|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-919 |
2.52e-32 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 135.58 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGKETGK-SYIKFGEKSSKVDIDFiAN 79
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKdDFTRIGGSGTEIELKF-EK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 80 DGREYNLKTEFFK-TKPKKQTLKDIIGSEYDGDIQEKLEELCGIkkgfeETYENIVIAKQNEFINIFKAKpKDREEIFNK 158
Cdd:PRK03918 80 NGRKYRIVRSFNRgESYLKYLDGSEVLEEGDSSVREWVERLIPY-----HVFLNAIYIRQGEIDAILESD-ESREKVVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 159 IFNtqiykemydsflkeaVDKYKSEKENLDSKINSLKENMEDKEQitnFLKEEKDVEKNLQDNFKNINVVSKNLENEIKD 238
Cdd:PRK03918 154 ILG---------------LDDYENAYKNLGEVIKEIKRRIERLEK---FIKRTENIEELIKEKEKELEEVLREINEISSE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 239 YETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAKKAKIIVKETEKSYLEyldIENKLKDLRENLDNLLEEQKLN 318
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELEEKVKELKELKEKA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 319 IQYqnniEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLedk 398
Cdd:PRK03918 293 EEY----IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE--- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 399 lkkttEIDILKKELVSKNDLFKIINIEELEKKLYNFQELEKELKLLEEQKII----FETEIKTLKKSSKEL--SNKICPF 472
Cdd:PRK03918 366 -----EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITArigeLKKEIKELKKAIEELkkAKGKCPV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 473 LNEKCQNLEDKEAedyfsskISIKTEELENLKKNIEEKTQILvekvvfEDKRKQYFELEKSIKDLELSLKNEEINLKEIE 552
Cdd:PRK03918 441 CGRELTEEHRKEL-------LEEYTAELKRIEKELKEIEEKE------RKLRKELRELEKVLKKESELIKLKELAEQLKE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 553 LDIKNLDMDIQKLIENQEfqNSQMLREKKKELEVELRNLNLDEKRenlknlLENLEIEKKKILKSQNSIESNLKEINEFL 632
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAE--EYEKLKEKLIKLKGEIKSLKKELEK------LEELKKKLAELEKKLDELEEELAELLKEL 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 633 KEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYlknNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKI 712
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKEL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 713 KNIKIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNKANLIRNEVGQMGRA 792
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 793 ISKYMLSGISNIASVNFNKITGRTERIEWSNEEKDKYAVYLV--GQERKIAFeqLSGGEQVSIAIAIRGTMTEYFT-NSK 869
Cdd:PRK03918 737 LKERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVKLFVVyqGKERPLTF--LSGGERIALGLAFRLALSLYLAgNIP 814
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1080658287 870 FMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAEKII 919
Cdd:PRK03918 815 LLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVI 864
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
1-921 |
1.72e-31 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 132.91 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNtkdRSGKETGKSYIKFGEKSSKVDIDFiAND 80
Cdd:NF041034 1 MKIERIFLENFLSHESSEVNFKGSINAIIGHNGAGKSSIIDGIVFSLFR---ESSRGNNEDLIKKGKKTATVELKL-EDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 81 GREYNLKTEFFKTKPKKQTLKDIIGSEYDG-DIQEKLEELCGIKKgfeETYENIVIAKQNEFINIFKAKPkdreEIFNKI 159
Cdd:NF041034 77 GKTYLIKRNIPNSYSDDDTISNLKTIARGStEVNQKIQEILNLDK---DVLLSTVIVRQGEIESIFKNLP----DVMKKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 160 FNTQIYKEmydsfLKEAVDKYKSEKENLDSKINSLKEnmeDKEQITNFLKEEKDVEKNLQDnfkninvVSKNLENEIKDY 239
Cdd:NF041034 150 LKIENLEK-----LTDSNGPIYSVIKEIENKLKYLES---EKERYESKEAEKEKLEKEIEE-------SKNKLEDLEIKK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 240 ETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAKKAKiivketeksylEYLDIENKLKDLRENLDNLLEEQKLNI 319
Cdd:NF041034 215 EEKEKELNDLKKEFEELEKKRERYDELTGRLSSLNKRINEIE-----------EDLKDLEKLKKEKEKLEKEIKEKEKLE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 320 QYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLEseiselkiKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKL 399
Cdd:NF041034 284 EKNEIISELKELIKSIKELKRQLNTLEKEIEEYKENLK--------KKKELEDKAKKYEELKREKEELEEKENEYNSLKS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 400 KKTTEIDILKKELVSKNDLFKIINIEELEKKLYNFQELEKELKLLEEQKIIFETEIKTLKKSSKELSNKICPFlnekCQN 479
Cdd:NF041034 356 RLNSLKKKLEEIENEISKLGIIINIEELKKKLDKLSEEINNKNNEKGEIKGRKEQLLKILKNLNNVKGNKCPV----CGR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 480 LEDKEAEDYFSSKISIKTEELENLKKNIEektqilvekvvfedkrKQYFELEKSIKDLElslknEEINLKEIELDIKnld 559
Cdd:NF041034 432 ELDEEHKKKIREEIEEKIKDLNKQISKLE----------------KEVNSLNKEKEELE-----NKINKLQEEKLIK--- 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 560 mdiqkliENQEFQNSQMLREKKKELEVELRNLN-LDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKED 638
Cdd:NF041034 488 -------LEKLLKELQRLKKEIEEIEKELKELEeSHEEYEEIKEELKELEPKYKEYLKVSNVTEEELEELERRLSEIKSE 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 639 TNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKID 718
Cdd:NF041034 561 LDELEKKYSELKEKIGDDREELTQIEKKIEKKIKEIKELKNKLEKLKEEIAKIEKEKEEIEKIENEIKELEEEISSLNFD 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 719 E-----LKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNKANLIRNEVGqmGRAI 793
Cdd:NF041034 641 EeryqnLKEKIEKLNKELNRIEQEISKLEGKIEALENDIDNLNSELEKIKEKLNKIPKLENAIKKLEKLREDLS--GSGL 718
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 794 SKYMLSGISNIASVNFNKITGRTE----RIEWSNE-----EKDKYAVYLVGQE-RKIAFEQLSGGEQVSIAIAIRGTMTE 863
Cdd:NF041034 719 QNYIISNVKSKIENNLNDILSKFDlsfsRVEIDFEiggktKKGKSEIKAYNTAgQDLDVNALSGGERISIALALRLAIAK 798
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 864 YFTNS-KFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAEKIIEL 921
Cdd:NF041034 799 SLMDEiGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEELKEISDYIISV 857
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-907 |
1.52e-25 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 113.84 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGKEtgkSYIKFGEKSSKVDIDFiAND 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEKIE---DMIKKGKNNLEVELEF-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 81 GREYNLKTEFFKTKPKKQTLKDI-----IGSEYDGDIQEKLEE-LCGIKKgfeETYENIVIAKQNEFINIFKAKPKDREE 154
Cdd:PRK01156 77 GHVYQIRRSIERRGKGSRREAYIkkdgsIIAEGFDDTTKYIEKnILGISK---DVFLNSIFVGQGEMDSLISGDPAQRKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 155 IFNKIFNTQIYKEMYDsFLKEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVSKNLEN 234
Cdd:PRK01156 154 ILDEILEINSLERNYD-KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 235 EIKDYETTEVELNNLVKNIKDEENKIKKylnilkeniieaKQAKKAKIIVKETEKSYLE--YLDIENKLKDLRENldnll 312
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKT------------AESDLSMELEKNNYYKELEerHMKIINDPVYKNRN----- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 313 eEQKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKK------ENLESEISELKIKEEDLDLKLKKYINLLDELEK 386
Cdd:PRK01156 296 -YINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIES 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 387 LENFKDKKLEDKLKKTTEI-DILKKELVSKNDLFKIINieELEKKLYNFQELEKELKLLEEQKIIFETEIKtlKKSSKEL 465
Cdd:PRK01156 375 LKKKIEEYSKNIERMSAFIsEILKIQEIDPDAIKKELN--EINVKLQDISSKVSSLNQRIRALRENLDELS--RNMEMLN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 466 SNKICPFLNEKCQNLEDKEAEDYFSSKISIKTEELENLKKNIEEktqiLVEKVVFEDKRKQYFELEKSIKdlelsLKNEE 545
Cdd:PRK01156 451 GQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKD----IDEKIVDLKKRKEYLESEEINK-----SINEY 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 546 INLKEIELDIKNLDMDIQKLIENQEFQNSQMLREKKKELEvelrnlNLDEKRENLKNLLENLE-IEKKKILKSQNSIESN 624
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLE------DLDSKRTSWLNALAVISlIDIETNRSRSNEIKKQ 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 625 LKEINEFLKEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEK 704
Cdd:PRK01156 596 LNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSR 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 705 VSNLEEKIK---------NIKIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKIlekissqeekqKKLLIEFKKLENK 775
Cdd:PRK01156 676 INDIEDNLKksrkalddaKANRARLESTIEILRTRINELSDRINDINETLESMKKI-----------KKAIGDLKRLREA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 776 FNKAN---LIRNEVGQMGRAISKYMLSGIsniaSVNFNKItgrteriewSNEEKDKYAVYLVGQERKIafEQLSGGEQVS 852
Cdd:PRK01156 745 FDKSGvpaMIRKSASQAMTSLTRKYLFEF----NLDFDDI---------DVDQDFNITVSRGGMVEGI--DSLSGGEKTA 809
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 853 IAIAIRGTMTEYFTNSK-FMILDEPTNNLDTERKKLLA---EYMGEILNNLEQSIIVTH 907
Cdd:PRK01156 810 VAFALRVAVAQFLNNDKsLLIMDEPTAFLDEDRRTNLKdiiEYSLKDSSDIPQVIMISH 868
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-189 |
2.15e-18 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 84.68 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 2 IIKKVQLENYRSHSNT-TVEFTKGVNLILGKNGRGKTSILEAISTVIFNtKDRSGKETGKSYIKFGEKSSKVDIDFiAND 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTeTIDFDDGLNLIVGPNGAGKSTILEAIRYALYG-KARSRSKLRSDLINVGSEEASVELEF-EHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 81 GREYnlkteffktkpkkqtlkdiigseydgdiqekleelcgikkgfeetyenIVIAKQNEFINIFKAKPKDREEIFNKIF 160
Cdd:COG0419 79 GKRY------------------------------------------------RIERRQGEFAEFLEAKPSERKEALKRLL 110
|
170 180
....*....|....*....|....*....
gi 1080658287 161 NTQIYKEMYDSfLKEAVDKYKSEKENLDS 189
Cdd:COG0419 111 GLEIYEELKER-LKELEEALESALEELAE 138
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-122 |
4.07e-15 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 77.89 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 2 IIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIfntkdrsgkeTGKSY--------IKFGEKSSKVD 73
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLA----------TGRSFrtardaelIRFGADGFRVR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1080658287 74 IDFiANDGREYNLKTEFFKTKPKKQTLkdiigseyDGDIQEKLEELCGI 122
Cdd:COG1195 71 AEV-ERDGREVRLGLGLSRGGKKRVRI--------NGKPVRRLSDLAGL 110
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-780 |
4.10e-14 |
|
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: 76.60 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 171 SFLKEAVDKYKSEKENLDSKINSL-KENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVSK---NLENEIKDYETTEVEL 246
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELNKLeKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKqkeELENELNLLEKEKLNI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 247 NNLVKNIKDEENKIKKYLNILKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIE 326
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 327 KLELSNKNLKVDISNleENISKNSEKKENLESEISELK-IKEEDLDLKLKKYI-NLLDELEKLENFKDKKLEDKLKKTTE 404
Cdd:TIGR04523 266 KKQLSEKQKELEQNN--KKIKELEKQLNQLKSEISDLNnQKEQDWNKELKSELkNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 405 IDILKKELVSKNDLFKIINIEELEKKlynfqeleKELKLLEEQKIIFETEIKTLKKSSKELSNKIcpflnekcqnLEDKE 484
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQ--------NEIEKLKKENQSYKQEIKNLESQINDLESKI----------QNQEK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 485 AEDYFSSKISIKTEELENLKKNIEE-KTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQ 563
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 564 KLIENQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEIN-----EFLKEIKED 638
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkENLEKEIDE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 639 TNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNV-LAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIK- 716
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKq 645
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080658287 717 -IDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNKAN 780
Cdd:TIGR04523 646 eVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLE 710
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-909 |
5.89e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGkeTGKSYIKFGEKSSKVDIDFiAND 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDD--TLDDVITIGAEEAEIELWF-EHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 81 GREYNLKTEFFKTKPKKQTLKDIIG---SEYDG--DIQEKLEELCGIKkgfEETYENIVIAKQNEFINIFKAKPKDREEI 155
Cdd:PRK02224 78 GGEYHIERRVRLSGDRATTAKCVLEtpeGTIDGarDVREEVTELLRMD---AEAFVNCAYVRQGEVNKLINATPSDRQDM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 156 FNKIFntQIYK-EMYD---SFLKEAVDKYKSEKENLDSKINSLKENMEDK---EQITNFLKEEKDVE---KNLQDNFKNI 225
Cdd:PRK02224 155 IDDLL--QLGKlEEYReraSDARLGVERVLSDQRGSLDQLKAQIEEKEEKdlhERLNGLESELAELDeeiERYEEQREQA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 226 NVVSKNLENEIKDYETTEVELNNLVKNIKDEENKI---KKYLNILKENIIEAKQA-----KKAKIIVKETEKSYLEYLDI 297
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELETLEAEIEDLRETIaetEREREELAEEVRDLRERleeleEERDDLLAEAGLDDADAEAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 298 ENKLKDLRENLDNL---LEEQKLNIQ--------YQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELkik 366
Cdd:PRK02224 313 EARREELEDRDEELrdrLEECRVAAQahneeaesLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 367 EEDLDLKLKKYINLLDELEKLENFKDKKLEDklkktteidilKKELVSKndlfkiinIEELEKKLynfqelekelkllee 446
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREE-----------RDELRER--------EAELEATL--------------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 447 qkiifETEIKTLKKSSKELSNKICPflnEKCQNLEDKEAEDYFSSKiSIKTEELENLKKNIEEKTQILVEKVvfeDKRKQ 526
Cdd:PRK02224 436 -----RTARERVEEAEALLEAGKCP---ECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERL---ERAED 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 527 YFELEKSIKDLELSLKNEEinlKEIELDIKNLDMDIQKLIEnqefqnsqmLREKKKELEVElrnlnLDEKRENLKNLLEN 606
Cdd:PRK02224 504 LVEAEDRIERLEERREDLE---ELIAERRETIEEKRERAEE---------LRERAAELEAE-----AEEKREAAAEAEEE 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 607 LEiEKKKILKSQNSIESNLKEINEFLKEIKEDTNKnIENIKLEIKTFENKLDNL---KNPYNEYLKNnvLAEDLDNLLLK 683
Cdd:PRK02224 567 AE-EAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALaelNDERRERLAE--KRERKRELEAE 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 684 VDKNIKElySLRTDKNLLKEKVSNLEEkikniKIDELKEKYDiikeelnEINKKLGSSQEKIENYKKILEKISSQEEKQK 763
Cdd:PRK02224 643 FDEARIE--EAREDKERAEEYLEQVEE-----KLDELREERD-------DLQAEIGAVENELEELEELRERREALENRVE 708
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 764 KLLI---EFKKLENKFN--KANLIRNEVGQMGRaiskyMLSGISNIASVNfnkitGRTERIEWSNE------EKDKYAvy 832
Cdd:PRK02224 709 ALEAlydEAEELESMYGdlRAELRQRNVETLER-----MLNETFDLVYQN-----DAYSHIELDGEyeltvyQKDGEP-- 776
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 833 lvgqerkIAFEQLSGGEQ----VSIAIAIRGTMTEYFTNSKFM---ILDEPTNNLDT---ERKKLLAEYMGEIlnNLEQS 902
Cdd:PRK02224 777 -------LEPEQLSGGERalfnLSLRCAIYRLLAEGIEGDAPLpplILDEPTVFLDSghvSQLVDLVESMRRL--GVEQI 847
|
....*..
gi 1080658287 903 IIVTHDD 909
Cdd:PRK02224 848 VVVSHDD 854
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-90 |
1.07e-13 |
|
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: 70.71 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 3 IKKVQLENYRS-HSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGKETGK--SYIKFGEKSSKVDIDFIAN 79
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHdpKLIREGEVRAQVKLAFENA 80
|
90
....*....|.
gi 1080658287 80 DGREYNLKTEF 90
Cdd:cd03240 81 NGKKYTITRSL 91
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-122 |
2.98e-13 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 72.11 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIfntkdrsgkeTGKS--------YIKFGEKSSKV 72
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLA----------PGRShrtardkeLIRFGAEAAVI 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1080658287 73 DIDfIANDGREYNLKTEffKTKPKKQTLKdIIGSEydgdiQEKLEELCGI 122
Cdd:PRK00064 71 HGR-VEKGGRELPLGLE--IDKKGGRKVR-INGEP-----QRKLAELAGL 111
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
822-921 |
2.18e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 822 SNEEKDKYAVYLVGQERKIA-FEQLSGGEQVSIAIAIrgTMteyFTNSKFMILDEPTNNLDTERKKLLAEYmgeiLNNLE 900
Cdd:cd03221 47 AGELEPDEGIVTWGSTVKIGyFEQLSGGEKMRLALAK--LL---LENPNLLLLDEPTNHLDLESIEALEEA----LKEYP 117
|
90 100
....*....|....*....|...
gi 1080658287 901 QS-IIVTHDDTF-REMAEKIIEL 921
Cdd:cd03221 118 GTvILVSHDRYFlDQVATKIIEL 140
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-85 |
8.11e-12 |
|
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: 65.31 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 3 IKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAIsTVIFNTKdRSGKETG---KSYIKFGEKSSKVDIDfIAN 79
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTAL-TIGLGGK-ASDTNRGsslKDLIKDGESSAKITVT-LKN 77
|
....*.
gi 1080658287 80 DGREYN 85
Cdd:cd03276 78 QGLDAN 83
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
799-921 |
1.13e-11 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 63.80 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 799 SGISNIASVnfnkITGRTE----RIEWSNEEKDKYAvyLVGQERKIAFE-QLSGGEQ--VSIAIAIrgtmteyFTNSKFM 871
Cdd:cd00267 36 SGKSTLLRA----IAGLLKptsgEILIDGKDIAKLP--LEELRRRIGYVpQLSGGQRqrVALARAL-------LLNPDLL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1080658287 872 ILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHD-DTFREMAEKIIEL 921
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVL 153
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
843-920 |
2.28e-11 |
|
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: 64.17 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 843 EQLSGGEQVSIAIAIRGTMTEYF-TNSKFMILDEPTNNLDTERKKL----LAEYMGEILNnlEQSIIVTHDDTFREMAEK 917
Cdd:cd03240 114 GRCSGGEKVLASLIIRLALAETFgSNCGILALDEPTTNLDEENIEEslaeIIEERKSQKN--FQLIVITHDEELVDAADH 191
|
...
gi 1080658287 918 IIE 920
Cdd:cd03240 192 IYR 194
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-913 |
1.81e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.99 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNT-TVEFTK--GVNLILGKNGRGKTSILEAISTVIF-------------NTKDRSGKETGKSYIK 64
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGThTIDFTAlgPIFLICGKTGAGKTTLLDAITYALYgklprrsevirslNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 65 FGEKSSKVDIDFIANDGREYNLKTEFFKTKPKKQTLKDIIGSEYDGDIQEKLEELCGIKKgfeETYENIVIAKQNEFINI 144
Cdd:TIGR00618 81 FSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDY---KTFTRVVLLPQGEFAQF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 145 FKAKPKDREEIFNKIFNTQIYKEM-YDSFLKEAVDKYKSEKENLDSKINSL------------KENMEDKE-QITNFLKE 210
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLaLMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtyherKQVLEKELkHLREALQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 211 EKDVEKNLQDNFKNINVVSKnLENEIKDYETTEVELNNLVKNIKDEENKIKKYLNILKeniiEAKQAKKAKIIVKETEKS 290
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP----LAAHIKAVTQIEQQAQRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 291 YLEYLDIENKLKDLRENLDNLLeEQKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDL 370
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 371 DLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDILKKELV------------SKNDLFKIINIEELEKKLYNFQELE 438
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQElqqryaelcaaaITCTAQCEKLEKIHLQESAQSLKER 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 439 KELKLLEEQKIIFETEIKTLK-KSSKELSNKICPFlNEKCQNLEDKEAEDYFSSKISIKTEELENLKKNIEEKTQILVEK 517
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPL-CGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 518 VVFEDKR-KQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIENQ--------------------------- 569
Cdd:TIGR00618 551 LTSERKQrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLseaedmlaceqhallrklqpeqdlqdv 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 570 ---EFQNSQMLREKKKELEVELRNLNLDEKRENLKNL----LENLEIEKKKILKSQNSIES------NLKEINEFLKEIK 636
Cdd:TIGR00618 631 rlhLQQCSQELALKLTALHALQLTLTQERVREHALSIrvlpKELLASRQLALQKMQSEKEQltywkeMLAQCQTLLRELE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 637 EDTNKN--------------IENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLLLKVDKNIKELYS--------- 693
Cdd:TIGR00618 711 THIEEYdrefneienassslGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELShlaaeiqff 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 694 ---LRTDKNLLKEKVSNLEEK------IKNIKIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKK 764
Cdd:TIGR00618 791 nrlREEDTHLLKTLEAEIGQEipsdedILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 765 LLIEFKKLENKFNKANLIRNEVGQmgRAISKYMLSGISNIASVNFNKITGRTE-RIEWSNEEKDKYAVYLVGQERKI-AF 842
Cdd:TIGR00618 871 IIQLSDKLNGINQIKIQFDGDALI--KFLHEITLYANVRLANQSEGRFHGRYAdSHVNARKYQGLALLVADAYTGSVrPS 948
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080658287 843 EQLSGGEQVSIAIAIRGTMTEYF-----TNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFRE 913
Cdd:TIGR00618 949 ATLSGGETFLASLSLALALADLLstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRE 1024
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
478-911 |
5.95e-10 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 63.22 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 478 QNLEDKEAEDYFSSKISIKTEELENLKKNI-EEKTQILVEKVVFEDKRKqyfeleKSIKDLELSLKNEEiNLKEIELDIK 556
Cdd:COG4694 100 ENIELEEEIEELEKEIEDLKKELDKLEKELkEAKKALEKLLEDLAKSIK------DDLKKLFASSGRNY-RKANLEKKLS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 557 NL--DMDIQKLIENQEFQNSQMLREKKKELEVELRNLnLDEKRENLKNLLENLEIE--KKKILKSQNS--IESNLKEIN- 629
Cdd:COG4694 173 ALksSSEDELKEKLKLLKEEEPEPIAPITPLPDLKAL-LSEAETLLEKSAVSSAIEelAALIQNPGNSdwVEQGLAYHKe 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 630 ---------------EFLKEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLkNNVLAEDLDNLLLKVDKNIKELYSL 694
Cdd:COG4694 252 eeddtcpfcqqelaaERIEALEAYFDDEYEKLLAALKDLLEELESAINALSALL-LEILRTLLPSAKEDLKAALEALNAL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 695 RTD-KNLLKEKVSNLEEKI---KNIKIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEK--ISSQEEKQKKLLIE 768
Cdd:COG4694 331 LETlLAALEEKIANPSTSIdldDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAheLAELKEDLSRYKAE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 769 FKKLENKFNKANLIRNEVGQMGRAIS---KYMLSGISNIASVNFN-KITGRTE-RIEWSNEEKDKYAVYLVGQERKIAFE 843
Cdd:COG4694 411 VEELIEELKTIKALKKALEDLKTEISeleAELSSVDEAADEINEElKALGFDEfSLEAVEDGRSSYRLKRNGENDAKPAK 490
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080658287 844 QLSGGEQVSIAIA-----IRGTMTEYftNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTF 911
Cdd:COG4694 491 TLSEGEKTAIALAyflaeLEGDENDL--KKKIVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIVLTHNLYF 561
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
844-921 |
8.33e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 60.06 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSII-VTHDDTFREMAEKIIE 920
Cdd:COG1136 144 QLSGGQQqrVAIARAL-------VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVmVTHDPELAARADRVIR 216
|
.
gi 1080658287 921 L 921
Cdd:COG1136 217 L 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
844-921 |
1.58e-09 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 59.04 E-value: 1.58e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSII-VTHDDTFREMAEKIIEL 921
Cdd:cd03255 140 ELSGGQQQRVAIA-RALAN----DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVvVTHDPELAEYADRIIEL 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
249-918 |
2.60e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 249 LVKNIKDEENKI-KKYLNILKENIIEAKQAKKAkiiVKETEKSYLEYLDIENKLKDLRENLDNLleeqklniqyQNNIEK 327
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEE---LKEAEEKEEEYAELQEELEELEEELEEL----------EAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 328 LELSNKNLKVDISNLEeniskNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENfkdkkledklkkttEIDI 407
Cdd:COG4717 114 LREELEKLEKLLQLLP-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEA--------------ELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 408 LKKELVSKNDLFKIINIEELEKKLYNFQELEKELKLLeeqkiifETEIKTLKKSSKELSNKIcpflnekcqnledkeaed 487
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL-------EEELEEAQEELEELEEEL------------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 488 yfsSKISIKTEELENLKKNIEEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIE 567
Cdd:COG4717 230 ---EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 568 NQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLE-----IEKKKILKSQNSIESNLKEINEFLKEIKEDTnkn 642
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEelqelLREAEELEEELQLEELEQEIAALLAEAGVED--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 643 ienikleIKTFENKLDNlknpYNEYLKNNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEkvsnleekiknikIDELKE 722
Cdd:COG4717 384 -------EEELRAALEQ----AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE-------------LEELEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 723 KYDIIKEELNEINKKLGSSQEKIENYKKIlEKISSQEEKQKKLLIEFKKLENKFNKANLIRNEVGQMGRAISKYMLSGIS 802
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 803 NIASVNFNKIT-GRTERIEWSneekDKYAVYLVGQE-RKIAFEQLSGGEQVSIAIAIRGTMTEYFTNSKF-MILDEPTNN 879
Cdd:COG4717 519 ERASEYFSRLTdGRYRLIRID----EDLSLKVDTEDgRTRPVEELSRGTREQLYLALRLALAELLAGEPLpLILDDAFVN 594
|
650 660 670
....*....|....*....|....*....|....*....
gi 1080658287 880 LDTERKKLLAEYMGEILNNlEQSIIVTHDDTFREMAEKI 918
Cdd:COG4717 595 FDDERLRAALELLAELAKG-RQVIYFTCHEELVELFQEE 632
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
837-921 |
4.00e-09 |
|
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: 56.60 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 837 ERKIAFEQLSGGEQVSIAIAIRGTMTEyFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAE 916
Cdd:cd03227 70 ELIFTRLQLSGGEKELSALALILALAS-LKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELAD 148
|
....*
gi 1080658287 917 KIIEL 921
Cdd:cd03227 149 KLIHI 153
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-44 |
2.57e-08 |
|
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: 56.15 E-value: 2.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1080658287 3 IKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAIS 44
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAIS 42
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-152 |
3.06e-08 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 56.59 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSgkETGKSYIKFGEKSSKVDiDFIAND 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRT--SRDKPLIRFGAEAFVIE-GRVSKG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080658287 81 GREYNLKTEFFKTKPKKQTLKDIIGseydgdiQEKLEELCGIKKgfeetyeNIVIAKQNefINIFKAKPKDR 152
Cdd:TIGR00611 78 DREVTIPLEGLLKKKGKKAKVNIDG-------QDKLSDLAGLLP-------MQLFAPED--LTLVKGSPKYR 133
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-781 |
3.81e-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: 57.44 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 158 KIFNTQIYKEMYDSFLKEAVDKYKSEkenLDSKINSLKENMEDKEQITNFLKEEKD--VEKNLQDNfkninvvSKNLENE 235
Cdd:pfam15921 203 KIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkIELLLQQH-------QDRIEQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 236 IKDYETTEVELNNLVKNIKDEENKIKKYLNILKEniieakQAKKAKIIvketeksYLEYL-DIENKLKDLRENLdnllee 314
Cdd:pfam15921 273 ISEHEVEITGLTEKASSARSQANSIQSQLEIIQE------QARNQNSM-------YMRQLsDLESTVSQLRSEL------ 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 315 QKLNIQYQNNIEKLE----LSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDEleklenf 390
Cdd:pfam15921 334 REAKRMYEDKIEELEkqlvLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 391 kdkkledKLKKTTEIDILKKELVSKN-------DLFKIINIE---ELEKKLYNFQELEKELKLLEEQKIIFETEIKTLKK 460
Cdd:pfam15921 407 -------DTGNSITIDHLRRELDDRNmevqrleALLKAMKSEcqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 461 SSKELSNK-------------ICPFLNEKCQNLEDKEAE-DYFSSKISIKTEELENLKKNIEEKTQILVE----KVVFED 522
Cdd:pfam15921 480 VVEELTAKkmtlessertvsdLTASLQEKERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQMAE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 523 KRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQ-KLIENQEFQnsqMLREKK----KELEVELRNLNLDEKR 597
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdRRLELQEFK---ILKDKKdakiRELEARVSDLELEKVK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 598 ------ENLKnLLENLEIEKKKILksqNSIESNLKEINEfLKEIKEDTNKNIENIKLEIKTFENKLD-NLKNPYNEYLKN 670
Cdd:pfam15921 637 lvnagsERLR-AVKDIKQERDQLL---NEVKTSRNELNS-LSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQT 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 671 -NVLA--EDLDNLLLKVDKNI-KELYSLRTDKNLLKEKVSNLEEKIKNIKidelKEKYdIIKEELNEINKKLGSSQEKIE 746
Cdd:pfam15921 712 rNTLKsmEGSDGHAMKVAMGMqKQITAKRGQIDALQSKIQFLEEAMTNAN----KEKH-FLKEEKNKLSQELSTVATEKN 786
|
650 660 670
....*....|....*....|....*....|....*
gi 1080658287 747 NYKKILEKISSQEEKQKKlliEFKKLENKFNKANL 781
Cdd:pfam15921 787 KMAGELEVLRSQERRLKE---KVANMEVALDKASL 818
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2-386 |
4.78e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.56 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 2 IIKKVQLENYRSHSN--TTVEFTK-GVNLILGKNGRGKTSILEAISTVIFNTKDRSGKEtGKSYIKFGEKSSKVDIDFiA 78
Cdd:PHA02562 3 KFKKIRYKNILSVGNqpIEIQLDKvKKTLITGKNGAGKSTMLEALTFALFGKPFRDIKK-GQLINSINKKDLLVELWF-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 79 NDGREYNLKTeffKTKPKKQTL----KDIIGSEYDGDIQEKLEELCGIK-KGFEEtyenIVIAKQNEFINIFKAKPKDRE 153
Cdd:PHA02562 81 YGEKEYYIKR---GIKPNVFEIycngKLLDESASSKDFQKYFEQMLGMNyKSFKQ----IVVLGTAGYVPFMQLSAPARR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 154 EIFNKIFNTQIYKEMyDSFLKEAVDKYKSEKENLDSKINSLKENMEDKEqitNFLKEEKDVEKNLQDNFKNINVVSKNLE 233
Cdd:PHA02562 154 KLVEDLLDISVLSEM-DKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYN---KNIEEQRKKNGENIARKQNKYDELVEEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 234 NEIK-DYETTEVELNNLVKNIKDEENKIKKYLNILKEniIEAKQAKKAKIIVK--------------ETEKSYLEylDIE 298
Cdd:PHA02562 230 KTIKaEIEELTDELLNLVMDIEDPSAALNKLNTAAAK--IKSKIEQFQKVIKMyekggvcptctqqiSEGPDRIT--KIK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 299 NKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYI 378
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
....*...
gi 1080658287 379 NLLDELEK 386
Cdd:PHA02562 386 DELDKIVK 393
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
824-921 |
5.86e-08 |
|
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: 54.01 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 824 EEKDKYAVYLVG----QERKIafEQLSGGEQ--VSIAIAIrgTMteyftNSKFMILDEPTNNLDTERKKLLAEYMGEiLN 897
Cdd:cd03225 112 EERVEEALELVGleglRDRSP--FTLSGGQKqrVAIAGVL--AM-----DPDILLLDEPTAGLDPAGRRELLELLKK-LK 181
|
90 100
....*....|....*....|....*.
gi 1080658287 898 NLEQSII-VTHD-DTFREMAEKIIEL 921
Cdd:cd03225 182 AEGKTIIiVTHDlDLLLELADRVIVL 207
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-167 |
9.60e-08 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 53.27 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 6 VQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGKETGKSYIKF-------GEKSSKVDIDFIA 78
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGdirigleGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 79 NDGR-EYNLKTEFFKTKPKKQTLKDIIGSEYDGDIQEKLEELcgIKKGFEETYENIVIAKQNEFINIFKAKPKDREEIFN 157
Cdd:pfam13476 81 NDGRyTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISE--LLKSDKIILPLLVFLGQEREEEFERKEKKERLEELE 158
|
170
....*....|
gi 1080658287 158 KIFNTQIYKE 167
Cdd:pfam13476 159 KALEEKEDEK 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
300-656 |
1.14e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 300 KLKDLRENLDNLLEE----QKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLK 375
Cdd:TIGR02169 682 RLEGLKRELSSLQSElrriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 376 KYINLLDELEKlenfkdkkledklkkttEIDILKKELvskNDLFKIINIEELEKKlyNFQELEKELKLLEEQKIIFETEI 455
Cdd:TIGR02169 762 ELEARIEELEE-----------------DLHKLEEAL---NDLEARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 456 KTLKKSSKElsnkicPFLNEKCQNLEDKeaEDYFSSKISIKTEELENLKKNIEEKTQILVEKVVFE-DKRKQYFELEKSI 534
Cdd:TIGR02169 820 KLNRLTLEK------EYLEKEIQELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 535 KDLELSLKNEEINLKEIELDI---KNLDMDIQKLIENQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEK 611
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIekkRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1080658287 612 KKILKSQNSIESNLKEINEfLKEIKEDTNKNIENIKLEIKTFENK 656
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDE-LKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-47 |
1.31e-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: 54.62 E-value: 1.31e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVI 47
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLL 47
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
593-764 |
1.41e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 593 LDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIkEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKN-- 670
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREELGERARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 671 ---------NVL--AEDLDNLLLKV-------DKNIKELYSLRTDKNLLKEKVSNLEEKIKNI--KIDELKEKYDIIKEE 730
Cdd:COG3883 97 rsggsvsylDVLlgSESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAELEAKLAELeaLKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....
gi 1080658287 731 LNEINKKLGSSQEKIENYKKILEKISSQEEKQKK 764
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
844-921 |
2.65e-07 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 54.45 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLD--TERKkllaeymgeILNNLEQS------IIVTHDDTFREMA 915
Cdd:COG2274 611 NLSGGQRQRLAIA-RALLR----NPRILILDEATSALDaeTEAI---------ILENLRRLlkgrtvIIIAHRLSTIRLA 676
|
....*.
gi 1080658287 916 EKIIEL 921
Cdd:COG2274 677 DRIIVL 682
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
844-921 |
2.94e-07 |
|
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: 52.33 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAeymgEILNNLEQS----IIVTHD-DTFREMAE 916
Cdd:COG1122 134 ELSGGQKqrVAIAGVL-------AMEPEVLVLDEPTAGLDPRGRRELL----ELLKRLNKEgktvIIVTHDlDLVAELAD 202
|
....*
gi 1080658287 917 KIIEL 921
Cdd:COG1122 203 RVIVL 207
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-82 |
8.71e-07 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 50.67 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 3 IKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVI-FNTKDRSGKETGKSYIKFGEKSSKVDIDFIANDG 81
Cdd:cd03277 3 IVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLgGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGNPG 82
|
.
gi 1080658287 82 R 82
Cdd:cd03277 83 N 83
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
137-765 |
8.72e-07 |
|
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: 53.13 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 137 KQNEFINIFKAKPKDREEIFNKIfntqiyKEMYDSFLKEaVDKYKSEKENLDSKINSLKENM-EDKEQITNFLKEEK--D 213
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKIINEM------KFMKDDFLNK-VDKFINFENNCKEKIDSEHEQFaELTNKIKAEISDDKlnD 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 214 VEKNLQDNFKNINVVSKNLENEIKDYETTEvELNNLVKNIKDEENKIKKYLNilKENIIEAKQAKKAKIIVKET--EKSY 291
Cdd:TIGR01612 888 YEKKFNDSKSLINEINKSIEEEYQNINTLK-KVDEYIKICENTKESIEKFHN--KQNILKEILNKNIDTIKESNliEKSY 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 292 LEYLDieNKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNkNLKVDISNLEENI-----SKNSEKKENLESEISELKIK 366
Cdd:TIGR01612 965 KDKFD--NTLIDKINELDKAFKDASLNDYEAKNNELIKYFN-DLKANLGKNKENMlyhqfDEKEKATNDIEQKIEDANKN 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 367 EEDLDLKLKKYI-NLLDELEKLenfkdkkledklkKTTEIDILKKELVSKNDLfKIINIEELEKKL--YNFQELEKELKl 443
Cdd:TIGR01612 1042 IPNIEIAIHTSIyNIIDEIEKE-------------IGKNIELLNKEILEEAEI-NITNFNEIKEKLkhYNFDDFGKEEN- 1106
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 444 leeqkIIFETEIKTLKKSSKELSNKICPFLNEKcqnledkeaedyfsSKISIKTEELENLKKNIEEKTQILVEKVVFEDK 523
Cdd:TIGR01612 1107 -----IKYADEINKIKDDIKNLDQKIDHHIKAL--------------EEIKKKSENYIDEIKAQINDLEDVADKAISNDD 1167
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 524 RKqyfELEKSIKDLELSLKNEeinlKEIELDIKNLDMDIQKLienqefqnsqmlrEKKKELEVELRNLNLDEKRENLKNL 603
Cdd:TIGR01612 1168 PE---EIEKKIENIVTKIDKK----KNIYDEIKKLLNEIAEI-------------EKDKTSLEEVKGINLSYGKNLGKLF 1227
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 604 LENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKN--IENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLL 681
Cdd:TIGR01612 1228 LEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMgiEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKS 1307
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 682 LKV-----------------DKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKIDELKEKYDIIKEELNEINKKLGSSQEK 744
Cdd:TIGR01612 1308 LKIiedfseesdindikkelQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDK 1387
|
650 660
....*....|....*....|.
gi 1080658287 745 IENYKKILEKISSQEEKQKKL 765
Cdd:TIGR01612 1388 SEKLIKKIKDDINLEECKSKI 1408
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
845-911 |
1.04e-06 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II 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. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most 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: 213193 [Multi-domain] Cd Length: 205 Bit Score: 50.33 E-value: 1.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080658287 845 LSGGEQVSIAIAIrgtmtEYFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTF 911
Cdd:cd03226 127 LSGGQKQRLAIAA-----ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF 188
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
844-921 |
1.24e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.44 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyfTNSKFMIL-DEPTNNLDTErkklLAEymgEILNNLEQS-------IIVTHDDTF-R 912
Cdd:COG2884 137 ELSGGEQqrVAIARAL--------VNRPELLLaDEPTGNLDPE----TSW---EIMELLEEInrrgttvLIATHDLELvD 201
|
....*....
gi 1080658287 913 EMAEKIIEL 921
Cdd:COG2884 202 RMPKRVLEL 210
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
1-423 |
1.48e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 52.05 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRS-HSNTTVEFTKGVNLILGKNGRGKTSILEAISTviFNTKDRSGKETGKSYIKFGEKSSKVDIDFIAN 79
Cdd:COG4694 1 MITKIKKLKNVGAfKDFGWLAFFKKLNLIYGENGSGKSTLSRILRS--LELGDTSSEVIAEFEIEAGGSAPNPSVRVFNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 80 DGREYNLKTEffktkpkKQTLKDIIGSEYDGDIQEKLEELCGIKKGFEE---TYENIVIAKQNEFINIFKAKPKDREEIF 156
Cdd:COG4694 79 DFVEENLRSG-------EEIKGIFTLGEENIELEEEIEELEKEIEDLKKeldKLEKELKEAKKALEKLLEDLAKSIKDDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 157 NKIFNTQIYKEMYDSFLKEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFKN--INVVSKNLEN 234
Cdd:COG4694 152 KKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLLEKsaVSSAIEELAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 235 EIKDYETTE-VE-------------------------LNNLVKNIKDEENKIKKYLNILKENIIEAKQ---AKKAKIIVK 285
Cdd:COG4694 232 LIQNPGNSDwVEqglayhkeeeddtcpfcqqelaaerIEALEAYFDDEYEKLLAALKDLLEELESAINalsALLLEILRT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 286 ETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKnLKVDISNLEENISKNSEKKENLESEISELKI 365
Cdd:COG4694 312 LLPSAKEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELLDE-LNDLIAALNALIEEHNAKIANLKAEKEEARK 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080658287 366 KEE-----DLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDILKKELVSKNDLFKIIN 423
Cdd:COG4694 391 KLEahelaELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAADEIN 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
319-738 |
1.48e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 319 IQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKL----KKYINLLDELEKLENFKDKK 394
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalrKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 395 LEDKLKKTTEIDILKKELVSKNDLFKII--NIEELEKKLYNFQELekelklleeqkiiFETEIKTLKKSSKELSNkicpf 472
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAeaEIEELEAQIEQLKEE-------------LKALREALDELRAELTL----- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 473 LNEKCQNLedkeaedyfsskisikTEELENLKKNIEEKTQILvekvvfEDKRKQYFELEKSIKDLELSLKNEEINLKEIE 552
Cdd:TIGR02168 815 LNEEAANL----------------RERLESLERRIAATERRL------EDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 553 LDIKNLDMDIQKLIENQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKIlksQNSIESNLKEINEFL 632
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEY 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 633 KEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDldnlllkVDKNIKELYS-LRTDKNLLKEKVSNLEEK 711
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIE-------EYEELKERYDfLTAQKEDLTEAKETLEEA 1022
|
410 420 430
....*....|....*....|....*....|..
gi 1080658287 712 IKniKIDE-----LKEKYDIIKEELNEINKKL 738
Cdd:TIGR02168 1023 IE--EIDRearerFKDTFDQVNENFQRVFPKL 1052
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
831-921 |
1.56e-06 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 50.10 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 831 VYLVGQERKIAfEQLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTerkkllaEYMGEILNNLEQS------ 902
Cdd:cd03292 124 VGLSHKHRALP-AELSGGEQqrVAIARAI-------VNSPTILIADEPTGNLDP-------DTTWEIMNLLKKInkagtt 188
|
90 100
....*....|....*....|.
gi 1080658287 903 -IIVTHDDT-FREMAEKIIEL 921
Cdd:cd03292 189 vVVATHAKElVDTTRHRVIAL 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
188-386 |
1.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 188 DSKINSLKENMEDKEqitnflKEEKDVEKNLQDNFKNINVVSKNLENEIKDYETTEVELNNLVKNIKDEENKIKKYLNIL 267
Cdd:COG3883 15 DPQIQAKQKELSELQ------AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 268 KENiieAKQAKKAKIIVKETE-----KSYLEYLDIENKLKDLRENLDNLLEEQKlniqyqNNIEKLELSNKNLKVDISNL 342
Cdd:COG3883 89 GER---ARALYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELK------ADKAELEAKKAELEAKLAEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080658287 343 EENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEK 386
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
230-681 |
2.00e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 230 KNLENEIKDYETTEVELNNLVKNIKDEENKIKKylniLKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLD 309
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 310 NLLEEQKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKK-ENLESEISELKIKEEDLDLKLKKYINLLDELEKle 388
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEE-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 389 nfKDKKLEDKLKKTTEIDILKKELVSKNDLFKIINIEELEKKLYNFQELEKELKLLEEQKIIFETEIKTLKKSSKELSNK 468
Cdd:COG4717 228 --ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 469 ICPFLNEKcQNLEDKEAEDYFSS---KISIKTEELENLKKNIEEKTQILVEkvvfedkrkqyfeLEKSIKDLELSLKNEE 545
Cdd:COG4717 306 ELQALPAL-EELEEEELEELLAAlglPPDLSPEELLELLDRIEELQELLRE-------------AEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 546 INLKEIELDIKNLDMDIQKLIENQEFQNsqmLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNL 625
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQE---LKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080658287 626 KEINEFLKEIKED-----TNKNIENIKLEIKTFENKLDNLknpYNEYLKNNVLAEDLDNLL 681
Cdd:COG4717 449 EELREELAELEAEleqleEDGELAELLQELEELKAELREL---AEEWAALKLALELLEEAR 506
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
842-921 |
2.66e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.22 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 842 FEQLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAEYmgeiLNNLEQS-IIVTHDDTF-REMAEK 917
Cdd:COG0488 150 VSELSGGWRrrVALARAL-------LSEPDLLLLDEPTNHLDLESIEWLEEF----LKNYPGTvLVVSHDRYFlDRVATR 218
|
....
gi 1080658287 918 IIEL 921
Cdd:COG0488 219 ILEL 222
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
137-712 |
2.68e-06 |
|
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: 51.17 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 137 KQNEFINIFKAKPKDREEIFNKIFNTQIYKEMYDSFLkeavDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEK 216
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL----NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 217 NLQDNFKNINVVSKNLENEI----KDYETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAKKaKIIVKETEKSYL 292
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIekkqQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-KIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 293 EyLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKN-----LKVDISNLEENI----SKNSEKKENLESEISEL 363
Cdd:TIGR04523 294 K-SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisqLNEQISQLKKELtnseSENSEKQRELEEKQNEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 364 KIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDILKKELVSKNDLFKII---------NIEELEKKLYNF 434
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLketiiknnsEIKDLTNQDSVK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 435 QEL--------EKELKLLEEQKIIFETEIKTLKKSSKELSNKICPFLNEKCQNLEDKEAEDYFSSKIS---IKTEELENL 503
Cdd:TIGR04523 453 ELIiknldntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISslkEKIEKLESE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 504 KKNIEEKTQILVEKVVFEDKRKQYFELEKSIkdleLSLKNEEINLKEIELDIKNLDMDIQKLIENQEFQNSQMlreKKKE 583
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKENLEKEI----DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL---IKEI 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 584 LEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLE-------IKTFENK 656
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESktkiddiIELMKDW 685
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080658287 657 LDNLKNPYNEYLKNNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKI 712
Cdd:TIGR04523 686 LKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
844-921 |
2.73e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.26 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMteyftNSKFMIL-DEPTNNLDTERKKllaEYMGeILNNLEQS----IIVTHDDTFREMAEKI 918
Cdd:PRK10535 144 QLSGGQQQRVSIA-RALM-----NGGQVILaDEPTGALDSHSGE---EVMA-ILHQLRDRghtvIIVTHDPQVAAQAERV 213
|
...
gi 1080658287 919 IEL 921
Cdd:PRK10535 214 IEI 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-608 |
2.82e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 260 IKKYLNILKEniiEAKQAKKAKII-----VKETEKSYLEYLDIENKLKDLRENLDNLLEEQKlniQYQNNIEKLELSNKN 334
Cdd:COG1196 198 LERQLEPLER---QAEKAERYRELkeelkELEAELLLLKLRELEAELEELEAELEELEAELE---ELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 335 LKVDISNLEENISKNSEKKENLESEISELkikEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDILKKELvs 414
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARL---EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 415 kndlfkiiniEELEKKLynfqelekelklleeqkiifETEIKTLKKSSKELSnkicpflnEKCQNLEDKEAEdyfssKIS 494
Cdd:COG1196 347 ----------EEAEEEL--------------------EEAEAELAEAEEALL--------EAEAELAEAEEE-----LEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 495 IKTEELENLKKNIEEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIENQEFQNS 574
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350
....*....|....*....|....*....|....
gi 1080658287 575 QMLREKKKELEVELRNLNLDEKRENLKNLLENLE 608
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
813-908 |
3.40e-06 |
|
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: 49.07 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 813 TGRTERIEW----SNEEKDK--YAVYLVG----QERKIAfeQLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNL 880
Cdd:cd03235 93 MGLYGHKGLfrrlSKADKAKvdEALERVGlselADRQIG--ELSGGQQqrVLLARAL-------VQDPDLLLLDEPFAGV 163
|
90 100 110
....*....|....*....|....*....|..
gi 1080658287 881 DTERKKLLAeymgEILNNLEQS----IIVTHD 908
Cdd:cd03235 164 DPKTQEDIY----ELLRELRREgmtiLVVTHD 191
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
498-779 |
3.54e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 498 EELENLKKNIEEKTQILvekvvfEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDiknLDMDIQKLIENQefqnSQML 577
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEI------ENVKSELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAE----LSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 578 REKKKELEVELRNLNLDEKRENLKNLLENLEIEkkkilksqnsiesNLKEINEFLKEIKEDTNKNIENIKLEIKTFENKL 657
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-------------ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 658 DNLKNPYNEylknnvLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKnikidELKEKYDIIKEELNEINKK 737
Cdd:TIGR02169 871 EELEAALRD------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS-----ELKAKLEALEEELSEIEDP 939
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1080658287 738 LGSSQEKIENyKKILEKIssqEEKQKKLLIEFKKLENKFNKA 779
Cdd:TIGR02169 940 KGEDEEIPEE-ELSLEDV---QAELQRVEEEIRALEPVNMLA 977
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
167-388 |
4.23e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 167 EMYDSFLKEAVDKYKSEKEN----LDSKINSLKENMEDKEQ-ITNFLKEEKDVekNLQDNFKNINVVSKNLENEIKDYET 241
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKalefLEEQLPELRKELEEAEAaLEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 242 TEVELNNLVKNIKDEENKIKKYLNILKEN-IIEAKQAKKAKIIVKETEKS------YLEYLDIENKLKDLRENLDNllEE 314
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpVIQQLRAQLAELEAELAELSarytpnHPDVIALRAQIAALRAQLQQ--EA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080658287 315 QKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKkenlESEISELkikEEDLDLKLKKYINLLDELEKLE 388
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRL---EREVEVARELYESLLQRLEEAR 378
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-316 |
4.56e-06 |
|
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: 49.90 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGKETGKSYIKFGEKSSKVDIDFIAND 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNIFENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 81 GREYNLKTEFFKTKPKKQTLKDIIGSEYDGDIQEKLEELCGIKKGFEETYENIVIAKQNEFINIFKAKPKDREEIFNKIF 160
Cdd:pfam13175 81 SFSIDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNNYYLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 161 NTQIYKEM-YDSFLKEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVSKNLENEIKDY 239
Cdd:pfam13175 161 KKNVFDKKsKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHENVLENLQIKKLLISADRNASDEDSEKINSL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 240 --ETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQK 316
Cdd:pfam13175 241 lgALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKIDKLKDFGYPPFLNPEIEIKKDDEDLPLNKN 319
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
836-908 |
5.63e-06 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain] Cd Length: 214 Bit Score: 48.45 E-value: 5.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080658287 836 QERKIAfeQLSGGEQVSIAIAiRGTMteyfTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQ-SIIVTHD 908
Cdd:cd03297 125 LNRYPA--QLSGGEKQRVALA-RALA----AQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIpVIFVTHD 191
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-92 |
6.16e-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: 48.03 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRS-HSNTTVEFTK----GVNLILGKNGRGKTSILEAISTVIFNTKDRSGKETG-KSYIKFGEKSSKVDI 74
Cdd:cd03279 1 MKPLKLELKNFGPfREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENlRSVFAPGEDTAEVSF 80
|
90 100
....*....|....*....|...
gi 1080658287 75 DFIANDG-----REYNLKTEFFK 92
Cdd:cd03279 81 TFQLGGKkyrveRSRGLDYDQFT 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
497-779 |
6.87e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 497 TEELENLKKNIEEKTQIlvekvvfedkRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIENQEFQnsqm 576
Cdd:TIGR02169 226 YELLKEKEALERQKEAI----------ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 577 LREKKKELEVELRNLnldekRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIkEDTNKNIENIKLEIKTFENK 656
Cdd:TIGR02169 292 VKEKIGELEAEIASL-----ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI-EEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 657 LDNLKNPYNEY-LKNNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIK--IDELKEKYDIIKEELNE 733
Cdd:TIGR02169 366 LEDLRAELEEVdKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaIAGIEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1080658287 734 INKKLGSSQEKIENYKKILEKISSQ----EEKQKKLLIEFKKLENKFNKA 779
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQElydlKEEYDRVEKELSKLQRELAEA 495
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-43 |
8.05e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 49.16 E-value: 8.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1080658287 3 IKKVQLENYRSHSNTTVEFTkGVNLILGKNGRGKTSILEAI 43
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLG-PLTVLIGANGSGKSNLLDAL 41
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
844-919 |
1.01e-05 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 47.52 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMteyfTNSKFMILDEPTNNLDTErkkLLAEYMgEILNNLEQS----IIVTHDDTF-REMAEKI 918
Cdd:cd03262 135 QLSGGQQQRVAIA-RALA----MNPKVMLFDEPTSALDPE---LVGEVL-DVMKDLAEEgmtmVVVTHEMGFaREVADRV 205
|
.
gi 1080658287 919 I 919
Cdd:cd03262 206 I 206
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-76 |
1.09e-05 |
|
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: 46.92 E-value: 1.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 3 IKKVQLENYRSHSNTT-VEFTKGVNLILGKNGRGKTSILEAISTVIFNTKD----RSGKETGKSYIKFGEKSSKVDIDF 76
Cdd:cd03239 1 IKQITLKNFKSYRDETvVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAklrrGSLLFLAGGGVKAGINSASVEITF 79
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
836-921 |
1.20e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.91 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 836 QERKIafEQLSGGEQVSIAIAirGTMTEyftNSKFMILDEPTNNLDTERKKLLAEYmgeiLNNLEQSII-VTHDDTF-RE 913
Cdd:COG0488 426 AFKPV--GVLSGGEKARLALA--KLLLS---PPNVLLLDEPTNHLDIETLEALEEA----LDDFPGTVLlVSHDRYFlDR 494
|
....*...
gi 1080658287 914 MAEKIIEL 921
Cdd:COG0488 495 VATRILEF 502
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
844-907 |
1.35e-05 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 46.27 E-value: 1.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNL-DTERKKLLaeymgEILNNLEQS----IIVTH 907
Cdd:cd03216 82 QLSVGERQMVEIA-RALAR----NARLLILDEPTAALtPAEVERLF-----KVIRRLRAQgvavIFISH 140
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
844-919 |
2.00e-05 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 46.73 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLD-TERKKLLaeymgEILNNLEQS-----IIVTHD-DTFREM 914
Cdd:cd03257 145 ELSGGQRqrVAIARAL-------ALNPKLLIADEPTSALDvSVQAQIL-----DLLKKLQEElgltlLFITHDlGVVAKI 212
|
....*
gi 1080658287 915 AEKII 919
Cdd:cd03257 213 ADRVA 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
833-921 |
2.20e-05 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 46.47 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 833 LVGQERKI-AF-EQLSGGEQ--VSIAIAIrgtmteyfTNSKFMIL-DEPTNNLDTErkklLAEYMGEILNNLEQS----I 903
Cdd:TIGR02673 124 QVGLEHKAdAFpEQLSGGEQqrVAIARAI--------VNSPPLLLaDEPTGNLDPD----LSERILDLLKRLNKRgttvI 191
|
90
....*....|....*....
gi 1080658287 904 IVTHD-DTFREMAEKIIEL 921
Cdd:TIGR02673 192 VATHDlSLVDRVAHRVIIL 210
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
579-804 |
2.39e-05 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 48.30 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 579 EKKKELEVELRNLNLDEkrENLKNLLENLEIEKKKILKSQNSIESNLKEIN----EFLKEIKEDTNKNIENIKLEIKTFE 654
Cdd:PRK00448 2 EMQEKFKKLLDQINIPD--DLQSEALESAEIEKVVVDKKSKKWEFHLKFPNilpiEDFKLFKEKLKQSFSHIADIKVTFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 655 NKLDNLknpyneYLKNNVLAEDLDNLLLKVDKNIKELYSLRTDK------NLLKEKVSN--LEEKIKNIKIDELKEKYDI 726
Cdd:PRK00448 80 IEVENI------TFTEELLLDYWNEIIEKAKKNSPLFKSLLKKQkvevegNKLIIKVNNeiERDHLKKKHLPKLIKQYEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 727 IKEELNEINKKLGSSQEKIENYKKILEKIssQEEKQKKLLIEFKKLE---NKFNKANLIRNEVGQMGRAISKYMLSGISN 803
Cdd:PRK00448 154 FGFGILKIDFEIDDSKEELEKFEAQKEEE--DEKLAKEALEAMKKLEaekKKQSKNFDPKEGPVQIGKKIDKEEITPMKE 231
|
.
gi 1080658287 804 I 804
Cdd:PRK00448 232 I 232
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
823-921 |
2.52e-05 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 46.07 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 823 NEEKDKYAVYLVG----QERKIAfeQLSGGEQVSIAIAirgtmTEYFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNN 898
Cdd:TIGR03608 111 KREKKKEALEKVGlnlkLKQKIY--ELSGGEQQRVALA-----RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE 183
|
90 100
....*....|....*....|...
gi 1080658287 899 LEQSIIVTHDDTFREMAEKIIEL 921
Cdd:TIGR03608 184 GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
845-921 |
2.69e-05 |
|
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: 45.45 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 845 LSGGEQVSIAIA---IRgtmteyftNSKFMILDEPTNNLD--TERkkllaeymgEILNNLEQ------SIIVTHDDTFRE 913
Cdd:cd03228 97 LSGGQRQRIAIAralLR--------DPPILILDEATSALDpeTEA---------LILEALRAlakgktVIVIAHRLSTIR 159
|
....*...
gi 1080658287 914 MAEKIIEL 921
Cdd:cd03228 160 DADRIIVL 167
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-755 |
2.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 416 NDLFKIINIEELEKKLynfqelekelKLLEEQKIIFETEIKTLKKSskelsnkicpfLNEKCQNLEDKEAEdyfSSKISI 495
Cdd:TIGR02168 671 SILERRREIEELEEKI----------EELEEKIAELEKALAELRKE-----------LEELEEELEQLRKE---LEELSR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 496 KTEELENLKKNIEEKTQILVEKVvfEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLiENQEFQNSQ 575
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERI--AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 576 MLREKKKELevELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIkEDTNKNIENIKLEIKTFEN 655
Cdd:TIGR02168 804 ALDELRAEL--TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI-EELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 656 KLDNLKNPYNEYLKN-NVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIkIDELKEKY----DIIKEE 730
Cdd:TIGR02168 881 ERASLEEALALLRSElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL-QERLSEEYsltlEEAEAL 959
|
330 340
....*....|....*....|....*
gi 1080658287 731 LNEINKKLGSSQEKIENYKKILEKI 755
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
830-918 |
2.93e-05 |
|
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: 45.93 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 830 AVYLVGQERKiAFEQLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAEYMGEilnNLEQS---II 904
Cdd:COG4133 118 AVGLAGLADL-PVRQLSAGQKrrVALARLL-------LSPAPLWLLDEPFTALDAAGVALLAELIAA---HLARGgavLL 186
|
90
....*....|....
gi 1080658287 905 VTHDDTFREMAEKI 918
Cdd:COG4133 187 TTHQPLELAAARVL 200
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-552 |
3.56e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 3 IKKVQLENYRSHSNTTV-EFTKGVNLILGKNGRGKTSILEAISTVIFNTKDRSGKETGKSYIKFGEKSSK------VDID 75
Cdd:TIGR02169 2 IERIELENFKSFGKKKViPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQsgneayVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 76 FIANDGR---EYNLKTEFFKTKPKKQTLKDIIGSEYD-GDIQEKLEELCGikkgFEETYeNIVIakQNEFINIFKAKPKD 151
Cdd:TIGR02169 82 FKNDDGKfpdELEVVRRLKVTDDGKYSYYYLNGQRVRlSEIHDFLAAAGI----YPEGY-NVVL--QGDVTDFISMSPVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 152 REEIFNKIfntqiykemydsflkEAVDKYKSEKENLDSKINSLKENMEDKEQItnfLKEEKDVEKNLQDNfKNINVVSKN 231
Cdd:TIGR02169 155 RRKIIDEI---------------AGVAEFDRKKEKALEELEEVEENIERLDLI---IDEKRQQLERLRRE-REKAERYQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 232 LENEIKDYETTEvelnnLVKNIKDEENKIKKYlnilkENIIEAKQAKKAKIIVKETEKSyLEYLDIENKLKDLRENLDNL 311
Cdd:TIGR02169 216 LLKEKREYEGYE-----LLKEKEALERQKEAI-----ERQLASLEEELEKLTEEISELE-KRLEEIEQLLEELNKKIKDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 312 LEEQKLNIQYQnnIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKL----KKYINLLDELEKL 387
Cdd:TIGR02169 285 GEEEQLRVKEK--IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIeeerKRRDKLTEEYAEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 388 ENFKDKKLEDKLKKTTEIDILKKELVSKNDlfkiiNIEELEKKLYNfqelekelklleeqkiiFETEIKTLKKSSKELSN 467
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYRE-----KLEKLKREINE-----------------LKRELDRLQEELQRLSE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 468 KIcPFLNEKCQNLEDKEAEdyFSSKISIKTEELENLKKNIEEKTQILvekvvfEDKRKQYFELEKSIKDLELSLKNEEIN 547
Cdd:TIGR02169 421 EL-ADLNAAIAGIEAKINE--LEEEKEDKALEIKKQEWKLEQLAADL------SKYEQELYDLKEEYDRVEKELSKLQRE 491
|
....*
gi 1080658287 548 LKEIE 552
Cdd:TIGR02169 492 LAEAE 496
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
844-921 |
3.64e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 46.27 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTEyftnSKFMILDEPTNNLDTERKKLLAEYMGEIlnNLEQS---IIVTHDDTFREMAEKIIE 920
Cdd:COG4181 146 QLSGGEQQRVALA-RAFATE----PAILFADEPTGNLDAATGEQIIDLLFEL--NRERGttlVLVTHDPALAARCDRVLR 218
|
.
gi 1080658287 921 L 921
Cdd:COG4181 219 L 219
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
94-787 |
4.25e-05 |
|
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: 47.74 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 94 KPKKQTLKDIIGSEYDGDIQEKLEElcGIKKGFEETYENIVIAKQnefiNIFKAKPKDREEIFNKIFNTQIYKEMYDSFL 173
Cdd:TIGR01612 516 KPDEVPSKNIIGFDIDQNIKAKLYK--EIEAGLKESYELAKNWKK----LIHEIKKELEEENEDSIHLEKEIKDLFDKYL 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 174 KEAVDKYKSEKENLDskinsLKENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVSK--------NLENEIKDYETTEVE 245
Cdd:TIGR01612 590 EIDDEIIYINKLKLE-----LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDELAKispyqvpeHLKNKDKIYSTIKSE 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 246 LNNLVKNikDEENKIKKYLNILKENIIEAKQAKK-------------AKIIVKETEKSYLEYLDIENKLKDLrenLDNLL 312
Cdd:TIGR01612 665 LSKIYED--DIDALYNELSSIVKENAIDNTEDKAklddlkskidkeyDKIQNMETATVELHLSNIENKKNEL---LDIIV 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 313 EEQK-LNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDL----DLKLKKYINLLDELEKL 387
Cdd:TIGR01612 740 EIKKhIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQinidNIKDEDAKQNYDKSKEY 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 388 ENFKDKKLEDKLKKTTEIDILKKELVSKNDLFkiINIEELEKKLYNFQELEKELKLLEEQKIIFETEIKTLKKS---SKE 464
Cdd:TIGR01612 820 IKTISIKEDEIFKIINEMKFMKDDFLNKVDKF--INFENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKfndSKS 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 465 LSNKICPFLNEKCQNLEDKEAEDYFSSKISIKTEELEN-------LKKNIEEKTQILVEKVVFEDKRKQYFELEKSIKDL 537
Cdd:TIGR01612 898 LINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKfhnkqniLKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKIN 977
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 538 ELSLKNEEINLKEIELDIKNLDMDIQKLIENQEFQNSQMLREKKKELEVELRnlNLDEKRENLKNLLENLEIE-KKKILK 616
Cdd:TIGR01612 978 ELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATN--DIEQKIEDANKNIPNIEIAiHTSIYN 1055
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 617 SQNSIESNL-KEINEFLKEIKEDTNKNIEN---IKLEIKTFeNKLDNLKNPYNEYLKN-NVLAEDLDNLLLKVDKNIKEL 691
Cdd:TIGR01612 1056 IIDEIEKEIgKNIELLNKEILEEAEINITNfneIKEKLKHY-NFDDFGKEENIKYADEiNKIKDDIKNLDQKIDHHIKAL 1134
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 692 YSLR--------------------TDKNLLKEKVSNLEEKIKNI--KIDELKEKYDIIKEELNEINK--KLGSSQEKIEN 747
Cdd:TIGR01612 1135 EEIKkksenyideikaqindledvADKAISNDDPEEIEKKIENIvtKIDKKKNIYDEIKKLLNEIAEieKDKTSLEEVKG 1214
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1080658287 748 Y---------KKILEKISSQEEKQKKLLIEFKK----LENKFNKANLIRNEVG 787
Cdd:TIGR01612 1215 InlsygknlgKLFLEKIDEEKKKSEHMIKAMEAyiedLDEIKEKSPEIENEMG 1267
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
173-914 |
4.39e-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: 47.35 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 173 LKEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVSKNLENEIKDYETTEVELNNLVKN 252
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 253 IKDEENKIKKYLNILKEniiEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSN 332
Cdd:TIGR00606 600 LASLEQNKNHINNELES---KEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 333 --------------KNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLenfKDKKLEDK 398
Cdd:TIGR00606 677 qsccpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE---IPELRNKL 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 399 LKKTTEIDILKKELVSKNDLFKIINIEELEKKLYNFQELEKELKLLEEQkiifETEIKTLKKSSKELSNKICPFLNEKCQ 478
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELK----DVERKIAQQAAKLQGSDLDRTVQQVNQ 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 479 NLEDKEAEdyfSSKISIKTEELENLKKNIEEKTQIL--------VEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKE 550
Cdd:TIGR00606 830 EKQEKQHE---LDTVVSKIELNRKLIQDQQEQIQHLksktnelkSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 551 IELDIKNLDMDIQKLI-ENQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQnsiESNLKEIN 629
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQqEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK---ETELNTVN 983
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 630 EFLKEI---KEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEdLDNLLLKVDKNIKELYSLRtdknlLKEKVS 706
Cdd:TIGR00606 984 AQLEECekhQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKE-VEEELKQHLKEMGQMQVLQ-----MKQEHQ 1057
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 707 NLEEKIKNIKIDELK--EKYDIIKEELNEINKKLGSSQ--EKIENYKKILEKISSQEEKQKKLLIEFKKLEnkfnkANLI 782
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLalGRQKGYEKEIKHFKKELREPQfrDAEEKYREMMIVMRTTELVNKDLDIYYKTLD-----QAIM 1132
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 783 RNEVGQMGR--AISKYMLSGISNIASVNFNKITGRTERIEWSNEEKDKYAVYLVGQERKIAFE---QLSGGEQVSIAIAI 857
Cdd:TIGR00606 1133 KFHSMKMEEinKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDmrgRCSAGQKVLASLII 1212
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080658287 858 RGTMTEYFTNSKFMI-LDEPTNNLDTERKKLLAEYMGEILNNLEQS-----IIVTHDDTFREM 914
Cdd:TIGR00606 1213 RLALAETFCLNCGIIaLDEPTTNLDRENIESLAHALVEIIKSRSQQrnfqlLVITHDEDFVEL 1275
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
843-919 |
5.12e-05 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain] Cd Length: 213 Bit Score: 45.59 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 843 EQLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSII-VTHDDTfrE---MAE 916
Cdd:cd03259 129 HELSGGQQqrVALARAL-------AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIyVTHDQE--EalaLAD 199
|
...
gi 1080658287 917 KII 919
Cdd:cd03259 200 RIA 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
486-775 |
5.88e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 486 EDYFSSKISIKTEELENLKKNIEEKTQILVEKVV-FEDKRKQYFELEKSIkdlelslkneeinlKEIELDIKNLDMDIQK 564
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEeLEELTAELQELEEKL--------------EELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 565 LieNQEFQNsqmLREKKKELEVELRnlnldEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEfLKEIKEDTNKNIE 644
Cdd:TIGR02168 286 L--QKELYA---LANEISRLEQQKQ-----ILRERLANLERQLEELEAQLEELESKLDELAEELAE-LEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 645 NIKLEIKTFENKLDNLKNPYNEYLKN-NVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKIDELKEK 723
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1080658287 724 YDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENK 775
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| IQG1 |
COG5261 |
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ... |
505-771 |
9.22e-05 |
|
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];
Pssm-ID: 227586 [Multi-domain] Cd Length: 1054 Bit Score: 46.42 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 505 KNIEEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELdiknldmdIQKLIEN-QEFQNSQMLREkkkE 583
Cdd:COG5261 676 KEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLT--------HEIIIEYlDNLYDPDSLVD---L 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 584 LEVELRNLNL--DEKRENLknlleNLEIEKKKILKSQNSIES---NLKEINEFLKEIKEDTNKNIENIKL---EIKTFEN 655
Cdd:COG5261 745 LLQELGELCSfpQDQRDTL-----NCLVTLPLFNRSDDPIRDlkqQLKRTRVYIIYVDAGTNLFEQLLRLlpsDEPATRN 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 656 KLDNLKNPYNEYLKNNVLAEDLDNLLLKVDKNIKELYSLR--TDKNLLKEKVSNLEEKIKNIK--IDELKEKYDIIKEEL 731
Cdd:COG5261 820 PLDLNPNIRDDPSVSSLKSMSLMKLKIRAIELLDELETLGfvSRENRYQPLLNEIAKDIINLDalYERRRAELDILQDSL 899
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1080658287 732 NEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKK 771
Cdd:COG5261 900 RNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSR 939
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-271 |
9.81e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 1 MIIKKVQLENYRSHSNTTVEFTKGVNLILGKNGRGKTSILEAISTVIfntKDRSGKETGKSYIKFGEKSSkvdidfiaND 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML---LERLEKEADELFKPQGRKPE--------LN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 81 GREYNLKTEFFKTKPKKQtlkdiigseydGDIQEKLEELCGIKKGFEETYENIVIAKQnefinifkakpkDREEIFNKIF 160
Cdd:COG4717 70 LKELKELEEELKEAEEKE-----------EEYAELQEELEELEEELEELEAELEELRE------------ELEKLEKLLQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 161 NTQIYKEMydSFLKEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFkninvvSKNLENEIKDYE 240
Cdd:COG4717 127 LLPLYQEL--EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLA 198
|
250 260 270
....*....|....*....|....*....|.
gi 1080658287 241 TTEVELNNLVKNIKDEENKIKKYLNILKENI 271
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-777 |
1.17e-04 |
|
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: 46.21 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 350 SEKKENLESEISELKIKEEDLDLKLKKYINLLDELeklenfkdkkledklkkTTEIDILKKElvskndlfkiinIEELEK 429
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDEL-----------------SQELSDASRK------------IGEIEK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 430 KLYnfqelekelklleeqkiIFETEIKTLKKSSKELSNKIcpflNEKCQNLEDKEAE-DYFSSKISIKTEELENLKKNIE 508
Cdd:TIGR02169 724 EIE-----------------QLEQEEEKLKERLEELEEDL----SSLEQEIENVKSElKELEARIEELEEDLHKLEEALN 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 509 EKTQILVEKVVfEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIENQEFQNSQMLREKKKELEVEL 588
Cdd:TIGR02169 783 DLEARLSHSRI-PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 589 RNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKTFENKLDNLKNpYNEYL 668
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE-IEDPK 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 669 KNNVLAEDLDNLLLKVDKNIKElyslrtdknlLKEKVSNLEEkIKNIKIDElkekYDIIKEELNEINKKLGSSQEKienY 748
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQR----------VEEEIRALEP-VNMLAIQE----YEEVLKRLDELKEKRAKLEEE---R 1002
|
410 420 430
....*....|....*....|....*....|
gi 1080658287 749 KKILEKISSQEEKQKKLLIE-FKKLENKFN 777
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEaFEAINENFN 1032
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
696-769 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080658287 696 TDKNLLKEKVSNLEEKIKNI--KIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEF 769
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAqaELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
752-919 |
1.27e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 44.70 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 752 LEKISSQEekqkkLLIEFKKLENKFNKANLIRNEVGQMGRAIskYMLSGISNIASVNFNKITGRTEriewSNEEKDKYAV 831
Cdd:PRK09493 50 LEEITSGD-----LIVDGLKVNDPKVDERLIRQEAGMVFQQF--YLFPHLTALENVMFGPLRVRGA----SKEEAEKQAR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 832 YLVGQ----ERKIAF-EQLSGGEQVSIAIAiRGTMTEyftnSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVT 906
Cdd:PRK09493 119 ELLAKvglaERAHHYpSELSGGQQQRVAIA-RALAVK----PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT 193
|
170
....*....|....
gi 1080658287 907 HDDTF-REMAEKII 919
Cdd:PRK09493 194 HEIGFaEKVASRLI 207
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
543-797 |
1.32e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 543 NEEINLKEIELDIKNLDMDIQ-KLIENQEFQNSQMLREKKKELEVELrnlnldEKRENLKNLLENLEIEKKKILKSQNSI 621
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYnKNIEEQRKKNGENIARKQNKYDELV------EEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 622 ESNLKEINEFLKEIK--------------------------EDTNKNIENIKLEIKTFENKLDNLKNPYNEylknnvlae 675
Cdd:PHA02562 254 SAALNKLNTAAAKIKskieqfqkvikmyekggvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDE--------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 676 dLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIK--IDELKEKYDIIKEELNEINkklgssqekiENYKKILE 753
Cdd:PHA02562 325 -LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKaaIEELQAEFVDNAEELAKLQ----------DELDKIVK 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1080658287 754 KISSQEEKQKKLLIEFKKLENKFNKANLIRNEVGQMGRAISKYM 797
Cdd:PHA02562 394 TKSELVKEKYHRGIVTDLLKDSGIKASIIKKYIPYFNKQINHYL 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-386 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 182 SEKENLDSKINSLKENMEDKEQItnfLKEEKDVEKNLQDNFKNINVVSKNLENEIKDYETtevELNNLVKNIKDEENKIK 261
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKE---LAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 262 KYLNILKENiiEAKQAKKAKIIVKETEKSYLEYL----DIENKLKDLReNLDNLLEEQKLNI-QYQNNIEKLELSNKNLK 336
Cdd:COG4942 94 ELRAELEAQ--KEELAELLRALYRLGRQPPLALLlspeDFLDAVRRLQ-YLKYLAPARREQAeELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080658287 337 VDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEK 386
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
453-817 |
1.64e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 453 TEIKTLKKSSKELSNKIcpfLNEKCQNLEDKEAEDYFSSKISIKTEELENLKKNIEE---KTQILVEKVVFEDKRKQYFE 529
Cdd:COG5022 810 KEYRSYLACIIKLQKTI---KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLlkkETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 530 LEKSIKDLE-LSLKNEEINLKEIELdiknldmdiQKLIENQEFQNSQMLREKKKELEVELRNLNLDEKRENlknllenlE 608
Cdd:COG5022 887 LKIDVKSISsLKLVNLELESEIIEL---------KKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSI--------E 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 609 IEKKKILKSQNSIESNLKEINeflkEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNvlaEDLDNLLLKVDKNI 688
Cdd:COG5022 950 YVKLPELNKLHEVESKLKETS----EEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY---GALQESTKQLKELP 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 689 KELYSLRTDKNLLKEKVSNLeeKIKNiKIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIE 768
Cdd:COG5022 1023 VEVAELQSASKIISSESTEL--SILK-PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVK 1099
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1080658287 769 FKKLENK--FNKANLIRNEVGQMGRAISKYMLSGISNIASVNFNKITGRTE 817
Cdd:COG5022 1100 DLEVTNRnlVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLS 1150
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
580-776 |
1.79e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 580 KKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKL----------- 648
Cdd:PRK05771 71 PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLlgfkyvsvfvg 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 649 EI-KTFENKLDNLKNPYNEYLKNNvlAEDLDNLLLKVDKNIKELySLRTDKNLLKEKVSNLEEKIKNIKIDELKEKYDII 727
Cdd:PRK05771 151 TVpEDKLEELKLESDVENVEYIST--DKGYVYVVVVVLKELSDE-VEEELKKLGFERLELEEEGTPSELIREIKEELEEI 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080658287 728 KEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENKF 776
Cdd:PRK05771 228 EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKTDKTF 276
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
842-908 |
2.01e-04 |
|
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: 43.19 E-value: 2.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080658287 842 FEQLSGGEQ--VSIAIAIRGtmteyftNSKFMILDEPTNNLD-TERKKLLaeymgEILNNLEQS-----IIVTHD 908
Cdd:cd03214 95 FNELSGGERqrVLLARALAQ-------EPPILLLDEPTSHLDiAHQIELL-----ELLRRLARErgktvVMVLHD 157
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
844-907 |
2.04e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.20 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080658287 844 QLSGGEQVSIAIAiRGTMteyfTNSKFMILDEPTNNLD--TERkkllaeymgEILNNLEQS------IIVTH 907
Cdd:PRK11160 475 QLSGGEQRRLGIA-RALL----HDAPLLLLDEPTEGLDaeTER---------QILELLAEHaqnktvLMITH 532
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
174-919 |
2.31e-04 |
|
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: 44.96 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 174 KEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVSKNLENEIKDYETTEVELNNLVKNI 253
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 254 KDEENKIKKYLNILKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNK 333
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVS 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 334 NLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDILKKELV 413
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEL 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 414 SKNDLFKIINIEELEKKLYN----FQELEKELKLLEEQKIIFETEIKTLKKSSKELSNKICPFLNEKCQNLEDKEAEDYF 489
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLeeglAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 490 SS--KISIKTEELENLKKNIEEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIE 567
Cdd:pfam02463 715 LKleAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 568 NQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEK-KKILKSQNSIESNLKEINEFLKEIKEDTNKNIENI 646
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELaLELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 647 KLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKIDELKEKYDI 726
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 727 IKEElnEINKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNKANLIRnEVGQMGRAISKYMLSGISNIAS 806
Cdd:pfam02463 955 KEEE--EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR-AIIEETCQRLKEFLELFVSINK 1031
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 807 VNFNKITGRTERIEWSNEEKDKYAVYLVGQERKIAF--------EQLSGGEQVSIAIAIRGTMTEYfTNSKFMILDEPTN 878
Cdd:pfam02463 1032 GWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPpgkgvknlDLLSGGEKTLVALALIFAIQKY-KPAPFYLLDEIDA 1110
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1080658287 879 NLDTERKKLLAEYMGEILNNLeQSIIVTHDDTFREMAEKII 919
Cdd:pfam02463 1111 ALDDQNVSRVANLLKELSKNA-QFIVISLREEMLEKADKLV 1150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
844-878 |
2.34e-04 |
|
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: 42.25 E-value: 2.34e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTN 878
Cdd:pfam00005 121 TLSGGQRqrVAIARAL-------LTKPKLLLLDEPTA 150
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-657 |
2.94e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 173 LKEAVDKYKSEKENLDSKINSLKENMEDKEQITNFLKEEKDVEKNL-----QDNFKNINVVSKNLENEIKDYETTEVELN 247
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 248 NLVKNIKDEENKIKKYLNILK-ENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQ-KLNIQYQNNI 325
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSEsENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeKLNQQKDEQI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 326 EKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENfkdkkledklKKTTEI 405
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN----------KIKQNL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 406 DILKKELVSKNDLFKIINIE--ELEKKLYNFQELEKELKLLEEqkiIFETEIKTLKKSSKELSNKICPfLNEKCQNLEDK 483
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEkkELEEKVKDLTKKISSLKEKIE---KLESEKKEKESKISDLEDELNK-DDFELKKENLE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 484 EAEDYFSSKISIKTEELENLKKNIEEKTQILVEKVV-FEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDI 562
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKeKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 563 QKLIENQEFQNSQMLREKKKELEVELRN----------LNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFL 632
Cdd:TIGR04523 641 NKLKQEVKQIKETIKEIRNKWPEIIKKIkesktkiddiIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKEL 720
|
490 500
....*....|....*....|....*
gi 1080658287 633 KEIKEDTNKNIENIKLEIKTFENKL 657
Cdd:TIGR04523 721 KKLDEFSKELENIIKNFNKKFDDAF 745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-388 |
3.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 127 EETYENIVIAKQNEFINIFKAKPKDREEIFNKIFNTQIYKEMYDSflKEAVDKYKSEKENLDSKINSLKENMEDKEQITN 206
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 207 FLKEEKDvEKNLQDNFKNINVVSKNLENEIKDYETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAKKAKIIVKE 286
Cdd:PTZ00121 1707 LKKKEAE-EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 287 TEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEK-KENLESEISELKI 365
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKhKFNKNNENGEDGN 1865
|
250 260
....*....|....*....|...
gi 1080658287 366 KEEDLDlklKKYINLLDELEKLE 388
Cdd:PTZ00121 1866 KEADFN---KEKDLKEDDEEEIE 1885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
529-764 |
3.64e-04 |
|
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: 44.67 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 529 ELEKSIKDLELSlkneEINLKEIELDIKNLDMDIQKL-IENQEFQNSQMLREKKKELEVELRNLN---LDEKRENLKNLL 604
Cdd:TIGR02169 171 KKEKALEELEEV----EENIERLDLIIDEKRQQLERLrREREKAERYQALLKEKREYEGYELLKEkeaLERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 605 ENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKT----FENKLDNLKNPYNEYLKN--------NV 672
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeLEAEIASLERSIAEKEREledaeerlAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 673 LAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNI--KIDELKEKYDIIKEELNEINKKLGSSQEKIENYKK 750
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250
....*....|....
gi 1080658287 751 ILEKIssQEEKQKK 764
Cdd:TIGR02169 407 ELDRL--QEELQRL 418
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
845-921 |
3.69e-04 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 42.20 E-value: 3.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080658287 845 LSGGEQVSIAIAiRGtmteYFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAEKIIEL 921
Cdd:cd03246 97 LSGGQRQRLGLA-RA----LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-77 |
3.86e-04 |
|
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: 41.96 E-value: 3.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080658287 5 KVQLENYRSH-SNTTVEFTKG-VNLILGKNGRGKTSILEAIstvIFNTKDRSGKETGKSYIKFGEKSSKVDIDFI 77
Cdd:cd03227 1 KIVLGRFPSYfVPNDVTFGEGsLTIITGPNGSGKSTILDAI---GLALGGAQSATRRRSGVKAGCIVAAVSAELI 72
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
489-780 |
4.03e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 489 FSSKISIKTEELENLKKNIEEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINL--KEIELDIKN--LDMDIQK 564
Cdd:PLN03229 407 FQEGVPVDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKlkKEIDLEYTEavIAMGLQE 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 565 LIEN--QEFQ--NSQ------MLREKKKELEVEL-RNLNLDEKRENLKNLLENL-EIEKKKILKSQNSIESNLK-EINEF 631
Cdd:PLN03229 487 RLENlrEEFSkaNSQdqlmhpVLMEKIEKLKDEFnKRLSRAPNYLSLKYKLDMLnEFSRAKALSEKKSKAEKLKaEINKK 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 632 LKEI--KEDTNKNIENIKLEI------------KTFENKLDNLKNPYNEYLKNNVLAEDLDnlLLKVDKNIKELYSLRTD 697
Cdd:PLN03229 567 FKEVmdRPEIKEKMEALKAEVassgassgdeldDDLKEKVEKMKKEIELELAGVLKSMGLE--VIGVTKKNKDTAEQTPP 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 698 KNlLKEKVSNLEEKIKN-----IKIDELKEKYDIIKEELNEINKKLG-SSQEKIENYK-----KILEKISSQE--EKQKK 764
Cdd:PLN03229 645 PN-LQEKIESLNEEINKkiervIRSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEqqikqKIAEALNSSElkEKFEE 723
|
330
....*....|....*.
gi 1080658287 765 LLIEFKKLENKFNKAN 780
Cdd:PLN03229 724 LEAELAAARETAAESN 739
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
845-921 |
4.40e-04 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 43.88 E-value: 4.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080658287 845 LSGGEQVSIAIAiRGtmteYFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAEKIIEL 921
Cdd:TIGR01842 455 LSGGQRQRIALA-RA----LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVL 526
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
575-778 |
4.62e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 575 QMLREKKKELevelrnLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEdtnkniENIKLEIktFE 654
Cdd:PLN02939 135 GMIQNAEKNI------LLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQ------EKIHVEI--LE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 655 NKLDNLKNPYNEYLKNNVLAEDLDNLLLKVDKniKELYSLRTDKNLLKEKVSNLEEKIKNIKIdeLKEKYDIIKEELNEI 734
Cdd:PLN02939 201 EQLEKLRNELLIRGATEGLCVHSLSKELDVLK--EENMLLKDDIQFLKAELIEVAETEERVFK--LEKERSLLDASLREL 276
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 735 NKKLGSSQ---------------EKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNK 778
Cdd:PLN02939 277 ESKFIVAQedvsklsplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK 335
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
842-906 |
5.29e-04 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 42.64 E-value: 5.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 842 FEQLSGGEQ--VSIAIairgtmtEYFTNSKFMILDEPTNNLDTerkkLLAEYMGEILNNLEQS---IIVT 906
Cdd:cd03234 141 VKGISGGERrrVSIAV-------QLLWDPKVLILDEPTSGLDS----FTALNLVSTLSQLARRnriVILT 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
845-919 |
5.47e-04 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain] Cd Length: 178 Bit Score: 41.79 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 845 LSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTErkklLAEYMGEILNNLEQS-----IIVTHD-DTFREMAEKI 918
Cdd:cd03229 101 LSGGQQQRVALA-RALAM----DPDVLLLDEPTSALDPI----TRREVRALLKSLQAQlgitvVLVTHDlDEAARLADRV 171
|
.
gi 1080658287 919 I 919
Cdd:cd03229 172 V 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
587-782 |
5.61e-04 |
|
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: 43.90 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 587 ELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDT---NKNIENIKLEIKTFENKLDNLKnp 663
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEELE-- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 664 ynEYLKNnvLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKIDELKEKYDIIKEELNEINKKLGSSQE 743
Cdd:TIGR02169 744 --EDLSS--LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080658287 744 KIE--NYKKILEKISSQEEKQKKLLIEFKKLENKFNKANLI 782
Cdd:TIGR02169 820 KLNrlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
269-778 |
5.88e-04 |
|
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: 43.56 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 269 ENIIEAKQAKKAKIIVKETEKSYL--EYLDIENKLKDLrenlDNLLEEQKLNIQYQNniEKLELSNKNLKVDISNLEENI 346
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLliQITEKENKMKDL----TFLLEESRDKANQLE--EKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 347 SKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDIL-----------KKELVSK 415
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtcsleellrteQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 416 NDLFKIINIeELEKKLYNFQELEKELKLLeeqkiifETEIKTLKKsskelsnkicpFLNEKCQNLEDKEAEDYFSSKISI 495
Cdd:pfam05483 376 EDQLKIITM-ELQKKSSELEEMTKFKNNK-------EVELEELKK-----------ILAEDEKLLDEKKQFEKIAEELKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 496 KTEELENLKKNIEEKTQILVEKVVFEDKRKQYFelEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIEnqefQNSQ 575
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY--LKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ----EASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 576 MLREKKKELEvelrNLNLDEKREnlKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKTFEN 655
Cdd:pfam05483 511 MTLELKKHQE----DIINCKKQE--ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 656 KLDNLKnpyneylknnVLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVS--NLEEKIKNIKIDELKEKYDIIKEELNE 733
Cdd:pfam05483 585 KEKQMK----------ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSaeNKQLNAYEIKVNKLELELASAKQKFEE 654
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1080658287 734 InkkLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNK 778
Cdd:pfam05483 655 I---IDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK 696
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
188-388 |
5.93e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 188 DSKINSLKENMEDKEQITNFLKEEKDVEKNLQDNFKNINVVS------------KNLENEIKDYETTEVELNNLVKNIKD 255
Cdd:PRK05771 42 NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSleelikdveeelEKIEKEIKELEEEISELENEIKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 256 EENKIKKYLNiLKENIIEAKQAKKAKIIV------------KETEKSYLEYLDiENKLKD------LRENLDNLLEEQKl 317
Cdd:PRK05771 122 EIERLEPWGN-FDLDLSLLLGFKYVSVFVgtvpedkleelkLESDVENVEYIS-TDKGYVyvvvvvLKELSDEVEEELK- 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080658287 318 niqyQNNIEKLELSN-KNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYinLLDELEKLE 388
Cdd:PRK05771 199 ----KLGFERLELEEeGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY--LEIELERAE 264
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
842-907 |
6.47e-04 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 42.38 E-value: 6.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080658287 842 FEQLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSII-VTH 907
Cdd:COG1119 140 FGTLSQGEQRRVLIA-RALVK----DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTH 201
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
843-921 |
8.07e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 40.99 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 843 EQLSGGEQVSIAIAiRgtmtEYFTNSKFMILDEPTNNLDTErkklLAEYMGEILNNLEQSII-VTHDDTFREMAEKIIEL 921
Cdd:cd03223 90 DVLSGGEQQRLAFA-R----LLLHKPKFVFLDEATSALDEE----SEDRLYQLLKELGITVIsVGHRPSLWKFHDRVLDL 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
844-919 |
9.20e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 41.92 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTEyftnSKFMILDEPTNNLDTErkkLLAEYMgEILNNLEQS----IIVTHD-DTFREMAEKI 918
Cdd:PRK11124 141 HLSGGQQQRVAIA-RALMME----PQVLLFDEPTAALDPE---ITAQIV-SIIRELAETgitqVIVTHEvEVARKTASRV 211
|
.
gi 1080658287 919 I 919
Cdd:PRK11124 212 V 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-714 |
1.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 473 LNEKCQNLEDKEAEDyfSSKISIKTEELENLKKNIEE-KTQILVEKVVFEDKRKQYFELEKSIKDLE-------LSLKNE 544
Cdd:COG1196 237 LEAELEELEAELEEL--EAELEELEAELAELEAELEElRLELEELELELEEAQAEEYELLAELARLEqdiarleERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 545 EINLKEIELDIKNLDMDIQKLIENQEFQNSQ--MLREKKKELEVELRNLN----------------LDEKRENLKNLLEN 606
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEealleaeaelaeaeeeLEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 607 LEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLLLKVDK 686
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|....*...
gi 1080658287 687 NIKELYSLRTDKNLLKEKVSNLEEKIKN 714
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
173-638 |
1.03e-03 |
|
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];
Pssm-ID: 440834 [Multi-domain] Cd Length: 835 Bit Score: 42.79 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 173 LKEAVDKYKSEKENLDSKINSLKENMEdkeqitnFLKEEKDVEKNLQDNFKNINVVSKNLENEIKDYETTEVELNNLVKN 252
Cdd:COG1221 365 VKKGLLKLKENREELDKLSEYLEEYLI-------ISPDTEKKLISEEDEYELPYNFYEIIEDKYEELKSEGLSEEEINKI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 253 IkdeENKIKKYLNILKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSN 332
Cdd:COG1221 438 I---SKDIESYFKKLIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKI 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 333 KNLKVDISNL---EENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDILK 409
Cdd:COG1221 515 INPQLNEIKKkyyEEFILAAEAIKIIEEELKILIPDEEEGFILLLLIELKEEKSLSENVIVVVVIAHGGAAASSSMAVVN 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 410 KELVSKNDLFKIINIEELEKKLYNFQELEKELKLLEEQKI-----------IFETEIKTLKKSSKELSNKICPFLNEKCQ 478
Cdd:COG1221 595 LLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGKGGLLlllddggslfgIIIIEEEGIIIVTVVIVSTTTVLEAAARK 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 479 -NLEDKEAEDYFSSKISIKTEELENLKKNIEEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKN 557
Cdd:COG1221 675 kLLELDLDEIIVLEELLKNPLESKKIKISTSKKKKIIVTTIAITTGEAGGILILILIIELLDKDLILIIIEILLIIIKEE 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 558 LDMDIQKLIENQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKE 637
Cdd:COG1221 755 ILEKIIEEKKEVIIIVIISIIPLIIPPIILLLALKLIILIEILVLLEILIDKEKIENIIKELLSLLNIIIVLLIIDILIL 834
|
.
gi 1080658287 638 D 638
Cdd:COG1221 835 I 835
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
454-745 |
1.05e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 454 EIKTLKKSSKELSNKIcpfLNEKCQNLEDKEAEDYFSSKISIKTEE------LENLKKNIEEKT--QILVEKVvfeDKRK 525
Cdd:PLN03229 444 QILKAKESSSKPSELA---LNEMIEKLKKEIDLEYTEAVIAMGLQErlenlrEEFSKANSQDQLmhPVLMEKI---EKLK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 526 QYFELEKSIKDLELSLKNEEINLKE-------IELDIK--NLDMDIQKLIenQEFQNSQMLREKKKELEVELRNLNL--- 593
Cdd:PLN03229 518 DEFNKRLSRAPNYLSLKYKLDMLNEfsrakalSEKKSKaeKLKAEINKKF--KEVMDRPEIKEKMEALKAEVASSGAssg 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 594 ----DEKRENLKNLLENLEIEKKKILKS---------QNSIESNLKEINEFLKE----IKEDTNKNIENIkLEIKTFENK 656
Cdd:PLN03229 596 deldDDLKEKVEKMKKEIELELAGVLKSmglevigvtKKNKDTAEQTPPPNLQEkiesLNEEINKKIERV-IRSSDLKSK 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 657 LDNLKNPYNEYLKNNVLAEDldNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKIDELKEKYDIIKEELNEINK 736
Cdd:PLN03229 675 IELLKLEVAKASKTPDVTEK--EKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKNDDDKEEDS 752
|
....*....
gi 1080658287 737 KLGSSQEKI 745
Cdd:PLN03229 753 KEDGSRVEV 761
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
844-921 |
1.07e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 42.58 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSII-VTHD-DTFREMAEKII 919
Cdd:COG1123 142 QLSGGQRqrVAIAMAL-------ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLlITHDlGVVAEIADRVV 214
|
..
gi 1080658287 920 EL 921
Cdd:COG1123 215 VM 216
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
593-768 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 593 LDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEIneflKEIKEDTNKNIENIKLEIKTFENKLDNLKNpyneylknnv 672
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAA----KTELEDLEKEIKRLELEIEEVEARIKKYEE---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 673 laedldnlLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNI--KIDELKEKYDIIKEELNEINKKLGSSQEKIENYKK 750
Cdd:COG1579 81 --------QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170
....*....|....*...
gi 1080658287 751 ILEKISSQEEKQKKLLIE 768
Cdd:COG1579 153 ELEAELEELEAEREELAA 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
844-919 |
1.18e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 41.66 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAIRGTMteyftNSKFMILDEPTNNLDterkkllAEYMGEILNNLEQ-------SIIVTHDDTF-REMA 915
Cdd:PRK11264 144 RLSGGQQQRVAIARALAM-----RPEVILFDEPTSALD-------PELVGEVLNTIRQlaqekrtMVIVTHEMSFaRDVA 211
|
....
gi 1080658287 916 EKII 919
Cdd:PRK11264 212 DRAI 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
709-795 |
1.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 709 EEKIKNIKIDELKEKYDIIKEELNEINKKLGSSQEKIEnykKILEKISSQEEKQKKLLIEFKKLENKFNKAnliRNEVGQ 788
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEER---REELGE 90
|
....*..
gi 1080658287 789 MGRAISK 795
Cdd:COG3883 91 RARALYR 97
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
842-881 |
1.25e-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: 1.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1080658287 842 FEQLSGGEQ--VSIAIAI-RGTmteyftnsKFMILDEPTNNLD 881
Cdd:COG1120 135 VDELSGGERqrVLIARALaQEP--------PLLLLDEPTSHLD 169
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
845-907 |
1.33e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.46 E-value: 1.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080658287 845 LSGGE-Q-VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTErkkllAEYmgEILNNLEQ------SIIVTH 907
Cdd:COG1132 477 LSGGQrQrIAIARAL-------LKDPPILILDEATSALDTE-----TEA--LIQEALERlmkgrtTIVIAH 533
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
844-919 |
1.49e-03 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 41.33 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDterkKLLAEYMGEILNNLEQ-----SIIVTHD-DTFREMA 915
Cdd:cd03261 136 ELSGGMKkrVALARAL-------ALDPELLLYDEPTAGLD----PIASGVIDDLIRSLKKelgltSIMVTHDlDTAFAIA 204
|
....
gi 1080658287 916 EKII 919
Cdd:cd03261 205 DRIA 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
845-921 |
1.58e-03 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 41.32 E-value: 1.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080658287 845 LSGGEQVSIAIAirgtmTEYFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNlEQSIIVTHDDTFREMAEKIIEL 921
Cdd:cd03252 139 LSGGQRQRIAIA-----RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAG-RTVIIIAHRLSTVKNADRIIVM 209
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
175-384 |
1.61e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 175 EAVDKYKSEKENLDSKINSLKENM-EDKEQITNFLKEEKDVEKNLQDNFKNINVVSKNLENEIKDYETTEVELNNLvkni 253
Cdd:PLN02939 156 EDLEKILTEKEALQGKINILEMRLsETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVL---- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 254 KDEENKIKKYLNILKENIIEAKQAKKaKIIVKETEKSYLE--YLDIENKLKDLR------------------ENLDNLLE 313
Cdd:PLN02939 232 KEENMLLKDDIQFLKAELIEVAETEE-RVFKLEKERSLLDasLRELESKFIVAQedvsklsplqydcwwekvENLQDLLD 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080658287 314 ------EQKLNIQYQNNieklELSNKNLKVDISNLEENISK-NSEKKENLESEISELKIKEEDLDLKLKKYINLLDEL 384
Cdd:PLN02939 311 ratnqvEKAALVLDQNQ----DLRDKVDKLEASLKEANVSKfSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
684-911 |
1.77e-03 |
|
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: 41.61 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 684 VDKNIKELYSLRTDKNLLKEKVSNLEEKIKNIKIDELKEKYDIIKE--------ELNEINKKLGSSQEKIENYKKILEKI 755
Cdd:pfam13304 66 LEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFppeaeelrLGLDVEERIELSLSELSDLISGLLLL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 756 SSQEEKQKKLLIEFKKLENKFNKANLIRNEVGQ-MGRAISKYMLSGISNIASVNFNKITGRTERIEWSNEEKDKYAVYLV 834
Cdd:pfam13304 146 SIISPLSFLLLLDEGLLLEDWAVLDLAADLALFpDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLE 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080658287 835 -GQERKIAFEQLSGGEQVSIAIAIrgTMTEYFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTF 911
Cdd:pfam13304 226 nGGGGELPAFELSDGTKRLLALLA--ALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
336-522 |
1.88e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 336 KVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDI--LKKELV 413
Cdd:PRK05771 78 KVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtVPEDKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 414 SKNDLFKIINIEELEKKLYNFqelekelklleeQKIIFETEIKTLKKSSKELsnKICPFLNEKCQNLED-KEAEDYFSSK 492
Cdd:PRK05771 158 EELKLESDVENVEYISTDKGY------------VYVVVVVLKELSDEVEEEL--KKLGFERLELEEEGTpSELIREIKEE 223
|
170 180 190
....*....|....*....|....*....|
gi 1080658287 493 ISIKTEELENLKKNIEEKTQILVEKVVFED 522
Cdd:PRK05771 224 LEEIEKERESLLEELKELAKKYLEELLALY 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
579-771 |
1.88e-03 |
|
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: 41.67 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 579 EKKKELEVELRNLNldEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKED---TNKNIENIKLEIKTFEN 655
Cdd:COG4942 20 DAAAEAEAELEQLQ--QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaLEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 656 KLDNLKNPYNEYLKNNVLAEDLDNLLLKVD-KNIKELYSLRTdknLLKEKVSNLEEKIknikidelkekydiikEELNEI 734
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSpEDFLDAVRRLQ---YLKYLAPARREQA----------------EELRAD 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1080658287 735 NKKLGSSQEKIENYKKILEKISSQEEKQKKLLIEFKK 771
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
185-388 |
2.03e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 185 ENLDSKINSLKENMEDKEQITNFLKEekDVEKNLQDNFKNINVVSK-------NLENEIKDYETTEVELNNLVKNIKDEE 257
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDGEQLSDFQLE--DLVGMIQNAEKNILLLNQarlqaleDLEKILTEKEALQGKINILEMRLSETD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 258 NKIK--------------KYLNILKENIIE-AKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQ 322
Cdd:PLN02939 184 ARIKlaaqekihveileeQLEKLRNELLIRgATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLE 263
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080658287 323 NNIEKLELSNKNLKVDISNLEENISKNS--------EKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLE 388
Cdd:PLN02939 264 KERSLLDASLRELESKFIVAQEDVSKLSplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE 337
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
844-909 |
2.04e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.92 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 844 QLSGGEQVSIAIAirgtmTEYFTNSKFMILDEPTNNLDTERKKLLAEYMGEIlnNLEQS---IIVTHDD 909
Cdd:PRK10584 146 QLSGGEQQRVALA-----RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL--NREHGttlILVTHDL 207
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-43 |
2.21e-03 |
|
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: 40.14 E-value: 2.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1080658287 3 IKKVQLENYRSH-SNTTVEFTKGVNLILGKNGRGKTSILEAI 43
Cdd:cd03278 1 LKKLELKGFKSFaDKTTIPFPPGLTAIVGPNGSGKSNIIDAI 42
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
844-908 |
2.44e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.57 E-value: 2.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERKKLLAEYMGEIlnNLEQS---IIVTHD 908
Cdd:PRK11629 145 ELSGGERQRVAIA-RALVN----NPRLVLADEPTGNLDARNADSIFQLLGEL--NRLQGtafLVVTHD 205
|
|
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
300-756 |
2.46e-03 |
|
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];
Pssm-ID: 440834 [Multi-domain] Cd Length: 835 Bit Score: 41.63 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 300 KLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISEL-KIKEEDLDLKLKKYI 378
Cdd:COG1221 371 KLKENREELDKLSEYLEEYLIISPDTEKKLISEEDEYELPYNFYEIIEDKYEELKSEGLSEEEInKIISKDIESYFKKLI 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 379 NLLDELEKLENFKDKKLEDKLKKTTEIDILKKELVSKNDLFKIINIeelekkLYNFQELEKELKLLEEQKIIFETEIKTL 458
Cdd:COG1221 451 FKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSSNLFIA------LSLHLLSTLLRIKKGKKIINPQLNEIKK 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 459 KKSSKELSNKICPFLNE--KCQNLEDKEAEDYFSSKISIKTEELENLKKNIEEKTQI----------LVEKVVFEDKRKQ 526
Cdd:COG1221 525 KYYEEFILAAEAIKIIEeeLKILIPDEEEGFILLLLIELKEEKSLSENVIVVVVIAHggaaasssmaVVNLLLLEVAVAA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 527 YFE-LEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIENQEfqnsqMLREKKKELEVELRNLNLDEKRENLKNLLE 605
Cdd:COG1221 605 IDDpPLEVVDVLIEEKTIVVIINKGKGGLLLLLDDGGSLFGIIII-----EEEGIIIVTVVIVSTTTVLEAAARKKLLEL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 606 NLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKTFENKLDNLKNPYNEYLKNNVLAEDLDNLLLKVD 685
Cdd:COG1221 680 DLDEIIVLEELLKNPLESKKIKISTSKKKKIIVTTIAITTGEAGGILILILIIELLDKDLILIIIEILLIIIKEEILEKI 759
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080658287 686 KNIKELYSLRTDKNL--LKEKVSNLEEKIKNIKIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKIS 756
Cdd:COG1221 760 IEEKKEVIIIVIISIipLIIPPIILLLALKLIILIEILVLLEILIDKEKIENIIKELLSLLNIIIVLLIIDIL 832
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-386 |
2.48e-03 |
|
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: 41.29 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 175 EAVDKYKSEKENLDSKINSLKENMED-KEQITNFLKEEKDVEKNLQDNFKNINVVSKNL---ENEIKDyetTEVELNNLV 250
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAlKKEEKALLKQLAALERRIAALARRIRALEQELaalEAELAE---LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 251 KNIKDEENKIKKYLNILKENiieaKQAKKAKIIVKETEKS-------YLEYL---------DIENKLKDLRENLDNLLEE 314
Cdd:COG4942 97 AELEAQKEELAELLRALYRL----GRQPPLALLLSPEDFLdavrrlqYLKYLaparreqaeELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080658287 315 QKlniQYQNNIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEK 386
Cdd:COG4942 173 RA---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
618-784 |
2.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 618 QNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKtFENKldnlknpyNEYLKnnvLAEDLDNLLLKVDKNIKELyslrtd 697
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK--------EEIHK---LRNEFEKELRERRNELQKL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 698 KNLLKEKVSNLEEKIKNI--KIDELKEKYDIIKEELNEINKKLGSSQEKIENYKKILEKISS-QEEKQKKLLIEFKKLEN 774
Cdd:PRK12704 88 EKRLLQKEENLDRKLELLekREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEEAKEILLEKVEEEA 167
|
170
....*....|
gi 1080658287 775 KFNKANLIRN 784
Cdd:PRK12704 168 RHEAAVLIKE 177
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
845-921 |
2.76e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 845 LSGGEQVSIAIAirgtmTEYFTNSK--FMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAEKIIEL 921
Cdd:cd03238 88 LSGGELQRVKLA-----SELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
844-919 |
2.78e-03 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 40.09 E-value: 2.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHDDTFREMAEKII 919
Cdd:NF038007 141 QLSGGQQQRVAIA-RAMVS----NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRII 211
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-87 |
2.82e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.80 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 3 IKKVQLENYRS-HSNTTVEFTKG------VNLILGKNGRGKTSILEAISTVI-FNTKDRSGKETGKSYIKFGEKS----S 70
Cdd:COG1106 2 LISFSIENFRSfKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFLRnLVLNSSQPGDKLVEPFLLDSESknepS 81
|
90
....*....|....*...
gi 1080658287 71 KVDIDFIANDGR-EYNLK 87
Cdd:COG1106 82 EFEILFLLDGVRyEYGFE 99
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
844-919 |
3.11e-03 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. 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: 213218 [Multi-domain] Cd Length: 234 Bit Score: 40.29 E-value: 3.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERKKLLAEYMGEILNNlEQSIIVTHDDTFREMAEKII 919
Cdd:cd03251 138 KLSGGQRQRIAIA-RALLK----DPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAHRLSTIENADRIV 207
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
493-637 |
3.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 493 ISIKTEELENLKKNIEEKTQILvekvvfEDKRKQYFELEKSIKDLELSLKNEEINLKEIEldiknldmdiQKLIENQEFQ 572
Cdd:PRK00409 511 IGEDKEKLNELIASLEELEREL------EQKAEEAEALLKEAEKLKEELEEKKEKLQEEE----------DKLLEEAEKE 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080658287 573 NSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKE 637
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-47 |
3.20e-03 |
|
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: 40.32 E-value: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1080658287 3 IKKVQLENYRSHSNTTV--EFTKGVNLILGKNGRGKTSILEAISTVI 47
Cdd:cd03272 1 IKQVIIQGFKSYKDQTViePFSPKHNVVVGRNGSGKSNFFAAIRFVL 47
|
|
| ClyA_XaxA-like |
cd22657 |
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ... |
597-740 |
3.22e-03 |
|
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and similar proteins; This model includes Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, both parts of two-component alpha-helical pore-forming toxins (alpha-PFTs). The xaxAB genes encoding the XaxAB toxin have also been also identified in various plant and human pathogens. XaxAB triggers necrosis and apoptosis in both insect hemocytes and mammalian cells. Structure studies show that component A binds to component B's back, forming a subunit; twelve to fifteen of these subunits then conjoin as the pore-forming toxin. Component A stabilizes each subunit on the membrane and activates component B, which then punctures the membrane by swinging out its lower end. Similarly, Yersinia enterocolitica YaxA, encoded by the yaxAB gene, forms a pore predominantly composed of decamers of YaxA-YaxB heterodimers. Although both subunits bear membrane-active moieties, only YaxA is capable of binding to membranes by itself and YaxB is subsequently recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices; pore formation then progresses by further oligomerization of YaxA-YaxB dimers. YaxAB has been found to be strongly upregulated by the Yersinia master regulator RovA, a transcriptional activator of Yersinia outer membrane protein invasion which is involved in bacterial attachment and invasion across the intestinal epithelium.
Pssm-ID: 439155 [Multi-domain] Cd Length: 306 Bit Score: 40.65 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 597 RENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTN---KNIENIKLEIKTFENKLDNLKNP----YNEYLK 669
Cdd:cd22657 62 EDDIKQVGSDLKLFAGSIISTGEQIIEIISDLGEYLEDIKEDIKeysKSTEEVKARLDDFRDELREELIPevklKLKLID 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 670 NNVLAEDLDNLLLKVDKNIKELYSLRTD-KNLLKEKVSNL-----------------EEKIKNIKiDELKEKYDIIKEEL 731
Cdd:cd22657 142 RNDLDEEIEELNEEIDELDEEIDELNKEyKKLVGLAFTGLaggpigllitggifgvkAEKIRKER-NELIAEREELIQKL 220
|
....*....
gi 1080658287 732 NEINKKLGS 740
Cdd:cd22657 221 KSKNRLLGS 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
843-918 |
3.40e-03 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 3.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080658287 843 EQLSGGEQVSIAIAiRGTMteyfTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSII-VTHD-DTFREMAEKI 918
Cdd:cd03299 128 ETLSGGEQQRVAIA-RALV----VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDfEEAWALADKV 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-608 |
3.75e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 187 LDSKINSLKENMEDKEQITNFLKEEKDVEKNL---QDNFKNINVVSKNLENEIKDYETtEVELNNLVKNIKDEENKIKKY 263
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAGISKYKERRKETERKLertRENLDRLEDILNELERQLKSLER-QAEKAERYKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 264 LNILKeniIEAKQAKKAkiivkETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQ-YQNNIEKLELSNKNLKVDISNL 342
Cdd:TIGR02168 229 LLVLR---LEELREELE-----ELQEELKEAEEELEELTAELQELEEKLEELRLEVSeLEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 343 EENISKNSEKKENLESEISELkikEEDLDLKLKKYINLLDELEKLENfkdkkledklkkttEIDILKKELVSKNDLFkii 422
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEEL---EAQLEELESKLDELAEELAELEE--------------KLEELKEELESLEAEL--- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 423 niEELEKKLYNFQELEKELklleeqkiifETEIKTLKKSSKELSNKIcpflnekcqNLEDKEAEdYFSSKISIKTEELEN 502
Cdd:TIGR02168 361 --EELEAELEELESRLEEL----------EEQLETLRSKVAQLELQI---------ASLNNEIE-RLEARLERLEDRRER 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 503 LKKNIEEKTQILVEKvVFEDKRKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLiENQEFQnsqmLREKKK 582
Cdd:TIGR02168 419 LQQEIEELLKKLEEA-ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA-ERELAQ----LQARLD 492
|
410 420
....*....|....*....|....*.
gi 1080658287 583 ELEVELRnlNLDEKRENLKNLLENLE 608
Cdd:TIGR02168 493 SLERLQE--NLEGFSEGVKALLKNQS 516
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
845-886 |
3.81e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 3.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1080658287 845 LSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERKK 886
Cdd:PRK10762 396 LSGGNQQKVAIA-RGLMT----RPKVLILDEPTRGVDVGAKK 432
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
844-919 |
3.99e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 40.66 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLD-TERKKLLaeymgEILNNLEQS-----IIVTHD-DTFREM 914
Cdd:COG1123 404 ELSGGQRqrVAIARAL-------ALEPKLLILDEPTSALDvSVQAQIL-----NLLRDLQRElgltyLFISHDlAVVRYI 471
|
....*
gi 1080658287 915 AEKII 919
Cdd:COG1123 472 ADRVA 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
480-766 |
4.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 480 LEDKEAEdYFSSKISIKTEELENLKKNIEEKTQILVEKVV--------FEDKRKQYFELEksikdLELSLKNEEINLKEI 551
Cdd:COG1196 222 LKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAelaeleaeLEELRLELEELE-----LELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 552 EldIKNLDMDIQKLIENQEFQNSQMLREKKKELEVELRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEF 631
Cdd:COG1196 296 E--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 632 LKEIKEDTNKNIENIKLEIKTFENKLDNLKNpyneylknnvLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEK 711
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEE----------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1080658287 712 IKNIKIDELKEkydiiKEELNEINKKLGSSQEKIENYKKILEKISSQEEKQKKLL 766
Cdd:COG1196 444 LEEAAEEEAEL-----EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
508-771 |
4.96e-03 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 40.98 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 508 EEKTQILVEKVVFEDKRKQYFELEKSIKDLELSLKNeeiNLKEIELDIKNLdMDIQKLIENQEFQNSQMLREKKKELEVE 587
Cdd:PRK00448 4 QEKFKKLLDQINIPDDLQSEALESAEIEKVVVDKKS---KKWEFHLKFPNI-LPIEDFKLFKEKLKQSFSHIADIKVTFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 588 LRNlnldekrenlknllENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIENIKLEIKTFENKL-DNLKNPYNE 666
Cdd:PRK00448 80 IEV--------------ENITFTEELLLDYWNEIIEKAKKNSPLFKSLLKKQKVEVEGNKLIIKVNNEIErDHLKKKHLP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 667 YLKNNVLAEDLDNLLLKVDKNIKELyslrtDKNLLKEKVSNLEEKIKNIKIDELKEKYDIIKEELNEINKKLGSSQEKIE 746
Cdd:PRK00448 146 KLIKQYEKFGFGILKIDFEIDDSKE-----ELEKFEAQKEEEDEKLAKEALEAMKKLEAEKKKQSKNFDPKEGPVQIGKK 220
|
250 260
....*....|....*....|....*...
gi 1080658287 747 NYKKILEKISSQEEKQKKLLIE---FKK 771
Cdd:PRK00448 221 IDKEEITPMKEINEEERRVVVEgyvFKV 248
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
833-908 |
4.99e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 40.08 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 833 LVG----QERKIAfeQLSGGEQ--VSIA--IAIRgtmteyftnSKFMILDEPTNNLDTE-RKKLLAEyMGEILNNLEQS- 902
Cdd:COG3842 122 LVGleglADRYPH--QLSGGQQqrVALAraLAPE---------PRVLLLDEPLSALDAKlREEMREE-LRRLQRELGITf 189
|
....*.
gi 1080658287 903 IIVTHD 908
Cdd:COG3842 190 IYVTHD 195
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
844-919 |
5.00e-03 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 39.50 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLD--TER--KKLLAEYMGEilnnlEQSIIVTHDDTFREMAEKII 919
Cdd:cd03245 140 GLSGGQRQAVALA-RALLN----DPPILLLDEPTSAMDmnSEErlKERLRQLLGD-----KTLIIITHRPSLLDLVDRII 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
844-921 |
5.62e-03 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 38.53 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQ--VSIAIAIrgtmteyFTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVTHD-DTFREMAEKIIE 920
Cdd:cd03230 95 KLSGGMKqrLALAQAL-------LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAI 167
|
.
gi 1080658287 921 L 921
Cdd:cd03230 168 L 168
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
843-908 |
6.07e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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: 213263 [Multi-domain] Cd Length: 239 Bit Score: 39.24 E-value: 6.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080658287 843 EQLSGGEQVSIAIAiRGTMTEyftnSKFMILDEPTNNLDTERKKLLAEYMGEILNNLE-QSIIVTHD 908
Cdd:cd03296 135 AQLSGGQRQRVALA-RALAVE----PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHD 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-647 |
6.45e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 231 NLENEIKDYETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAKkakiivketeksyleyLDIENKLKDLRENLDN 310
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----------------EELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 311 LLEEqklniqyqnnIEKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKlenf 390
Cdd:TIGR02168 738 LEAE----------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE---- 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 391 kdkkledklkkttEIDILKKELVSKNDlfkiinieelekklyNFQELEKELKLLEEQKIIFETEIKTLKKSSKELSNKIc 470
Cdd:TIGR02168 804 -------------ALDELRAELTLLNE---------------EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI- 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 471 PFLNEKCQNLEDKEAEdyfsskISIKTEELENLKKNIEEKTQILVEKvvFEDKRKQYFELEKSIKDLELSLKNEEINLKE 550
Cdd:TIGR02168 855 ESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRELEELREKLAQ 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 551 IELDIKNLDMDIQKLIE--NQEFQ---------------NSQMLREKKKELEVELRNL---NLD--EKRENLKNLLENLE 608
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQErlSEEYSltleeaealenkiedDEEEARRRLKRLENKIKELgpvNLAaiEEYEELKERYDFLT 1006
|
410 420 430
....*....|....*....|....*....|....*....
gi 1080658287 609 IEKKKILKSQNSIESNLKEINeflKEIKEDTNKNIENIK 647
Cdd:TIGR02168 1007 AQKEDLTEAKETLEEAIEEID---REARERFKDTFDQVN 1042
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
184-376 |
6.82e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 184 KENLDSKINSLKENMEDKEQITNFLKEEKDVEKnlqdnfknINVVSKNLENEIKDYETTEVELNNLVKNIKDEENKIKKY 263
Cdd:COG5022 926 KTELIARLKKLLNNIDLEEGPSIEYVKLPELNK--------LHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNF 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 264 LNILKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKNLKVDISN-- 341
Cdd:COG5022 998 KKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENsl 1077
|
170 180 190
....*....|....*....|....*....|....*
gi 1080658287 342 LEENISKNSEKKENLESEISELKIKEEDLDLKLKK 376
Cdd:COG5022 1078 LDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPA 1112
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
561-676 |
8.25e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 39.67 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 561 DIQKLIENQE-FQnsQMLREKKKELEVElRNLNLDEKRENLKNLLENLEIEKKKILKSQNSIESNLKEINEFLKEIKEdt 639
Cdd:PRK05431 3 DIKLIRENPEaVK--EALAKRGFPLDVD-ELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKE-- 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1080658287 640 nknienIKLEIKTFENKLDNLKNPYNEYLKN--NVLAED 676
Cdd:PRK05431 78 ------LKEEIKALEAELDELEAELEELLLRipNLPHDS 110
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
844-921 |
8.57e-03 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. 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: 213223 [Multi-domain] Cd Length: 241 Bit Score: 39.09 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 844 QLSGGEQVSIAIAiRGTMteyfTNSKFMILDEPTNNLDTERKKLLAEYMGEILNNLEQSIIVT-HD-DTFREMAEKIIEL 921
Cdd:cd03256 144 QLSGGQQQRVAIA-RALM----QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSlHQvDLAREYADRIVGL 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
843-921 |
8.69e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 39.92 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 843 EQLSGGEQVSIAIAiRGTMTEyftnSKFMILDEPTNNLDTER----KKLLAEYMGEIlnnleqsIIVTHDDTFRE-MAEK 917
Cdd:TIGR03719 160 TKLSGGERRRVALC-RLLLSK----PDMLLLDEPTNHLDAESvawlERHLQEYPGTV-------VAVTHDRYFLDnVAGW 227
|
....
gi 1080658287 918 IIEL 921
Cdd:TIGR03719 228 ILEL 231
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
124-820 |
8.76e-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: 40.03 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 124 KGFEETYENIVIAKQNEFINIFKAKPKDREEIFNKIFNTQIYKEMYDSFLKEAVDKYKSEKENLDSK-INSLKENMEDKE 202
Cdd:TIGR01612 1000 KYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKnIELLNKEILEEA 1079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 203 Q--ITNFLK-EEKDVEKNLQDNFKNINVVSKNLENEIK-DYETTEVELNNLVKNIKDEENKIKKYLNILKENIIEAKQAK 278
Cdd:TIGR01612 1080 EinITNFNEiKEKLKHYNFDDFGKEENIKYADEINKIKdDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVA 1159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 279 KAKII---VKETEKSYLEYLDIENKLKDLRENLDNLLEEQKLNIQYQNNIEKLELSNKNLKVDISNLeenisknsekken 355
Cdd:TIGR01612 1160 DKAISnddPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKL------------- 1226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 356 LESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEIDIL--------KKELVSKNDLFKIINIEEL 427
Cdd:TIGR01612 1227 FLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFnishdddkDHHIISKKHDENISDIREK 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 428 EKKLYNFQELEKELKLLEEQKIIFETEIKTLKKSSKELSNKICPFLN----EKCQNLEDKEAE-----DYFSSKISIKTE 498
Cdd:TIGR01612 1307 SLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilklNKIKKIIDEVKEytkeiEENNKNIKDELD 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 499 ELENLKKNIEEKTQILVEKVVFEDK--RKQYFELEKSIKDLELSLKNEEINLKEIELDIKNLDMDIQKLIENQEFQN--S 574
Cdd:TIGR01612 1387 KSEKLIKKIKDDINLEECKSKIESTldDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADnkS 1466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 575 QMLREKKKELEVELRNLNLDEKRENLknllENLEIEKKKILKSQNSIESNLKEINEFLKEIKEDTNKNIEnikLEIKtfe 654
Cdd:TIGR01612 1467 QHILKIKKDNATNDHDFNINELKEHI----DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSA---LAIK--- 1536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 655 NKLDNLKNPYNEYLKNnvLAEDLDNLLLKVDKNIKELYSLRTDKNLLKEKVSNLEEKIKNI---------------KIDE 719
Cdd:TIGR01612 1537 NKFAKTKKDSEIIIKE--IKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAidiqlslenfenkflKISD 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 720 LKEKYDIIKEELNEINKKLGSS---------QEKIENYKKILEKISSQEEKQKKLLIEFKKLENKFNKANLIRNEVGQMG 790
Cdd:TIGR01612 1615 IKKKINDCLKETESIEKKISSFsidsqdtelKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHK 1694
|
730 740 750
....*....|....*....|....*....|
gi 1080658287 791 RAISKYMLSGISNIASVNFNKITGRTERIE 820
Cdd:TIGR01612 1695 KNYEIGIIEKIKEIAIANKEEIESIKELIE 1724
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
845-921 |
9.00e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 9.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080658287 845 LSGGEQVSIAIAiRGTMTeyftNSKFMILDEPTNNLDTERkkllAEYMGEILNNLEQSII-VTHDDTF-REMAEKIIEL 921
Cdd:PRK11147 157 LSGGWLRKAALG-RALVS----NPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIfISHDRSFiRNMATRIVDL 226
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
156-304 |
9.78e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 38.55 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 156 FNKIFNtQIYKEMYDsFLKEAVDKYKSEKENLDSKINSLKENMEDKEQ-ITNFLKEEKDVEKNLQDNFKNINVVSKNLEN 234
Cdd:cd21116 67 YNNTFQ-SYYPDLIE-LADNLIKGDQGAKQQLLQGLEALQSQVTKKQTsVTSFINELTTFKNDLDDDSRNLQTDATKAQA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 235 EIKDYETTEVELNNLVKNIKDEENKIKKYLNI----------LKENIIEAKQAKKAKIIVKETEKSYLEYLDIENKLKDL 304
Cdd:cd21116 145 QVAVLNALKNQLNSLAEQIDAAIDALEKLSNDwqtldsdikeLITDLEDAESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
326-431 |
9.89e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080658287 326 EKLELSNKNLKVDISNLEENISKNSEKKENLESEISELKIKEEDLDLKLKKYINLLDELEKLENFKDKKLEDKLKKTTEI 405
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474
|
90 100
....*....|....*....|....*.
gi 1080658287 406 DILKKELVSKNDlfkiiNIEELEKKL 431
Cdd:COG2433 475 ERLERELEEERE-----RIEELKRKL 495
|
|
| |
