
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
248-913 |
8.11e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 248 RSAEELK-EMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGgILRSLEDALAEAQRVNTKSQSAFD----LKKK 322
Cdd:pfam15921 138 QSQEDLRnQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEG-VLQEIRSILVDFEEASGKKIYEHDsmstMHFR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 323 NLACEESK-RKELEKNmvedsktLAAKEKEVKKITDGLHALQEASNKDAEALAaaQQHFNAVSAGLSSNEDgaeatlagQ 401
Cdd:pfam15921 217 SLGSAISKiLRELDTE-------ISYLKGRIFPVEDQLEALKSESQNKIELLL--QQHQDRIEQLISEHEV--------E 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQA----EVKKMDSGYRKDQEALEAVKRLKE-KLEAEMKKLNYEENKEE 476
Cdd:pfam15921 280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLANSELT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 477 SLLEKRRQLSRDIGRLKETYEALLA----RFPNLRFAYKDPEKNWNRNC-------------------VKGLVASLISVK 533
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKEQNKRLWDRDTgnsitidhlrrelddrnmeVQRLEALLKAMK 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 534 D----------------------TSATTALELVAGERLYNVVvdTEVTGKKL-LERGELKrrytiipLNKISARCIAPET 590
Cdd:pfam15921 440 SecqgqmerqmaaiqgkneslekVSSLTAQLESTKEMLRKVV--EELTAKKMtLESSERT-------VSDLTASLQEKER 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 591 LRVAQNL-VGPDNVHVALSLVEYKpELQKAMEFVFGTTFVCD----NMDNAKKVAfdkRIMTRTVTLGGDVFDPHGTLSG 665
Cdd:pfam15921 511 AIEATNAeITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEalklQMAEKDKVI---EILRQQIENMTQLVGQHGRTAG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 666 GARSQAASI----------LTKFQELKDVQDElRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLL-QTKLQ 734
Cdd:pfam15921 587 AMQVEKAQLekeindrrleLQEFKILKDKKDA-KIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnEVKTS 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 735 QSSYHKQQEELDALKKTI----EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDA---QKKLDCAKTKADA 807
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDA 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 808 SSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDT 887
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
730 740
....*....|....*....|....*.
gi 110347420 888 VIKAKYAEVAKHKEQNNdsqLKIKEL 913
Cdd:pfam15921 826 IIQRQEQESVRLKLQHT---LDVKEL 848
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
668-1025 |
9.77e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.92 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 668 RSQAASILTKFQELKDvqdELRIKENELRALEEELAGLKNTAEKYRQ----LKQQWEMKTEEADLLQTklqqssyhkqqe 743
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQ---ELSKKESELLALQTKLETLTNQNSDCKQhievLKESLTAKEQRAAILQT------------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 744 ELDALKKTIEESEETL-KNTKEIQRKAEE--------------------KYEVLENKMKN-AEAERERE-----LKDAQK 796
Cdd:pfam10174 346 EVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirdlkdmldvkerKINVLQKKIENlQEQLRDKDkqlagLKERVK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 797 KLDCAKTKADASSKKMKEKQQEVEAITLEL-EELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEV 875
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 876 TKQKEVITAQDTVIKAKYAEVAKHKEQ--------------------NNDSQLKIKELDHNISKHKREAEDGAAKVSKML 935
Cdd:pfam10174 506 SSLASSGLKKDSKLKSLEIAVEQKKEEcsklenqlkkahnaeeavrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLL 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 936 ------------KDYDWINAE----RHLFGQPNSAYDFKTNNPKEagqRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYN 999
Cdd:pfam10174 586 gilrevenekndKDKKIAELEsltlRQMKEQNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
|
410 420
....*....|....*....|....*.
gi 110347420 1000 DLMKKKRIVENDKSKILTTIEDLDQK 1025
Cdd:pfam10174 663 ALEKTRQELDATKARLSSTQQSLAEK 688
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
677-839 |
1.35e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 677 KFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQ-QSSYHKQQEELDALKKTIEES 755
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 756 EETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTS 835
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
....
gi 110347420 836 YKQQ 839
Cdd:COG4717 239 AALE 242
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-123 |
2.96e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 60.17 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVS 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYLL---APGRSHRTARDKELI-RFGAEA---AVIH 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110347420 81 ITFDNSdkkqsplGFEVHDEITVTRQvvigGRNKYLINGVNAN 123
Cdd:PRK00064 72 GRVEKG-------GRELPLGLEIDKK----GGRKVRINGEPQR 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-925 |
3.76e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 160 EILSMIEEAagtRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSY-LEYQKVMREIEHLSRLYIAYQ 238
Cdd:PTZ00121 1095 EAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 239 fllAEDTK----------VRSAEELKEMQDKVIKLQEELSENDKKIkalnheiEELEKRKDKETGGILRSLEDALAEAqr 308
Cdd:PTZ00121 1172 ---AEDAKkaeaarkaeeVRKAEELRKAEDARKAEAARKAEEERKA-------EEARKAEDAKKAEAVKKAEEAKKDA-- 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 309 vntksqsafdlkkknlacEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEasnKDAEALAAAQQHFNAVSAGLS 388
Cdd:PTZ00121 1240 ------------------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---RKADELKKAEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 389 SNEDGAEatlagqmmacknDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKL 468
Cdd:PTZ00121 1299 EEKKKAD------------EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 469 NYEENKEESLLEKRRQLSRDIGRLKETYEAllarfpnLRFAYKDPEKnwnrncvkglvASLISVKDTSATTALELVAGER 548
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEA-------KKKAEEDKKK-----------ADELKKAAAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 549 LYNVVVDTEVTGKKLLERGELKRRytiiplnkisarciaPETLRVAQNLV-GPDNVHVALSLVEYKPELQKAMEFVFGTT 627
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKK---------------AEEAKKAEEAKkKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 628 FVCDNMDNAKKVAFDKRIMTRTVTlgGDVFDPHGTLSGGARSQAASILTKFQELKDVqDELRiKENELRALEEelaglKN 707
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKA-DELK-KAEELKKAEE-----KK 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 708 TAEKYRQLKQQWEMKTEEADLLQT--KLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLEnKMKNAEA 785
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEA 1643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 786 ERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAiksyeSQIEVMAAEVAKNK 865
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKA 1718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 866 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAE 925
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-95 |
6.97e-09 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 56.84 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03276 1 IESITLKNFMCHR-HLQIE-FGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLI-KDGE---SSAKITVT 74
|
90
....*....|...
gi 110347420 83 FDNSDKKQSPLGF 95
Cdd:cd03276 75 LKNQGLDANPLCV 87
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-97 |
7.38e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 59.17 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYaQRTEVNgFDPLfNAITGLNGSGKSNILDSICFL--LGISNLSQVRASN--LQDLVYKNGQAGITKAS 78
Cdd:COG4637 2 ITRIRIKNFKSL-RDLELP-LGPL-TVLIGANGSGKSNLLDALRFLsdAARGGLQDALARRggLEELLWRGPRTITEPIR 78
|
90
....*....|....*....
gi 110347420 79 VSITFDNSDkkQSPLGFEV 97
Cdd:COG4637 79 LELEFAEED--ERDLRYEL 95
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-109 |
1.33e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.46 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICF-LLGISNLSQVRASNLQDLVYKngqaGITKASVSI 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLIRE----GEVRAQVKL 75
|
90 100
....*....|....*....|....*...
gi 110347420 82 TFDNSDKKQsplgFEVHDEITVTRQVVI 109
Cdd:cd03240 76 AFENANGKK----YTITRSLAILENVIF 99
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-84 |
3.09e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 57.32 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLqdlvYKNGQAGITKASVS 80
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDF----YLGDDPDLPEIEIE 74
|
....
gi 110347420 81 ITFD 84
Cdd:COG3593 75 LTFG 78
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
744-898 |
4.99e-08 |
|
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: 55.32 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 744 ELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSKkmkekQQEVE 820
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRN-----NKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347420 821 AITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAK 898
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
689-860 |
5.83e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 689 RIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKL----QQSSYHKQQEELDALKKTIEESEETLKNTKE 764
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 765 IQRKAEEKYEVLENKMkNAEAERERELKDAQKKLDCAKTKADASSKK-MKEKQQEVEAITLELEELKREHTSYKQQLEAV 843
Cdd:COG4717 147 RLEELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170
....*....|....*..
gi 110347420 844 NEAIKSYESQIEVMAAE 860
Cdd:COG4717 226 EEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
669-1142 |
6.14e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 669 SQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYH---KQQEEL 745
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 746 DALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKK---------------------------- 797
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlfl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 798 ----LDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQE 873
Cdd:COG4717 282 vlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 874 EV------TKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHL 947
Cdd:COG4717 362 ELqleeleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 948 fgqpnsaydfktnnpKEAGQRLQKL-QEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKK 1026
Cdd:COG4717 442 ---------------EELEEELEELrEELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1027 NQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEgqtvldGLEFKVALGNTWKENLTELSGGQRSLVALSL---ILSMLL 1103
Cdd:COG4717 507 EEYREERLPPVLERASEYFSRLTDGRYRLIRIDE------DLSLKVDTEDGRTRPVEELSRGTREQLYLALrlaLAELLA 580
|
490 500 510
....*....|....*....|....*....|....*....
gi 110347420 1104 FKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIV 1142
Cdd:COG4717 581 GEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIY 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1026 |
1.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 677 KFQELKDVQDELRIKENELRALEEelagLKNTAEKYRQlKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESE 756
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 757 ETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADA-SSKKMKEKQQEVEAITLE---------- 825
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEekkkadelkk 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 826 ------------LEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK----ESVNKAQEEVTKQKEVITAQDTVI 889
Cdd:PTZ00121 1554 aeelkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 890 KAKYAEVAKHKEQNNDSQLKIKELDHNISKH--KREAEDGAAKVSKMLKDYDwinAERHlfgqpnsaydfKTNNPKEAGQ 967
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKAEE---DEKK-----------AAEALKKEAE 1699
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 968 RLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKK 1026
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
678-1029 |
1.70e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 55.47 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 678 FQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEmkteeadllqtklqqsSYHKQQEELDALKKTIEESEE 757
Cdd:pfam05622 96 VLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVE----------------TYKKKLEDLGDLRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 758 tlKNTKEIQRKAEekyevLENKMKNAEAER------ERELKDAQKKLDCAKTKADA---SSKKMKEK----QQEVEAITL 824
Cdd:pfam05622 160 --RNAEYMQRTLQ-----LEEELKKANALRgqletyKRQVQELHGKLSEESKKADKlefEYKKLEEKlealQKEKERLII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 825 E-------LEELKREHTSYKQQLEAVNEAIKSYESqIEVMAAEV--AKNKESVNKAQEEvtkQKEVITAQDTVIKAKYAE 895
Cdd:pfam05622 233 ErdtlretNEELRCAQLQQAELSQADALLSPSSDP-GDNLAAEImpAEIREKLIRLQHE---NKMLRLGQEGSYRERLTE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 896 VAKH-----------KEQNNDSQLKIKELDHNISKHKRE-------AEDGAAKVSKMLKDYDWINaERHLFGQPNSAYdF 957
Cdd:pfam05622 309 LQQLledanrrknelETQNRLANQRILELQQQVEELQKAlqeqgskAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQ-I 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347420 958 KTNNPKEAGQRLQKLQEMKEKL-GRNVNMRAMnvlteaEERYndlmkkKRIVENDKSKILTtiedLDQKKNQA 1029
Cdd:pfam05622 387 EELEPKQDSNLAQKIDELQEALrKKDEDMKAM------EERY------KKYVEKAKSVIKT----LDPKQNPA 443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
664-1031 |
1.82e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 664 SGGARSQAASILTkfqELKDVQDELRIKEN----ELRALEEELAGLKNtaeKYRQLKQQWEMKTEE---------ADLLQ 730
Cdd:pfam15921 287 ASSARSQANSIQS---QLEIIQEQARNQNSmymrQLSDLESTVSQLRS---ELREAKRMYEDKIEElekqlvlanSELTE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 731 TKLQQSSYHKQQEELD-ALKKTIEESEetlKNTKEIQRKAEEKYEVLENKMKNAeaererelkdaqkkldcakTKADASS 809
Cdd:pfam15921 361 ARTERDQFSQESGNLDdQLQKLLADLH---KREKELSLEKEQNKRLWDRDTGNS-------------------ITIDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 810 KKMKEKQQEVEAITLELEELKRE-HTSYKQQLEAVNEAIKSYEsQIEVMAAEVAKNKESVNKAQEEVTKQKEVITA---- 884
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESsert 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 885 ----------QDTVIKAKYAEVAKHKEQNNdsqLKIKELDH--NISKHKR--EAEDGAAKVSKMLKD------YDWINAE 944
Cdd:pfam15921 498 vsdltaslqeKERAIEATNAEITKLRSRVD---LKLQELQHlkNEGDHLRnvQTECEALKLQMAEKDkvieilRQQIENM 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 945 RHLFGQPNSAYDF----KTNNPKEAGQRLQKLQEMK-EKLGRNVNMRamnvltEAEERYNDLMKKKRIVENDKSKILTTI 1019
Cdd:pfam15921 575 TQLVGQHGRTAGAmqveKAQLEKEINDRRLELQEFKiLKDKKDAKIR------ELEARVSDLELEKVKLVNAGSERLRAV 648
|
410
....*....|..
gi 110347420 1020 EDLDQKKNQALN 1031
Cdd:pfam15921 649 KDIKQERDQLLN 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
681-926 |
2.14e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 681 LKDVQDELRIKENELR-ALEEE---LAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKK 750
Cdd:PRK02224 312 VEARREELEDRDEELRdRLEECrvaAQAHNEEAESLRedadDLEERAEELREEAAELESELEeaREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 751 TIEESEETLKNTKEIQRKAEEKYEVLE---NKMKNAEAERERELKDAQKKLDCAKTKADASskKMKEKQQEVEaitlele 827
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELReerDELREREAELEATLRTARERVEEAEALLEAG--KCPECGQPVE------- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 828 elKREHTsykqqleavnEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTV----IKAKYAE--VAKHKE 901
Cdd:PRK02224 463 --GSPHV----------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIerleERREDLEelIAERRE 530
|
250 260
....*....|....*....|....*
gi 110347420 902 QNNDSQLKIKELDHNISKHKREAED 926
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEE 555
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
675-944 |
3.03e-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: 54.64 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 675 LTKFQELKDVQDELRIKENELRALEEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKKTI 752
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLES---QINDLESKIQNQEKLNQQKDEQIKklQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 753 EESEETLKNTKEIQRKAEEKYEVLENKMKnaeaERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 832
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRE----SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 833 HTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ--KEVITAQDTVIKAKYAEVAKHKEQNNDSQLKI 910
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
250 260 270
....*....|....*....|....*....|....
gi 110347420 911 KELDHNISKHKREAEDGAAKVSKMLKDYDWINAE 944
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
986-1144 |
3.54e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.08 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 986 RAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKdfgsIFSTLLPGANAMLAPPEGQTVL 1065
Cdd:COG3950 97 RLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVRE----ALNKLLPDFKDIRIDRDPGRLV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1066 ----DGLEFkvalgntwkeNLTELSGGQRSLVAL--SLILSMLLFKPAP--------IYILDEVDAALDLSHTQNIGQML 1131
Cdd:COG3950 173 ildkNGEEL----------PLNQLSDGERSLLALvgDLARRLAELNPALenplegegIVLIDEIDLHLHPKWQRRILPDL 242
|
170
....*....|...
gi 110347420 1132 RTHFTHSQFIVVS 1144
Cdd:COG3950 243 RKIFPNIQFIVTT 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
680-897 |
3.74e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 680 ELKDVQDELRIKENELRALEEELAGLKNTAEkyrQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETL 759
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 760 KNTKEIQRKAEEKYEVLE------------------NKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 822 ITLELEELKREHTSYKQQLEAvneAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVA 897
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-90 |
4.67e-07 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 51.83 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSqvRASNLQDLVyKNGQagiTKASVS 80
Cdd:cd03277 3 IVRIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLLG--RAKKVGEFV-KRGC---DEGTIE 74
|
90
....*....|.
gi 110347420 81 IT-FDNSDKKQ 90
Cdd:cd03277 75 IElYGNPGNIQ 85
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
662-892 |
5.02e-07 |
|
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: 54.46 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 662 TLSGGARS---QAASILTKFQE-LKDVQDELRIKENELRALEEELAGLKNTAekyrqlKQQWEMKTEEADLLQTKLQQ-- 735
Cdd:pfam12128 262 HLHFGYKSdetLIASRQEERQEtSAELNQLLRTLDDQWKEKRDELNGELSAA------DAAVAKDRSELEALEDQHGAfl 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 736 ----SSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKnaeAERERELKDAQKKLDcaktkadaSSKK 811
Cdd:pfam12128 336 dadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK---EQNNRDIAGIKDKLA--------KIRE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 812 MKEKQQEVEAITLE-LE-ELKREHtsyKQQLEAVNEAIKSYESQIE--------VMAAE-----VAKNKESVNKAQEEVT 876
Cdd:pfam12128 405 ARDRQLAVAEDDLQaLEsELREQL---EAGKLEFNEEEYRLKSRLGelklrlnqATATPelllqLENFDERIERAREEQE 481
|
250
....*....|....*..
gi 110347420 877 K-QKEVITAQDTVIKAK 892
Cdd:pfam12128 482 AaNAEVERLQSELRQAR 498
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
692-870 |
6.22e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 692 ENELRALEEELAgLKNTAEKYRQLKQQWEMKTeeadlLQTKLQ--QSSYHKQQEELDALKKTIEESEEtlkNTKEIQRKA 769
Cdd:pfam05667 309 TNEAPAATSSPP-TKVETEEELQQQREEELEE-----LQEQLEdlESSIQELEKEIKKLESSIKQVEE---ELEELKEQN 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 770 EEKYEVLENKMKNAEaererELKDAQKKLDCAKTKADASSKKMKEKQQEVEA----ITLELEELKREHTSYKQQLEAVNE 845
Cdd:pfam05667 380 EELEKQYKVKKKTLD-----LLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180
....*....|....*....|....*
gi 110347420 846 AIKSYESQIEVMAAEvAKNKESVNK 870
Cdd:pfam05667 455 EIKELREKIKEVAEE-AKQKEELYK 478
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
709-905 |
6.86e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 709 AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKnTKEIQRKAEEKYEVLENKMKNAEAERE 788
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLA-AQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 789 RELKDAQKKLDCAKTKADASSKKMKE---KQQEVEAITLELEELKREHTSYKQQlEAVNEAIKSYESQIEVMAAEVAKNK 865
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAeakKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110347420 866 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNND 905
Cdd:PRK09510 219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-821 |
6.99e-07 |
|
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: 51.85 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGLKntaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQ----QEELDALKKTIEE 754
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 755 SEETLKNTKEIQRKAEEKYEVLENKMknaeAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAEL----AELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-934 |
1.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 422 KLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLA 501
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 502 RFPNLRFAYKD-PEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVV--------DTEVTGKKLLERGELKRR 572
Cdd:PRK03918 274 EIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleeKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 573 YTIIP-----LNKISARCIAPETLRVAQNLVGPDNVHVALSLVE-YKPELQKAMEFVFGTTFVCDNMDNAKKVAFD--KR 644
Cdd:PRK03918 354 LEELEerhelYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkAKEEIEEEISKITARIGELKKEIKELKKAIEelKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 645 IMTRTVTLGGDVFDPH-GTLSGGARSQAASILTKFQELKDVQDELRIKENELRAL---EEELAGLKNTAEKYRQLK---- 716
Cdd:PRK03918 434 AKGKCPVCGRELTEEHrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEeklk 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 717 ----QQWEMKTEEADLLQTKL-----QQSSYHKQQEELDALKKTIEESEETLKNT--------KEIQRKAEEKYEVLENK 779
Cdd:PRK03918 514 kynlEELEKKAEEYEKLKEKLiklkgEIKSLKKELEKLEELKKKLAELEKKLDELeeelaellKELEELGFESVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 780 MKNAE---------AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTsyKQQLEAVNEAIKSY 850
Cdd:PRK03918 594 LKELEpfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLEL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 851 ESQIEVMAAEVAKNKESVNKAQEEVTKQKEVitaqdtviKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGA-A 929
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlS 743
|
....*
gi 110347420 930 KVSKM 934
Cdd:PRK03918 744 KVGEI 748
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
663-911 |
1.29e-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: 52.07 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 663 LSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLkntAEKYRQLKQQWEMKTEEADLLQTKLQQssyhkQQ 742
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARRIRALEQELAA-----LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 743 EELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSK---KMKEKQQEV 819
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 820 EAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKH 899
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 110347420 900 KEQNNDSQLKIK 911
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-63 |
1.69e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 51.15 E-value: 1.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 1 MHIKSIILEGFKSYAQRtEVN-GFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQ 63
Cdd:COG3950 1 MRIKSLTIENFRGFEDL-EIDfDNPPRLTVLVGENGSGKTTLLEAIALALSglLSRLDDVKFRKLL 65
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-89 |
1.78e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 50.35 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 8 LEGFKSYAQRTEVN----GFDPLFnAITGLNGSGKSNILDSICFLLgisnLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:cd03279 8 LKNFGPFREEQVIDftglDNNGLF-LICGPTGAGKSTILDAITYAL----YGKTPRYGRQENLRSVFAPGEDTAEVSFTF 82
|
....*.
gi 110347420 84 DNSDKK 89
Cdd:cd03279 83 QLGGKK 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
734-932 |
1.94e-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: 51.69 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 734 QQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSK 810
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIralEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 811 KMKEKQQEVEAITLELEELKREHT-------------------------SYKQQLEAVNEAIKSYESQIEVMAAEVAKNK 865
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 866 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 932
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-126 |
1.96e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 50.76 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVykngQAGITKASVSIT 82
Cdd:cd03242 1 LKSLELRNFRNYA-ELELE-FEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI----RWGAEEAKISAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 110347420 83 FDNSdkkqsplGFEVHDEITVTRqvviGGRNKYLINGVNANNTR 126
Cdd:cd03242 72 LERQ-------GGELALELTIRS----GGGRKARLNGIKVRRLS 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
665-892 |
3.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 665 GGARSQAASILTKFQE-LKDVQDELRIKENE-----LRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTklqqsSY 738
Cdd:PRK02224 172 SDARLGVERVLSDQRGsLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLE-----EH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 739 HKQQEELDALKKTIEESEETLkntkeiqRKAEEKYEVLENKMKNAEAERErELKDAQKKL--DCAKTKADAsskkmkekq 816
Cdd:PRK02224 247 EERREELETLEAEIEDLRETI-------AETEREREELAEEVRDLRERLE-ELEEERDDLlaEAGLDDADA--------- 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 817 qevEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEV-TKQKEVITAQDTVIKAK 892
Cdd:PRK02224 310 ---EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAaELESELEEAREAVEDRR 383
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
670-934 |
4.38e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 670 QAASILTKFQeLKDVQDELRIKENELRaleEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQQssYHKQQEELD-AL 748
Cdd:pfam05557 1 RAELIESKAR-LSQLQNEKKQMELEHK---RARIELEK---KASALKRQLDRESDRNQELQKRIRL--LEKREAEAEeAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 749 KKTIEESEETLKNTKEIQRKAEEKYEVLEnkmknaeaererelkDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE 828
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLA---------------DAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 829 LKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVikAKYAEVAKHKEQNNDSQL 908
Cdd:pfam05557 137 LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL--ARIPELEKELERLREHNK 214
|
250 260
....*....|....*....|....*.
gi 110347420 909 KIKELDHNISKHKREAEDGAAKVSKM 934
Cdd:pfam05557 215 HLNENIENKLLLKEEVEDLKRKLERE 240
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
678-880 |
4.39e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 678 FQELKDVQDELRIKENELRALEEELAGLKNT----AEKYRQLKQQWEMKTEEADLLQTKL-----QQSSYHKQQEELDAL 748
Cdd:COG1340 35 NEELKELAEKRDELNAQVKELREEAQELREKrdelNEKVKELKEERDELNEKLNELREELdelrkELAELNKAGGSIDKL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 749 KKTIEESEETLKN---TKEIQRKAEEKYEVLENKMKNAEAERE--RELKDAQKKLDCAKTKADASSKKMKEKQQEVEAIT 823
Cdd:COG1340 115 RKEIERLEWRQQTevlSPEEEKELVEKIKELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELH 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 824 LELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 880
Cdd:COG1340 195 EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRK 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-879 |
5.97e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 422 KLKHAQQELKNKQAEVKKmdsgYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEE------SLLEKRRQLSRDIGRLKET 495
Cdd:COG4717 72 ELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 496 YEALLARFPNLRFaykdpeknwnrncvkgLVASLISVKDTSATTALELVAGERLYNVVVDTEVTgKKLLERGELKRRYTI 575
Cdd:COG4717 148 LEELEERLEELRE----------------LEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 576 IpLNKISARCIAPETLRvaQNLVGPDNVHVALSLVEykpELQKAMEFVFGTTFVCDnmdnakKVAFDKRIMTRTVTLGGD 655
Cdd:COG4717 211 L-EEELEEAQEELEELE--EELEQLENELEAAALEE---RLKEARLLLLIAAALLA------LLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 656 VFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGL--------KNTAEKYRQLKQQWEMKTEEAD 727
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 728 lLQTKLQQSSYHKQQEELdaLKKTIEESEETLK---NTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQK-----KLD 799
Cdd:COG4717 359 -LEEELQLEELEQEIAAL--LAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeleeELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 800 CAKTKADASSKKMKEKQQEVEAITLELEELKREHTsykqqLEAVNEAIKSYESQIEVMAAEVAKNK---ESVNKAQEEVT 876
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKlalELLEEAREEYR 510
|
...
gi 110347420 877 KQK 879
Cdd:COG4717 511 EER 513
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
674-853 |
6.59e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 674 ILTKFQELKDVQDELRIKENELRALEEELAglkntAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIE 753
Cdd:pfam05262 182 VVEALREDNEKGVNFRRDMTDLKERESQED-----AKRAQQLKEELDKKQIDADKAQQKADFA-----QDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 754 ESEETLKNTKEIQR--KAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKR 831
Cdd:pfam05262 252 QKQQEAKNLPKPADtsSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKRE 331
|
170 180
....*....|....*....|..
gi 110347420 832 EHTSYKQQLEAVNEAIKSYESQ 853
Cdd:pfam05262 332 PVAEDLQKTKPQVEAQPTSLNE 353
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
679-880 |
7.70e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWemktEEADLLQTKLQQssyhkqqeELDALKKTI------ 752
Cdd:COG3096 903 DAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADY----LQAKEQQRRLKQ--------QIFALSEVVqrrphf 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 753 --EESEETLKNTKEIQrkaeekyEVLENKMKNAEAERER---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVE 820
Cdd:COG3096 971 syEDAVGLLGENSDLN-------EKLRARLEQAEEARREareQLRQAQAQYSqynqvlaSLKSSRDAKQQTLQELEQELE 1043
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347420 821 AITL----ELEELKREHTS-YKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 880
Cdd:COG3096 1044 ELGVqadaEAEERARIRRDeLHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
738-1028 |
8.96e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 738 YHKQQEELDALKKTIEESEETLKntKEIQRKAEekyevLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQq 817
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLE--KFIKRTEN-----IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 818 EVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVnkaqEEVTKQKEVitaqdtviKAKYAEVA 897
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV----KELKELKEK--------AEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 898 KHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERhlfgqpnSAYDFKTNNPKEAGQRLQKLQEMKE 977
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 110347420 978 KLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQ 1028
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
180-1026 |
9.15e-06 |
|
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: 50.05 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 180 AAQKTIEKKEAKLKEIKTILE--EEITPTIQKLKEE----RSSYLEYQKVMREIEH-LSRLYIAYQFLLAEDTKVRSAEe 252
Cdd:TIGR00606 235 SSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEikalKSRKKQMEKDNSELELkMEKVFQGTDEQLNDLYHNHQRT- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 253 LKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALA-EAQRVNTKSQSAFDLKKKNLACE---- 327
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERGPFSErqik 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 328 ----------ESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEat 397
Cdd:TIGR00606 394 nfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 398 lagqmmacknDISKAQTEAKQAQMKLKHAQqelKNKQAEVKKMDSGYRKDQEAleAVKRLKEKLEAEMKKLNYEENKEES 477
Cdd:TIGR00606 472 ----------RILELDQELRKAERELSKAE---KNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 478 LL-------EKRRQLSRDIGRLKETYEALLARFPNLR-----FAYKDPEKNWNRNCVKGLVASLISV--------KDTSA 537
Cdd:TIGR00606 537 MEmltkdkmDKDEQIRKIKSRHSDELTSLLGYFPNKKqledwLHSKSKEINQTRDRLAKLNKELASLeqnknhinNELES 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 538 TTALELVAGERLYNVV--VDTEVTGKKLLERGElKRRYTIIPLNKISARCIAPETLRVAQNlvgPDNVHVALSLVEYKPE 615
Cdd:TIGR00606 617 KEEQLSSYEDKLFDVCgsQDEESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDEN---QSCCPVCQRVFQTEAE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 616 LQKamefvfgttfVCDNMDNAKKVAFDKriMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQdelrikeNEL 695
Cdd:TIGR00606 693 LQE----------FISDLQSKLRLAPDK--LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-------NKL 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 696 RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLqqSSYHKQQEELDALKKTIEE------SEETLKNTKEIQRKA 769
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV--TIMERFQMELKDVERKIAQqaaklqGSDLDRTVQQVNQEK 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 770 EEKYEVLENKMKNAE------AERERELKDAQKKLDCAKTKADASSKKMKEKQQ---EVEAITLELEELKREHTSYKQQL 840
Cdd:TIGR00606 832 QEKQHELDTVVSKIElnrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQD 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 841 EAVNEAIKSYESQIEVMaaeVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKE-QNNDSQLKIKELDHNISK 919
Cdd:TIGR00606 912 SPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEE 988
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 920 HKREAEDGAAKVSKMLKDYDwINAERHLFGQPNSAYDFKTNnpkeagqrlqKLQEMKEKLGRNVNMRAMNVLTEAEERYN 999
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQDID-TQKIQERWLQDNLTLRKREN----------ELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
890 900
....*....|....*....|....*..
gi 110347420 1000 DLMKKKRIVENDKSKILTTIEDLDQKK 1026
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
680-855 |
1.02e-05 |
|
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: 48.38 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 680 ELKDVQDELRIKENELRALEEELAGLKNTAEKYRQlkqqwEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 759
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 760 KNTKEiqrkaeekYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREhtsY 836
Cdd:COG1579 86 RNNKE--------YEALQKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---L 154
|
170
....*....|....*....
gi 110347420 837 KQQLEAVNEAIKSYESQIE 855
Cdd:COG1579 155 EAELEELEAEREELAAKIP 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1053-1133 |
1.08e-05 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 47.85 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1053 NAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03225 103 NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLK 178
|
.
gi 110347420 1133 T 1133
Cdd:cd03225 179 K 179
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
679-864 |
1.13e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 49.47 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDEL---RIKENELRALEEELAGLKntaekyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEeldalKKTIEES 755
Cdd:pfam09726 402 QDIKKLKAELqasRQTEQELRSQISSLTSLE------RSLKSELGQLRQENDLLQTKLHNAVSAKQKD-----KQTVQQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 756 EETLKNTKEiQRKAEEKYEVLENKMKnaeaeRERELKDAQKKLDCAKTKAD-ASSKKMKEKQQEVEAITLEL-----EEL 829
Cdd:pfam09726 471 EKRLKAEQE-ARASAEKQLAEEKKRK-----KEEEATAARAVALAAASRGEcTESLKQRKRELESEIKKLTHdiklkEEQ 544
|
170 180 190
....*....|....*....|....*....|....*
gi 110347420 830 KREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKN 864
Cdd:pfam09726 545 IRELEIKVQELRKYKESEKDTEVLMSALSAMQDKN 579
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-100 |
1.25e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 48.89 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 2 HIKSIILEGFKSYAQRTEVN----GFDPL-FNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITK 76
Cdd:COG1106 1 MLISFSIENFRSFKDELTLSmvasGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEP 80
|
90 100
....*....|....*....|....
gi 110347420 77 ASVSITFdNSDKKQSPLGFEVHDE 100
Cdd:COG1106 81 SEFEILF-LLDGVRYEYGFELDKE 103
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
776-939 |
1.28e-05 |
|
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: 48.00 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 776 LENKMKNAEAERE---RELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAV--NEAIKSY 850
Cdd:COG1579 15 LDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 851 ESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDsqlKIKELDHNISKHKREAEDGAAK 930
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAK 171
|
170
....*....|
gi 110347420 931 VSK-MLKDYD 939
Cdd:COG1579 172 IPPeLLALYE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
742-878 |
1.32e-05 |
|
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: 48.00 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 742 QEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAE-----RERELKDAQKKLDCAKTKADASSKKMKEKQ 816
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347420 817 QEveaitleLEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 878
Cdd:COG1579 117 ER-------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-1168 |
1.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 668 RSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSSYHKQQEELDA 747
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTPEKLEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 748 LKKTIEESEETLKNTKEIQRKAEEKYEVLE---NKMKNAE-------------------AERERELKDAQKKLdcakTKA 805
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKEL----KEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 806 DASSKKMKEKQQEVEAITLELEELKREHTSYKQqLEAVNEAIKSYE-SQIEVMAAEVAKNKESVNKAQ------------ 872
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgeikslkkelek 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 873 -EEVTKQKEVITAQDTVIKAKYAEVAK-----------------------HKEQNN--DSQLKIKELDHNISKHKREAED 926
Cdd:PRK03918 551 lEELKKKLAELEKKLDELEEELAELLKeleelgfesveeleerlkelepfYNEYLElkDAEKELEREEKELKKLEEELDK 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 927 GAAKVSKMLKDYDWINAERHLFGQPNSAYDF--KTNNPKEAGQRLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKK 1004
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKA 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1005 KRIVENDKsKILTTIEDLDQK----KNQALNIAWQKVNKDFGSIFSTLLPGANAmlappegQTVLDGLEFKVALGNTW-- 1078
Cdd:PRK03918 710 KKELEKLE-KALERVEELREKvkkyKALLKERALSKVGEIASEIFEELTEGKYS-------GVRVKAEENKVKLFVVYqg 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1079 -KENLTELSGGQRSLVALS--LILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNAN 1154
Cdd:PRK03918 782 kERPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKiPQVIIVSHDEELKDAAD 861
|
570
....*....|....
gi 110347420 1155 VLFKTKFVDGVSTV 1168
Cdd:PRK03918 862 YVIRVSLEGGVSKV 875
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
632-1026 |
1.50e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 632 NMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELrikenelraLEEELAGLKNTAEK 711
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL---------LRTEQQRLEKNEDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 712 YRQLKQQWEMKTEEADLLqTKLQQSsyhkQQEELDALKKTIEESEETLKNTKEIQRKAEEkYEVLENKMKNAEAEREREL 791
Cdd:pfam05483 379 LKIITMELQKKSSELEEM-TKFKNN----KEVELEELKKILAEDEKLLDEKKQFEKIAEE-LKGKEQELIFLLQAREKEI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 792 KDAQKKLDCAKTKADASSKKMKEKQQEVE--------------AITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVM 857
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 858 AAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLK----IKELDHNISKHKREAEDGAAKVSK 933
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQIENKNKNIEE 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 934 MLKDYDWINAERHLFGQPNSAYDFKTNNPK-EAGQRLQKLQEMKEKLGRNVNMRAMnvlteAEERYNDLMKKKRIVENDK 1012
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKI-----SEEKLLEEVEKAKAIADEA 687
|
410
....*....|....
gi 110347420 1013 SKILTTIEDLDQKK 1026
Cdd:pfam05483 688 VKLQKEIDKRCQHK 701
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
147-489 |
1.73e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 147 QGRITKVLNMKPPEILSMIEEAAGTRMyEYKKIAAQKTIEKKEAKLKEIKTILE-EEITPTIQKLKEE-RSSYLEYQKVM 224
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSElREAKRMYEDKI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 225 REIEHlsrlyiayQFLLA--EDTKVRS-----AEELKEMQDKvikLQEELSENDKKIKALNHEIEELEKRKDKETGG--- 294
Cdd:pfam15921 345 EELEK--------QLVLAnsELTEARTerdqfSQESGNLDDQ---LQKLLADLHKREKELSLEKEQNKRLWDRDTGNsit 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 295 ---ILRSLEDALAEAQRVNT-----KSQSAFDLKKKnLACEESKRKELEKnmvedSKTLAAKEKEVKKItdgLHALQEAS 366
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEAllkamKSECQGQMERQ-MAAIQGKNESLEK-----VSSLTAQLESTKEM---LRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 367 NKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMKLKHAQQE---LKNKQAEVKKMDSG 443
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNA--------EITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQ 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 110347420 444 YRKDQEALEAvkrLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDI 489
Cdd:pfam15921 557 MAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
668-882 |
2.28e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 668 RSQAASILTKFQELKDVQDELRIKENELRaleEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEelda 747
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELR---EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 748 lKKTIEESEEtLKNTKEIQRKAEEKYEVLENKMKNAEAERErELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELE 827
Cdd:COG1340 136 -KELVEKIKE-LEKELEKAKKALEKNEKLKELRAELKELRK-EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 828 ELKREHTSYKQQLEAVNEAIKSYESQI-----EVMAAEVAKNKESVNKAQEEVTKQKEVI 882
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELrelrkELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
720-916 |
2.46e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 720 EMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEES-EETLKNTKEIQR-KAEEKYEVLE--NKMKNAE-----AERERE 790
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApAKLRQAQAELEAlKDDNDEETREtlSTLSLRQlesrlAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 791 LKDAQKKLDCA-------KTKADASSKKMKEKQQEVEAITLELEELKRE---------------------HTSYKQQLEA 842
Cdd:PRK11281 137 LQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKVGgkalrpsqrvllqaeqallnaQNDLQRKSLE 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347420 843 VNEAIKS-YESQIEVMAAEVAKNKESVNKAQEEVTkQKEVITAQDTVIKAKYAEVAKHKEQNNdsqLKIKELDHN 916
Cdd:PRK11281 217 GNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAIN-SKRLTLSEKTVQEAQSQDEAARIQANP---LVAQELEIN 287
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1081-1143 |
2.52e-05 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 46.27 E-value: 2.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347420 1081 NLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:cd03214 94 PFNELSGGERQRV----LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
684-892 |
2.86e-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: 48.63 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 684 VQDELRIKENELRALEEELAGLKNTAE----KYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEEldalkktieeseetl 759
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTEllndRLRKSTLQVEQLTTELAAERSTSQKSESARQQLE--------------- 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 760 KNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQ 839
Cdd:pfam01576 945 RQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQ 1024
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 840 LEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQ---EEVTKQKEVITAQDTVIKAK 892
Cdd:pfam01576 1025 AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQrelDDATESNESMNREVSTLKSK 1080
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
679-1033 |
3.44e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGlknTAEKYRQLKQQWEMKTEEADLLQTKLQQSS--YHKQQEELDALKKTIEESE 756
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKemLRKVVEELTAKKMTLESSE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 757 ETLKntkEIQRKAEEKYEVLEnkMKNAEAERERELKDAQ-KKLDCAKTKADasskKMKEKQQEVEAITLELEELKREHTS 835
Cdd:pfam15921 496 RTVS---DLTASLQEKERAIE--ATNAEITKLRSRVDLKlQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEI 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 836 YKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTvikakyaevakhkeqnndsqlKIKELDH 915
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA---------------------KIRELEA 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 916 NISKHKREAEDGAAKVSKMLKDYDWINAERhlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmramNVLTEAE 995
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQER----------DQLLNEVKTSRNELNSLSEDYEVLKRNFR----NKSEEME 691
|
330 340 350
....*....|....*....|....*....|....*...
gi 110347420 996 ERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIA 1033
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
679-923 |
3.55e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDEL----RIKENELRALEEELAGLKNTAEKYrqLKQQWEMKTE--EADLLQTKLQQSS------YHKQQEELD 746
Cdd:pfam05483 432 EELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHY--LKEVEDLKTEleKEKLKNIELTAHCdkllleNKELTQEAS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 747 ALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKM---------KEKQ- 816
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENArsieyevlkKEKQm 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 817 -----------QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK----ESVNKAQEEVTKQK-- 879
Cdd:pfam05483 590 kilenkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKqkfeEIIDNYQKEIEDKKis 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 110347420 880 ------EVITAQDTVIKAkyaeVAKHKEQNNDSQLKIKELDHNISKHKRE 923
Cdd:pfam05483 670 eeklleEVEKAKAIADEA----VKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
742-1017 |
3.61e-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: 48.04 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 742 QEELDA-LKKTIEESEETLKNTKEIQRKAEEKYEVLENKmKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:TIGR00618 151 QGEFAQfLKAKSKEKKELLMNLFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 821 AITLELEELKREHTSYKQQLEAVNEAiksyeSQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTviKAKYAEVAKHK 900
Cdd:TIGR00618 230 HLREALQQTQQSHAYLTQKREAQEEQ-----LKKQQLLKQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 901 EQNNDsqlKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYD-FKTNNPKEAGQRLQKLQEMKEkl 979
Cdd:TIGR00618 303 TQIEQ---QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhIRDAHEVATSIREISCQQHTL-- 377
|
250 260 270
....*....|....*....|....*....|....*...
gi 110347420 980 gRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILT 1017
Cdd:TIGR00618 378 -TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
687-926 |
3.68e-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: 48.41 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 687 ELRIKENELRALEEELAGLKN--TAEKYRQ--LKQQWEMKTEEADLLQTKLQQSSYH--------KQQEELDALKKTIEE 754
Cdd:COG3096 279 ERRELSERALELRRELFGARRqlAEEQYRLveMARELEELSARESDLEQDYQAASDHlnlvqtalRQQEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 755 SEETLKNTKEIQRKAEEKYEVLENKMKNAEAERER---ELKDAQKKLDCAKTKADA---SSKKMKEKQQEVEAITLELEE 828
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSlksQLADYQQALDVQQTRAIQyqqAVQALEKARALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 829 LKREHTSYKQQLEAVNEAIKSYESQIEVmaAEVAKNK-----ESVNKAQEEVTKQ------KEVIT---------AQDTV 888
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSV--ADAARRQfekayELVCKIAGEVERSqawqtaRELLRryrsqqalaQRLQQ 516
|
250 260 270
....*....|....*....|....*....|....*...
gi 110347420 889 IKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAED 926
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE 554
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
677-1020 |
3.88e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 677 KFQELKDVQDELRIKENELRALEEELAGLKNTAEK--YRQLKQQWEMKTEEADLLQTKLQQS--SYHKQQEELDALKKTI 752
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNnkIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 753 EESEetlKNTKEIQRKAEEKYEVLEnKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 832
Cdd:TIGR04523 352 TNSE---SENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 833 HTSYKQQLEAVNEAIKSYES---------------------QIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKA 891
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNqdsvkeliiknldntresletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 892 KYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNS------AYDFKTNNPKEA 965
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieelkqTQKSLKKKQEEK 587
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347420 966 GQRLQKLQEMKEKLGRNVNMRAMNV------LTEAEERYNDLMKKKRIVENDKSKILTTIE 1020
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKEKKIsslekeLEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
23-376 |
4.10e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 23 FDPLFNAITGLNGSGKSNILDSICFLLGisnlsqVRASnlQDLVyKNGQAgitKASVSITFDNSDKKQ-----SPLGFEV 97
Cdd:COG0497 20 FGPGLTVLTGETGAGKSILLDALGLLLG------GRAD--ASLV-RHGAD---KAEVEAVFDLSDDPPlaawlEENGLDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 98 HD-EITVTRQVVIGGRNKYLINGVNANNTRVQDLFcsvglnvnnpHFLI-MQG-----RItkvlnMKPPEILSMIEEAAG 170
Cdd:COG0497 88 DDgELILRREISADGRSRAFINGRPVTLSQLRELG----------ELLVdIHGqhehqSL-----LDPDAQRELLDAFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 171 TR--MYEYKkiAAQKTIEKKEAKLKEIKTILEEeitptiqklKEERSSYLEYQkvMREIEHLSRLYIAYQFLLAEDTKVR 248
Cdd:COG0497 153 LEelLEEYR--EAYRAWRALKKELEELRADEAE---------RARELDLLRFQ--LEELEAAALQPGEEEELEEERRRLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 249 SAEELKEmqdKVIKLQEELSEND----KKIKALNHEIEELEkRKDKETGGILRSLEDALAEAQ----------------- 307
Cdd:COG0497 220 NAEKLRE---ALQEALEALSGGEggalDLLGQALRALERLA-EYDPSLAELAERLESALIELEeaaselrryldslefdp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 308 ----RVNTKSQSAFDLKKKN-------LACEESKRKELEK--NMVEDSKTLAAKEKEVKKITDGL-HALQEASNKDAEAL 373
Cdd:COG0497 296 erleEVEERLALLRRLARKYgvtveelLAYAEELRAELAEleNSDERLEELEAELAEAEAELLEAaEKLSAARKKAAKKL 375
|
...
gi 110347420 374 AAA 376
Cdd:COG0497 376 EKA 378
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
740-841 |
4.90e-05 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 44.10 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 740 KQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEV 819
Cdd:pfam13863 3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|..
gi 110347420 820 EAITLELEELKREHTSYKQQLE 841
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLE 104
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-308 |
5.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 181 AQKTIEKKEAKLKEIKT-----ILEEEITPTIQKLKEERSSYLEYQKVMREIEH--------LSRLYIAYQFLLAEDTKV 247
Cdd:COG3206 187 LRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEArlaalraqLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347420 248 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQR 308
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA 327
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-472 |
5.63e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 47.42 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 3 IKSII-LEGFKSYAQRTEVNGFDPLfNAITGLNGSGK---SNILDSICfllgisnlsqvrasnlqdlvyKNGQAGITKAS 78
Cdd:COG4694 2 ITKIKkLKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE---------------------LGDTSSEVIAE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 79 VSITFDNSDKKQSPLGF-------EVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLfcSVGLNVNNPHFLIMQGRIT 151
Cdd:COG4694 60 FEIEAGGSAPNPSVRVFnrdfveeNLRSGEEIKGIFTLGEENIELEEEIEELEKEIEDL--KKELDKLEKELKEAKKALE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 152 KVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEK-------------KEAKLKEIKTILEEEITPTIQKLKEERSSYL 218
Cdd:COG4694 138 KLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSAlksssedelkeklKLLKEEEPEPIAPITPLPDLKALLSEAETLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 219 EYQKVMREIEHLSRLyiayQFLLAEDTKVRSAEELKEMQDKVI------KLQEEL---------SENDKKIKALNHEIEE 283
Cdd:COG4694 218 EKSAVSSAIEELAAL----IQNPGNSDWVEQGLAYHKEEEDDTcpfcqqELAAERiealeayfdDEYEKLLAALKDLLEE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 284 LEKRKDKETGGILRSLEDALAEA-QRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAakeKEVKKITDGLHAL 362
Cdd:COG4694 294 LESAINALSALLLEILRTLLPSAkEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELL---DELNDLIAALNAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 363 QEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAGQmmacKNDISKAQTEAKQAQmKLKHAQQELKNKQAEVKKmds 442
Cdd:COG4694 371 IEEHNAKIANLKAEKE--EARKKLEAHELAELKEDLSRY----KAEVEELIEELKTIK-ALKKALEDLKTEISELEA--- 440
|
490 500 510
....*....|....*....|....*....|
gi 110347420 443 gyrkdqeALEAVKRLKEKLEAEMKKLNYEE 472
Cdd:COG4694 441 -------ELSSVDEAADEINEELKALGFDE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
743-947 |
5.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 743 EELDALKKTIEESEETLKNTKEIQRKAEEkyevLENKMKNAEAERErELKDAQKKLDCAKTKADASsKKMKEKQQEVEAI 822
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELE-ELREELEKLEKLLQLLPLY-QELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 823 TLELEELKREHTSYKQQLEavneaiksyesQIEVMAAEVAKNKESVNKAQEEVTKQKEvitaqdtvikakyAEVAKHKEQ 902
Cdd:COG4717 145 PERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLSLATE-------------EELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110347420 903 NNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHL 947
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
263-503 |
6.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 263 LQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRvntksqsafdlkKKNLACEESKRKELEKNMVEDS 342
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE--------LEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 343 KTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMK 422
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELA--------ELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 423 LKHAQQELKNK-QAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMKKLNyeenkeeSLLEKRRQLSRDIGRLKETYE 497
Cdd:COG3206 296 LRAQIAALRAQlQQEAQRILASLEAELEALQAreasLQAQLAQLEARLAELP-------ELEAELRRLEREVEVARELYE 368
|
....*.
gi 110347420 498 ALLARF 503
Cdd:COG3206 369 SLLQRL 374
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
711-945 |
6.48e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 711 KYRQLKQQWEMKTEEADLLQTKLQqsSYHKQQEELDAlkktieeseetlKNTKEIQRKaEEKYEVLENKMKNAEAERErE 790
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIK--TYNKNIEEQRK------------KNGENIARK-QNKYDELVEEAKTIKAEIE-E 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 791 LKDaqKKLDCAKTKADASSKkMKEKQQEVEAITLELEELKREHTSY---------KQQLEAVNEAIKSYESQIevmaAEV 861
Cdd:PHA02562 239 LTD--ELLNLVMDIEDPSAA-LNKLNTAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITKIKDKL----KEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 862 AKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWI 941
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
....
gi 110347420 942 NAER 945
Cdd:PHA02562 392 VKTK 395
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
669-912 |
7.10e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 669 SQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNT-AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQ--EEL 745
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDElNAQVKELREEAQELREKRDELNEKVKELKEERDElnEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 746 DALKKTIEESEETLKNTKEIQR---KAEEKYEVLENKMKNA----EAERE--RELKDAQKKLDCAKtKADASSKKMKEKQ 816
Cdd:COG1340 88 NELREELDELRKELAELNKAGGsidKLRKEIERLEWRQQTEvlspEEEKElvEKIKELEKELEKAK-KALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 817 QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEV 896
Cdd:COG1340 167 AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
250
....*....|....*.
gi 110347420 897 AKHKEQNNDSQLKIKE 912
Cdd:COG1340 247 KKLRKKQRALKREKEK 262
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
698-821 |
7.50e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 698 LEEELAGLkntAEKYRQLKQQW---EMKTEEADLLQTKLQQSsYHKQQEELDALKKTIEES-EETLKNTKEiqRKAEEKY 773
Cdd:PRK00409 518 LNELIASL---EELERELEQKAeeaEALLKEAEKLKEELEEK-KEKLQEEEDKLLEEAEKEaQQAIKEAKK--EADEIIK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 110347420 774 EVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
679-885 |
9.22e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEElagLKNTAEKYRQLKQQW---------------EMKTEEADLLQTKLQQSSYHKQ-- 741
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQ---EQQQRSQLEQAKEGLsalnrllprlnlladETLADRVEEIREQLDEAEEAKRfv 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 742 --------------------QEELDALKKTIEESEETLKNTKE--------IQRKAEEKY--------------EVLENK 779
Cdd:PRK04863 914 qqhgnalaqlepivsvlqsdPEQFEQLKQDYQQAQQTQRDAKQqafaltevVQRRAHFSYedaaemlaknsdlnEKLRQR 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 780 MKNAEAERER---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVEAITL----ELEELKREHTS-YKQQLEAVN 844
Cdd:PRK04863 994 LEQAEQERTRareQLRQAQAQLAqynqvlaSLKSSYDAKRQMLQELKQELQDLGVpadsGAEERARARRDeLHARLSANR 1073
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 110347420 845 EAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 885
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
679-880 |
1.05e-04 |
|
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: 45.02 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEA-DLLQTKLQQ-SSYHKQQEELDALKKTIEES- 755
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTeERLAEALEKlEEAEKAADESERGRKVLENRa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 756 ----------EETLKNTKEIQRKAEEKYEVLENKMKNAEAERERelkdaqkkldcAKTKADASSKKMKEKQQEVEAIT-- 823
Cdd:pfam00261 88 lkdeekmeilEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-----------AEERAELAESKIVELEEELKVVGnn 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347420 824 ---LELEELK---REHtSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 880
Cdd:pfam00261 157 lksLEASEEKaseRED-KYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-446 |
1.11e-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: 45.91 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAE----AQRVNTKSQSAF 317
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-ELRAELEAQKEELAEllraLYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 318 DLKKKNLAcEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAT 397
Cdd:COG4942 125 LLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110347420 398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRK 446
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
171-507 |
1.58e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 171 TRMYEYKKIAAQKTIEKKEAKLKEI---KTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKv 247
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 248 rsAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK--------RKDKETGGILRSLEDALAE--AQRVNTKSQSAF 317
Cdd:PRK03918 451 --KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeselIKLKELAEQLKELEEKLKKynLEELEKKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 318 DLKKK---------NLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLS 388
Cdd:PRK03918 529 KLKEKliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 389 SNEDGAEATLAgQMMACKNDISKAQTE------------AKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKR 456
Cdd:PRK03918 609 DAEKELEREEK-ELKKLEEELDKAFEElaetekrleelrKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 110347420 457 LKEKLEAEMKKLnyEENKEEslLEKRRQLSRDIGRLKETYEALLARFPNLR 507
Cdd:PRK03918 688 RREEIKKTLEKL--KEELEE--REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-503 |
1.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 161 ILSMIEEAAGTRMYEY------KKIAAQKTIEKKEAKLKEIKTILEE--EITPTIQKLKEE----RSSYLEYQKVMREIE 228
Cdd:COG4717 43 IRAMLLERLEKEADELfkpqgrKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEEleelEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 229 HLSRLYIAYQFLLAEDTKVRS----AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALA 304
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAElperLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 305 EAQRVNTKSQSAFDLKKKNLaceESKRKELEKnmVEDSKTLAAKEKEVKKITDGLHALqeasnkdaeALAAAQQHFNAVS 384
Cdd:COG4717 203 ELQQRLAELEEELEEAQEEL---EELEEELEQ--LENELEAAALEERLKEARLLLLIA---------AALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 385 AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK-----MDSGYRKDQEALEAVKRLKE 459
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 110347420 460 --KLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARF 503
Cdd:COG4717 349 lqELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1062-1143 |
1.97e-04 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.02 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1062 QTVLDGLEFKVALGNtwkENLtelSGGQRSLVALSLILsmllFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFI 1141
Cdd:cd03244 123 ESLPGGLDTVVEEGG---ENL---SVGQRQLLCLARAL----LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVL 192
|
..
gi 110347420 1142 VV 1143
Cdd:cd03244 193 TI 194
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
679-856 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLlQTKLQQ--SSYHKQQEELDALKKTIEESE 756
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAElsARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 757 EtlkntkEIQRKAEEKYEVLENKMKNAEAeRERELKDAQKKLDcaktkadASSKKMKEKQQEVEAITLELEELKREHTSY 836
Cdd:COG3206 305 A------QLQQEAQRILASLEAELEALQA-REASLQAQLAQLE-------ARLAELPELEAELRRLEREVEVARELYESL 370
|
170 180
....*....|....*....|
gi 110347420 837 KQQLEAVNEAIKSYESQIEV 856
Cdd:COG3206 371 LQRLEEARLAEALTVGNVRV 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-507 |
2.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 199 LEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE---DTKVRSAEELKEMQDKVIKLQEELSENDKKIK 275
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 276 ALNHEIEELEKRKDK-ETGGILRSLEDALAEAQRV------------NTKSQSAFDLKKKNLAC-----------EESKR 331
Cdd:COG4717 217 EAQEELEELEEELEQlENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFlvlgllallflLLARE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 332 KELEKNMVEDSKTLAAKE----KEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEdgAEATLAGQMMACKN 407
Cdd:COG4717 297 KASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE--EELQLEELEQEIAA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 408 DISKAQTEAKQA-QMKLKHAQ--QELKNKQAEVKKMDSGYRKDQEALEAV---KRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:COG4717 375 LLAEAGVEDEEElRAALEQAEeyQELKEELEELEEQLEELLGELEELLEAldeEELEEELEELEEELEELEEELEELREE 454
|
330 340
....*....|....*....|....*...
gi 110347420 482 RRQLSRDIGRLKE--TYEALLARFPNLR 507
Cdd:COG4717 455 LAELEAELEQLEEdgELAELLQELEELK 482
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
680-912 |
2.72e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 680 ELKDVQDELRIKENELRALEEELAGLKNTaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 759
Cdd:NF033838 175 ELEIAESDVEVKKAELELVKEEAKEPRDE-EKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 760 KNTKEIQRKAEEKYEVL---------ENKMKNAEA------------ERERELKDAQKKLDCAKTKADASSKKMKEKQQE 818
Cdd:NF033838 254 ATSEQDKPKRRAKRGVLgepatpdkkENDAKSSDSsvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 819 VEAITLELEELKREHTSYKQQLEAVNEAIKSyesqievmaaevAKNKESVNKAQEEVTKQKEVITAQDTVI--KAKYAEV 896
Cdd:NF033838 334 NTYKTLELEIAESDVKVKEAELELVKEEAKE------------PRNEEKIKQAKAKVESKKAEATRLEKIKtdRKKAEEE 401
|
250
....*....|....*.
gi 110347420 897 AKHKEQNNDsqlKIKE 912
Cdd:NF033838 402 AKRKAAEED---KVKE 414
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1081-1120 |
2.81e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.94 E-value: 2.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110347420 1081 NLTELSGGQRSLVALSLILSmllfKPAPIYILDEVDAALD 1120
Cdd:cd03237 112 EVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLD 147
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-934 |
2.89e-04 |
|
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: 45.11 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 677 KFQELKdvQDELRiKENELRALEEELAGLKNTAEKYRQLK---------QQWEMKTE-EADLLQTKLQQSSYHKQQEELD 746
Cdd:pfam17380 292 KFEKME--QERLR-QEKEEKAREVERRRKLEEAEKARQAEmdrqaaiyaEQERMAMErERELERIRQEERKRELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 747 ALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLEL 826
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 827 EELKREHTSYKQQLeavnEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTK--QKEVITAQDTVIKAKYAEVAKHKEQnN 904
Cdd:pfam17380 449 ERVRLEEQERQQQV----ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEM-E 523
|
250 260 270
....*....|....*....|....*....|
gi 110347420 905 DSQLKIKEldhniSKHKREAEDGAAKVSKM 934
Cdd:pfam17380 524 ERQKAIYE-----EERRREAEEERRKQQEM 548
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
689-885 |
2.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 689 RIKENELRALEEELAGL----KNTAEKYRQLKQQwEMKtEEADLLQTKLQQSsYHKQQEELDALKKTIEESEETLKNTKE 764
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALL-EAK-EEIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 765 IQRKAEEKyevLENKMKNAEaERERELKDAQKKLDcaktkadassKKMKEKQQEVEAITleleELKREhtsykqqlEAVN 844
Cdd:PRK12704 104 LLEKREEE---LEKKEKELE-QKQQELEKKEEELE----------ELIEEQLQELERIS----GLTAE--------EAKE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110347420 845 EAIKSYESQIEVMAAEVAKNKEsvNKAQEEVTKQKEVITAQ 885
Cdd:PRK12704 158 ILLEKVEEEARHEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
201-926 |
3.17e-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: 45.21 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 201 EEITPTIQKLKEERSSYLEyqkVMREIEHLSRLYIAYQFLLAEDTKVRSA------EEL----KEMQDKVIKLQEELSEN 270
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLES---AELRLSHLHFGYKSDETLIASRQEERQEtsaelnQLLrtldDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 271 DKKIKALNHEIEELEKRKdketggilRSLEDALAEaqrvntksQSAFDLKKknlacEESKRKELEkNMVEDSKTLAAKEK 350
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH--------GAFLDADIE--------TAAADQEQ-----LPSWQSELE-NLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 351 EVKKITDGLHALQEASNKDaeALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQEL 430
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 431 KNKQAEV----------KKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN-YEENKEESLLEKRRQLSRDIGRLKETYEAL 499
Cdd:pfam12128 450 KLRLNQAtatpelllqlENFDERIERAREEQEAANAEVERLQSELRQARkRRDQASEALRQASRRLEERQSALDELELQL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 500 LARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGER-LYNVVVD---TEVTGKKLLERgELKRRyti 575
Cdd:pfam12128 530 FPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELnLYGVKLDlkrIDVPEWAASEE-ELRER--- 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 576 iplnkisaRCIAPETLRVAQNLVGPDNVHVALSLVEYKpELQKAMEfvFGTTFVCDNMDNAKKVAFDKRIMTRTVTlggd 655
Cdd:pfam12128 606 --------LDKAEEALQSAREKQAAAEEQLVQANGELE-KASREET--FARTALKNARLDLRRLFDEKQSEKDKKN---- 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 656 vfdphgtlsggaRSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQ---WEMKTEEADLLQTK 732
Cdd:pfam12128 671 ------------KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvveGALDAQLALLKAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 733 LQQSSYHKQQeeLDALKKtieeseetlKNTKEIQRKAEEKYEVlenkmknaeAERERELKDAQKKL-DCAKTKADASSKK 811
Cdd:pfam12128 739 AARRSGAKAE--LKALET---------WYKRDLASLGVDPDVI---------AKLKREIRTLERKIeRIAVRRQEVLRYF 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 812 --MKEK-QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEvmaaevaKNKESVNKAQEEVTkqkEVITAQDTV 888
Cdd:pfam12128 799 dwYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE-------MERKASEKQQVRLS---ENLRGLRCE 868
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 110347420 889 IKaKYAEVAKHKEqNNDSQLKIKE----LDHNISKHKREAED 926
Cdd:pfam12128 869 MS-KLATLKEDAN-SEQAQGSIGErlaqLEDLKLKRDYLSES 908
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1079-1144 |
3.41e-04 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 42.76 E-value: 3.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 1079 KENLteLSGGQRSLVALSLilsMLLfKPAPIYILDEVDAALDlSHTQN-IGQMLRTHFTHSQFIVVS 1144
Cdd:cd03228 93 RENI--LSGGQRQRIAIAR---ALL-RDPPILILDEATSALD-PETEAlILEALRALAKGKTVIVIA 152
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
708-936 |
3.55e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.04 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 708 TAEKYRQLKQQWEMKTEEADLLQTKLQQSSYhkqQEELDALKKTIEESEETLKNTKEIQRKAEEKyevlenKMKNAEAER 787
Cdd:PTZ00108 1100 TKEKVEKLNAELEKKEKELEKLKNTTPKDMW---LEDLDKFEEALEEQEEVEEKEIAKEQRLKSK------TKGKASKLR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 788 ERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEaiksyESQIEVMAAEVAKNKES 867
Cdd:PTZ00108 1171 KPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDD-----EEQKTKPKKSSVKRLKS 1245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 868 VNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHK-REAEDGAAKVSKMLK 936
Cdd:PTZ00108 1246 KKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGsKPSSPTKKKVKKRLE 1315
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
144-468 |
3.86e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 144 LIMQGRITKVLNMKPPEILSMIEEAAGT--------RMYEYKKiAAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKE 212
Cdd:PRK10246 152 LLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHK-SARTELEKLQAQASGVALLTPEQvqsLTASLQVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 213 ERSSYLEYQKVM-REIEHLSRLYIAYQFLLAEDTKVRSA-EELKEMQDKVIKLqeELSENDKKIKALNHEIEELEKRkdk 290
Cdd:PRK10246 231 EEKQLLTAQQQQqQSLNWLTRLDELQQEASRRQQALQQAlAAEEKAQPQLAAL--SLAQPARQLRPHWERIQEQSAA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 291 etggilrsLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK------EVKkitdGLHALQE 364
Cdd:PRK10246 306 --------LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnELA----GWRAQFS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 365 ASNKDAEALAAAQQHFNAVSAGLS---------SNEDGAEA--------TLAGQMMACKNDISKAQTEAKQAQMKLKHAQ 427
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNalpaitltlTADEVAAAlaqhaeqrPLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 110347420 428 QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEkLEAEMKKL 468
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDL 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-392 |
4.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 182 QKTIEKKEAKLKEIKTILEE--EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE----DTKVRSAE---- 251
Cdd:COG4913 606 FDNRAKLAALEAELAELEEElaEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaelEAELERLDassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 252 ELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggilrsLEDALAEAQRVNTKSQSAFDLKKKNLaceeskR 331
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LEQAEEELDELQDRLEAAEDLARLEL------R 748
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 332 KELEKnMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNA--------VSAGLSSNED 392
Cdd:COG4913 749 ALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadLDADLESLPE 816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-462 |
5.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 175 EYKKIAAQ-KTIEKKEAKLKEIKTILEEEIT--PTIQKLKEERSSYLEYQKVMREI--EHLSRLYIAYQFLLAEDTKVRS 249
Cdd:PRK03918 460 ELKRIEKElKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEKLKKYnlEELEKKAEEYEKLKEKLIKLKG 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 250 --------AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKsqsafdlkK 321
Cdd:PRK03918 540 eikslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA--------E 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQeaSNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagq 401
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEE----- 684
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347420 402 mmackndISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE 462
Cdd:PRK03918 685 -------LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1082-1132 |
5.15e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 5.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 110347420 1082 LTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:PRK11231 136 LTDLSGGQRQRA----FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1084-1144 |
5.28e-04 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 43.09 E-value: 5.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347420 1084 ELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLRT-HFTHSQFIVVS 1144
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAM---EP-EVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVT 191
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
667-945 |
5.38e-04 |
|
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: 44.19 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 667 ARSQAASILTKfQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSsyHKQQEELD 746
Cdd:TIGR00618 201 LRSQLLTLCTP-CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE----AQEEQLKKQQLLKQL--RARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 747 ALKKTIEESEETL-------------KNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMK 813
Cdd:TIGR00618 274 AQEAVLEETQERInrarkaaplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 814 EK--QQEVEAITLELEELKREHT------SYKQQLEAVNEAIKSYESQIEVMAAEVAknKESVNKAQEEVTKQKEVITAQ 885
Cdd:TIGR00618 354 EIhiRDAHEVATSIREISCQQHTltqhihTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHAKK 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347420 886 DTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHK-REAEDGAAKVSKMLKDYDWINAER 945
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQIHLQETRKKAVV 492
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
785-945 |
5.47e-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: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 785 AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKN 864
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 865 KESVNKAQ------------EEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 932
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170
....*....|...
gi 110347420 933 KMLKDYDWINAER 945
Cdd:COG3883 179 EQEALLAQLSAEE 191
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-378 |
5.74e-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: 43.60 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 180 AAQKTIEKKEAKLKEIKtileEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaedtkvrsaEELKEMQDK 259
Cdd:COG4942 17 AQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALE----------------------RRIAALARR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 260 VIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI-------------------------------------------- 295
Cdd:COG4942 71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaparre 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 296 -LRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALA 374
Cdd:COG4942 151 qAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
....
gi 110347420 375 AAQQ 378
Cdd:COG4942 231 RLEA 234
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
682-900 |
6.03e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 682 KDVQDELRIKENELRALEEELAGLKNTAEkyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQ-----EELDALKKTIEESE 756
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIE--EQRKKNGENIARKQNKYDELVEEAKTIKAEieeltDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 757 ETLK--NTKEIQRKAE-----------EKYEVLENKMKNAEAERER------ELKDAQKKLDCAKTKADasskKMKEKQQ 817
Cdd:PHA02562 255 AALNklNTAAAKIKSKieqfqkvikmyEKGGVCPTCTQQISEGPDRitkikdKLKELQHSLEKLDTAID----ELEEIMD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 818 EVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKqkevitaqdtvIKAKYAEVA 897
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK-----------IVKTKSELV 399
|
...
gi 110347420 898 KHK 900
Cdd:PHA02562 400 KEK 402
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
665-880 |
6.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 665 GGARSQAASILTKFQELKDVQDELRikeNELRALEEELAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQQSSYHK 740
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELR---EEAAELESELEEAREAVEDRReeieELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 741 Q--QEELDALKKTIEESEETLKNTKEIQRKAE----------------------------EKYEVLENKMKNAEAERER- 789
Cdd:PRK02224 415 EelREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEv 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 790 --------ELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEV 861
Cdd:PRK02224 495 eerleraeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250
....*....|....*....
gi 110347420 862 AknkeSVNKAQEEVTKQKE 880
Cdd:PRK02224 575 A----ELNSKLAELKERIE 589
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
641-874 |
6.23e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 641 FDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENeLRALEEELAGLKNTAEKYRQlkqqwe 720
Cdd:cd22656 63 FKDDTYPSIVSLAGDIYNYAQNAGGTIDSYYAEILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQD------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 721 mkteEADLLQTKLQ--QSSYHKQQEELDALKKTI------EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELK 792
Cdd:cd22656 136 ----KAAKVVDKLTdfENQTEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 793 DAQKKLDcAKTKADASSKKMKEK----QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEvmAAEVAKNKesV 868
Cdd:cd22656 212 DDEAKLA-AALRLIADLTAADTDldnlLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIP--AAILAKLE--L 286
|
....*.
gi 110347420 869 NKAQEE 874
Cdd:cd22656 287 EKAIEK 292
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
679-862 |
6.45e-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: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGLKNT-AEKYRQLKQQWE---MKTEEADLLQTKLQQSSYHKQQEELDALKKTIEE 754
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARalyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 755 SEETLKNTKEIQRKAEEKYEVLENKMKNAEAERErELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHT 834
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKA-ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
170 180
....*....|....*....|....*...
gi 110347420 835 SYKQQLEAVNEAIKSYESQIEVMAAEVA 862
Cdd:COG3883 210 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
677-812 |
6.52e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 677 KFQELK-DVQDELRIKENELRALEEELaglkntAEKYRQLKQQWE-MKTEEADLLQtklQQSSYHKQQEELDALKKTIEE 754
Cdd:PRK12704 65 EIHKLRnEFEKELRERRNELQKLEKRL------LQKEENLDRKLElLEKREEELEK---KEKELEQKQQELEKKEEELEE 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347420 755 SEETLKntKEIQR-----KAEEKYEVLENKMKNAEAERERELKDAQKKldcAKTKADASSKKM 812
Cdd:PRK12704 136 LIEEQL--QELERisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEE---AKEEADKKAKEI 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-467 |
8.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE--------LEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 322 KNLACE-----ESKRKELEKNMVEDSKTLAAkekevkkITDGLHALQEASNKDAEALAAAQQhfnavsaglssnedgAEA 396
Cdd:COG3883 86 EELGERaralyRSGGSVSYLDVLLGSESFSD-------FLDRLSALSKIADADADLLEELKA---------------DKA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347420 397 TLAGQmmacKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKK 467
Cdd:COG3883 144 ELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-301 |
8.30e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 27 FNAITGLNGSGKSNILDSICFLLGIsnlsqvrASNLQDLVYKNGQAGITKASVSITFDNSDKKqsPLGFEVHdeitvtrq 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADF-------DALVIGLTDERSRNGGIGGIPSLLNGIDPKE--PIEFEIS-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 107 vviggrnKYLINGVNAnntrvqdlfcSVGLNVNNPHFLimqgritkvlnmkppEILSMIEEAAGTRMYEYKKIAaqKTIE 186
Cdd:pfam13304 64 -------EFLEDGVRY----------RYGLDLEREDVE---------------EKLSSKPTLLEKRLLLREDSE--EREP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 187 KKEAKLKEIKTILEEEItpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEE 266
Cdd:pfam13304 110 KFPPEAEELRLGLDVEE--RIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR 187
|
250 260 270
....*....|....*....|....*....|....*....
gi 110347420 267 LS----ENDKKIKALNHEIEELEKRKDKETGGILRSLED 301
Cdd:pfam13304 188 LVrglkLADLNLSDLGEGIEKSLLVDDRLRERGLILLEN 226
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
674-909 |
8.42e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 674 ILTKFQELKDVQDELRIKENELRALEEELAGLKNTAE--KYRQLKQQWEMKTEEADLL----QTKLQQSSYHKQQEELDA 747
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlNDKLKKNKDKINKLNSDLSkinsEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 748 LKKTIEESEETL-KNTKEIQRKAEE------KYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASS------KK 811
Cdd:TIGR04523 129 LEKQKKENKKNIdKFLTEIKKKEKEleklnnKYNDLKKQKEELENELnllEKEKLNIQKNIDKIKNKLLKLElllsnlKK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 812 MKEKQQEVEAITLELEE----LKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVI---TA 884
Cdd:TIGR04523 209 KIQKNKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIkelEK 288
|
250 260
....*....|....*....|....*
gi 110347420 885 QDTVIKAKYAEVAKHKEQNNDSQLK 909
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELK 313
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
175-350 |
8.65e-04 |
|
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: 43.57 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 175 EYKKIAAQKTIE----KKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQ----KVMREIEHLSRLYI-------AYQF 239
Cdd:pfam17380 338 EQERMAMEREREleriRQEERKRELERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVKIleeerqrKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 240 LLAEDTKVRSAEElKEMQDKVIKLQEELSENDKKIK----ALNHEIEEL----EKRKDKETGGILRSLEDALAEAQRVNT 311
Cdd:pfam17380 418 QKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRleeqERQQQVERLrqqeEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
170 180 190
....*....|....*....|....*....|....*....
gi 110347420 312 KSQSaFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK 350
Cdd:pfam17380 497 LEKE-LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
724-1006 |
9.28e-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: 43.67 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 724 EEADLLQTKLQ-QSSYHKQQEE--------LDALKKTIEESEETLKNTKEIQRKaeekyevLENKMKNAEAERERELKDA 794
Cdd:pfam12128 604 ERLDKAEEALQsAREKQAAAEEqlvqangeLEKASREETFARTALKNARLDLRR-------LFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 795 QKKLDCAKTKADASSKKMKEKQQEVEAitlELEELKREHTSYKQQ-LEAVNEAIKSYESQIevmaaevaknkesvnkaqe 873
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLE---EQKEQKREARTEKQAyWQVVEGALDAQLALL------------------- 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 874 evtkqKEVITAQDTVIKAKyaevAKHKEQNNDSQLKIKELD-HNISKHKREAEDGAAKVSKMLKD----YDWINAERHLF 948
Cdd:pfam12128 735 -----KAAIAARRSGAKAE----LKALETWYKRDLASLGVDpDVIAKLKREIRTLERKIERIAVRrqevLRYFDWYQETW 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347420 949 GQPNSAYDFKTNNPKEAGQRLQ---KLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKR 1006
Cdd:pfam12128 806 LQRRPRLATQLSNIERAISELQqqlARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
775-895 |
9.34e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 775 VLENKMKNAEAERERELKDAQKKLDCAKtkadasSKKMKEKQQEVEAITLELEelkREHTSYKQQLEAVNEAIKSYESQI 854
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK------KEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 110347420 855 EVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAE 895
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
687-864 |
9.64e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 687 ELRIKENELRALEEELAGLKNT--AEKYR--QLKQQWEMKTEEADLLQTKLQQSSYHKQ---------------QEELDA 747
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQlaAEQYRlvEMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqekieryQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 748 LKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAererELKDAQKKLDCAKTKADA---SSKKMKEKQQEVEAITL 824
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS----QLADYQQALDVQQTRAIQyqqAVQALERAKQLCGLPDL 435
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110347420 825 ELEELKREHTSYKQQLEAVNEAIKSYESQIEVmaAEVAKN 864
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSV--AQAAHS 473
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
803-945 |
9.91e-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: 42.22 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 803 TKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKEsvnkAQEEVTKQKEvi 882
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----QLGNVRNNKE-- 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347420 883 taqdtvIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAER 945
Cdd:COG1579 91 ------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
667-873 |
1.07e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 667 ARSQAASILTKF--QELKDVQDELRIKENELRALEEElAGLKNTAEKYRQLKQQweMKTEEADLLQTKLQQSSYHKQQEE 744
Cdd:COG3206 168 LRREEARKALEFleEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 745 LDALKKTIEESEETLKNTKEIQRkaeekyevLENKMKNAEAERER----------ELKDAQKKLdcaktkADASSKKMKE 814
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQ--------LRAQLAELEAELAElsarytpnhpDVIALRAQI------AALRAQLQQE 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 815 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSY---ESQIEVMAAEVAKNKES----VNKAQE 873
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELyeslLQRLEE 376
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
696-945 |
1.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 696 RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETLKNTKEIQRKAEEKYEV 775
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 776 LENKMKNAEAERER---ELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA-----VNEAI 847
Cdd:COG4372 106 LQEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 848 KSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEV-AKHKEQNNDSQLKIKELDHNISKHKREAED 926
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAlSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250
....*....|....*....
gi 110347420 927 GAAKVSKMLKDYDWINAER 945
Cdd:COG4372 266 AILVEKDTEEEELEIAALE 284
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-420 |
1.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETggilRSLEDALAEAQR-----------VNTKSQSAFDL 319
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR----EELGERARALYRsggsvsyldvlLGSESFSDFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 320 KKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180
....*....|....*....|.
gi 110347420 400 GQMMACKNDISKAQTEAKQAQ 420
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
807-931 |
1.19e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 807 ASSKKMKEKQQEVEAITLELEELKREhtsYKQQLEAVNEAIKSYESQIEVMAaevaknKESVNKAQEEVtkqKEVITAQD 886
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEAEKEA------QQAIKEAKKEA---DEIIKELR 594
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 110347420 887 TVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV 931
Cdd:PRK00409 595 QLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-298 |
1.47e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.59 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSIcfllgisnlsqvrasnlqDLVYKNGQAGITKASVS 80
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEID-LDEDLTVLIGKNNSGKSSILEAL------------------DIFLNNKEKFFEDDFLV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 81 ITFDNSDKKQSPLgFEVHDEITVTRQVVI-----GGRNKYLINGVNANNTRvQDLFCSVGLNVNNPHFLIMQGRITKVLN 155
Cdd:pfam13175 61 LYLKDVIKIDKED-LNIFENISFSIDIEIdveflLILFGYLEIKKKYLCLA-SKGKAKEYEKTLHPKGANKADLLLELKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 156 MKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEakLKEIKTILEEEITPTIQKLKEE--RSSYLEYQKVMREIEHLSRL 233
Cdd:pfam13175 139 SDLKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYE--LPSLKEEFLNSEKEEIKVDKEDlkKLINELEKSINYHENVLENL 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347420 234 YIAYQFLLAE-DTKVRSAEELKEMQDKVI--KLQEELSENDKKIKALNHEIEELeKRKDKETGGILRS 298
Cdd:pfam13175 217 QIKKLLISADrNASDEDSEKINSLLGALKqrIFEEALQEELELTEKLKETQNKL-KEIDKTLAEELKN 283
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1066-1120 |
1.50e-03 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 42.78 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 110347420 1066 DGLEFKVAlgntwkENLTELSGGQRSLVALSlilsMLLFKPAPIYILDEVDAALD 1120
Cdd:TIGR02203 457 LGLDTPIG------ENGVLLSGGQRQRLAIA----RALLKDAPILILDEATSALD 501
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1085-1134 |
1.52e-03 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 41.31 E-value: 1.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110347420 1085 LSGGQRSLVALSLilsmLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTH 1134
Cdd:COG4133 132 LSAGQKRRVALAR----LLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
248-499 |
1.53e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 248 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-----RKDKETGGILRSLEDA--LAEAQRVNTKSQSAFDLK 320
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikreKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLK 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 321 KKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHA-LQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG5022 866 KETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESeIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEG 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 400 GQMMACKNDISKAQTEAKQaqmKLKHAQQELKNkqaEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLL 479
Cdd:COG5022 946 PSIEYVKLPELNKLHEVES---KLKETSEEYED---LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK 1019
|
250 260
....*....|....*....|...
gi 110347420 480 EKRRQLSR---DIGRLKETYEAL 499
Cdd:COG5022 1020 ELPVEVAElqsASKIISSESTEL 1042
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
794-870 |
1.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 794 AQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNK 870
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
801-878 |
1.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347420 801 AKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 878
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1005 |
1.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 667 ARSQAASILTKFQELKDVQDELRIKENELRALEEELaGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELD 746
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAF-GKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 747 ALK--KTIEESEETLKNTK-------EIQRKAEEKYEVlENKMKNAEAERERELKDAQ--KKLDCAKTKAD---ASSKKM 812
Cdd:PTZ00121 1141 KAEeaRKAEDAKRVEIARKaedarkaEEARKAEDAKKA-EAARKAEEVRKAEELRKAEdaRKAEAARKAEEerkAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 813 KEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYES--------QIEVMAAEVAKNKESVNKAQE-----EVTKQK 879
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEarmahfarRQAAIKAEEARKADELKKAEEkkkadEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 880 EVITAQDTVIKAKYAEVAKH-KEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFK 958
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 110347420 959 TNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKK 1005
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1081-1132 |
1.82e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 41.57 E-value: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 110347420 1081 NLTELSGGQRSLVAlsliLSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:COG1120 134 PVDELSGGERQRVL----IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLR 181
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1062-1114 |
1.84e-03 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 39.94 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 110347420 1062 QTVLDGLEFKVALGNTWKENLTELSGGQRSLVAlsliLSMLLFKPAPIYILDE 1114
Cdd:pfam00005 99 EEALEKLGLGDLADRPVGERPGTLSGGQRQRVA----IARALLTKPKLLLLDE 147
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
681-902 |
2.08e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 681 LKDVQDELRIKENEL----RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESE 756
Cdd:PRK01156 185 IDYLEEKLKSSNLELenikKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS--SLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 757 ETLKNTKEIQRK---AEEKYEVLENKMKNAEAERERE----------LKDAQKKLDCAKTKADASSKKMKE--------- 814
Cdd:PRK01156 263 SDLSMELEKNNYykeLEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVlqkdyndyi 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 815 -KQQEVEAITLELEELKREHTSYK---QQLEAVNEAIKSYESQIEVMAAEVAK-------NKESVNKAQEEVTKQKEVIT 883
Cdd:PRK01156 343 kKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFISEilkiqeiDPDAIKKELNEINVKLQDIS 422
|
250
....*....|....*....
gi 110347420 884 AQDTVIKAKYAEVAKHKEQ 902
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDE 441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
679-811 |
2.09e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.75 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAglkNTAEKYRQLKQQWEMKTEEAdllqtKLQQSSYHKQQEELDALKKTIEESEET 758
Cdd:TIGR02794 80 AEKQRAAEQARQKELEQRAAAEKAA---KQAEQAAKQAEEKQKQAEEA-----KAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 110347420 759 LKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKK 811
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1064-1132 |
2.38e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.59 E-value: 2.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 1064 VLDGLEFkVALGNTWKENLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03235 113 VDEALER-VGLSELADRQIGELSGGQQQRV----LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-882 |
2.42e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQE------ELDALKKTI 752
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 753 EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAE-------------------RERELKDAQKKLDCAKTKADASSKKMK 813
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisdledelnkddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 814 EKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVI 882
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1059-1143 |
2.67e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1059 PEGQTVLDGLE-FKVALgNTWKENLTELSGGQRSLVALsliLSMLLFKPApIYILDEVDAALDLSHTQNIGQMLrTHFTH 1137
Cdd:PRK10247 112 PDPAIFLDDLErFALPD-TILTKNIAELSGGEKQRISL---IRNLQFMPK-VLLLDEITSALDESNKHNVNEII-HRYVR 185
|
....*.
gi 110347420 1138 SQFIVV 1143
Cdd:PRK10247 186 EQNIAV 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1084-1143 |
2.75e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.54 E-value: 2.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 1084 ELSGGQRSLVALsliLSMLLFKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:COG4136 133 TLSGGQRARVAL---LRALLAEPRAL-LLDEPFSKLDAALRAQFREFVFEQIRQRGIPAL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-481 |
3.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 239 FLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKetggilrsLEDALAEAQRvntksqsafd 318
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQA---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 319 lkkknlaceesKRKELEKNMVEDSKTLAAKEKEVKKItdgLHALQEASNK--------DAEALAAAQQHFNAVSAGLSSN 390
Cdd:COG3883 66 -----------EIDKLQAEIAEAEAEIEERREELGER---ARALYRSGGSvsyldvllGSESFSDFLDRLSALSKIADAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 391 EDgaeatLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNY 470
Cdd:COG3883 132 AD-----LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
250
....*....|.
gi 110347420 471 EENKEESLLEK 481
Cdd:COG3883 207 AAEAAAAAAAA 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-482 |
3.61e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347420 408 DISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKR 482
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
177-425 |
3.65e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 177 KKIAAQKTIEKKEAKLKEIKtILEEEITPTIQKLkEERSSYLEYQKVmreiehlsrlyiayQFLLAEDTKVRSAEELKEM 256
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFK-ILKDKKDAKIREL-EARVSDLELEKV--------------KLVNAGSERLRAVKDIKQE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 257 QDKVIKlQEELSENDKKIKALNHEI---------EELEKRKDK-------------ETGGILRSLEDALAEAQRVNTKSQ 314
Cdd:pfam15921 655 RDQLLN-EVKTSRNELNSLSEDYEVlkrnfrnksEEMETTTNKlkmqlksaqseleQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 315 SAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDA---EALAAAQQHFNAVSAGLSSNE 391
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVANMEVAL 813
|
250 260 270
....*....|....*....|....*....|....
gi 110347420 392 DGAEAtlagQMMACKNDISKAQTEAkqAQMKLKH 425
Cdd:pfam15921 814 DKASL----QFAECQDIIQRQEQES--VRLKLQH 841
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
689-885 |
3.77e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 689 RIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEE--LDALKKTIEESEETLKNTKEIQ 766
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQaaKQAEEKQKQAEEAKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 767 RKAEEKYEVLENKMKNAEAERERELK---DAQKKLDCAKTKADASSKKMKEKQQEVEAitlelEELKREHTSYKQQLEAv 843
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-----EEAKAKAEAAKAKAAA- 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110347420 844 nEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 885
Cdd:TIGR02794 208 -EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
251-501 |
3.86e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-RKDKETGG--ILRSLEDALAEAQRVNTKSQSAFD------LKK 321
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKeLTNSESENseKQRELEEKQNEIEKLKKENQSYKQeiknleSQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAE---ATL 398
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtqlKVL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 399 AGQMMACKNDISKAQTEAKQAQ---MKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEK----LEAEMKKLNYE 471
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdLEDELNKDDFE 553
|
250 260 270
....*....|....*....|....*....|
gi 110347420 472 ENKEEsLLEKRRQLSRDIGRLKETYEALLA 501
Cdd:TIGR04523 554 LKKEN-LEKEIDEKNKEIEELKQTQKSLKK 582
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
692-842 |
4.05e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 692 ENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTklqqssyhkQQEELDALK------KTIEESEETLKNTKEI 765
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRF---------QLEELEAAAlqpgeeEELEEERRRLSNAEKL 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347420 766 QRKAEEKYEVLENKMKNAEAererELKDAQKKLDcaktKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA 842
Cdd:COG0497 225 REALQEALEALSGGEGGALD----LLGQALRALE----RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF 293
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
688-878 |
4.79e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 688 LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEAdllqtklQQSSYHKQQEELDALKKTIEESEETLKNTKEIQR 767
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEK-------EEERRLDEMMEEERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 768 KAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYK----QQLEAV 843
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 110347420 844 NEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 878
Cdd:pfam13868 154 DERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
741-900 |
4.94e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 741 QQEELDALKKTIEEseetlknTKEIQRKAEEKyevleNKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:TIGR02794 56 QQQKKPAAKKEQER-------QKKLEQQAEEA-----EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 821 AITLELEELKREHTSYKQQlEAVNEAIKSYESQIEVMAAEVAKNK--ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAK 898
Cdd:TIGR02794 124 AKAKQAAEAKAKAEAEAER-KAKEEAAKQAEEEAKAKAAAEAKKKaeEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAK 202
|
..
gi 110347420 899 HK 900
Cdd:TIGR02794 203 AK 204
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
696-855 |
5.23e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 696 RALEEELAGLKNTAEKYRQLKQQWEMKTEEadlLQTKLQQssyhkQQEELDALKKTIEESE---ETLKNTKEIQRKAEEK 772
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEKLMSEIQQENKR---LTEPLQK-----AQEEVEELRKQLENYEkdkQSLKNLKARLKVLEKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 773 -------YEVLENKMKNAEAER-------ERELKDAQKKLDCaktKADASSKKMKEKQQEVEAITLELEELKR----EHT 834
Cdd:pfam13851 101 lkdlkweHEVLEQRFEKVERERdelydkfEAAIQDVQQKTGL---KNLLLEKKLQALGETLEKKEAQLNEVLAaanlDPD 177
|
170 180
....*....|....*....|.
gi 110347420 835 SYKQQLEAVNEAIKSYESQIE 855
Cdd:pfam13851 178 ALQAVTEKLEDVLESKNQLIK 198
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
256-477 |
6.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 256 MQDKVIKLQEELSENDKKIKALNHEIEELEKrKDKETGGILRSLEDALAEAQRVntksqsafdlkkknlacEESKRKELE 335
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQT-DSSNTDTALTTLEEALSEKERI-----------------IERLKEQRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 336 KNMVEDSKTLAAKEKEVKKITDGLHALQ-EASNKDAEALAAAQQHFNAVSAGLssNEDGAEATLAGQMMACKNDISKAQT 414
Cdd:pfam10174 461 REDRERLEELESLKKENKDLKEKVSALQpELTEKESSLIDLKEHASSLASSGL--KKDSKLKSLEIAVEQKKEECSKLEN 538
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347420 415 EAKQAQM-------------KLKHAQQELKNKQAEVKKMDSGYRKDQEAL---EAVKRLKEKLEAEMKKLNYEENKEES 477
Cdd:pfam10174 539 QLKKAHNaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILrevENEKNDKDKKIAELESLTLRQMKEQN 617
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
667-884 |
6.66e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 667 ARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTaekyrqlkqQWEMKTEEADLLQTKLQQSSYHKQQEELD 746
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT---------SWLNALAVISLIDIETNRSRSNEIKKQLN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 747 ALKKTIEESEETLKNTKEIQ----RKAEEKYEVLENKMKNAEaERERELKDAQKKLDCAKTKadasSKKMKEKQQEVEAI 822
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSYIdksiREIENEANNLNNKYNEIQ-ENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEI 672
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347420 823 TLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITA 884
Cdd:PRK01156 673 TSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
241-370 |
8.61e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 241 LAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKdketggilRSLEDALAEAQRVNTKSQSAFDLK 320
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV--------EELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 110347420 321 KKNLACEESKRKELEK--NMVED-SKTLAAKEKEVKKITDGLHALQEASNKDA 370
Cdd:COG2433 454 RSEERREIRKDREISRldREIERlERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
688-866 |
8.81e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 688 LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTE-EADLLQTKLQQSSYHK---------------QQEELDALKKT 751
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSlKAEVLIQKFGRSLKAKkrfsllkketiylqsAQRVELAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 752 IEESEE--TLKNTKEIQRKAEEKY----------EVLENKMKNAEAERERELK---DAQKKLDCAKTKADASSK------ 810
Cdd:COG5022 885 QELKIDvkSISSLKLVNLELESEIielkkslssdLIENLEFKTELIARLKKLLnniDLEEGPSIEYVKLPELNKlheves 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 811 KMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKE 866
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKE 1020
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-49 |
9.36e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 37.99 E-value: 9.36e-03
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
663-866 |
9.44e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 663 LSGGARSQAASILTKFQELKDVQDELRIKENELRAlEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyhkqq 742
Cdd:NF041483 420 LKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRA-EAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADA----- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 743 EELDALKKTieESE----ETLKNTKEIQRKAEEKYEvlenkMKNAEAERERelKDAQKKLDCAKTKADASSKKMKEK-QQ 817
Cdd:NF041483 494 DELRSTATA--ESErvrtEAIERATTLRRQAEETLE-----RTRAEAERLR--AEAEEQAEEVRAAAERAARELREEtER 564
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110347420 818 EVEAITLEL-EELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKE 866
Cdd:NF041483 565 AIAARQAEAaEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETE 614
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-473 |
9.65e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 190 AKLKEIKTI-LEEEITPTIQKLKE----------ERSSYLEYQKVMREIEHLSRL------YIAYQFLLAE---DTKVRS 249
Cdd:PRK05771 4 VRMKKVLIVtLKSYKDEVLEALHElgvvhiedlkEELSNERLRKLRSLLTKLSEAldklrsYLPKLNPLREekkKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 250 AEELKEMQDkviklqEELSENDKKIKALNHEIEELEKRKdketggilRSLEDALAEAQRVntksqSAFDLKKKNLAcees 329
Cdd:PRK05771 84 LEELIKDVE------EELEKIEKEIKELEEEISELENEI--------KELEQEIERLEPW-----GNFDLDLSLLL---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347420 330 krkeleknmveDSKTLAAKEKEVKKiTDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmacKNDI 409
Cdd:PRK05771 141 -----------GFKYVSVFVGTVPE-DKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELK------KLGF 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347420 410 SKAQT-EAKQAQMKLKHAQQELKNKQAEVKKMDSGYRK-DQEALEAVKRLKEKLEAEMKKLNYEEN 473
Cdd:PRK05771 203 ERLELeEEGTPSELIREIKEELEEIEKERESLLEELKElAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| |
