|
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 |
2.72e-157 |
|
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: 500.27 E-value: 2.72e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 2 YVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 82 TFDNSDKKqsplGFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463 80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLR 241
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 242 AEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 322 KNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 402 MIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKDQDAFEAVKKAKEKLETEMKKLNYEENKEEKLLEK 481
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 482 HRQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKNWNRNSVKGLVASLINVKDNSTATALEVVAGERLYNVVVDTEVTAK 561
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 562 KLLEKGELKRRYTIIPLNKISARCIAPEtLRVAQNLVGPDNVHVALSLVDYKPELQKGMEFVFGTTFVCNNMDNAKKVAF 641
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLL-IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 642 DKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEM 721
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 722 KTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCA 801
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 802 KTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQI 881
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 882 ITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHLFGQPNSAYDFKTNN 961
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 962 PKEAGQRLQKLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDF 1041
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1042 GSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 673132010 1122 SHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1144 |
5.08e-129 |
|
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: 424.85 E-value: 5.08e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 2 YVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNG---QAGITKAS 78
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 79 VSITFDNSDKkqsPLGFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKP 158
Cdd:TIGR02168 79 VELVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 159 PEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQ 238
Cdd:TIGR02168 155 EERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 239 FLRAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGG--------------------KLKS 298
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneisrleqqkqilreRLAN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 299 LEDACAEAQRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQ 378
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 379 HFNAVSAGLSSNEDGAEAtLAGQMIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEvkkmdsgykKDQDAFEAVKKAK 458
Cdd:TIGR02168 394 QIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------ELQEELERLEEAL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 459 EKLETEMKKLNyeenkeekllEKHRQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKNWNRNS----VKGLVASLINVkD 534
Cdd:TIGR02168 464 EELREELEEAE----------QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgILGVLSELISV-D 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 535 NSTATALEVVAGERLYNVVVDTEVTAKK---LLEKGELKRRyTIIPLNKISARCIAPETLRVAQNlvGPDNVHVALSLVD 611
Cdd:TIGR02168 533 EGYEAAIEAALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVK 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 612 YKPELQKGMEFVFGTTFVCNNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELRTK 691
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 692 ENELRALEEELAGLKnvaEKYRQLKQQWEMKTEEGDLLQTKLqqssyHKQQEELDALKKTIEESEETLKSTKEIQKKAEE 771
Cdd:TIGR02168 690 EEKIAELEKALAELR---KELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 772 KYEALE---NKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIK 848
Cdd:TIGR02168 762 EIEELEerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 849 AYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAA 928
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 929 AKVSKMLSDYDWINAE-KHLFGQPNSAY-----------DFKTNNPKEAGQRLQKLQEVKEKLGrNVNLRAMNVLTEAEE 996
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRiDNLQERLSEEYsltleeaealeNKIEDDEEEARRRLKRLENKIKELG-PVNLAAIEEYEELKE 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 997 RYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALG 1075
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaGIEIFAQPP 1080
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 1076 NTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1144
Cdd:TIGR02168 1081 GKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1168 |
3.42e-120 |
|
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: 400.21 E-value: 3.42e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 2 YVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK-NGQAGITKASVS 80
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNgKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 81 ITFDNSDKKQSplgfeahDEITVTRQVVIGGRNK---YLINGVNANNTRVQDLFCSVGLNVNNPHFlIMQGRITKVLNMK 157
Cdd:TIGR02169 80 VTFKNDDGKFP-------DELEVVRRLKVTDDGKysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 238 QFLRAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGG-------KLKSLEDACAEAQR-V 309
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkeKIGELEAEIASLERsI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 310 NTKSQSAFDLKKKnLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSS 389
Cdd:TIGR02169 311 AEKERELEDAEER-LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 390 NEDGAEAtLAGQMIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKkdqDAFEAVKKAKEKLETEMKKLN 469
Cdd:TIGR02169 390 YREKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLAADLS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 470 YEENKEEKLLEKHRQLSRDINNLKGKHEALLAKFPNL---QFAYKDPEK--NWNRNSVKGLVASLINVKDnSTATALEVV 544
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeerVRGGRAVEEvlKASIQGVHGTVAQLGSVGE-RYATAIEVA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 545 AGERLYNVVVDTEVTAKKLLEKgeLKR----RYTIIPLNKISARCIAPETLRVaqnlvgPDNVHVALSLVDYKPELQKGM 620
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEAIEL--LKRrkagRATFLPLNKMRDERRDLSILSE------DGVIGFAVDLVEFDPKYEPAF 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 621 EFVFGTTFVCNNMDNAKkvafdkRIM--TRTVTLGGDVFDPHGTLSGGARSQAASILTKFQ---EVKDVQDELRTKENEL 695
Cdd:TIGR02169 617 KYVFGDTLVVEDIEAAR------RLMgkYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaELQRLRERLEGLKREL 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 696 RALEEELAGLKNVAEKYRQLKQQWEMKTEEgdlLQTKLQQSsyhkqQEELDALKKTIEESEETLKSTkeiqkkaEEKYEA 775
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGE---IEKEIEQL-----EQEEEKLKERLEELEEDLSSL-------EQEIEN 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 776 LENKMKNAEAEREkelkdaQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIE 855
Cdd:TIGR02169 756 VKSELKELEARIE------ELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 856 KMAAEVAKNKESVNKAQDelmKQKQIITAQDNIIKDKcaevAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKML 935
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKK----EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 936 SDYDWINAE----KHLFGQPNSAYDFKTNNPKEAGQR-------------LQKLQEVKEKLGRN------VNLRAMNVLT 992
Cdd:TIGR02169 903 RKIEELEAQiekkRKRLSELKAKLEALEEELSEIEDPkgedeeipeeelsLEDVQAELQRVEEEiralepVNMLAIQEYE 982
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 993 EAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGanamlappEGQTVLD------ 1066
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGG--------TGELILEnpddpf 1054
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1067 --GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1144
Cdd:TIGR02169 1055 agGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVS 1134
|
1210 1220
....*....|....*....|....*
gi 673132010 1145 LKEGMFNNA-NVLFKTKFVDGVSTV 1168
Cdd:TIGR02169 1135 LRSPMIEYAdRAIGVTMRRNGESQV 1159
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-172 |
4.23e-102 |
|
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: 323.10 E-value: 4.23e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 81 ITFDNSDKKQSPLGFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:cd03273 81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
|
170
....*....|..
gi 673132010 161 ILSMIEEAAGTR 172
Cdd:cd03273 161 KESLTELSGGQR 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1157 |
2.50e-85 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 299.16 E-value: 2.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNGQAG---ITKA 77
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 78 SVSITFDNSDKKqSPLGFeahDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMK 157
Cdd:COG1196 79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILeEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:COG1196 154 PEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDIL-GELERQLEPLERQAEKAERYRELKEELKELEAELLLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 238 QFLRAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGG---KLKSLEDACAEAQRVNTKSQ 314
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 315 SAfdlkKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDgA 394
Cdd:COG1196 313 EL----EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-E 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 395 EATLAGQMIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKDQDAFEAVKKAKEKLETEMKKLNYEENK 474
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 475 EEKLLEKHRQLSRDINNLKGKH-------EALLAKFPNLQFAYKDPEKNWNRNSVKGLVASLINVkDNSTATALEVVAGE 547
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAaarllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 548 RLYNVVVDTEVTAKKLLE--KGELKRRYTIIPLNKISARciAPETLRVAQNLVGPDNVHVALSLVDYKPELQKGMEFVFG 625
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEylKAAKAGRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 626 TTFVCNNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASiltkfqevkdvqdELRTKENELRALEEELAgl 705
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------ALLEAEAELEELAERLA-- 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 706 knvaekyrqlkqqwemkteegdllqtklqqssyhkqqEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEA 785
Cdd:COG1196 690 -------------------------------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 786 EREKELkdaqkkldcaktkadasskkmkekQQEVEAITLELEELKREHASNEqqldavneaikayegqiekmaaevaknk 865
Cdd:COG1196 733 EREELL------------------------EELLEEEELLEEEALEELPEPP---------------------------- 760
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 866 esvnkaqdelmkqkqiitaqdniikdkcaevakhnlqnnesqlkikeldhsiskhkreaddaaakvskmlsdydwinaek 945
Cdd:COG1196 --------------------------------------------------------------------------------
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 946 hlfgqpnsaydfktnNPKEAGQRLQKLQEVKEKLGrNVNLRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQK 1025
Cdd:COG1196 761 ---------------DLEELERELERLEREIEALG-PVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRE 824
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1026 KNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLF 1104
Cdd:COG1196 825 TRERFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRL 904
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|...
gi 673132010 1105 KPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:COG1196 905 NPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1074-1168 |
5.26e-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: 214.85 E-value: 5.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1074 LGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA 1153
Cdd:cd03273 156 MGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNA 235
|
90
....*....|....*
gi 673132010 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 ... |
520-639 |
2.85e-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: 124.65 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 520 NSVKGLVASLINVKDNsTATALEVVAGERLYNVVVDTEVTAKKLLEKGELKR--RYTIIPLNKISARCIAPETLRvAQNL 597
Cdd:smart00968 1 PGVLGRVADLISVDPK-YETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 673132010 598 VGPDNVHVALSLVDYKPELQKGMEFVFGTTFVCNNMDNAKKV 639
Cdd:smart00968 79 PEPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1085-1167 |
5.81e-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: 120.11 E-value: 5.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTKFVD 1163
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 673132010 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 |
6.74e-28 |
|
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: 113.51 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 3 VKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVYKNGQAGITKASVSIT 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPSVMSAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 83 FDNSDKKqsplgFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEIL 162
Cdd:cd03272 80 FDNSDNR-----FPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQ 154
|
..
gi 673132010 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 |
2.61e-25 |
|
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: 103.93 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 3 VKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQdLVYKNGQAGITKASVSIT 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLF-LAGGGVKAGINSASVEIT 78
|
....
gi 673132010 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 ... |
4-89 |
2.29e-24 |
|
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: 101.77 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 4 KSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK--NGQAGITKASVSI 81
Cdd:cd03278 2 KKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAgsETRKPANFAEVTL 80
|
....*...
gi 673132010 82 TFDNSDKK 89
Cdd:cd03278 81 TFDNSDGR 88
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1081-1157 |
2.13e-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: 99.08 E-value: 2.13e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 673132010 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 ... |
519-640 |
6.74e-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: 95.02 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 519 RNSVKGLVASLINVKDNsTATALEVVAGERLYNVVVDTEVTAKKLLE--KGELKRRYTIIPLNKISARCIAPETLRVAqn 596
Cdd:pfam06470 1 LKGVLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIEflKKNKLGRATFLPLDRLKPRPRRPGADLKG-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 673132010 597 lvgpdNVHVALSLVDYKPELQKGMEFVFGTTFVCNNMDNAKKVA 640
Cdd:pfam06470 78 -----GAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-159 |
1.01e-20 |
|
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: 92.64 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 4 KSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVY--KNGQAGITKASVSI 81
Cdd:cd03275 2 KRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYraRVGKPDSNSAYVTA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 82 TFDNSDKkqsplgfeahdEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 159
Cdd:cd03275 80 VYEDDDG-----------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPP 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1082-1167 |
5.93e-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: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1082 LTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154
|
....*...
gi 673132010 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 |
4.90e-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: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*...
gi 673132010 1161 FVDGVSTV 1168
Cdd:cd03272 235 FRNKVSTI 242
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1085-1156 |
4.04e-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: 4.04e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 673132010 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 ... |
1078-1156 |
3.03e-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: 75.80 E-value: 3.03e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 1078 WKeNLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03274 122 WK-NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-83 |
3.96e-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: 75.41 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGIsNLSQVRASNLQDLVYK-NGQAGITKASV 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLIHNsAGHPNLDSCSV 79
|
....
gi 673132010 80 SITF 83
Cdd:cd03274 80 EVHF 83
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-83 |
2.95e-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: 2.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 5 SIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRasnlqdlvYKNGQAGITKASVSITF 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
241-977 |
1.59e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 241 RAEDtkERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQRVNTKSQSAFDLK 320
Cdd:PTZ00121 1219 KAED--AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 321 KknlASEETKRKELQNSMAEDSKALAAKEK--EVKKITDGLHGLQEASNKDAEALAAAQQhfnAVSAGLSSNEDGAEAT- 397
Cdd:PTZ00121 1297 K---AEEKKKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAE---AAADEAEAAEEKAEAAe 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 398 LAGQMIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKdqdAFEAVKKAKEKLETEMKKLNYEENKEEK 477
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK---ADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 478 LLEKHRQLSRDINNLKGKHEallaKFPNLQFAYKDPEKNWNRNSVKGLVASLINVKDNSTATALEVVAGERLYNVvvdTE 557
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAE----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---EE 1520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 558 VTAKKLLEKGELKRRytiiplnkisarciaPETLRVAQNLVGPDNVHVAlslvdykPELQKGMEfvfgttfvCNNMDNAK 637
Cdd:PTZ00121 1521 AKKADEAKKAEEAKK---------------ADEAKKAEEKKKADELKKA-------EELKKAEE--------KKKAEEAK 1570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 638 KVAFDKRIMTRTVTLggdvfdphgtLSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQ 717
Cdd:PTZ00121 1571 KAEEDKNMALRKAEE----------AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 718 QWEMKTEEGDLLqtklqqssyhKQQEELDALKKtieesEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKElkDAQKK 797
Cdd:PTZ00121 1641 KEAEEKKKAEEL----------KKAEEENKIKA-----AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 798 LDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAV------NEAIKAYEGQIEKMAAEVAKNKESVNKA 871
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 872 QDELMKQKQIITAQDNI--IKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDW-INAEKHLF 948
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFnKNNENGED 1863
|
730 740
....*....|....*....|....*....
gi 673132010 949 GQPNSAYDFKTNNPKEAGQRLQKLQEVKE 977
Cdd:PTZ00121 1864 GNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-203 |
8.49e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 68.50 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 4 KSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSqvRASNLQDLVYKngqaGITKASVSITF 83
Cdd:COG0419 3 LRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINV----GSEEASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 84 DNSDKkqsplgfeahdEITVTRQvviggrnkylingvnanntrvqdlfcsvglnvnnphflimQGRITKVLNMKPPEILS 163
Cdd:COG0419 76 EHGGK-----------RYRIERR----------------------------------------QGEFAEFLEAKPSERKE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 673132010 164 MIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTI--LEEEI 203
Cdd:COG0419 105 ALKRLLGLEIYEELKERLKELEEALESALEELAELqkLKQEI 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1024 |
8.15e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 677 KFQEVKDVQdELRTKENELRALEE----------ELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQE--E 744
Cdd:PTZ00121 1225 KAEAVKKAE-EAKKDAEEAKKAEEernneeirkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEkkK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 745 LDALKKTIEE----------SEETLKSTKEIQKKAEEKYEALENKMKNAEAER------EKELKDAQKKLDCAKTKADAS 808
Cdd:PTZ00121 1304 ADEAKKKAEEakkadeakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdeaeaaEEKAEAAEKKKEEAKKKADAA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 809 SKKMKEKQQEVEAiTLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNI 888
Cdd:PTZ00121 1384 KKKAEEKKKADEA-KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 889 IKD----KCAEVAKhnlQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEkhlfgQPNSAYDFKTNNPKE 964
Cdd:PTZ00121 1463 KKKaeeaKKADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 965 AGQRLQKLQEVKeklgRNVNLRAMNVLTEAEERYNdlMKKKRIVENDKSKILATIEDLDQ 1024
Cdd:PTZ00121 1535 KADEAKKAEEKK----KADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKK 1588
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1046-1144 |
8.39e-12 |
|
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: 64.57 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1046 STLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKEN---LTELSGGQRSLVALSLILsmlLFKPaPIYILDEVDAALDLS 1122
Cdd:cd00267 39 STLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRigyVPQLSGGQRQRVALARAL---LLNP-DLLLLDEPTSGLDPA 114
|
90 100
....*....|....*....|...
gi 673132010 1123 HTQNIGQMLRTHF-THSQFIVVS 1144
Cdd:cd00267 115 SRERLLELLRELAeEGRTVIIVT 137
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
679-1142 |
1.55e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMkTEEGDLLQTKLQQSsyhkqQEELDALKKTIEESEET 758
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAEL-----PERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 759 LKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQ 838
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 839 Q-----------------------------LDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNII 889
Cdd:COG4717 242 EerlkearlllliaaallallglggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 890 KDkcaEVAKHNLQNNESQLKIKELDHSIskhkREADDAAAKVSKMLSDYDWINAEKH---LFGQPNS----AYDFKTNNP 962
Cdd:COG4717 322 EE---LLAALGLPPDLSPEELLELLDRI----EELQELLREAEELEEELQLEELEQEiaaLLAEAGVedeeELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 963 KEAGQRLQKLQEVKEKL----GRNVNLRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQ---------- 1028
Cdd:COG4717 395 EEYQELKEELEELEEQLeellGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQleedgelael 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1029 -------------------ALNIAWQ---------------KVNKDFGSIFSTLLPGANAMLAPPEgqtvldGLEFKV-- 1072
Cdd:COG4717 475 lqeleelkaelrelaeewaALKLALElleeareeyreerlpPVLERASEYFSRLTDGRYRLIRIDE------DLSLKVdt 548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 673132010 1073 ALGNTWKenLTELSGGQRSLVALSL---ILSMLLFKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIV 1142
Cdd:COG4717 549 EDGRTRP--VEELSRGTREQLYLALrlaLAELLAGEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIY 618
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-898 |
1.91e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 668 RSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSsyhkqQEELDA 747
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL-----EERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 748 LKKTIEESEETLKSTKEIQKKAEE--KYEALENKMKNAEAEREKELKDAQKKLDCAKTKAdassKKMKEKQQEVEAITLE 825
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 673132010 826 LEELKREHASNEQQLDAVNEAiKAYEGQIEKMAAEVA-KNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAK 898
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-126 |
7.91e-11 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 65.18 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 2 YVKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVSI 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELE-FSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELI-RFGADG---FRVRA 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 673132010 82 TFDNSDKkqsplgfeahdEITVTRQVVIGGRNKYLINGVNANNTR 126
Cdd:COG1195 72 EVERDGR-----------EVRLGLGLSRGGKKRVRINGKPVRRLS 105
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-196 |
1.15e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 62.13 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 6 IILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:pfam13476 1 LTIENFRSF-RDQTID-FSKGLTLITGPNGSGKTTILDAIKLALYgkTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 84 DNSDKKQSplgfeahDEITVTRQVVIGGRNKY-----LINGVNANNTRVQDLFCSvgLNVNNPHFLIM-QGRITKVLNMK 157
Cdd:pfam13476 79 ENNDGRYT-------YAIERSRELSKKKGKTKkkeilEILEIDELQQFISELLKS--DKIILPLLVFLgQEREEEFERKE 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 673132010 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIK 196
Cdd:pfam13476 150 KKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-886 |
1.67e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 65.76 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYaQRTEVNGFDPL--FNAITGLNGSGKSNILDSICFLLgisnLSQVRASNlQDLVYKNGQAGITKAS 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL----YGKLPRRS-EVIRSLNSLYAAPSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 79 VSITFDNSDKKQSplgFEAHDEITVTR---------QVVI---GGRNKYLINGVNANNTRVQDLfcsvgLNVNNPHF--- 143
Cdd:TIGR00618 75 AFAELEFSLGTKI---YRVHRTLRCTRshrkteqpeQLYLeqkKGRGRILAAKKSETEEVIHDL-----LKLDYKTFtrv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 144 -LIMQGRITKVLNMKPPEILSMIEEAAGTRMYEykKIAAQKTIEKKEAKLKEIKTILEEEI----TPTIQKLKEERSSYL 218
Cdd:TIGR00618 147 vLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYT--QLALMEFAKKKSLHGKAELLTLRSQLltlcTPCMPDTYHERKQVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 219 EyQKVMREIEHLSRLYIAYQFLRAEDTKERSAG----ELKEMQDKIVNLQEVLSENEKKIKALNceieelERRKDKETGG 294
Cdd:TIGR00618 225 E-KELKHLREALQQTQQSHAYLTQKREAQEEQLkkqqLLKQLRARIEELRAQEAVLEETQERIN------RARKAAPLAA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 295 KLKSLEDACAEAQRVNTKSQSAFDLKKKNLAS-----------EETKRKELQNSMAEDSKALAA-KEKEVKKITDGLHGL 362
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKraahvkqqssiEEQRRLLQTLHSQEIHIRDAHeVATSIREISCQQHTL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 363 QEASNKDAEALAAAQQHFNAVSAGLS--SNEDGAEATLAGQMIACKNDISKAQTEaKQAQMKLKHAQQELKSKQAEVKKM 440
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDilQREQATIDTRTSAFRDLQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 441 dsgykKDQDAFEAVKKAKEKLETEMKKLNYeenkeekllekHRQLSRDinnlkgkhEALLAKFPNLQFAYKDPEKNWNRN 520
Cdd:TIGR00618 457 -----EKIHLQESAQSLKEREQQLQTKEQI-----------HLQETRK--------KAVVLARLLELQEEPCPLCGSCIH 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 521 SVKGLVASLINVKDNSTATALE------VVAGERLYNVVVDTEVTAKKLLEKGELKRRYTIIPLNKISA-RCIAPETLRV 593
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRsKEDIPNLQNI 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 594 aqnlvgpdnvhvalsLVDYKPELQKgmefvfgttfvcnNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAAS 673
Cdd:TIGR00618 593 ---------------TVRLQDLTEK-------------LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 674 ILTKFQEVKDVQDE------LRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQ---TKLQQSS--YHKQQ 742
Cdd:TIGR00618 645 LTALHALQLTLTQErvrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLReleTHIEEYDreFNEIE 724
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 743 EELDALKKTIEESEETL-KSTKEIQKKAEEKYEALENKMKNA------EAEREKELKDAQKKLDCAKTKADASSKKMKEK 815
Cdd:TIGR00618 725 NASSSLGSDLAAREDALnQSLKELMHQARTVLKARTEAHFNNneevtaALQTGAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 816 QQEVE--------AITLELEELKREHASNEQQLdavnEAIKAYEGQIEKMAAEVAKNKesvnKAQDELMK-QKQIITAQD 886
Cdd:TIGR00618 805 EAEIGqeipsdedILNLQCETLVQEEEQFLSRL----EEKSATLGEITHQLLKYEECS----KQLAQLTQeQAKIIQLSD 876
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1030 |
2.10e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 667 ARSQAASILTKFQEVKDVQDELRTKENELRALEEelagLKNVAEKYRQLKQQWEMKTEEgdllqtKLQQSSYHKQQEEL- 745
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEEDKKKADELKKAAAA------KKKADEAKKKAEEKk 1431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 746 --DALKKTIEESeetlKSTKEIQKKAEEKYEALENKMKNAEAEREKELK---DAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:PTZ00121 1432 kaDEAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 821 aitlelEELKREHASNEQQLDAVNEAIKAYegqiEKMAAEVAKNKESVNKAqDELMKQKQIITAQDNiikdKCAEVAKHN 900
Cdd:PTZ00121 1508 ------AKKKADEAKKAEEAKKADEAKKAE----EAKKADEAKKAEEKKKA-DELKKAEELKKAEEK----KKAEEAKKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 901 LQNNESQLKIKELDHSISKHKREaddaaaKVSKMLSDYDWINAEKhlfGQPNSAYDFKTNNPKEAGQRLQKLQEVKEKLG 980
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIE------EVMKLYEEEKKMKAEE---AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 673132010 981 RNVNlRAMNVLTEAEERYNDLMKKKRIVENDKSKI--LATIEDLDQKKNQAL 1030
Cdd:PTZ00121 1644 EEKK-KAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-909 |
2.53e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 160 EILSMIEEAagtRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSY-LEYQKVMREIEHLSRLYIAYq 238
Cdd:PTZ00121 1095 EAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEAR- 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 239 flRAEDTKE----------RSAGELKEMQDKIVNLQEVLSENEKKIKALNC--------EIEELERRKDKETGGKLKSLE 300
Cdd:PTZ00121 1171 --KAEDAKKaeaarkaeevRKAEELRKAEDARKAEAARKAEEERKAEEARKaedakkaeAVKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 301 DACAEAQRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHF 380
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 381 NAVSAGLSSNEDGAEATLAG--QMIACKNDISKAQTEAKQAQMKLKHAQQ---ELKSKQAEVKKMDSGYKKDQD----AF 451
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAkaEAEAAADEAEAAEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEAKKKAEEdkkkAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 452 EAVKKAKEKLETEMKKLNYEENKEEKLLEKHRQLSRDINNLKGKHEallakfpnlqfaykdpEKNWNRNSVKGlvASLIN 531
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----------------EAKKAEEAKKK--AEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 532 VKDNSTATALEVVAGERLYNVVVDTEVTAKKLLEKGELKRRytiiplnkisarciaPETLRVAQNLVGPDnvhvalslvd 611
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK---------------ADEAKKAEEAKKAD---------- 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 612 ykpELQKGMEfvfgttfvCNNMDNAKKVAFDKRimtrtvtlggdvfdphgtlsgGARSQAASILTKFQEVKDVQDELRTK 691
Cdd:PTZ00121 1526 ---EAKKAEE--------AKKADEAKKAEEKKK---------------------ADELKKAEELKKAEEKKKAEEAKKAE 1573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 692 ENEL----RALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKSTKEIQK 767
Cdd:PTZ00121 1574 EDKNmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 768 KAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKR-EHASNEQQLDAVN-E 845
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaEELKKAEEENKIKaE 1733
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 846 AIKAYEGQIEKMAAEVAKNKESVNKAQ----DELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLK 909
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAhlkkEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
23-130 |
3.70e-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: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 23 FDPLFNAITGLNGSGKSNILDSICFLLGIsnlsqvRASNlqDLVykngQAGITKASVSITFDNSDK-----KQSPLGFEA 97
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGG------RASA--DLI----RSGAEKAVVEGVFDISDEeeakaLLLELGIED 86
|
90 100 110
....*....|....*....|....*....|...
gi 673132010 98 HDEITVTRQVVIGGRNKYLINGVNANNTRVQDL 130
Cdd:cd03241 87 DDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1028 |
6.85e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 675 LTKFQEVKDVQDELRTKENELRALEEELaglknvAEKYRQLKQQWEMKTEEGDLLQTKLQQSsyhKQQEELDALKKtiee 754
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAA------KKKAEEAKKAAEAAKAEAEAAADEAEAA---EEKAEAAEKKK---- 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 755 sEETLKSTKEIQKKAEEKYEALENKMKnaeAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHA 834
Cdd:PTZ00121 1374 -EEAKKKADAAKKKAEEKKKADEAKKK---AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 835 SN--EQQLDAVNEAIKAYEgqiEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKE 912
Cdd:PTZ00121 1450 KKkaEEAKKAEEAKKKAEE---AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 913 LDHSISKHKREADDAAAKVSKmlsdydwinAEKHLfgqpnsaydfKTNNPKEAGQRLQKLQEVKEKLGRNVNLRAMNVLT 992
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKK---------ADELK----------KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
330 340 350
....*....|....*....|....*....|....*..
gi 673132010 993 EAEE-RYNDLMKKKRIVENDKSKILATIEDLDQKKNQ 1028
Cdd:PTZ00121 1588 KAEEaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
744-898 |
8.82e-10 |
|
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: 60.32 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 744 ELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAER---EKELKDAQKKLDCAKTKADASSKkmkekQQEVE 820
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRN-----NKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 821 AITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAK 898
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
670-889 |
2.22e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 670 QAASILTKFQEVKDVQDELRTKENELRALEEelagLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALK 749
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELLEP----IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 750 KTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAER----EKELKDAQKKLDCAKTKADasskkmkEKQQEVEAITLE 825
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRA-------RLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 673132010 826 LEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNII 889
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-123 |
3.16e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 60.17 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVS 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYLL---APGRSHRTARDKELI-RFGAEA---AVIH 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 673132010 81 ITFDNsdkkqsplgfeAHDEITVTRQVVIGGRNKYLINGVNAN 123
Cdd:PRK00064 72 GRVEK-----------GGRELPLGLEIDKKGGRKVRINGEPQR 103
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-95 |
1.83e-08 |
|
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: 55.68 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 3 VKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03276 1 IESITLKNFMCHR-HLQIE-FGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLI-KDGE---SSAKITVT 74
|
90
....*....|...
gi 673132010 83 FDNSDKKQSPLGF 95
Cdd:cd03276 75 LKNQGLDANPLCV 87
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-874 |
2.75e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 198 ILEE-EITPTIQKLKEERSSYLEYQKVM----REIEHLSRLYIAYQ-FLRAEDTKE-----RSAGELKEMQDKIVNLQEV 266
Cdd:COG4913 217 MLEEpDTFEAADALVEHFDDLERAHEALedarEQIELLEPIRELAErYAAARERLAeleylRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 267 LSENEKKIKALNCEIEELERRKDkETGGKLKSLEDACAEAqrvntksqsafDLKKKNLASEETKRKElqnsmaedsKALA 346
Cdd:COG4913 297 LEELRAELARLEAELERLEARLD-ALREELDELEAQIRGN-----------GGDRLEQLEREIERLE---------RELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 347 AKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmiackndiskAQTEAKQAQMKLKHA 426
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---------------ALAEAEAALRDLRRE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 427 QQELKSKQAEVKKMDSGYKKDQDAfeavkkAKEKLETEMkklnyeenkeekllekhrqlsrdinnlkGKHEAllakfpNL 506
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLA------LRDALAEAL----------------------------GLDEA------EL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 507 QFaykdpeknwnrnsvkglVASLINVKDNSTA--TALEVVAGERLYNVVVDTEVTAK--KLLEKGELKRRytiIPLNKIS 582
Cdd:COG4913 461 PF-----------------VGELIEVRPEEERwrGAIERVLGGFALTLLVPPEHYAAalRWVNRLHLRGR---LVYERVR 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 583 ARCIAPETLRVAQN-LVGpdnvhvalsLVDYKP-ELQKGMEFVFGTTF--VCnnMDNAKkvAFDKriMTRTVTLGGDVFD 658
Cdd:COG4913 521 TGLPDPERPRLDPDsLAG---------KLDFKPhPFRAWLEAELGRRFdyVC--VDSPE--ELRR--HPRAITRAGQVKG 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 659 PHGTLSGGARSQAASILtkfqeV--KDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEmktEEGDLLQTKLQQS 736
Cdd:COG4913 586 NGTRHEKDDRRRIRSRY-----VlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ---ERREALQRLAEYS 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 737 -------SYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAER---EKELKDAQKKLDCAKTKAD 806
Cdd:COG4913 658 wdeidvaSAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLE 737
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 807 ASSKKmkekqqEVEAITLELEELKREhasnEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDE 874
Cdd:COG4913 738 AAEDL------ARLELRALLEERFAA----ALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
660-913 |
3.11e-08 |
|
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: 58.21 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 660 HGTLSGGARSQAASI----------LTKFQEVKDVQDElRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLL 729
Cdd:pfam15921 581 HGRTAGAMQVEKAQLekeindrrleLQEFKILKDKKDA-KIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 730 -QTKLQQSSYHKQQEELDALKKTI----EESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDA---QKKLDCA 801
Cdd:pfam15921 660 nEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAK 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 802 KTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQI 881
Cdd:pfam15921 740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
250 260 270
....*....|....*....|....*....|..
gi 673132010 882 ITAQDNIIKDKCAEVAKHNLQNNesqLKIKEL 913
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKLQHT---LDVKEL 848
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-87 |
5.42e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.48 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 4 KSIILEGFKSYaQRTEVNgFDPLfNAITGLNGSGKSNILDSICFL--LGISNLSQVRASN--LQDLVYKNGQAGITKASV 79
Cdd:COG4637 3 TRIRIKNFKSL-RDLELP-LGPL-TVLIGANGSGKSNLLDALRFLsdAARGGLQDALARRggLEELLWRGPRTITEPIRL 79
|
....*...
gi 673132010 80 SITFDNSD 87
Cdd:COG4637 80 ELEFAEED 87
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-792 |
8.63e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGqagiTKASVS 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVE-FDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGG----SGTEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 81 ITFDNSDKKqsplgfeahdeITVTRQVVIGgrNKYLINGVNANNTRVQDLFCS------VGLNVNNPHFLIMQGRITKVL 154
Cdd:PRK03918 75 LKFEKNGRK-----------YRIVRSFNRG--ESYLKYLDGSEVLEEGDSSVRewverlIPYHVFLNAIYIRQGEIDAIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 155 nmkppeilsmieEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEI---------TPTIQKLKEERSSYLEyqKVMR 225
Cdd:PRK03918 142 ------------ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIerlekfikrTENIEELIKEKEKELE--EVLR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 226 EIEHLSRLYIAyqfLRAEDTK-ERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKdKETGGKLKSLEDACA 304
Cdd:PRK03918 208 EINEISSELPE---LREELEKlEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 305 EAQRVNTKSQSAFDL---------KKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQeasnKDAEALAA 375
Cdd:PRK03918 284 ELKELKEKAEEYIKLsefyeeyldELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE----KRLEELEE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 376 AQQHFNAVSAgLSSNEDGAEATLAGQMIackNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKdqdAFEAVK 455
Cdd:PRK03918 360 RHELYEEAKA-KKEELERLKKRLTGLTP---EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK---AIEELK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 456 KAKEKLETEMKKLNYEENKEEKllekhRQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKNwnrnsvkglvaslinVKDN 535
Cdd:PRK03918 433 KAKGKCPVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEEKERKLRKELRELEKV---------------LKKE 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 536 STATALEVVAgERLYNVVVDTEVTAKKLLEKGELKRRYTIIPLNKISARciapetlrvaqnlvgpdnvhvalsLVDYKPE 615
Cdd:PRK03918 493 SELIKLKELA-EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE------------------------IKSLKKE 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 616 LQKGMEFVFGTTFVCNNMDNAKKVAfdKRIMTRTVTLG-GDVFDPHGTLSggarsQAASILTKFQEVKDVQDELRTKENE 694
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEEL--AELLKELEELGfESVEELEERLK-----ELEPFYNEYLELKDAEKELEREEKE 620
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 695 LRALEEE-------LAGLKNVAEKYR----QLKQQW---EMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLK 760
Cdd:PRK03918 621 LKKLEEEldkafeeLAETEKRLEELRkeleELEKKYseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
810 820 830
....*....|....*....|....*....|..
gi 673132010 761 STKEIQKKAEEKYEALENKMKNAEAEREKELK 792
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-109 |
9.52e-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: 53.77 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 3 VKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICF-LLGISNLSQVRASNLQDLVYKngqaGITKASVSI 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLIRE----GEVRAQVKL 75
|
90 100
....*....|....*....|....*...
gi 673132010 82 TFDNSDKKQsplgFEAHDEITVTRQVVI 109
Cdd:cd03240 76 AFENANGKK----YTITRSLAILENVIF 99
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-927 |
1.12e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 246 KERSAGELKEMQDKIVNLQEVLSENEKKikalncEIEELERRKDKETGGKLKSLEDA-------------CAEAQRVNTK 312
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDAR------KAEEARKAEDAKRVEIARKAEDArkaeearkaedakKAEAARKAEE 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 313 SQSAFDLKKknlaSEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAvsaGLSSNED 392
Cdd:PTZ00121 1187 VRKAEELRK----AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE---EIRKFEE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 393 GAEATLAGQMIACKNDISKAQTEAKQAQMKLKhaQQELKsKQAEVKKMDSGYKKDQDAFEAvKKAKEKLETEMKKLNyee 472
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKK--ADEAK-KAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKAD--- 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 473 nkeekllekhrQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKNWNRNSVKGLVASliNVKDNSTATALEVVAGERLYNV 552
Cdd:PTZ00121 1333 -----------AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK--KKADAAKKKAEEKKKADEAKKK 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 553 VVDTEVTAKKLLEKGELKRRYTIIPlNKISARCIAPETLRVAQNLVGPDNVhvalslvDYKPELQKGMEFVFGTTFVCNN 632
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKADEA-------KKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 633 MDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKY 712
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 713 R---QLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEES----EETLKSTKEIQKKAEEKyealenKMKNAEA 785
Cdd:PTZ00121 1552 KkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAKKAEEA------KIKAEEL 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 786 EREKELKdaqKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHasnEQQLDAVNEAIKAYEGqiEKMAAEVAKNK 865
Cdd:PTZ00121 1626 KKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAEED--EKKAAEALKKE 1697
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673132010 866 ESVNKAQDELMKQKqiitAQDniiKDKCAEVAKhnlQNNESQLKIKELDHSISKHKREADDA 927
Cdd:PTZ00121 1698 AEEAKKAEELKKKE----AEE---KKKAEELKK---AEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-821 |
1.17e-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: 54.16 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEgdlLQTKLQQSSYHKQ----QEELDALKKTIEE 754
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNNKEyealQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 673132010 755 SEETLKSTKEIQKKAEEKYEALENKMknaeAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAEL----AELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-84 |
1.18e-07 |
|
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: 55.39 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLqdlvYKNGQAGITKASVS 80
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDF----YLGDDPDLPEIEIE 74
|
....
gi 673132010 81 ITFD 84
Cdd:COG3593 75 LTFG 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1053 |
1.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 677 KFQEVKDVQDELRTKENELRALEEelagLKNVAEKYRQlKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESE 756
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 757 ETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADA-SSKKMKEKQQEVEAITLE---------- 825
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEekkkadelkk 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 826 ------------LEELKREHASNEQQLDAVNEAIKAYEGQIE----------KMAAEVAKNKESVNKAQDELMKQKQIIT 883
Cdd:PTZ00121 1554 aeelkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklyeeekKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 884 AQDNIIKDKCAEVAK-HNLQNNESQLKIK--ELDHSISKHKREADDAAAkvskmlSDYDWINAEKHLFGQPNSAYDFKTN 960
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKaEELKKAEEENKIKaaEEAKKAEEDKKKAEEAKK------AEEDEKKAAEALKKEAEEAKKAEEL 1707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 961 NPKEA-----GQRLQKLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMKKKRI----------VENDKSKILATIEDLDQK 1025
Cdd:PTZ00121 1708 KKKEAeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkkeeekkAEEIRKEKEAVIEEELDE 1787
|
410 420
....*....|....*....|....*...
gi 673132010 1026 KNQALNIAWQKVNKDFGSIFSTLLPGAN 1053
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
986-1144 |
2.30e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.85 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 986 RAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKdfgsIFSTLLPGANAMLAPPEGQTVL 1065
Cdd:COG3950 97 RLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVRE----ALNKLLPDFKDIRIDRDPGRLV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1066 ----DGLEFkvalgntwkeNLTELSGGQRSLVAL--SLILSMLLFKPAP--------IYILDEVDAALDLSHTQNIGQML 1131
Cdd:COG3950 173 ildkNGEEL----------PLNQLSDGERSLLALvgDLARRLAELNPALenplegegIVLIDEIDLHLHPKWQRRILPDL 242
|
170
....*....|...
gi 673132010 1132 RTHFTHSQFIVVS 1144
Cdd:COG3950 243 RKIFPNIQFIVTT 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-463 |
2.56e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1 MYVKSIILEGFKSYAQrTEVnGFDPLFNAITGLNGSGKSNILDSiCF--LLGISNLSQVrasnLQDLVYKngqaGITKAS 78
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADL-RLEDGVTVIHGVNGSGKSSLLEA-CFfaLYGSKALDDT----LDDVITI----GAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 79 VSITFdnsdkkqSPLGFEAH---------DEITVTRQVVIGGRNkyLINGVNANNTRVQDLfcsvgLNVNNPHFL----I 145
Cdd:PRK02224 70 IELWF-------EHAGGEYHierrvrlsgDRATTAKCVLETPEG--TIDGARDVREEVTEL-----LRMDAEAFVncayV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 146 MQGRITKVLNMKPPEILSMIEEAAGT-RMYEYKKIAA--------------------QKTIEKKEAK------------L 192
Cdd:PRK02224 136 RQGEVNKLINATPSDRQDMIDDLLQLgKLEEYRERASdarlgvervlsdqrgsldqlKAQIEEKEEKdlherlngleseL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 193 KEIKTILE--EEITPTIQKLKEERSSYLE-YQKVMREIEHL------SRLYIAyqflRAEDTKERSAGELKEMQDKIVNL 263
Cdd:PRK02224 216 AELDEEIEryEEQREQARETRDEADEVLEeHEERREELETLeaeiedLRETIA----ETEREREELAEEVRDLRERLEEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 264 QEVLSE-------NEKKIKALNCEIEELERRKD-------------KETGGKLKSLEDACAEAQRVNTKSQSAFDLKKKN 323
Cdd:PRK02224 292 EEERDDllaeaglDDADAEAVEARREELEDRDEelrdrleecrvaaQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 324 LASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDG---AEATL-A 399
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERveeAEALLeA 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 400 GQMIACKNDISKAQ-----TEAKQAQMKLKHAQQELKSKQAEVkkmdsgyKKDQDAFEAVKKAKEKLET 463
Cdd:PRK02224 452 GKCPECGQPVEGSPhvetiEEDRERVEELEAELEDLEEEVEEV-------EERLERAEDLVEAEDRIER 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
677-1027 |
4.90e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 677 KFQEVKDVQDELRTKENELRALEEELAGLKNVAEK--YRQLKQQWEMKTEEGDLLQTKLQQS--SYHKQQEELDALKKTI 752
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNnkIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 753 EESE-ETLKSTKEIQKKAEE-KYEALENKMKNAEAER-EKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEEL 829
Cdd:TIGR04523 352 TNSEsENSEKQRELEEKQNEiEKLKKENQSYKQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 830 KREHASNEQQLDAVNEAI--------------KAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAE 895
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDsvkeliiknldntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 896 VAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHLFGQPNSAYDFKTNNPKEAGQRLQKLQEV 975
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 673132010 976 KEKLGRNVNLRamNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKN 1027
Cdd:TIGR04523 592 DQKEKEKKDLI--KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
667-905 |
1.24e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 667 ARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKN----VAEKYRQLKQQWEMKTEEGDLLQTKlqQSSYHKQQ 742
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEerdeLNEKLNELREELDELRKELAELNKA--GGSIDKLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 743 EELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKnaEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAI 822
Cdd:COG1340 116 KEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKK--ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 823 TLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITA----QDNIIKDKCAEVAK 898
Cdd:COG1340 194 HEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAlkreKEKEELEEKAEEIF 273
|
....*..
gi 673132010 899 HNLQNNE 905
Cdd:COG1340 274 EKLKKGE 280
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-90 |
1.32e-06 |
|
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: 50.67 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 5 SIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSqvRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03277 5 RIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLLG--RAKKVGEFV-KRGC---DEGTIEIE 76
|
....*....
gi 673132010 83 -FDNSDKKQ 90
Cdd:cd03277 77 lYGNPGNIQ 85
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-89 |
1.51e-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: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 8 LEGFKSYAQRTEVN----GFDPLFnAITGLNGSGKSNILDSICFLLgisnLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:cd03279 8 LKNFGPFREEQVIDftglDNNGLF-LICGPTGAGKSTILDAITYAL----YGKTPRYGRQENLRSVFAPGEDTAEVSFTF 82
|
....*.
gi 673132010 84 DNSDKK 89
Cdd:cd03279 83 QLGGKK 88
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
147-491 |
1.52e-06 |
|
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: 52.81 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 147 QGRITKVLNMKPPEILSMIEEAAGTRMyEYKKIAAQKTIEKKEAKLKEIKTILE-EEITPTIQKLKEE-RSSYLEYQKVM 224
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSElREAKRMYEDKI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 225 REIEhlSRLYIA-YQFLRAEDTKERSAGELKEMQDKivnLQEVLSENEKKIKALNCEIEELERRKDKETGGKL------K 297
Cdd:pfam15921 345 EELE--KQLVLAnSELTEARTERDQFSQESGNLDDQ---LQKLLADLHKREKELSLEKEQNKRLWDRDTGNSItidhlrR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 298 SLEDACAEAQRVNtksqsafdlkkknlASEETKRKELQNSMAEDSKALAAKEKEVKKI---TDGLHGLQEASNKDAEALA 374
Cdd:pfam15921 420 ELDDRNMEVQRLE--------------ALLKAMKSECQGQMERQMAAIQGKNESLEKVsslTAQLESTKEMLRKVVEELT 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 375 A-------AQQHFNAVSAGLSSNEDGAEATLAgqmiacknDISKAQTEAKQAQMKLKHAQQE---LKSKQAEVKKMDSGY 444
Cdd:pfam15921 486 AkkmtlesSERTVSDLTASLQEKERAIEATNA--------EITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQM 557
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 673132010 445 KKDQDAFEAVkkaKEKLETEMKKLNYEENKEEKLLEKHRQLSRDINN 491
Cdd:pfam15921 558 AEKDKVIEIL---RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-1168 |
1.58e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 668 RSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQqwemKTEEGDLLQTKLQQSSYHKQQEELDA 747
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTPEKLEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 748 L---KKTIEESEETLKSTK-EIQKKAEEKYEALEnKMKNAE-------------------AEREKELKDAQKKLdcakTK 804
Cdd:PRK03918 396 LekaKEEIEEEISKITARIgELKKEIKELKKAIE-ELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKEL----KE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 805 ADASSKKMKEKQQEVEAITLELEELKREHASNEQ-----------QLDAVNEAIKAYEGQIEKMA---AEVAKNKESVNK 870
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkyNLEELEKKAEEYEKLKEKLIklkGEIKSLKKELEK 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 871 AQdELMKQKQIITAQDNIIKDKCAEVAKH---------------------------NLQNNESQLKIKEldHSISKHKRE 923
Cdd:PRK03918 551 LE-ELKKKLAELEKKLDELEEELAELLKEleelgfesveeleerlkelepfyneylELKDAEKELEREE--KELKKLEEE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 924 ADDAAAKVSKMLSDYDWINAEKHLFGQPNSAYDFKtnNPKEAGQRLQK-LQEVKEKLGRNVNLR--AMNVLTEAEERYND 1000
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSReLAGLRAELEELEKRReeIKKTLEKLKEELEE 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1001 LMKKKRIVENDKsKILATIEDLDQK----KNQALNIAWQKVNKDFGSIFSTLLPGANAmlappegQTVLDGLEFKVALGN 1076
Cdd:PRK03918 706 REKAKKELEKLE-KALERVEELREKvkkyKALLKERALSKVGEIASEIFEELTEGKYS-------GVRVKAEENKVKLFV 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1077 TW---KENLTELSGGQRSLVALS--LILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMF 1150
Cdd:PRK03918 778 VYqgkERPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKiPQVIIVSHDEELK 857
|
570
....*....|....*...
gi 673132010 1151 NNANVLFKTKFVDGVSTV 1168
Cdd:PRK03918 858 DAADYVIRVSLEGGVSKV 875
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
785-945 |
1.66e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 785 AEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKN 864
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 865 KESVNKAQ------------DELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVS 932
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170
....*....|...
gi 673132010 933 KMLSDYDWINAEK 945
Cdd:COG3883 179 EQEALLAQLSAEE 191
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-63 |
2.24e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 50.77 E-value: 2.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 673132010 1 MYVKSIILEGFKSYAQRtEVN-GFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQ 63
Cdd:COG3950 1 MRIKSLTIENFRGFEDL-EIDfDNPPRLTVLVGENGSGKTTLLEAIALALSglLSRLDDVKFRKLL 65
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
632-964 |
2.49e-06 |
|
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: 52.03 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 632 NMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQE-VKDVQDELRTKENELRALEEELaglknvae 710
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAtTCSLEELLRTEQQRLEKNEDQL-------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 711 kyRQLKQQWEMKTEEGDLLqTKLQQSsyhkQQEELDALKKTIEESEETLKSTKEIQKKAEEkYEALENKMKNAEAEREKE 790
Cdd:pfam05483 380 --KIITMELQKKSSELEEM-TKFKNN----KEVELEELKKILAEDEKLLDEKKQFEKIAEE-LKGKEQELIFLLQAREKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 791 LKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELkrehASNEQQLDAVNeaiKAYEGQIEKMAAEVAKNKESV-- 868
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL----TAHCDKLLLEN---KELTQEASDMTLELKKHQEDIin 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 869 NKAQDELMkQKQIitaqdniikdkcaevakHNLQNNESQLKiKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHLF 948
Cdd:pfam05483 525 CKKQEERM-LKQI-----------------ENLEEKEMNLR-DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK 585
|
330
....*....|....*.
gi 673132010 949 GQPNSAYDFKTNNPKE 964
Cdd:pfam05483 586 EKQMKILENKCNNLKK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
742-1021 |
2.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 742 QEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAER-----EKELKDAQKKLDcaktKADASSkkmkekq 816
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaEREIAELEAELE----RLDASS------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 817 QEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAqdniikdkcAEV 896
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---------ERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 897 AKHNLQNNESQLKiKELDHSISKHKREADDAAAKVSKMLSDY--DWINAEKHLFGQPNSAYDFKtnnpkeagQRLQKLQE 974
Cdd:COG4913 756 AAALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRAFnrEWPAETADLDADLESLPEYL--------ALLDRLEE 826
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 673132010 975 vkeklgrnvnlramNVLTEAEERYNDLMKKKriVENDKSKILATIED 1021
Cdd:COG4913 827 --------------DGLPEYEERFKELLNEN--SIEFVADLLSKLRR 857
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
679-874 |
2.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGL-KNVAEKYRQLKQQW-EMKTEEGDL--LQTKLQQSSYHKQQEELDALKKTIEE 754
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELGERArALYRSGGSVsyLDVLLGSESFSDFLDRLSALSKIADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 755 SEETLKSTKEIQKKAEEKYEALENKMKNAEAEReKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAitlELEELKREHA 834
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALK-AELEAAKAELEAQQAEQEALLAQLSAEEAAAEA---QLAELEAELA 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 673132010 835 SNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDE 874
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
681-892 |
2.67e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.55 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 681 VKDVQDELRTKENELRALEEELAGLKNVAEkyRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQ-----EELDALKKTIEES 755
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIE--EQRKKNGENIARKQNKYDELVEEAKTIKAEieeltDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 756 EETLK--STKEIQKKAEEKYEALENKM-----------KNAEAEREK------ELKDAQKKLDCAKTKADasskKMKEKQ 816
Cdd:PHA02562 254 SAALNklNTAAAKIKSKIEQFQKVIKMyekggvcptctQQISEGPDRitkikdKLKELQHSLEKLDTAID----ELEEIM 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 673132010 817 QEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELmkqKQIITAQDNIIKDK 892
Cdd:PHA02562 330 DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL---DKIVKTKSELVKEK 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
735-1028 |
2.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 735 QSSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEaEREKELKDAQKKLDcaktkadasskKMKE 814
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELE-----------KLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 815 KQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQD--ELMKQKQIITAQDNIIKDK 892
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 893 CAEVAKhNLQNNESQLK-IKELDHSISKHKREADDAAAKVSKMLSDYDwinaekhlfgqpnsaydfktnnpkEAGQRLQK 971
Cdd:PRK03918 309 LREIEK-RLSRLEEEINgIEERIKELEEKEERLEELKKKLKELEKRLE------------------------ELEERHEL 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 972 LQEVKEKLGRNVNLRAM---NVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQ 1028
Cdd:PRK03918 364 YEEAKAKKEELERLKKRltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
679-868 |
3.25e-06 |
|
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: 51.39 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDEL---RTKENELRALEEELAGLKnvaekyRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEeldalKKTIEES 755
Cdd:pfam09726 402 QDIKKLKAELqasRQTEQELRSQISSLTSLE------RSLKSELGQLRQENDLLQTKLHNAVSAKQKD-----KQTVQQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 756 EETLKSTKEiQKKAEEKYEALENKMKnaeaeREKELKDAQKKLDCAKTKAD-ASSKKMKEKQQEVEAITLELEELKREha 834
Cdd:pfam09726 471 EKRLKAEQE-ARASAEKQLAEEKKRK-----KEEEATAARAVALAAASRGEcTESLKQRKRELESEIKKLTHDIKLKE-- 542
|
170 180 190
....*....|....*....|....*....|....
gi 673132010 835 sneqqldavnEAIKAYEGQIEkmaaEVAKNKESV 868
Cdd:pfam09726 543 ----------EQIRELEIKVQ----ELRKYKESE 562
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-868 |
3.32e-06 |
|
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: 49.54 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKNVAEkyrqlkqqwemkteegdllqtklqqssyhKQQEELDALKKTIEESEET 758
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLE-----------------------------AAKTELEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 759 LKSTKEIQKKAEEKYEALENkmknaeaerEKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQ 838
Cdd:COG1579 68 IEEVEARIKKYEEQLGNVRN---------NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180 190
....*....|....*....|....*....|
gi 673132010 839 QLDAVNEAIKAYEGQIEKMAAEVAKNKESV 868
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
691-1025 |
3.97e-06 |
|
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: 51.36 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 691 KENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQ----QSSYHKQ-------------------QEELDA 747
Cdd:pfam10174 270 REEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLEtltnQNSDCKQhievlkesltakeqraailQTEVDA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 748 LKKTIEESEETL-KSTKEIQKKAEE--------------------KYEALENKMKN-AEAEREKE-----LKDAQKKLDC 800
Cdd:pfam10174 350 LRLRLEEKESFLnKKTKQLQDLTEEkstlageirdlkdmldvkerKINVLQKKIENlQEQLRDKDkqlagLKERVKSLQT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 801 AKTKADASSKKMKEKQQEVEAItleLEELKREHASNEQQ----LDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELM 876
Cdd:pfam10174 430 DSSNTDTALTTLEEALSEKERI---IERLKEQREREDRErleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHAS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 877 KQKQIITAQDNIIKDKCAEVAK---------------HNLQ-----NNESQLKIKELDHSISKHKREADDAAAKVSKMLS 936
Cdd:pfam10174 507 SLASSGLKKDSKLKSLEIAVEQkkeecsklenqlkkaHNAEeavrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLG 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 937 DYDWINAEKHLFGQPNSAYD------FKTNNPKEA-------GQRLQKLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMK 1003
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELEsltlrqMKEQNKKVAnikhgqqEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEK 666
|
410 420
....*....|....*....|..
gi 673132010 1004 KKRIVENDKSKILATIEDLDQK 1025
Cdd:pfam10174 667 TRQELDATKARLSSTQQSLAEK 688
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
663-911 |
4.22e-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: 50.53 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 663 LSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELaglKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQssyhkQQ 742
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE---KALLKQLAALERRIAALARRIRALEQELAA-----LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 743 EELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSK---KMKEKQQEV 819
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 820 EAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKH 899
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 673132010 900 NLQNNESQLKIK 911
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
708-878 |
4.64e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 708 VAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKStKEIQKKAEEKYEALENKMKNAEAER 787
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAA-QEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 788 EKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAItleleelkrehasnEQQLDAVNEAIKAYEGQIEKMAAEVAKNK-- 865
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA--------------EAAKKAAAEAKKKAEAEAAAKAAAEAKKKae 204
|
170
....*....|....
gi 673132010 866 -ESVNKAQDELMKQ 878
Cdd:PRK09510 205 aEAKKKAAAEAKKK 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
680-874 |
4.89e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 680 EVKDVQDELRTKENELRALEEELAGLKNVAEkyrQLKQQWEMKTEEGDLLQTKLQQSsyhkqQEELDALKKTIEESEETL 759
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 760 KSTKEIQKKAEEKYEALE------------------NKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 673132010 822 itlELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDE 874
Cdd:COG3883 169 ---AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-126 |
5.12e-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: 49.60 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 3 VKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVykngQAGITKASVSIT 82
Cdd:cd03242 1 LKSLELRNFRNYA-ELELE-FEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI----RWGAEEAKISAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 673132010 83 FDNsdkkqsplgfeahDEITVTRQVVI--GGRNKYLINGVNANNTR 126
Cdd:cd03242 72 LER-------------QGGELALELTIrsGGGRKARLNGIKVRRLS 104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
677-930 |
5.54e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 677 KFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQ---QWEMKTEEGDLLQTKLQQ--SSYHKQQEELDALKKT 751
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLEEeiNGIEERIKELEEKEER 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 752 IEESEETLKSTK---EIQKKAEEKYEALENKMKNAEAEREKElkdAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE 828
Cdd:PRK03918 340 LEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRL---TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 829 LKREHASNEQQLDAVNEA-------------------IKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNII 889
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 673132010 890 KDKcaEVAKhnlqnnesqlKIKELDHSISKHKREADDAAAK 930
Cdd:PRK03918 497 KLK--ELAE----------QLKELEEKLKKYNLEELEKKAE 525
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
740-841 |
5.86e-06 |
|
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: 46.41 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 740 KQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEV 819
Cdd:pfam13863 3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|..
gi 673132010 820 EAITLELEELKREHASNEQQLD 841
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLE 104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
662-879 |
6.60e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 662 TLSGGARSQAASILTKFQEV----KDVQDELRTKENELRALEEELAGLKNVAekyrqlKQQWEMKTEEGDLLQTKLQQ-- 735
Cdd:pfam12128 262 HLHFGYKSDETLIASRQEERqetsAELNQLLRTLDDQWKEKRDELNGELSAA------DAAVAKDRSELEALEDQHGAfl 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 736 ----SSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMK---NAEAEREKELKDAQKKlDCAKTKADAS 808
Cdd:pfam12128 336 dadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKeqnNRDIAGIKDKLAKIRE-ARDRQLAVAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 809 SKKMKEKQQ---EVEAITLELEELKREHASN----EQQLDAVN------EAIKAYEGQIEKMAAEVAKNKESVNKAQDEL 875
Cdd:pfam12128 415 DDLQALESElreQLEAGKLEFNEEEYRLKSRlgelKLRLNQATatpellLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
....
gi 673132010 876 MKQK 879
Cdd:pfam12128 495 RQAR 498
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
674-853 |
9.73e-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: 49.62 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 674 ILTKFQEVKDVQDELRTKENELRALEEELAglknvAEKYRQLKQQWEMKTEEGDLLQTKLQQSSyhkqqeelDALKKTIE 753
Cdd:pfam05262 182 VVEALREDNEKGVNFRRDMTDLKERESQED-----AKRAQQLKEELDKKQIDADKAQQKADFAQ--------DNADKQRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 754 ESEETLKSTKEIQKKAE-----EKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE 828
Cdd:pfam05262 249 EVRQKQQEAKNLPKPADtsspkEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQK 328
|
170 180
....*....|....*....|....*
gi 673132010 829 LKREHASNEQQLDAVNEAIKAYEGQ 853
Cdd:pfam05262 329 KREPVAEDLQKTKPQVEAQPTSLNE 353
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1053-1133 |
9.77e-06 |
|
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: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1053 NAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03225 103 NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLK 178
|
.
gi 673132010 1133 T 1133
Cdd:cd03225 179 K 179
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
666-928 |
1.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 666 GARSQAASILTKFQEVKDvqdELRTKENELRALEEELAGLK----NVAEKYRQLKQQWEMKTEEGDLLQTKLQ------- 734
Cdd:PRK02224 360 ELREEAAELESELEEARE---AVEDRREEIEELEEEIEELRerfgDAPVDLGNAEDFLEELREERDELREREAeleatlr 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 735 --QSSYHKQQEELDALK--------------KTIEESEETLKSTKEIQKKAEEKYEALENKMknaeaEREKELKDAQKKL 798
Cdd:PRK02224 437 taRERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERL-----ERAEDLVEAEDRI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 799 DCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVA---KNKESVNKAQDEL 875
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAelnSKLAELKERIESL 591
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 876 MKQKQIITAQDNII------KDKCAEVAKhnlQNNESQLKIKELDHSISKHKREADDAA 928
Cdd:PRK02224 592 ERIRTLLAAIADAEdeierlREKREALAE---LNDERRERLAEKRERKRELEAEFDEAR 647
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
675-945 |
1.69e-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: 49.25 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 675 LTKFQEVKDVQDELRTKENELRALEEELAGLKNvaeKYRQLKQQWEMKTEEGDLLQTKLQ--QSSYHKQQEELDALKKTI 752
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLES---QINDLESKIQNQEKLNQQKDEQIKklQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 753 EESEETLKSTKEIQKKAEEKYEALENKMKnaeaEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 832
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRE----SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 833 HASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMK---QKQIITAQDNIIKDKCAEVAKHNlQNNESQLK 909
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKEIDEKNKEIEELKQTQKSLKK-KQEEKQEL 590
|
250 260 270
....*....|....*....|....*....|....*.
gi 673132010 910 IKELDHSISKHKREADDAAAKVSKMLSDYDWINAEK 945
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
694-1028 |
1.70e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 694 ELRALEEELAGLKNVAEKYRQLKQQWEMKTEE---GDLLQTKLQQSsyhkqQEELDALKKTIEESEETLKSTKEIQKKAE 770
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRAEisnIDYLEEKLKSS-----NLELENIKKQIADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 771 EKYEALENKMKNAEAE--REKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELK-----------REHASNE 837
Cdd:PRK01156 225 IEYNNAMDDYNNLKSAlnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyknrnyiNDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 838 QQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSI 917
Cdd:PRK01156 305 NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 918 sKHKREADDAAAKVSKMLSDYDWINAEkhlFGQPNSAYDFKTNNPKEAGQRLQKLQEVKEKLGRNVN-LRAMNV-----L 991
Cdd:PRK01156 385 -NIERMSAFISEILKIQEIDPDAIKKE---LNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVcpvcgT 460
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 673132010 992 TEAEERYNDLMK----KKRIVENDKSKILATIEDLDQKKNQ 1028
Cdd:PRK01156 461 TLGEEKSNHIINhyneKKSRLEEKIREIEIEVKDIDEKIVD 501
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1081-1143 |
2.51e-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: 2.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 673132010 1081 NLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:cd03214 94 PFNELSGGERQRV----LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
679-879 |
2.70e-05 |
|
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: 46.95 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKN-VAEKYRQLKQQWEMKTEEGDLLQTKLQQ-SSYHKQQEELDALKKTIEES- 755
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAeVAALNRRIQLLEEELERTEERLAEALEKlEEAEKAADESERGRKVLENRa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 756 ----------EETLKSTKEIQKKAEEKYEALENKMKNAEAEREKelkdaqkkldcAKTKADASSKKMKEKQQEVEAITLE 825
Cdd:pfam00261 88 lkdeekmeilEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-----------AEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 673132010 826 LE--ELKREHAS-----NEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQK 879
Cdd:pfam00261 157 LKslEASEEKASeredkYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEK 217
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
180-1039 |
3.00e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 180 AAQKTIEKKEAKLKEIKTILE--EEITPTIQKLKEE----RSSYLEYQKVMREIEHLSRLYIAYQFLRAEDTKERSAGEL 253
Cdd:TIGR00606 235 SSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEikalKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 254 KEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACA-EAQRVNTKSQSAFDLKKKNLASE----- 327
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERGPFSErqikn 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 328 ---------ETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATL 398
Cdd:TIGR00606 395 fhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 399 A--GQMIACKNDISKAQTEA-----KQAQMKLKHAQQEL-KSKQAE-------------VKKMDSGYKKDQDAFEAVKKA 457
Cdd:TIGR00606 475 EldQELRKAERELSKAEKNSltetlKKEVKSLQNEKADLdRKLRKLdqemeqlnhhtttRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 458 KEKLETEMKKLNYEENKEEKLLEKHRQLSRDINNLKGKhealLAKFpNLQFAYKDPEKNWNRNSVKGLVASLINVKDN-- 535
Cdd:TIGR00606 555 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDR----LAKL-NKELASLEQNKNHINNELESKEEQLSSYEDKlf 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 536 -STATALEVVAGERLYNVVVDTEVTAKKLLEKGELKRRYTIIPLNKISARCiaPETLRVAQN---------------LVG 599
Cdd:TIGR00606 630 dVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC--PVCQRVFQTeaelqefisdlqsklRLA 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 600 PDNVHVALSLVDykpELQKGMEFVFGTTFVCNNMDNaKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGaRSQAASILTKFQ 679
Cdd:TIGR00606 708 PDKLKSTESELK---KKEKRRDEMLGLAPGRQSIID-LKEKEIPELRNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEE 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 680 EVKDVQDEL--------RTKENElRALEEELAGLKNV--AEKYRQLKQQWEMKTEEGDLLQTK--LQQSSYHKQQEELDA 747
Cdd:TIGR00606 783 SAKVCLTDVtimerfqmELKDVE-RKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKieLNRKLIQDQQEQIQH 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 748 LKKTIEESE-------ETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:TIGR00606 862 LKSKTNELKseklqigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 821 AITLELEELKREHASNEQQLDAVNEAIKAY----EGQIEKMAAEVAKNKESVNKAQDELMKQKQIITA---QDNIIKDkc 893
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkiQERWLQD-- 1019
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 894 aevakhNLQNNESQLKIKELDHSISKHKREADDaaAKVSKMLSDYDWINAEKHLFGqpnsaydfktNNPKEAGQRLQKLQ 973
Cdd:TIGR00606 1020 ------NLTLRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIK----------RNHVLALGRQKGYE 1081
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 673132010 974 evKEKLGRNVNLRAMNvLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNK 1039
Cdd:TIGR00606 1082 --KEIKHFKKELREPQ-FRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
687-926 |
3.94e-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: 48.02 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 687 ELRTKENELRALEEELAGLKN--VAEKYRQ--LKQQWEMKTEEGDLLQTKLQQSSYH--------KQQEELDALKKTIEE 754
Cdd:COG3096 279 ERRELSERALELRRELFGARRqlAEEQYRLveMARELEELSARESDLEQDYQAASDHlnlvqtalRQQEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 755 SEETLKSTKEIQKKAEEKYEALENKMKNAEAErEKELK----DAQKKLDCAKTKA--------------------DASSK 810
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEE-VDSLKsqlaDYQQALDVQQTRAiqyqqavqalekaralcglpDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 811 KMKEKQQEVEAitlELEELKREHASNEQQLD----AVNEAIKAYEgQIEKMAAEVAKNkESVNKAQdELMKQ---KQIIT 883
Cdd:COG3096 438 NAEDYLAAFRA---KEQQATEEVLELEQKLSvadaARRQFEKAYE-LVCKIAGEVERS-QAWQTAR-ELLRRyrsQQALA 511
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 673132010 884 AQDNIIKDKCAEVAK--HNLQNNESQLkiKELDHSISKHKREADD 926
Cdd:COG3096 512 QRLQQLRAQLAELEQrlRQQQNAERLL--EEFCQRIGQQLDAAEE 554
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
4-100 |
4.17e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.96 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 4 KSIILEGFKSYAQRTEVN----GFDPL-FNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKAS 78
Cdd:COG1106 3 ISFSIENFRSFKDELTLSmvasGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPSE 82
|
90 100
....*....|....*....|..
gi 673132010 79 VSITFdNSDKKQSPLGFEAHDE 100
Cdd:COG1106 83 FEILF-LLDGVRYEYGFELDKE 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
680-848 |
4.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 680 EVKDVQDELRTKENELRALEEELAGLKnvaEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETl 759
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELK---GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 760 KSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASS----------------------KKMKE--K 815
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpeylalldrleedglpeyeERFKEllN 841
|
170 180 190
....*....|....*....|....*....|...
gi 673132010 816 QQEVEAITLELEELKREHASNEQQLDAVNEAIK 848
Cdd:COG4913 842 ENSIEFVADLLSKLRRAIREIKERIDPLNDSLK 874
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
705-997 |
4.74e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 705 LKNVAEKYRQLKQQWEMKtEEGDLLQTklqQSSYHKQQEELDALKKTIEESEETLKSTKEiqkKAEEKYEALENKMknae 784
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK-EEKDLHER---LNGLESELAELDEEIERYEEQREQARETRD---EADEVLEEHEERR---- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 785 aEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEElKREHASNEQQLDAVneAIKAYEGQIEkmaaEVAKN 864
Cdd:PRK02224 251 -EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE-ERDDLLAEAGLDDA--DAEAVEARRE----ELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 865 KESVnkaQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAe 944
Cdd:PRK02224 323 DEEL---RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE- 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 673132010 945 khlfgqpnsAYDFKTNNPKEAGQRLQKLQEVKEKL-GRNVNLRAmnVLTEAEER 997
Cdd:PRK02224 399 ---------RFGDAPVDLGNAEDFLEELREERDELrEREAELEA--TLRTARER 441
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
23-123 |
6.69e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 23 FDPLFNAITGLNGSGKSNILDSICFLLGisnlsqVRASnlQDLVyKNGQAgitKASVSITFDNSDKKQ-----SPLGFEA 97
Cdd:COG0497 20 FGPGLTVLTGETGAGKSILLDALGLLLG------GRAD--ASLV-RHGAD---KAEVEAVFDLSDDPPlaawlEENGLDL 87
|
90 100
....*....|....*....|....*..
gi 673132010 98 HD-EITVTRQVVIGGRNKYLINGVNAN 123
Cdd:COG0497 88 DDgELILRREISADGRSRAFINGRPVT 114
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
678-1029 |
7.16e-05 |
|
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: 46.99 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 678 FQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEmkteegdllqtklqqsSYHKQQEELDALKKTIEESEE 757
Cdd:pfam05622 96 VLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVE----------------TYKKKLEDLGDLRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 758 tlKSTKEIQKKAEekyeaLENKMKNAEAER------EKELKDAQKKLDCAKTKADA---SSKKMKEK----QQEVEAITL 824
Cdd:pfam05622 160 --RNAEYMQRTLQ-----LEEELKKANALRgqletyKRQVQELHGKLSEESKKADKlefEYKKLEEKlealQKEKERLII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 825 E-------LEELKREHASNEQQLDAVNEAIKAYEGqIEKMAAEV--AKNKESVNKAQDE----LMKQ----KQIITAQDN 887
Cdd:pfam05622 233 ErdtlretNEELRCAQLQQAELSQADALLSPSSDP-GDNLAAEImpAEIREKLIRLQHEnkmlRLGQegsyRERLTELQQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 888 IIKDkcAEVAKHNL--QNNESQLKIKELDHSISKHKRE-------ADDAAAKVSKMLSDYDWINaEKHLFGQPNSAYdFK 958
Cdd:pfam05622 312 LLED--ANRRKNELetQNRLANQRILELQQQVEELQKAlqeqgskAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQ-IE 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673132010 959 TNNPKEAGQRLQKLQEVKEKL-GRNVNLRAMnvlteaEERYndlmkkKRIVENDKSkilaTIEDLDQKKNQA 1029
Cdd:pfam05622 388 ELEPKQDSNLAQKIDELQEALrKKDEDMKAM------EERY------KKYVEKAKS----VIKTLDPKQNPA 443
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
692-821 |
7.46e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 692 ENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEgdllQTKLQQSSYHKQQEEL-DALKKTIEESEETLKSTKEIQKKAe 770
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEK----LQEEEDKLLEEAEKEAqQAIKEAKKEADEIIKELRQLQKGG- 600
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 673132010 771 ekyealenkmknAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:PRK00409 601 ------------YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
678-933 |
8.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 678 FQEVKDVQDELRTKENELRALEEELAGLKNVA-------EKYRQLKQQWEMKTEE--GDLLQTKLQQSSYHKQQEELDAL 748
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEElrDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 749 KKTIEESEETLKS-TKEIQKKAEEKYEALEnKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAI----- 822
Cdd:PRK02224 351 ADDLEERAEELREeAAELESELEEAREAVE-DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELrerea 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 823 --TLELEELKREHASNEQQLDAVN--------------EAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQD 886
Cdd:PRK02224 430 elEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 673132010 887 NI--IKDKCAEVAK----HNLQNNESQLKIKELDHSISKHKREADDAAAKVSK 933
Cdd:PRK02224 510 RIerLEERREDLEEliaeRRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
667-878 |
9.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 667 ARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEmkteegdLLQTKLQQssyhkQQEELD 746
Cdd:COG4913 642 ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLE-------ELEAELEE-----LEEELD 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 747 ALKKTIEESEETLKSTKEIQKKAEEKYEALENKMK-----NAEAEREKELKDA--QKKLDCAKTKADASSKKMKEKQQEV 819
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEEL 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 673132010 820 EAItleLEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAE-----VAKNKESVNKAQDELMKQ 878
Cdd:COG4913 790 ERA---MRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVAD 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-446 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 241 RAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDkETGGKLKSLEDACAE----AQRVNTKSQSA 316
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-ELRAELEAQKEELAEllraLYRLGRQPPLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 317 FDLKKKNLASEETK----------RKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAG 386
Cdd:COG4942 124 LLLSPEDFLDAVRRlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 387 LSSNEDGAEATLAgqmiackndisKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKK 446
Cdd:COG4942 204 LEKELAELAAELA-----------ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
667-842 |
1.29e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 667 ARSQAASILTKF--QEVKDVQDELRTKENELRALEEE-------------LAGLKNVAEKYRQLKQQWEMKTEEGDLLQT 731
Cdd:COG3206 168 LRREEARKALEFleEQLPELRKELEEAEAALEEFRQKnglvdlseeakllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 732 KL----QQSSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELK----DAQKKLDCAKT 803
Cdd:COG3206 248 QLgsgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrilaSLEAELEALQA 327
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 673132010 804 KADASSKKMKEKQQEVEAIT---LELEELKREHASNEQQLDA 842
Cdd:COG3206 328 REASLQAQLAQLEARLAELPeleAELRRLEREVEVARELYES 369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
711-929 |
1.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 711 KYRQLKQQWEMKTEEGDLLQTKLQQSsyhkqQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKE 790
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAL-----QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 791 LKDAQKKLDCAK---------------TKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIE 855
Cdd:COG3883 92 ARALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 673132010 856 KMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAA 929
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
743-924 |
1.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 743 EELDALKKTIEESEETLKSTKEIQKKAEEkyeaLENKMKNAEAEREkELKDAQKKLDCAKTKADASsKKMKEKQQEVEAI 822
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELE-ELREELEKLEKLLQLLPLY-QELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 823 TLELEELKREHA---SNEQQLDAVNEAIKAYEGQIEKMAAEV-AKNKESVNKAQDELMKQKQIITAQDNIIKDkcAEVAK 898
Cdd:COG4717 145 PERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEE--AQEEL 222
|
170 180
....*....|....*....|....*.
gi 673132010 899 HNLQNNESQLKIKELDHSISKHKREA 924
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEA 248
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
717-870 |
1.77e-04 |
|
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: 45.79 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 717 QQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKS--------TKEIQKKAEekyEALENKMKNAEAERE 788
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQElekeikklESSIKQVEE---ELEELKEQNEELEKQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 789 KELK--------DAQKKLDCAKTKADASSKKMKEKQQEVE----AITLELEELKREHASNEQQLDAVNEAIKAYEGQIEK 856
Cdd:pfam05667 386 YKVKkktldllpDAEENIAKLQALVDASAQRLVELAGQWEkhrvPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
170
....*....|....
gi 673132010 857 MAAEvAKNKESVNK 870
Cdd:pfam05667 466 VAEE-AKQKEELYK 478
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1062-1143 |
1.77e-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: 44.41 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1062 QTVLDGLEFKVALGNtwkENLtelSGGQRSLVALSLILsmllFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFI 1141
Cdd:cd03244 123 ESLPGGLDTVVEEGG---ENL---SVGQRQLLCLARAL----LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVL 192
|
..
gi 673132010 1142 VV 1143
Cdd:cd03244 193 TI 194
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
794-870 |
1.94e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 673132010 794 AQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNK 870
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
761-933 |
2.00e-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: 45.14 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 761 STKEIQKKAEEKYEALENKMKNAEaereKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQL 840
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 841 DAVNEAIKAYEGQIEKMAAEVAK-----------NKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLK 909
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180
....*....|....*....|....
gi 673132010 910 IKELDHSISKHKREADDAAAKVSK 933
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAE 196
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
801-878 |
2.02e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 801 AKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQ 878
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
684-875 |
2.34e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 684 VQDELRTKENELRALEEELAGLKN----VAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELD--ALKKTIEESEE 757
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSntelLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQnkELKAKLQEMEG 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 758 TLKStkeiqkKAEEKYEALENKMKNAEAEREKELKDAQkkldcaktkadASSKKMKEKQQEVEAITLELEELKREHASNE 837
Cdd:pfam01576 960 TVKS------KFKSSIAALEAKIAQLEEQLEQESRERQ-----------AANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
170 180 190
....*....|....*....|....*....|....*...
gi 673132010 838 QQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDEL 875
Cdd:pfam01576 1023 DQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQREL 1060
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
743-878 |
2.36e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 45.25 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 743 EELDAlKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAErekeLKDAQKKLDCAKT---KADASSKKMKEKQQEV 819
Cdd:PRK12472 198 EAEDA-ARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAE----LKRADKALAAAKTdeaKARAEERQQKAAQQAA 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 820 EAITlELEELKREHASNEQQLDAVNEAIKAYEgqiekmaaevAKNKESVNKAQDELMKQ 878
Cdd:PRK12472 273 EAAT-QLDTAKADAEAKRAAAAATKEAAKAAA----------AKKAETAKAATDAKLAL 320
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1081-1120 |
2.57e-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: 2.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 673132010 1081 NLTELSGGQRSLVALSLILSmllfKPAPIYILDEVDAALD 1120
Cdd:cd03237 112 EVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLD 147
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
760-931 |
2.73e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 760 KSTKEIQKKAEEKYEA-LENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE-LKREHASN- 836
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRiLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnLDRKLELLe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 837 --EQQLDAVNEAIKAYEGQIEKMAAEVaknKESVNKAQDELMKQKQiITAQD--NIIKDKCAEVAKHnlqnnESQLKIKE 912
Cdd:PRK12704 107 krEEELEKKEKELEQKQQELEKKEEEL---EELIEEQLQELERISG-LTAEEakEILLEKVEEEARH-----EAAVLIKE 177
|
170
....*....|....*....
gi 673132010 913 ldhSISKHKREADDAAAKV 931
Cdd:PRK12704 178 ---IEEEAKEEADKKAKEI 193
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
740-947 |
2.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 740 KQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKelkdaqkkldcaktkadasskkmKEKQQEV 819
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-----------------------LEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 820 EAITLELEELKREHASNEQQLDAVNEAIKAYEG---QIEKMAAEVAKNKESVnkaqDELMKQKQIITAQdniikdkcaEV 896
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEEL----EELLEQLSLATEE---------EL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 673132010 897 AKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHL 947
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1079-1144 |
3.36e-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: 3.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 673132010 1079 KENLteLSGGQRSLVALSLilsMLLfKPAPIYILDEVDAALDlSHTQN-IGQMLRTHFTHSQFIVVS 1144
Cdd:cd03228 93 RENI--LSGGQRQRIAIAR---ALL-RDPPILILDEATSALD-PETEAlILEALRALAKGKTVIVIA 152
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
669-912 |
3.73e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 669 SQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKN-VAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQ--EEL 745
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDeLNAQVKELREEAQELREKRDELNEKVKELKEERDElnEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 746 DALKKTIEE----SEETLKSTKEIqKKAEEKYEALENKMKNA----EAERE--KELKDAQKKLDCAKtKADASSKKMKEK 815
Cdd:COG1340 88 NELREELDElrkeLAELNKAGGSI-DKLRKEIERLEWRQQTEvlspEEEKElvEKIKELEKELEKAK-KALEKNEKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 816 QQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAE 895
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250
....*....|....*..
gi 673132010 896 VAKHNLQNNESQLKIKE 912
Cdd:COG1340 246 LKKLRKKQRALKREKEK 262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
696-945 |
4.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 696 RALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSsyhkqQEELDALKKTIEESEETLKSTKEIQKKAEEKYEA 775
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 776 LENKMKNAEAERE---KELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQL-----DAVNEAI 847
Cdd:COG4372 106 LQEEAEELQEELEelqKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqalseAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 848 KAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDK-CAEVAKHNLQNNESQLKIKELDHSISKHKREADD 926
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKlGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250
....*....|....*....
gi 673132010 927 AAAKVSKMLSDYDWINAEK 945
Cdd:COG4372 266 AILVEKDTEEEELEIAALE 284
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1084-1144 |
4.71e-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: 4.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673132010 1084 ELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLRT-HFTHSQFIVVS 1144
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAM---EP-EVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVT 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1082-1132 |
5.12e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 5.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 673132010 1082 LTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:PRK11231 136 LTDLSGGQRQRA----FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
735-866 |
5.36e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 735 QSSYHKQQEELDALKKTIEES----EETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLdcaktkadasSK 810
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELerelEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA----------QQ 577
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 811 KMKEKQQEVEAITLELEELKREHAS--NEQQLDavnEAIKAYEGQIEKMAAEVAKNKE 866
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYAsvKAHELI---EARKRLNKANEKKEKKKKKQKE 632
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
686-871 |
5.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 686 DELRTKENELRALEEELAGLKNVAEKYRQL-KQQW---EMKTEEGDL------LQTKLQQSSYH--------KQQEELDA 747
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRELYTSRRQLaAEQYrlvEMARELAELneaesdLEQDYQAASDHlnlvqtalRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 748 LKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAERE---KELKDAQKKLDCAKTKADASskkmkekQQEVEAitl 824
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelkSQLADYQQALDVQQTRAIQY-------QQAVQA--- 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 673132010 825 eLEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEV--AKNKESVNKA 871
Cdd:PRK04863 423 -LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELlsLEQKLSVAQA 470
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1033 |
5.98e-04 |
|
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: 44.34 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 681 VKDVQDELRTKENELRALEEELAGLKnvAEKYRQLKQQW---EMKTEEGDLLQTKLQQSSYHKQQ-----EELDALKKTI 752
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMK--SECQGQMERQMaaiQGKNESLEKVSSLTAQLESTKEMlrkvvEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 753 EESEETLkstKEIQKKAEEKYEALEnkMKNAEAEREKELKDAQ-KKLDCAKTKADasskKMKEKQQEVEAITLELEELKR 831
Cdd:pfam15921 492 ESSERTV---SDLTASLQEKERAIE--ATNAEITKLRSRVDLKlQELQHLKNEGD----HLRNVQTECEALKLQMAEKDK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 832 EHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKqiitaqdnIIKDKcaevakhnlqnneSQLKIK 911
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK--------ILKDK-------------KDAKIR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 912 ELDHSISKHKREADDAAAKVSKMLSDYDWINAEKhlfgqpnsayDFKTNNPKEAGQRLQKLQEVKEKLGRNVNlramNVL 991
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKQER----------DQLLNEVKTSRNELNSLSEDYEVLKRNFR----NKS 687
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 673132010 992 TEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIA 1033
Cdd:pfam15921 688 EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
680-945 |
6.34e-04 |
|
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: 43.95 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 680 EVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKL----QQSSYHKQ-----QEELDALKK 750
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIenmtQLVGQHGRtagamQVEKAQLEK 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 751 TIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCA---KTKADASSKKMKEKQQEVEAITLELE 827
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdiKQERDQLLNEVKTSRNELNSLSEDYE 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 828 ELKREHASNEQQLDAVNEAIKAyegQIEKMAAEVAKNK---ESVNKAQDELMK-----QKQIITAQDNI--IKDKCAEVA 897
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKM---QLKSAQSELEQTRntlKSMEGSDGHAMKvamgmQKQITAKRGQIdaLQSKIQFLE 754
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 673132010 898 KHNLQNNESQLKIKELDHSISKhkrEADDAAAKVSKMLSDYDWINAEK 945
Cdd:pfam15921 755 EAMTNANKEKHFLKEEKNKLSQ---ELSTVATEKNKMAGELEVLRSQE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-392 |
6.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 182 QKTIEKKEAKLKEIKTILEE--EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYI-----AYQFLRAEDTKER---SAG 251
Cdd:COG4913 606 FDNRAKLAALEAELAELEEElaEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaEREIAELEAELERldaSSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 252 ELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRkdketggkLKSLEDACAEAQRVNtksQSAFDLKKKNLASE-ETK 330
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKE--------LEQAEEELDELQDRL---EAAEDLARLELRALlEER 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 673132010 331 RKELqnsmaedskALAAKEKEVKK-ITDGLHGLQEASNKDAEALAAAQQHFNA--------VSAGLSSNED 392
Cdd:COG4913 755 FAAA---------LGDAVERELREnLEERIDALRARLNRAEEELERAMRAFNRewpaetadLDADLESLPE 816
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
756-874 |
6.98e-04 |
|
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: 43.30 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 756 EETLKSTKEIQKKAEEKYEALEnKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKR-EHA 834
Cdd:TIGR02794 60 KPAAKKEQERQKKLEQQAEEAE-KQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAkAEA 138
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 673132010 835 SNEQQLDAvnEAIKAYEGQIEKMAAEVAKNKESVNKAQDE 874
Cdd:TIGR02794 139 EAERKAKE--EAAKQAEEEAKAKAAAEAKKKAEEAKKKAE 176
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
709-930 |
7.05e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 709 AEKYRQLKQQWEMKTEEGDLLQTKLQQSSYhkqQEELDALKKTIEESEETLKSTKEIQKKAEEKyealenKMKNAEAERE 788
Cdd:PTZ00108 1101 KEKVEKLNAELEKKEKELEKLKNTTPKDMW---LEDLDKFEEALEEQEEVEEKEIAKEQRLKSK------TKGKASKLRK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 789 KELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESV 868
Cdd:PTZ00108 1172 PKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673132010 869 NKAQDELMKQKQIITAQDNIIKDKCAEVAkhnlqNNESQLKIKELDHSISKHKREADDAAAK 930
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVSA-----VQYSPPPPSKRPDGESNGGSKPSSPTKK 1308
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
639-860 |
7.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 639 VAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGL--------KNVAE 710
Cdd:COG4717 262 LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 711 KYRQLKQQWEMKTEEGDLlQTKLQQSSYHKQQEELdaLKKTIEESEETLKSTKEIQkkaeEKYEALENKMKNAEAEREKE 790
Cdd:COG4717 342 LLDRIEELQELLREAEEL-EEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQA----EEYQELKEELEELEEQLEEL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 791 LKDAQKKLDcaktkadasskkmkekQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAE 860
Cdd:COG4717 415 LGELEELLE----------------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
742-996 |
8.66e-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: 43.80 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 742 QEELDA-LKKTIEESEETLKSTKEIQKKAEEKYEALENKmKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:TIGR00618 151 QGEFAQfLKAKSKEKKELLMNLFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 821 AITLELEELKREHASNEQQLDAVNEAIkayegQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNiiKDKCAEVAKHN 900
Cdd:TIGR00618 230 HLREALQQTQQSHAYLTQKREAQEEQL-----KKQQLLKQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 901 LQ--------NNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHLFGQPNSAYDFKTNNPKEAG--QRLQ 970
Cdd:TIGR00618 303 TQieqqaqriHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltQHIH 382
|
250 260
....*....|....*....|....*.
gi 673132010 971 KLQEVKEKLGRNVNLRAMNVLTEAEE 996
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQRE 408
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-100 |
9.34e-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: 9.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 673132010 27 FNAITGLNGSGKSNILDSICFLLGIsnlsqvrASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEAHDE 100
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADF-------DALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLE 67
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
679-859 |
9.47e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENEL-------RALEEELAGLKNVAEKYRQLKQQWEMKTEEgDLLQTKLQQSSYHKQQEEldALKKT 751
Cdd:pfam04012 29 QAIRDMQSELVKARQALaqtiarqKQLERRLEQQTEQAKKLEEKAQAALTKGNE-ELAREALAEKKSLEKQAE--ALETQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 752 IEESEETLKSTKEIQKKAEEKYEALENKmKNAEAEREKELKdAQKKLDCAKTKADASS-----KKMKEKQQEVEAITLEL 826
Cdd:pfam04012 106 LAQQRSAVEQLRKQLAALETKIQQLKAK-KNLLKARLKAAK-AQEAVQTSLGSLSTSSatdsfERIEEKIEEREARADAA 183
|
170 180 190
....*....|....*....|....*....|...
gi 673132010 827 EELkREHASNEQQLDAVNEAIKAYEGQIEKMAA 859
Cdd:pfam04012 184 AEL-ASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-344 |
1.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 161 ILSMIEEAAGTRMYEY------KKIAAQKTIEKKEAKLKEIKTILEE---------EITPTIQKLKEERSSYLEYQKVMR 225
Cdd:COG4717 43 IRAMLLERLEKEADELfkpqgrKPELNLKELKELEEELKEAEEKEEEyaelqeeleELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 226 EIEHLSRLYIAYQFLRAE-DTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACA 304
Cdd:COG4717 123 KLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 673132010 305 EAQRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKA 344
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
742-876 |
1.19e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 742 QEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQE 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 822 ITLELEELKrehasneQQLDAVNEAIKAYEGQIEKM----AAEVAKNKESVNKAQDELM 876
Cdd:smart00787 237 LESKIEDLT-------NKKSELNTEIAEAEKKLEQCrgftFKEIEKLKEQLKLLQSLTG 288
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
682-840 |
1.28e-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: 42.89 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 682 KDVQDELRTKENELRALEE-ELAGLKNVAEKYRQLKQ-QWEMKTEEGDLLQTKLQQ------SSYHKQQEEL-DALKKTI 752
Cdd:pfam10174 589 REVENEKNDKDKKIAELESlTLRQMKEQNKKVANIKHgQQEMKKKGAQLLEEARRRednladNSQQLQLEELmGALEKTR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 753 EESEETLKSTKEIQKKAEEKyealENKMKNAEAEREKELKDA----QKKLDCAKTKADA-------SSKKMKEKQQEVEA 821
Cdd:pfam10174 669 QELDATKARLSSTQQSLAEK----DGHLTNLRAERRKQLEEIlemkQEALLAAISEKDAniallelSSSKKKKTQEEVMA 744
|
170
....*....|....*....
gi 673132010 822 itleleeLKREHASNEQQL 840
Cdd:pfam10174 745 -------LKREKDRLVHQL 756
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
668-861 |
1.29e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 668 RSQAASILTKFQE-VKDVQDELRTKENELRALEEELAGLKnvAEKyRQLKQQWEMKTEEGDLLQTKLQQ----------- 735
Cdd:COG1842 11 RANINALLDKAEDpEKMLDQAIRDMEEDLVEARQALAQVI--ANQ-KRLERQLEELEAEAEKWEEKARLalekgredlar 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 736 ---SSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAeREKELKdAQKKLDCAKTKADASS--- 809
Cdd:COG1842 88 ealERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKA-RAKAAK-AQEKVNEALSGIDSDDats 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 673132010 810 --KKMKEKQQEVEAITLELEELkREHASNEQQLDAVNEAIKAyEGQIEKMAAEV 861
Cdd:COG1842 166 alERMEEKIEEMEARAEAAAEL-AAGDSLDDELAELEADSEV-EDELAALKAKM 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
679-863 |
1.42e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEgdllQTKLQQssyhkqqeELDALKKTI------ 752
Cdd:COG3096 903 DAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQ----QRRLKQ--------QIFALSEVVqrrphf 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 753 --EESEETLKSTKEIQkkaeekyEALENKMKNAEAEREK---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVE 820
Cdd:COG3096 971 syEDAVGLLGENSDLN-------EKLRARLEQAEEARREareQLRQAQAQYSqynqvlaSLKSSRDAKQQTLQELEQELE 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 673132010 821 AITL------------ELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAK 863
Cdd:COG3096 1044 ELGVqadaeaeerariRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1066-1120 |
1.49e-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: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 673132010 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 |
1.51e-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: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 673132010 1085 LSGGQRSLVALSLilsmLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTH 1134
Cdd:COG4133 132 LSAGQKRRVALAR----LLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1062-1114 |
1.71e-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: 40.32 E-value: 1.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 673132010 1062 QTVLDGLEFKVALGNTWKENLTELSGGQRSLVAlsliLSMLLFKPAPIYILDE 1114
Cdd:pfam00005 99 EEALEKLGLGDLADRPVGERPGTLSGGQRQRVA----IARALLTKPKLLLLDE 147
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1081-1132 |
1.81e-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: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 673132010 1081 NLTELSGGQRSLVAlsliLSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:COG1120 134 PVDELSGGERQRVL----IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLR 181
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
673-880 |
1.84e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 673 SILTKFQEVKDVQDELRTKENELRALEEElaglKNVAEKYRQlKQQWEMKTEEGDLLQTKLQQSSyHKQQEELDALKKTI 752
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRRLEVE----RKRREQEEQ-RRLQQEQLERAEKMREELELEQ-QRRFEEIRLRKQRL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 753 EesEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEaitlelEELKR- 831
Cdd:pfam15709 397 E--EERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLA------EEQKRl 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 673132010 832 EHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQ 880
Cdd:pfam15709 469 MEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-335 |
1.85e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 181 AQKTIEKKEAKLKEIKT-----ILEEEITPTIQKLKEERSSYLEYQKVMREIEH--------LSRLYIAYQFLRAEDTKE 247
Cdd:COG3206 187 LRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEArlaalraqLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 248 RSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQ-RVNTKSQSAFDLKKK--NL 324
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQaREASLQAQLAQLEARlaEL 346
|
170
....*....|.
gi 673132010 325 ASEETKRKELQ 335
Cdd:COG3206 347 PELEAELRRLE 357
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
689-885 |
1.85e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.14 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 689 RTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEE--LDALKKTIEESEETLKSTKEIQ 766
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQaaKQAEEKQKQAEEAKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 767 KKAEEKYE--ALENKMKNAEAEREKELK-DAQKKLDCAKTKADASSKKMKEKQQEVEAitlelEELKREHASNEQQLDAv 843
Cdd:TIGR02794 134 AKAEAEAErkAKEEAAKQAEEEAKAKAAaEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-----EEAKAKAEAAKAKAAA- 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 673132010 844 nEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQ 885
Cdd:TIGR02794 208 -EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
685-1037 |
2.01e-03 |
|
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: 42.52 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 685 QDELRTKENELRALEEELAGL----KNVAEKYRQLKQ--------------QWEMKTEEGDLLQTKLQQSSYHKQQ---- 742
Cdd:pfam12128 346 QEQLPSWQSELENLEERLKALtgkhQDVTAKYNRRRSkikeqnnrdiagikDKLAKIREARDRQLAVAEDDLQALEselr 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 743 EELDALKKTIEESEETLKS--------------TKEIQKKAEEKYEALEnKMKNAEAEREKELKDAQKKLDCAKTKADAS 808
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSrlgelklrlnqataTPELLLQLENFDERIE-RAREEQEAANAEVERLQSELRQARKRRDQA 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 809 SKKMKEKQQEVEAITLELEELkrehasnEQQLDAVNEAIKAYegqiekMAAEVAKNKESVNKAQD-ELMKQKQIITAQDN 887
Cdd:pfam12128 505 SEALRQASRRLEERQSALDEL-------ELQLFPQAGTLLHF------LRKEAPDWEQSIGKVISpELLHRTDLDPEVWD 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 888 IIKDKCAEVAKHNL-----QNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEkhlFGQPNSAYDFKTNNP 962
Cdd:pfam12128 572 GSVGGELNLYGVKLdlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE---LEKASREETFARTAL 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 673132010 963 KEAGQRLQKLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKV 1037
Cdd:pfam12128 649 KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-950 |
2.05e-03 |
|
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: 42.42 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 677 KFQEVKdvQDELRtKENELRALEEELAGLKNVAEKYRQLK---------QQWEMKTE-EGDLLQTKLQQSSYHKQQEELD 746
Cdd:pfam17380 292 KFEKME--QERLR-QEKEEKAREVERRRKLEEAEKARQAEmdrqaaiyaEQERMAMErERELERIRQEERKRELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 747 ALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLEL 826
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 827 EELKREHASNEQQLdavnEAIKAYEGQIEKMAAEVAKNKESVNKAQD--------ELMKQKQIITAQDNiiKDKCAEVAK 898
Cdd:pfam17380 449 ERVRLEEQERQQQV----ERLRQQEEERKRKKLELEKEKRDRKRAEEqrrkilekELEERKQAMIEEER--KRKLLEKEM 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 899 HNLQN---NESQLKIKELDHSISK---HKREADDAAAKVSKMLSDYDWINAEKHLFGQ 950
Cdd:pfam17380 523 EERQKaiyEEERRREAEEERRKQQemeERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-462 |
2.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 175 EYKKIAAQ-KTIEKKEAKLKEIKTILEEEIT--PTIQKLKEERSSYLEYQKVMREI--EHLSRLYIAYQFLRAEDTK--- 246
Cdd:PRK03918 460 ELKRIEKElKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEKLKKYnlEELEKKAEEYEKLKEKLIKlkg 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 247 -----ERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQRVNTKsqsafdlkK 321
Cdd:PRK03918 540 eikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA--------E 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 322 KNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQeaSNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagq 401
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEE----- 684
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 673132010 402 miackndISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKDQDAFEAVKKAKEKLE 462
Cdd:PRK03918 685 -------LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
688-900 |
2.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 688 LRTKENELRALEEELAGLKNVAEKYRQLKQQWEmkteegdLLQTKLQQSsyhKQQeeLDALKKTI--------EESEETL 759
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQ-------QAQQTQRDA---KQQ--AFALTEVVqrrahfsyEDAAEML 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 760 KSTKEIQkkaeekyEALENKMKNAEAEREK---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVEAITL----E 825
Cdd:PRK04863 981 AKNSDLN-------EKLRQRLEQAEQERTRareQLRQAQAQLAqynqvlaSLKSSYDAKRQMLQELKQELQDLGVpadsG 1053
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 673132010 826 LEELKREHASN-EQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQdNIIKDKCAEVAKHN 900
Cdd:PRK04863 1054 AEERARARRDElHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA-KAGWCAVLRLVKDN 1128
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1064-1132 |
2.36e-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: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 1064 VLDGLEFkVALGNTWKENLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03235 113 VDEALER-VGLSELADRQIGELSGGQQQRV----LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
152-410 |
2.50e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 152 KVLNMKPPEILSMIEEAAGTRMY----EYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREI 227
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 228 EHLSRLYIAYQFLRAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKD-----KETGGKLKSLEDA 302
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeelkKAEEENKIKAEEA 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 303 CAEAQRVNTKSQSA----------FDLKKKNLASEETKRKELQNSMAE-----DSKALAAKEKEVKKITDGLHGLQEASN 367
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAkkdeeekkkiAHLKKEEEKKAEEIRKEKEAVIEEeldeeDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 673132010 368 KDAEALAAAQQHFNAVS--AGLSSNEDGAEATLAGQMIACKNDIS 410
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIkeVADSKNMQLEEADAFEKHKFNKNNEN 1860
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1059-1143 |
2.61e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1059 PEGQTVLDGLE-FKVALgNTWKENLTELSGGQRSLVALsliLSMLLFKPApIYILDEVDAALDLSHTQNIGQMLrTHFTH 1137
Cdd:PRK10247 112 PDPAIFLDDLErFALPD-TILTKNIAELSGGEKQRISL---IRNLQFMPK-VLLLDEITSALDESNKHNVNEII-HRYVR 185
|
....*.
gi 673132010 1138 SQFIVV 1143
Cdd:PRK10247 186 EQNIAV 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1084-1143 |
2.73e-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: 2.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 1084 ELSGGQRSLVALsliLSMLLFKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:COG4136 133 TLSGGQRARVAL---LRALLAEPRAL-LLDEPFSKLDAALRAQFREFVFEQIRQRGIPAL 188
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-49 |
2.93e-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: 41.43 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 673132010 1 MYVKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLL 49
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEID-LDEDLTVLIGKNNSGKSSILEALDIFL 47
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
745-875 |
2.98e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.39 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 745 LDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKK----LDCAKTKADASSKKMKEK-QQEV 819
Cdd:COG0711 26 LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEaeaiAEEAKAEAEAEAERIIAQaEAEI 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 673132010 820 EAItleleelkREHASNEQQLDAVNEAIKAYEGQIEKMAAEvAKNKESVNKAQDEL 875
Cdd:COG0711 106 EQE--------RAKALAELRAEVADLAVAIAEKILGKELDA-AAQAALVDRFIAEL 152
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-453 |
3.03e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 41.65 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 8 LEGFKSYAQRTEVNGFDPLfNAITGLNGSGK---SNILDSICfllgisnlsqvrasnlqdlvyKNGQAGITKASVSITFD 84
Cdd:COG4694 8 LKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE---------------------LGDTSSEVIAEFEIEAG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 85 NSDKKQSPLGFEA-------HDEITVTRQVVIGGRNKYLINGVNANNTRVQDLfcSVGLNVNNPHFLIMQGRITKVLNMK 157
Cdd:COG4694 66 GSAPNPSVRVFNRdfveenlRSGEEIKGIFTLGEENIELEEEIEELEKEIEDL--KKELDKLEKELKEAKKALEKLLEDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEK-------------KEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVM 224
Cdd:COG4694 144 AKSIKDDLKKLFASSGRNYRKANLEKKLSAlksssedelkeklKLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 225 REIEHLSRLYIAYQ---FLRA----EDTKERS-----AGELKEmqDKIVNLQEVLSEN-EKKIKALNCEIEELERRKDKE 291
Cdd:COG4694 224 SAIEELAALIQNPGnsdWVEQglayHKEEEDDtcpfcQQELAA--ERIEALEAYFDDEyEKLLAALKDLLEELESAINAL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 292 TGGKLKSLEDACAEA-QRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKALAakeKEVKKITDGLHGLQEASNKDA 370
Cdd:COG4694 302 SALLLEILRTLLPSAkEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELL---DELNDLIAALNALIEEHNAKI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 371 EALAAAQqhfnavSAGLSSNEDGAEATLAGQMIACKNDISKAQTEAKQAQmKLKHAQQELKSKQAEVKKMDSGYKKDQDA 450
Cdd:COG4694 379 ANLKAEK------EEARKKLEAHELAELKEDLSRYKAEVEELIEELKTIK-ALKKALEDLKTEISELEAELSSVDEAADE 451
|
...
gi 673132010 451 FEA 453
Cdd:COG4694 452 INE 454
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
144-468 |
3.08e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 144 LIMQGRITKVLNMKPPEILSMIEEAAGT--------RMYEYKKiAAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKE 212
Cdd:PRK10246 152 LLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHK-SARTELEKLQAQASGVALLTPEQvqsLTASLQVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 213 ERSSYLEYQKVM-REIEHLSRL-YIAYQFLRAEDTKERSAGELKEMQDKIVNLQevLSENEKKIKALNCEIEELERRkdk 290
Cdd:PRK10246 231 EEKQLLTAQQQQqQSLNWLTRLdELQQEASRRQQALQQALAAEEKAQPQLAALS--LAQPARQLRPHWERIQEQSAA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 291 etggklksLEDACAEAQRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKALAAKEKeVKKITDGLHG-----LQEA 365
Cdd:PRK10246 306 --------LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDR-FRQWNNELAGwraqfSQQT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 366 SNKD-----AEALAAAQQHFNAV-SAGLS-SNEDGAEA--------TLAGQMIACKNDISKAQTEAKQAQMKLKHAQQEL 430
Cdd:PRK10246 377 SDREqlrqwQQQLTHAEQKLNALpAITLTlTADEVAAAlaqhaeqrPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQ 456
|
330 340 350
....*....|....*....|....*....|....*...
gi 673132010 431 KSKQAEVKKMDSGYKKDQDAFEAVKKAKEkLETEMKKL 468
Cdd:PRK10246 457 TQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDL 493
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
724-1044 |
3.14e-03 |
|
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: 41.75 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 724 EEGDLLQTKLQ-QSSYHKQQEE-LDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCA 801
Cdd:pfam12128 604 ERLDKAEEALQsAREKQAAAEEqLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 802 KTKADASSKKMKEKQQEVEAitlELEELKREHASNEQQ-LDAVNEAIKAYEGQIEkmaAEVAKNKESVNKAQDELMKQKQ 880
Cdd:pfam12128 684 LNSLEAQLKQLDKKHQAWLE---EQKEQKREARTEKQAyWQVVEGALDAQLALLK---AAIAARRSGAKAELKALETWYK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 881 IITAQDNIIKDKCAEVAKhnlqnnesqlKIKELDHSISkhkreadDAAAKVSKMLSDYDWINaekHLFGQPNSAYDFKTN 960
Cdd:pfam12128 758 RDLASLGVDPDVIAKLKR----------EIRTLERKIE-------RIAVRRQEVLRYFDWYQ---ETWLQRRPRLATQLS 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 961 NPKEAGQRLQ----------KLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMKKKRIVENDK---------SKILATIED 1021
Cdd:pfam12128 818 NIERAISELQqqlarliadtKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAnseqaqgsiGERLAQLED 897
|
330 340
....*....|....*....|...
gi 673132010 1022 LdQKKNQALNIAWQKVNKDFGSI 1044
Cdd:pfam12128 898 L-KLKRDYLSESVKKYVEHFKNV 919
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
740-939 |
3.26e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 740 KQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAERE-----KELKDAQKKLdcaKTKADASSKKMKE 814
Cdd:TIGR01612 1497 GCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDseiiiKEIKDAHKKF---ILEAEKSEQKIKE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 815 KQQevEAITLElEELKREHASNEQQLDaVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDelmKQKQIITAQDNIIKDKCA 894
Cdd:TIGR01612 1574 IKK--EKFRIE-DDAAKNDKSNKAAID-IQLSLENFENKFLKISDIKKKINDCLKETES---IEKKISSFSIDSQDTELK 1646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 673132010 895 EVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYD 939
Cdd:TIGR01612 1647 ENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVD 1691
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
685-811 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 685 QDELRTKENELRALEEELAglkNVAEKYRQLKQQWEMKTEEgdllqTKLQQSSYHKQQEELDALKKTIEESEETLKSTKE 764
Cdd:TIGR02794 86 AEQARQKELEQRAAAEKAA---KQAEQAAKQAEEKQKQAEE-----AKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAK 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 673132010 765 IQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKK 811
Cdd:TIGR02794 158 AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
679-875 |
3.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKL-----QQSSYHKQQEELDALKKTIE 753
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaeterEREELAEEVRDLRERLEELE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 754 ESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREH 833
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 673132010 834 ASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDEL 875
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
670-866 |
3.65e-03 |
|
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: 41.65 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 670 QAASILTKFQeVKDVQDELRTKENELRaleEELAGLKNvaeKYRQLKQQWEMKTEEGDLLQTKLQQssYHKQQEELD-AL 748
Cdd:pfam05557 1 RAELIESKAR-LSQLQNEKKQMELEHK---RARIELEK---KASALKRQLDRESDRNQELQKRIRL--LEKREAEAEeAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 749 KKTIEESEETLKSTKEIQKKAEEKYEALEnkmknaeaerekelkDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE 828
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLA---------------DAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 673132010 829 LKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKE 866
Cdd:pfam05557 137 LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE 174
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
137-355 |
3.85e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.57 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 137 NVNNPhflIMQGriTKVLNMKPPEILSMIEEAAGTRMYEY--KKIAAQKTIEKKEAKLKEIKTILEEEItptiQKLKEER 214
Cdd:pfam10168 514 SVSNP---ILSA--DKLSSPSPQECLQLLSRATQVFREEYlkKHDLAREEIQKRVKLLKLQKEQQLQEL----QSLEEER 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 215 ssyleyqKVMREiehlsrlyiayqflRAEDTKERSAgELKEMQDKIVN-LQEVL----------SENEKKIKalnceiEE 283
Cdd:pfam10168 585 -------KSLSE--------------RAEKLAEKYE-EIKDKQEKLMRrCKKVLqrlnsqlpvlSDAEREMK------KE 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 673132010 284 LERRKDKetggkLKSLEDACAEA-------QRVNTKSQSafDLKKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKI 355
Cdd:pfam10168 637 LETINEQ-----LKHLANAIKQAkkkmnyqRYQIAKSQS--IRKKSSLSLSEKQRKTIKEILKQLGSEIDELIKQVKDI 708
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
740-970 |
3.96e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.30 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 740 KQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEAL---ENKMK-NAEAEREKE----LKDAQKKLDCAKTKADASSKK 811
Cdd:pfam18971 604 KSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKsgnKNKMEaKAQANSQKDeifaLINKEANRDARAIAYTQNLKG 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 812 MK-EKQQEVEAITLELEELKRE----HASNEQQLDAVNEAIKAYEGQIEKMA--AEVAKNKESVNKAQDELMKQKQIITA 884
Cdd:pfam18971 684 IKrELSDKLEKISKDLKDFSKSfdefKNGKNKDFSKAEETLKALKGSVKDLGinPEWISKVENLNAALNEFKNGKNKDFS 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 885 QDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADdaAAKVSKMLSDYDWINAEKhLFGQPNSAYDFKTNNPKE 964
Cdd:pfam18971 764 KVTQAKSDLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGD--FSRVEQVLADLKNFSKEQ-LAQQAQKNEDFNTGKNSE 840
|
....*.
gi 673132010 965 AGQRLQ 970
Cdd:pfam18971 841 LYQSVK 846
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
682-926 |
4.03e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 682 KDVQDELRTKENELRAL---EEELAGLKNVAEKYRQLKQQWEmkteegDLLQTKL-QQSSYHKQQEEldALKKTIEESEE 757
Cdd:COG5185 222 LEKAKEIINIEEALKGFqdpESELEDLAQTSDKLEKLVEQNT------DLRLEKLgENAESSKRLNE--NANNLIKQFEN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 758 TLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLEleelKREHASNE 837
Cdd:COG5185 294 TKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKE----EIENIVGE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 838 QQLDAVNEAIKAYEGQIEKMAAEV-AKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHS 916
Cdd:COG5185 370 VELSKSSEELDSFKDTIESTKESLdEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
250
....*....|
gi 673132010 917 ISKHKREADD 926
Cdd:COG5185 450 LNKVMREADE 459
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
741-855 |
4.03e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 741 QQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREK----------ELKDAQKKLDcAKTKADASSK 810
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaelagAGAAAEGRAG-ELAQELDSEK 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 673132010 811 KM-KEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIE 855
Cdd:PRK09039 130 QVsARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIA 175
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
685-880 |
4.54e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.36 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 685 QDELRTKENELRALEEELaglKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKSTKE 764
Cdd:NF012221 1605 QAQRDAILEESRAVTKEL---TTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRHV 1681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 765 IQ----KKAEEKYEAlenkmknAEAEREKELKDAQKKLDCAKTKAdasskkmkeKQQEVEAITLELEELKREHASNEqql 840
Cdd:NF012221 1682 DNqqkvKDAVAKSEA-------GVAQGEQNQANAEQDIDDAKADA---------EKRKDDALAKQNEAQQAESDANA--- 1742
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 673132010 841 dAVNEAIKAyeGQIEKMAAEvakNKesVNKAQDELMKQKQ 880
Cdd:NF012221 1743 -AANDAQSR--GEQDASAAE---NK--ANQAQADAKGAKQ 1774
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
675-875 |
4.63e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 675 LTKFQEVKDVQDELRTkeNELRALEEELAGLKNVAEKYRQLKQQWEMKTEEgDLLQTKLQQssYHKQQEELDALKKTIEE 754
Cdd:PRK04778 63 EEKFEEWRQKWDEIVT--NSLPDIEEQLFEAEELNDKFRFRKAKHEINEIE-SLLDLIEED--IEQILEELQELLESEEK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 755 S----EETLKSTKEIQKKAEEK-------YEALENKMKNAEAEREK--ELKD------AQKKLDCAKTKADASSKKMKE- 814
Cdd:PRK04778 138 NreevEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEEFSQfvELTEsgdyveAREILDQLEEELAALEQIMEEi 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 815 ----KQQEVE-------------------------AITLELEELKREHASNEQQL-----DAVNEAIKAYEGQIEKM--- 857
Cdd:PRK04778 218 pellKELQTElpdqlqelkagyrelveegyhldhlDIEKEIQDLKEQIDENLALLeeldlDEAEEKNEEIQERIDQLydi 297
|
250
....*....|....*....
gi 673132010 858 -AAEVAKNKEsVNKAQDEL 875
Cdd:PRK04778 298 lEREVKARKY-VEKNSDTL 315
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
752-1025 |
4.67e-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: 41.26 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 752 IEESEETLKStkEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVE-AITLELEELK 830
Cdd:pfam15921 243 VEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARnQNSMYMRQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 831 REHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKI 910
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 911 KEL-------DHSISKHKREADDAAAKVSKMLSDYDWINAE-KHLFGQPNSAYDFKTNNPKEAGQRLQKLQEVKEKLGRN 982
Cdd:pfam15921 401 KRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 673132010 983 V-NLRAMNVLTEAEER-----YNDLMKKKRIVENDKSKILATIEDLDQK 1025
Cdd:pfam15921 481 VeELTAKKMTLESSERtvsdlTASLQEKERAIEATNAEITKLRSRVDLK 529
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
679-925 |
4.71e-03 |
|
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: 41.25 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRtkenelralEEELAGLKNVAEKYRQLKQQWEMKTEEGDL-LQTKLQQSSYHKQQEELDALKKTIEESEE 757
Cdd:pfam05483 471 KEVEDLKTELE---------KEKLKNIELTAHCDKLLLENKELTQEASDMtLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 758 TLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNE 837
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 838 QQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIIT-AQDNIIKdkcaEVAKHNLQNNES---------- 906
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiSEEKLLE----EVEKAKAIADEAvklqkeidkr 697
|
250 260
....*....|....*....|
gi 673132010 907 -QLKIKELDHSISKHKREAD 925
Cdd:pfam05483 698 cQHKIAEMVALMEKHKHQYD 717
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
686-884 |
4.92e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 686 DELRTKENELRALEEELAGLKNVAEKYRQLKQQWE-MKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKS--- 761
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDles 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 762 -TKEIQ--------------KKAEEKYEALENKMKNAEaEREKELKDAQKKLDCAKTKadasSKKMKEKQQEVEAITLEL 826
Cdd:PRK01156 602 rLQEIEigfpddksyidksiREIENEANNLNNKYNEIQ-ENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEITSRI 676
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 673132010 827 EELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITA 884
Cdd:PRK01156 677 NDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
670-930 |
5.13e-03 |
|
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: 41.11 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 670 QAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKT-----EEGDLL----QTKLQQSSYHK 740
Cdd:TIGR00618 363 VATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsafrdLQGQLAhakkQQELQQRYAEL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 741 QQE--------------ELDALKKTIEESEETLKSTKEIQKKAEEKyEALENKMKNAEAEREKELKDAQKKLDCAKTKAD 806
Cdd:TIGR00618 443 CAAaitctaqceklekiHLQESAQSLKEREQQLQTKEQIHLQETRK-KAVVLARLLELQEEPCPLCGSCIHPNPARQDID 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 807 ASSKKmkekQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIE-------KMAAEVAKNKESVNKAQDELMKQK 879
Cdd:TIGR00618 522 NPGPL----TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQeiqqsfsILTQCDNRSKEDIPNLQNITVRLQ 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 673132010 880 QIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAK 930
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
674-925 |
5.48e-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: 40.77 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 674 ILTKFQEVKDVQDELRTKENELRALEEELAGLK-NVAEKYRQLKQQWEMKTE-EGDLL----QTKLQQSSYHKQQEELDA 747
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqQIKDLNDKLKKNKDKINKlNSDLSkinsEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 748 LKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREkELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELE 827
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE-ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 828 ELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELmkqKQIITAQDNIIK---DKCAEVAKHNLQNN 904
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL---NQLKDEQNKIKKqlsEKQKELEQNNKKIK 284
|
250 260
....*....|....*....|.
gi 673132010 905 ESQLKIKELDHSISKHKREAD 925
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKE 305
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-922 |
5.92e-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: 40.77 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELaglKNVAEKYRQLKQQW-EMKTEEGDLLQTKLQQSSyhkqqeELDALKKTIEESEE 757
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEK---KELEEKVKDLTKKIsSLKEKIEKLESEKKEKES------KISDLEDELNKDDF 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 758 TLKST---KEIQKKAEEKyealeNKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHA 834
Cdd:TIGR04523 553 ELKKEnleKEIDEKNKEI-----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 835 SNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELD 914
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP 707
|
....*...
gi 673132010 915 HSISKHKR 922
Cdd:TIGR04523 708 KLEEKYKE 715
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
678-797 |
6.69e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 678 FQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQwemkteegdllqtklqqssyhkQQEELDALKKTIEESEE 757
Cdd:PRK11448 134 FVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA----------------------QQQELVALEGLAAELEE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 673132010 758 TlkstkeiQKKAEEKYEALENKMKNAEAEREKELKDAQKK 797
Cdd:PRK11448 192 K-------QQELEAQLEQLQEKAAETSQERKQKRKEITDQ 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-516 |
6.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 181 AQKTIEKKEA----KLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIE-----HLSRLYIAYQFLRAEDTKErsAG 251
Cdd:PTZ00121 1539 AKKAEEKKKAdelkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEearieEVMKLYEEEKKMKAEEAKK--AE 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 252 ELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQRVNTKSQSAFDLKKKNLASEETKR 331
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 332 KELQNSMAEDSKALAA----------KEKEVKKI-TDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAG 400
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAeekkkaeelkKAEEENKIkAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 401 QMIACKNDISKaqtEAKQAQMKLKHAQQELKSKQAEVKKmdsGYKKDQdafEAVKKAKEKLETEMKKLNYEENKEEKLLE 480
Cdd:PTZ00121 1777 KEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIE---GGKEGN---LVINDSKEMEDSAIKEVADSKNMQLEEAD 1847
|
330 340 350
....*....|....*....|....*....|....*.
gi 673132010 481 KHRQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKN 516
Cdd:PTZ00121 1848 AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
641-813 |
6.87e-03 |
|
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: 40.05 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 641 FDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELrTKENELRALEEELAGLKNVAEKYRQlkqqwe 720
Cdd:cd22656 63 FKDDTYPSIVSLAGDIYNYAQNAGGTIDSYYAEILELIDDLADATDDE-ELEEAKKTIKALLDDLLKEAKKYQD------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 721 mkteEGDLLQTKLQ--QSSYHKQQEELDALKKTI------EESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELK 792
Cdd:cd22656 136 ----KAAKVVDKLTdfENQTEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIA 211
|
170 180
....*....|....*....|.
gi 673132010 793 DAQKKLDcAKTKADASSKKMK 813
Cdd:cd22656 212 DDEAKLA-AALRLIADLTAAD 231
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
720-885 |
7.04e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 720 EMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEES-EETLKSTKEIQK-------KAEEKYEALENK-MKNAEAEREKE 790
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApAKLRQAQAELEAlkddndeETRETLSTLSLRqLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 791 LKDAQKKLDCA-------KTKADASSKKMKEKQQEVEAITLELEELK-REHASNEQQLDAVNEAIKAYEGQIEKMAAEVA 862
Cdd:PRK11281 137 LQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKvGGKALRPSQRVLLQAEQALLNAQNDLQRKSLE 216
|
170 180
....*....|....*....|...
gi 673132010 863 KNkesvNKAQDELMKQKQIITAQ 885
Cdd:PRK11281 217 GN----TQLQDLLQKQRDYLTAR 235
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
688-878 |
8.54e-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: 39.90 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 688 LRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEgdllqtkLQQSSYHKQQEELDALKKTIEESEETLKSTKEIQK 767
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEE-------KEEERRLDEMMEEERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 768 KAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHAS----NEQQLDAV 843
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkelEKEEEREE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 673132010 844 NEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQ 878
Cdd:pfam13868 154 DERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-49 |
8.55e-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: 38.38 E-value: 8.55e-03
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
725-875 |
8.66e-03 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 40.04 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 725 EGDLLQTKLQQSSYHKQQ--EELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLdcak 802
Cdd:smart00806 65 DGSVLVLNVEELDEVKKHidDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARPAASPSPVLASSSSAI---- 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 673132010 803 TKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAK--NKESVNKAQDEL 875
Cdd:smart00806 141 SLANNPDKLNKEQRAELKSLQRELAVLRQTHNSFFTEIKESIKDILEKIDKFKSSSLSASGssNRAYVESSKKKL 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-799 |
8.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673132010 679 QEVKDVQDELRTKENELRALEEELAGLKNVAEKYR----QLKQQWEMKTEEGDLLQTKLQQSSYHKQQ----EELDALKK 750
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgNVRNNKEYEALQKEIESLKRRISDLEDEIlelmERIEELEE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 673132010 751 TIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLD 799
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| |
